ID   BASI_HUMAN              Reviewed;         385 AA.
AC   P35613; A6NJW1; D3YLG5; Q7Z796; Q8IZL7;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 2.
DT   02-OCT-2024, entry version 238.
DE   RecName: Full=Basigin {ECO:0000305};
DE   AltName: Full=5F7;
DE   AltName: Full=Collagenase stimulatory factor;
DE   AltName: Full=Extracellular matrix metalloproteinase inducer;
DE            Short=EMMPRIN;
DE   AltName: Full=Hepatoma-associated antigen {ECO:0000303|PubMed:15688292};
DE            Short=HAb18G {ECO:0000303|PubMed:15688292};
DE   AltName: Full=Leukocyte activation antigen M6;
DE   AltName: Full=OK blood group antigen;
DE   AltName: Full=Tumor cell-derived collagenase stimulatory factor;
DE            Short=TCSF;
DE   AltName: CD_antigen=CD147;
DE   Flags: Precursor;
GN   Name=BSG {ECO:0000312|HGNC:HGNC:1116}; ORFNames=UNQ6505/PRO21383;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   PubMed=1634773;
RA   Kasinrerk W., Fiebiger E., Stefanova I., Baumruker T., Knapp W.,
RA   Stockinger H.;
RT   "Human leukocyte activation antigen M6, a member of the Ig superfamily, is
RT   the species homologue of rat OX-47, mouse basigin, and chicken HT7
RT   molecule.";
RL   J. Immunol. 149:847-854(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RX   PubMed=1783610; DOI=10.1093/oxfordjournals.jbchem.a123657;
RA   Miyauchi T., Masuzawa Y., Muramatsu T.;
RT   "The basigin group of the immunoglobulin superfamily: complete conservation
RT   of a segment in and around transmembrane domains of human and mouse basigin
RT   and chicken HT7 antigen.";
RL   J. Biochem. 110:770-774(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   PubMed=7812975;
RA   Biswas C., Zhang Y., Decastro R., Guo H., Nakamura T., Kataoka H.,
RA   Nabeshima K.;
RT   "The human tumor cell-derived collagenase stimulatory factor (renamed
RT   EMMPRIN) is a member of the immunoglobulin superfamily.";
RL   Cancer Res. 55:434-439(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 2).
RA   Wakasugi H., Scamps C., Yang G., Vancong N., Bernheim A., Tursz T.,
RA   Harada N.;
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 2).
RA   Decastro R., Zhang Y., Kataoka H., Coon J., Biswas C.;
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RX   PubMed=9767135; DOI=10.1016/s0378-1119(98)00400-4;
RA   Guo H., Majmudar G., Jensen T.C., Biswas C., Toole B.P., Gordon M.K.;
RT   "Characterization of the gene for human EMMPRIN, a tumor cell surface
RT   inducer of matrix metalloproteinases.";
RL   Gene 220:99-108(1998).
RN   [7]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 2).
RA   Sato T., Takita M., Noguchi Y., Hirata M., Sakai T., Ito A.;
RT   "Regulation of EMMPRIN/CD147 expression and its function of controlling
RT   matrix metalloproteinases production and cell-surface localization in co-
RT   culture of human uterine cervical carcinoma SKG-II cells and human uterine
RT   cervical fibroblasts.";
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 2).
RA   Kim D., Kanai Y., Choi H., Shin H., Kim J., Teraoka H., Shigeta Y.,
RA   Chairoungdua A., Babu E., Anzai N., Iribe Y., Endou H.;
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC   TISSUE=Retina;
RX   PubMed=12939332; DOI=10.1167/iovs.02-0995;
RA   Ochrietor J.D., Moroz T.P., van Ekeris L., Clamp M.F., Jefferson S.C.,
RA   deCarvalho A.C., Fadool J.M., Wistow G., Muramatsu T., Linser P.J.;
RT   "Retina-specific expression of 5A11/Basigin-2, a member of the
RT   immunoglobulin gene superfamily.";
RL   Invest. Ophthalmol. Vis. Sci. 44:4086-4096(2003).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), SUBUNIT (ISOFORMS 2 AND 3),
RP   SUBCELLULAR LOCATION (ISOFORMS 2; 3 AND 4), ALTERNATIVE PROMOTER USAGE,
RP   TISSUE SPECIFICITY (ISOFORMS 2; 3 AND 4), AND GLYCOSYLATION (ISOFORMS 2; 3
RP   AND 4).
RX   PubMed=21536654; DOI=10.1128/mcb.05160-11;
RA   Liao C.G., Kong L.M., Song F., Xing J.L., Wang L.X., Sun Z.J., Tang H.,
RA   Yao H., Zhang Y., Wang L., Wang Y., Yang X.M., Li Y., Chen Z.N.;
RT   "Characterization of basigin isoforms and the inhibitory function of
RT   basigin-3 in human hepatocellular carcinoma proliferation and invasion.";
RL   Mol. Cell. Biol. 31:2591-2604(2011).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   SeattleSNPs variation discovery resource;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [13]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [14]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [15]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [16]
RP   PROTEIN SEQUENCE OF 22-36 (ISOFORM 1).
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally verified
RT   cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [17]
RP   PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RX   PubMed=1846736; DOI=10.1016/0003-9861(91)90332-d;
RA   Nabeshima K., Lane W.S., Biswas C.;
RT   "Partial sequencing and characterization of the tumor cell-derived
RT   collagenase stimulatory factor.";
RL   Arch. Biochem. Biophys. 285:90-96(1991).
RN   [18]
RP   FUNCTION (ISOFORM 2).
RX   PubMed=11688976; DOI=10.1006/bbrc.2001.5847;
RA   Yurchenko V., O'Connor M., Dai W.W., Guo H., Toole B., Sherry B.,
RA   Bukrinsky M.;
RT   "CD147 is a signaling receptor for cyclophilin B.";
RL   Biochem. Biophys. Res. Commun. 288:786-788(2001).
RN   [19]
RP   FUNCTION (ISOFORM 2) (MICROBIAL INFECTION), AND INTERACTION WITH PPIA
RP   (ISOFORM 2).
RX   PubMed=11353871; DOI=10.1073/pnas.111583198;
RA   Pushkarsky T., Zybarth G., Dubrovsky L., Yurchenko V., Tang H., Guo H.,
RA   Toole B., Sherry B., Bukrinsky M.;
RT   "CD147 facilitates HIV-1 infection by interacting with virus-associated
RT   cyclophilin A.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:6360-6365(2001).
RN   [20]
RP   FUNCTION (ISOFORM 2).
RX   PubMed=12553375; DOI=10.1023/a:1021350718226;
RA   Caudroy S., Polette M., Nawrocki-Raby B., Cao J., Toole B.P., Zucker S.,
RA   Birembaut P.;
RT   "EMMPRIN-mediated MMP regulation in tumor and endothelial cells.";
RL   Clin. Exp. Metastasis 19:697-702(2002).
RN   [21]
RP   FUNCTION (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), AND TISSUE
RP   SPECIFICITY (ISOFORM 2).
RX   PubMed=11992541; DOI=10.1002/ijc.10390;
RA   Kanekura T., Chen X., Kanzaki T.;
RT   "Basigin (CD147) is expressed on melanoma cells and induces tumor cell
RT   invasion by stimulating production of matrix metalloproteinases by
RT   fibroblasts.";
RL   Int. J. Cancer 99:520-528(2002).
RN   [22]
RP   FUNCTION (ISOFORM 2), MUTAGENESIS (ISOFORM 2), AND INTERACTION WITH PPIA
RP   (ISOFORM 2).
RX   PubMed=11943775; DOI=10.1074/jbc.m201593200;
RA   Yurchenko V., Zybarth G., O'Connor M., Dai W.W., Franchin G., Hao T.,
RA   Guo H., Hung H.C., Toole B., Gallay P., Sherry B., Bukrinsky M.;
RT   "Active site residues of cyclophilin A are crucial for its signaling
RT   activity via CD147.";
RL   J. Biol. Chem. 277:22959-22965(2002).
RN   [23]
RP   REVIEW.
RX   PubMed=12792908; DOI=10.14670/hh-18.981;
RA   Muramatsu T., Miyauchi T.;
RT   "Basigin (CD147): a multifunctional transmembrane protein involved in
RT   reproduction, neural function, inflammation and tumor invasion.";
RL   Histol. Histopathol. 18:981-987(2003).
RN   [24]
RP   GLYCOSYLATION AT ASN-160 AND ASN-268.
RX   PubMed=12754519; DOI=10.1038/nbt827;
RA   Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT   "Identification and quantification of N-linked glycoproteins using
RT   hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL   Nat. Biotechnol. 21:660-666(2003).
RN   [25]
RP   FUNCTION (ISOFORM 2).
RX   PubMed=15833850; DOI=10.1158/0008-5472.can-04-3605;
RA   Tang Y., Nakada M.T., Kesavan P., McCabe F., Millar H., Rafferty P.,
RA   Bugelski P., Yan L.;
RT   "Extracellular matrix metalloproteinase inducer stimulates tumor
RT   angiogenesis by elevating vascular endothelial cell growth factor and
RT   matrix metalloproteinases.";
RL   Cancer Res. 65:3193-3199(2005).
RN   [26]
RP   FUNCTION (ISOFORM 2) (MICROBIAL INFECTION), INTERACTION WITH PPIA (ISOFORM
RP   2), AND SUBCELLULAR LOCATION (ISOFORM 2).
RX   PubMed=15688292; DOI=10.1086/427811;
RA   Chen Z., Mi L., Xu J., Yu J., Wang X., Jiang J., Xing J., Shang P.,
RA   Qian A., Li Y., Shaw P.X., Wang J., Duan S., Ding J., Fan C., Zhang Y.,
RA   Yang Y., Yu X., Feng Q., Li B., Yao X., Zhang Z., Li L., Xue X., Zhu P.;
RT   "Function of HAb18G/CD147 in invasion of host cells by severe acute
RT   respiratory syndrome coronavirus.";
RL   J. Infect. Dis. 191:755-760(2005).
RN   [27]
RP   INTERACTION WITH PPIL2 (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), AND
RP   MUTAGENESIS (ISOFORM 2).
RX   PubMed=15946952; DOI=10.1074/jbc.m503770200;
RA   Pushkarsky T., Yurchenko V., Vanpouille C., Brichacek B., Vaisman I.,
RA   Hatakeyama S., Nakayama K.I., Sherry B., Bukrinsky M.I.;
RT   "Cell surface expression of CD147/EMMPRIN is regulated by cyclophilin 60.";
RL   J. Biol. Chem. 280:27866-27871(2005).
RN   [28]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [29]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Melanoma;
RX   PubMed=17081065; DOI=10.1021/pr060363j;
RA   Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA   Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA   Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT   "Proteomic and bioinformatic characterization of the biogenesis and
RT   function of melanosomes.";
RL   J. Proteome Res. 5:3135-3144(2006).
RN   [30]
RP   FUNCTION (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), AND INTERACTION
RP   WITH SLC16A1 (ISOFORM 2).
RX   PubMed=17127621; DOI=10.1080/09687860600841967;
RA   Manoharan C., Wilson M.C., Sessions R.B., Halestrap A.P.;
RT   "The role of charged residues in the transmembrane helices of
RT   monocarboxylate transporter 1 and its ancillary protein basigin in
RT   determining plasma membrane expression and catalytic activity.";
RL   Mol. Membr. Biol. 23:486-498(2006).
RN   [31]
RP   INTERACTION WITH AJAP1 (ISOFORM 2), AND SUBCELLULAR LOCATION (ISOFORM 2).
RX   PubMed=17267690; DOI=10.1091/mbc.e06-07-0637;
RA   Schreiner A., Ruonala M., Jakob V., Suthaus J., Boles E., Wouters F.,
RA   Starzinski-Powitz A.;
RT   "junction protein shrew-1 influences cell invasion and interacts with
RT   invasion-promoting protein CD147.";
RL   Mol. Biol. Cell 18:1272-1281(2007).
RN   [32]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [33]
RP   FUNCTION (ISOFORM 2).
RX   PubMed=19837976; DOI=10.1182/blood-2009-04-217380;
RA   Bougatef F., Quemener C., Kellouche S., Naimi B., Podgorniak M.P.,
RA   Millot G., Gabison E.E., Calvo F., Dosquet C., Lebbe C., Menashi S.,
RA   Mourah S.;
RT   "EMMPRIN promotes angiogenesis through hypoxia-inducible factor-2alpha-
RT   mediated regulation of soluble VEGF isoforms and their receptor VEGFR-2.";
RL   Blood 114:5547-5556(2009).
RN   [34]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160 AND ASN-268.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [35]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160 AND ASN-268.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [36]
RP   FUNCTION (ISOFORM 2) (MICROBIAL INFECTION).
RX   PubMed=20147391; DOI=10.1128/jvi.02168-09;
RA   Watanabe A., Yoneda M., Ikeda F., Terao-Muto Y., Sato H., Kai C.;
RT   "CD147/EMMPRIN acts as a functional entry receptor for measles virus on
RT   epithelial cells.";
RL   J. Virol. 84:4183-4193(2010).
RN   [37]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [38]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [39]
RP   FUNCTION (ISOFORM 2), AND INTERACTION WITH SLC16A12 (ISOFORM 2).
RX   PubMed=21778275; DOI=10.1167/iovs.10-6579;
RA   Castorino J.J., Gallagher-Colombo S.M., Levin A.V., Fitzgerald P.G.,
RA   Polishook J., Kloeckener-Gruissem B., Ostertag E., Philp N.J.;
RT   "Juvenile cataract-associated mutation of solute carrier SLC16A12 impairs
RT   trafficking of the protein to the plasma membrane.";
RL   Invest. Ophthalmol. Vis. Sci. 52:6774-6784(2011).
RN   [40]
RP   INTERACTION WITH PPIA.
RX   PubMed=21245143; DOI=10.1074/jbc.c110.181347;
RA   Song F., Zhang X., Ren X.B., Zhu P., Xu J., Wang L., Li Y.F., Zhong N.,
RA   Ru Q., Zhang D.W., Jiang J.L., Xia B., Chen Z.N.;
RT   "Cyclophilin A (CyPA) induces chemotaxis independent of its peptidylprolyl
RT   cis-trans isomerase activity: direct binding between CyPA and the
RT   ectodomain of CD147.";
RL   J. Biol. Chem. 286:8197-8203(2011).
RN   [41]
RP   FUNCTION (ISOFORMS 1 AND 2) (MICROBIAL INFECTION), INTERACTION WITH
RP   P.FALCIPARUM RH5 (ISOFORMS 1 AND 2) (MICROBIAL INFECTION), GLYCOSYLATION,
RP   VARIANTS ASN-152; LEU-176; PRO-206; LYS-208 AND VAL-269, AND MUTAGENESIS OF
RP   ASN-160; ASN-268 AND ASN-302.
RX   PubMed=22080952; DOI=10.1038/nature10606;
RA   Crosnier C., Bustamante L.Y., Bartholdson S.J., Bei A.K., Theron M.,
RA   Uchikawa M., Mboup S., Ndir O., Kwiatkowski D.P., Duraisingh M.T.,
RA   Rayner J.C., Wright G.J.;
RT   "Basigin is a receptor essential for erythrocyte invasion by Plasmodium
RT   falciparum.";
RL   Nature 480:534-537(2011).
RN   [42]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [43]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [44]
RP   INTERACTION WITH P.FALCIPARUM RH5 (ISOFORM 2) (MICROBIAL INFECTION), AND
RP   MUTAGENESIS OF (ISOFORM 2).
RX   PubMed=24297912; DOI=10.1073/pnas.1320771110;
RA   Wanaguru M., Liu W., Hahn B.H., Rayner J.C., Wright G.J.;
RT   "RH5-Basigin interaction plays a major role in the host tropism of
RT   Plasmodium falciparum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:20735-20740(2013).
RN   [45]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362 AND SER-368, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [46]
RP   FUNCTION (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM 1), TISSUE SPECIFICITY
RP   (ISOFORM 1), AND INTERACTION WITH NXNL1 (ISOFORM 1).
RX   PubMed=25957687; DOI=10.1016/j.cell.2015.03.023;
RA   Ait-Ali N., Fridlich R., Millet-Puel G., Clerin E., Delalande F.,
RA   Jaillard C., Blond F., Perrocheau L., Reichman S., Byrne L.C.,
RA   Olivier-Bandini A., Bellalou J., Moyse E., Bouillaud F., Nicol X.,
RA   Dalkara D., van Dorsselaer A., Sahel J.A., Leveillard T.;
RT   "Rod-derived cone viability factor promotes cone survival by stimulating
RT   aerobic glycolysis.";
RL   Cell 161:817-832(2015).
RN   [47]
RP   FUNCTION (ISOFORM 2) (MICROBIAL INFECTION), INTERACTION WITH P.FACILPARUM
RP   RH5 (ISOFORM 2)(MICROBIAL INFECTION), SUBCELLULAR LOCATION (ISOFORM 2),
RP   TISSUE SPECIFICITY (ISOFORM 2), AND BIOTECHNOLOGY (ISOFORM 2).
RX   PubMed=26195724; DOI=10.1084/jem.20150032;
RA   Zenonos Z.A., Dummler S.K., Mueller-Sienerth N., Chen J., Preiser P.R.,
RA   Rayner J.C., Wright G.J.;
RT   "Basigin is a druggable target for host-oriented antimalarial
RT   interventions.";
RL   J. Exp. Med. 212:1145-1151(2015).
RN   [48]
RP   FUNCTION (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), INTERACTION WITH
RP   VEGFA AND VEGFR2 (ISOFORM 2), MUTAGENESIS (ISOFORM 2), AND REGION (ISOFORM
RP   2).
RX   PubMed=25825981; DOI=10.18632/oncotarget.2870;
RA   Khayati F., Perez-Cano L., Maouche K., Sadoux A., Boutalbi Z.,
RA   Podgorniak M.P., Maskos U., Setterblad N., Janin A., Calvo F., Lebbe C.,
RA   Menashi S., Fernandez-Recio J., Mourah S.;
RT   "EMMPRIN/CD147 is a novel coreceptor of VEGFR-2 mediating its activation by
RT   VEGF.";
RL   Oncotarget 6:9766-9780(2015).
RN   [49]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [50]
RP   INTERACTION WITH XKR8.
RX   PubMed=27503893; DOI=10.1073/pnas.1610403113;
RA   Suzuki J., Imanishi E., Nagata S.;
RT   "Xkr8 phospholipid scrambling complex in apoptotic phosphatidylserine
RT   exposure.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9509-9514(2016).
RN   [51]
RP   FUNCTION (ISOFORM 2), AND INTERACTION WITH SLC16A11 (ISOFORM 2).
RX   PubMed=28666119; DOI=10.1016/j.cell.2017.06.011;
RG   MEDIA Consortium;
RG   SIGMA T2D Consortium;
RA   Rusu V., Hoch E., Mercader J.M., Tenen D.E., Gymrek M., Hartigan C.R.,
RA   DeRan M., von Grotthuss M., Fontanillas P., Spooner A., Guzman G.,
RA   Deik A.A., Pierce K.A., Dennis C., Clish C.B., Carr S.A., Wagner B.K.,
RA   Schenone M., Ng M.C.Y., Chen B.H., Centeno-Cruz F., Zerrweck C., Orozco L.,
RA   Altshuler D.M., Schreiber S.L., Florez J.C., Jacobs S.B.R., Lander E.S.;
RT   "Type 2 diabetes variants disrupt function of SLC16A11 through two distinct
RT   mechanisms.";
RL   Cell 170:199-212(2017).
RN   [52]
RP   FUNCTION (ISOFORM 2) (MICROBIAL INFECTION), SUBCELLULAR LOCATION (ISOFORM
RP   2), AND TISSUE SPECIFICITY (ISOFORM 2).
RX   PubMed=28409866; DOI=10.1111/cmi.12747;
RA   Aniweh Y., Gao X., Hao P., Meng W., Lai S.K., Gunalan K., Chu T.T.,
RA   Sinha A., Lescar J., Chandramohanadas R., Li H.Y., Sze S.K., Preiser P.R.;
RT   "P. falciparum RH5-Basigin interaction induces changes in the cytoskeleton
RT   of the host RBC.";
RL   Cell. Microbiol. 19:0-0(2017).
RN   [53]
RP   FUNCTION (MICROBIAL INFECTION) (ISOFORM 2), AND SUBCELLULAR LOCATION
RP   (ISOFORM 2).
RX   PubMed=29739904; DOI=10.1128/mbio.00781-18;
RA   Vanarsdall A.L., Pritchard S.R., Wisner T.W., Liu J., Jardetzky T.S.,
RA   Johnson D.C.;
RT   "CD147 Promotes Entry of Pentamer-Expressing Human Cytomegalovirus into
RT   Epithelial and Endothelial Cells.";
RL   MBio 9:0-0(2018).
RN   [54]
RP   REVIEW ON FUNCTION (MICROBIAL FUNCTION), AND REVIEW ON INTERACTION WITH
RP   SARS-COV-2 SPIKE GLYCOPROTEIN (MICROBIAL FUNCTION).
RX   PubMed=32307653; DOI=10.1007/s12015-020-09976-7;
RA   Ulrich H., Pillat M.M.;
RT   "CD147 as a Target for COVID-19 Treatment: Suggested Effects of
RT   Azithromycin and Stem Cell Engagement.";
RL   Stem. Cell. Rev. Rep. 16:434-440(2020).
RN   [55]
RP   FUNCTION (MICROBIAL FUNCTION), AND INTERACTION WITH SARS-COV-2 SPIKE
RP   GLYCOPROTEIN (MICROBIAL FUNCTION).
RX   PubMed=33432067; DOI=10.1038/s41598-020-80464-1;
RA   Shilts J., Crozier T.W.M., Greenwood E.J.D., Lehner P.J., Wright G.J.;
RT   "No evidence for basigin/CD147 as a direct SARS-CoV-2 spike binding
RT   receptor.";
RL   Sci. Rep. 11:413-413(2021).
RN   [56]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 140-321, SUBUNIT (ISOFORM 2), AND
RP   DISULFIDE BONDS.
RX   PubMed=18430721; DOI=10.1074/jbc.m802694200;
RA   Yu X.-L., Hu T., Du J.-M., Ding J.-P., Yang X.-M., Zhang J., Yang B.,
RA   Shen X., Zhang Z., Zhong W.-D., Wen N., Jiang H., Zhu P., Chen Z.-N.;
RT   "Crystal structure of HAb18G/CD147: implications for immunoglobulin
RT   superfamily homophilic adhesion.";
RL   J. Biol. Chem. 283:18056-18065(2008).
RN   [57]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 13-219, IDENTIFICATION BY MASS
RP   SPECTROMETRY, SUBUNIT (ISOFORM 1), AND DISULFIDE BONDS.
RX   PubMed=19768682; DOI=10.1002/prot.22577;
RA   Luo J., Teplyakov A., Obmolova G., Malia T., Wu S.-J., Beil E., Baker A.,
RA   Swencki-Underwood B., Zhao Y., Sprenkle J., Dixon K., Sweet R.,
RA   Gilliland G.L.;
RT   "Structure of the EMMPRIN N-terminal domain 1: dimerization via beta-strand
RT   swapping.";
RL   Proteins 77:1009-1014(2009).
RN   [58] {ECO:0007744|PDB:3QQN, ECO:0007744|PDB:3QR2}
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 23-138, FUNCTION (ISOFORM 1),
RP   DISULFIDE BOND, AND MUTAGENESIS OF CYS-67.
RX   PubMed=21620857; DOI=10.1016/j.jmb.2011.04.060;
RA   Redzic J.S., Armstrong G.S., Isern N.G., Jones D.N., Kieft J.S.,
RA   Eisenmesser E.Z.;
RT   "The retinal specific CD147 Ig0 domain: from molecular structure to
RT   biological activity.";
RL   J. Mol. Biol. 411:68-82(2011).
RN   [59] {ECO:0007744|PDB:4U0Q}
RP   X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 140-385, INTERACTION WITH
RP   P.FACILPARUM RH5 (ISOFORM 2) (MICROBIAL INFECTION), AND DISULFIDE BONDS.
RX   PubMed=25132548; DOI=10.1038/nature13715;
RA   Wright K.E., Hjerrild K.A., Bartlett J., Douglas A.D., Jin J., Brown R.E.,
RA   Illingworth J.J., Ashfield R., Clemmensen S.B., de Jongh W.A., Draper S.J.,
RA   Higgins M.K.;
RT   "Structure of malaria invasion protein RH5 with erythrocyte basigin and
RT   blocking antibodies.";
RL   Nature 515:427-430(2014).
RN   [60] {ECO:0007744|PDB:5X0T}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 138-217, AND DISULFIDE BONDS.
RA   Zhang M.-Y., Lin P., Zhu P., Chen Z.-N.;
RT   "Crystal structure of CD147 C2 domain in complex with Fab of its monoclonal
RT   antibody.";
RL   Submitted (JAN-2017) to the PDB data bank.
RN   [61] {ECO:0007744|PDB:6LYY, ECO:0007744|PDB:6LZ0, ECO:0007744|PDB:7CKO, ECO:0007744|PDB:7CKR, ECO:0007744|PDB:7DA5}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.95 ANGSTROMS) OF 140-385 IN COMPLEX
RP   WITH INHIBITORS; LACTATE AND SLC16A1.
RX   PubMed=33333023; DOI=10.1016/j.cell.2020.11.043;
RA   Wang N., Jiang X., Zhang S., Zhu A., Yuan Y., Xu H., Lei J., Yan C.;
RT   "Structural basis of human monocarboxylate transporter 1 inhibition by
RT   anti-cancer drug candidates.";
RL   Cell 184:370-383.e13(2021).
RN   [62]
RP   VARIANT LYS-208.
RX   PubMed=9130641; DOI=10.1002/eji.1830270414;
RA   Spring F.A., Holmes C.H., Simpson K.L., Mawby W.J., Mattes M.J., Okubo Y.,
RA   Parsons S.F.;
RT   "The Ok(a) blood group antigen is a marker for the M6 leukocyte activation
RT   antigen, the human homolog of OX-47 antigen, basigin and neurothelin, an
RT   immunoglobulin superfamily molecule that is widely expressed in human cells
RT   and tissues.";
RL   Eur. J. Immunol. 27:891-897(1997).
RN   [63]
RP   VARIANTS VAL-13; ALA-16 AND PHE-26.
RX   PubMed=32867305; DOI=10.3390/genes11091010;
RA   Latini A., Agolini E., Novelli A., Borgiani P., Giannini R., Gravina P.,
RA   Smarrazzo A., Dauri M., Andreoni M., Rogliani P., Bernardini S.,
RA   Helmer-Citterich M., Biancolella M., Novelli G.;
RT   "COVID-19 and Genetic Variants of Protein Involved in the SARS-CoV-2 Entry
RT   into the Host Cells.";
RL   Genes (Basel) 11:0-0(2020).
CC   -!- FUNCTION: [Isoform 1]: Essential for normal retinal maturation and
CC       development (By similarity). Acts as a retinal cell surface receptor
CC       for NXNL1 and plays an important role in NXNL1-mediated survival of
CC       retinal cone photoreceptors (PubMed:25957687). In association with
CC       glucose transporter SLC16A1/GLUT1 and NXNL1, promotes retinal cone
CC       survival by enhancing aerobic glycolysis and accelerating the entry of
CC       glucose into photoreceptors (PubMed:25957687). May act as a potent
CC       stimulator of IL6 secretion in multiple cell lines that include
CC       monocytes (PubMed:21620857). {ECO:0000250|UniProtKB:P18572,
CC       ECO:0000269|PubMed:21620857, ECO:0000269|PubMed:25957687}.
CC   -!- FUNCTION: [Isoform 1]: (Microbial infection) Erythrocyte receptor for
CC       P.falciparum RH5 which is essential for erythrocyte invasion by the
CC       merozoite stage of P.falciparum isolates 3D7 and Dd2.
CC       {ECO:0000269|PubMed:22080952}.
CC   -!- FUNCTION: [Isoform 2]: Signaling receptor for cyclophilins, essential
CC       for PPIA/CYPA and PPIB/CYPB-dependent signaling related to chemotaxis
CC       and adhesion of immune cells (PubMed:11688976, PubMed:11943775). Plays
CC       an important role in targeting monocarboxylate transporters
CC       SLC16A1/GLUT1, SLC16A11 and SLC16A12 to the plasma membrane
CC       (PubMed:17127621, PubMed:21778275, PubMed:28666119). Acts as a
CC       coreceptor for vascular endothelial growth factor receptor 2
CC       (KDR/VEGFR2) in endothelial cells enhancing its VEGFA-mediated
CC       activation and downstream signaling (PubMed:25825981). Promotes
CC       angiogenesis through EPAS1/HIF2A-mediated up-regulation of VEGFA
CC       (isoform VEGF-165 and VEGF-121) and KDR/VEGFR2 in endothelial cells
CC       (PubMed:19837976). Plays a key role in regulating tumor growth,
CC       invasion, metastasis and neoangiogenesis by stimulating the production
CC       and release of extracellular matrix metalloproteinases and KDR/VEGFR2
CC       by both tumor cells and stromal cells (fibroblasts and endothelial
CC       cells) (PubMed:11992541, PubMed:12553375, PubMed:15833850).
CC       {ECO:0000269|PubMed:11688976, ECO:0000269|PubMed:11943775,
CC       ECO:0000269|PubMed:11992541, ECO:0000269|PubMed:12553375,
CC       ECO:0000269|PubMed:15833850, ECO:0000269|PubMed:17127621,
CC       ECO:0000269|PubMed:19837976, ECO:0000269|PubMed:21778275,
CC       ECO:0000269|PubMed:25825981, ECO:0000269|PubMed:28666119}.
CC   -!- FUNCTION: [Isoform 2]: (Microbial infection) Erythrocyte receptor for
CC       P.falciparum RH5 which is essential for erythrocyte invasion by the
CC       merozoite stage of P.falciparum isolates 3D7, Dd2, 7G8 and HB3
CC       (PubMed:22080952, PubMed:26195724). Binding of P.falciparum RH5 results
CC       in BSG dimerization which triggers an increase in intracellular Ca(2+)
CC       in the erythrocyte (PubMed:28409866). This essential step leads to a
CC       rearrangement of the erythrocyte cytoskeleton required for the
CC       merozoite invasion (PubMed:28409866). {ECO:0000269|PubMed:22080952,
CC       ECO:0000269|PubMed:26195724, ECO:0000269|PubMed:28409866}.
CC   -!- FUNCTION: [Isoform 2]: (Microbial infection) Can facilitate human SARS
CC       coronavirus (SARS-CoV-1) infection via its interaction with virus-
CC       associated PPIA/CYPA. {ECO:0000269|PubMed:15688292}.
CC   -!- FUNCTION: [Isoform 2]: (Microbial infection) Can facilitate HIV-1
CC       infection via its interaction with virus-associated PPIA/CYPA.
CC       {ECO:0000269|PubMed:11353871}.
CC   -!- FUNCTION: [Isoform 2]: (Microbial infection) First described as a
CC       receptor for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-
CC       2), it is not required for SARS-CoV-2 infection.
CC       {ECO:0000269|PubMed:33432067, ECO:0000303|PubMed:32307653}.
CC   -!- FUNCTION: [Isoform 2]: (Microbial infection) Acts as a receptor for
CC       measles virus. {ECO:0000269|PubMed:20147391}.
CC   -!- FUNCTION: [Isoform 2]: (Microbial infection) Promotes entry of
CC       pentamer-expressing human cytomegalovirus (HCMV) into epithelial and
CC       endothelial cells. {ECO:0000269|PubMed:29739904}.
CC   -!- SUBUNIT: [Isoform 1]: Homooligomer (PubMed:19768682). Interacts with
CC       NXNL1 (PubMed:25957687). Interacts with SLC2A1 and SLC16A1/GLUT1 (By
CC       similarity). Interacts with XKR8; promoting its localization at the
CC       cell membrane (PubMed:27503893). {ECO:0000250|UniProtKB:P17790,
CC       ECO:0000269|PubMed:19768682, ECO:0000269|PubMed:25957687,
CC       ECO:0000269|PubMed:27503893}.
CC   -!- SUBUNIT: [Isoform 1]: (Microbial infection) Interacts with P.falciparum
CC       (isolate 3D7) RH5/PfRH5; the interaction is required for the invasion
CC       of the host erythrocytes by the parasite at the merozoite stage.
CC       {ECO:0000269|PubMed:22080952}.
CC   -!- SUBUNIT: [Isoform 2]: Homooligomer (PubMed:18430721). Forms
CC       heterooligomers with isoform 3 (PubMed:21536654). Interacts with VEGFA
CC       and KDR/VEGFR2 (PubMed:25825981). Interacts with PPIA/CYPA
CC       (PubMed:11353871, PubMed:11943775, PubMed:15688292, PubMed:21245143).
CC       Interacts with PPIL2; regulates BSG transport to the cell membrane
CC       (PubMed:15946952). Interacts with SLC16A1; interaction mediates SLC16A3
CC       targeting to the plasma membrane (PubMed:17127621). Interacts with
CC       SLC16A12 (PubMed:21778275). Interacts with SLC16A11 (PubMed:28666119).
CC       Interacts with AJAP1 (PubMed:17267690). Interacts with SLC1A3, ATP1B2,
CC       MAG and L1CAM (By similarity). Interacts with SLC16A3; interaction
CC       mediates SLC16A3 targeting to the plasma membrane.
CC       {ECO:0000250|UniProtKB:P18572, ECO:0000250|UniProtKB:P26453,
CC       ECO:0000269|PubMed:11353871, ECO:0000269|PubMed:11943775,
CC       ECO:0000269|PubMed:15688292, ECO:0000269|PubMed:15946952,
CC       ECO:0000269|PubMed:17127621, ECO:0000269|PubMed:17267690,
CC       ECO:0000269|PubMed:18430721, ECO:0000269|PubMed:21245143,
CC       ECO:0000269|PubMed:21536654, ECO:0000269|PubMed:21778275,
CC       ECO:0000269|PubMed:25825981, ECO:0000269|PubMed:28666119}.
CC   -!- SUBUNIT: [Isoform 2]: (Microbial infection) Interacts with P.falciparum
CC       (isolates 3D7 or 7G8) RH5/PfRH5; the interaction is required for the
CC       invasion of the host erythrocytes by the parasite at the merozoite
CC       stage. {ECO:0000269|PubMed:22080952, ECO:0000269|PubMed:24297912,
CC       ECO:0000269|PubMed:25132548, ECO:0000269|PubMed:26195724}.
CC   -!- SUBUNIT: [Isoform 2]: (Microbial infection) Does not interact with
CC       severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike
CC       glycoprotein, even if previous works were based on a putative
CC       interaction. {ECO:0000269|PubMed:33432067,
CC       ECO:0000303|PubMed:32307653}.
CC   -!- SUBUNIT: [Isoform 3]: Forms heterooligomers with isoform 2.
CC       {ECO:0000269|PubMed:21536654}.
CC   -!- SUBUNIT: Interacts with SLC16A6; this interaction mediates targeting to
CC       the plasma membrane. {ECO:0000250|UniProtKB:P26453}.
CC   -!- INTERACTION:
CC       P35613; P05067: APP; NbExp=2; IntAct=EBI-750709, EBI-77613;
CC       P35613; Q9UJC3: HOOK1; NbExp=3; IntAct=EBI-750709, EBI-746704;
CC       P35613; Q92542: NCSTN; NbExp=6; IntAct=EBI-750709, EBI-998440;
CC       P35613; P62937: PPIA; NbExp=2; IntAct=EBI-750709, EBI-437708;
CC       P35613; PRO_0000025592 [P49768]: PSEN1; NbExp=6; IntAct=EBI-750709, EBI-2606356;
CC       P35613; Q8NCK7: SLC16A11; NbExp=5; IntAct=EBI-750709, EBI-21840241;
CC       P35613; P0DTC2: S; Xeno; NbExp=7; IntAct=EBI-750709, EBI-25474821;
CC       P35613-2; Q13520: AQP6; NbExp=3; IntAct=EBI-11037868, EBI-13059134;
CC       P35613-2; Q7RTY0: SLC16A13; NbExp=3; IntAct=EBI-11037868, EBI-12243266;
CC       P35613-2; Q8IFM5: RH5; Xeno; NbExp=3; IntAct=EBI-11037868, EBI-22304327;
CC       P35613-2; B2L3N7; Xeno; NbExp=5; IntAct=EBI-11037868, EBI-16118096;
CC   -!- SUBCELLULAR LOCATION: Melanosome {ECO:0000269|PubMed:17081065}.
CC       Note=Identified by mass spectrometry in melanosome fractions from stage
CC       I to stage IV. {ECO:0000269|PubMed:17081065}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC       {ECO:0000269|PubMed:25957687}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:P26453}. Photoreceptor inner segment
CC       {ECO:0000250|UniProtKB:P18572}. Cell projection, cilium, photoreceptor
CC       outer segment {ECO:0000250|UniProtKB:P18572}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane
CC       {ECO:0000269|PubMed:11992541, ECO:0000269|PubMed:15688292,
CC       ECO:0000269|PubMed:15946952, ECO:0000269|PubMed:17127621,
CC       ECO:0000269|PubMed:21536654, ECO:0000269|PubMed:25825981,
CC       ECO:0000269|PubMed:26195724, ECO:0000269|PubMed:28409866,
CC       ECO:0000269|PubMed:29739904}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:P26453}. Endosome {ECO:0000269|PubMed:29739904}.
CC       Endoplasmic reticulum membrane {ECO:0000269|PubMed:15688292}; Single-
CC       pass type I membrane protein {ECO:0000250|UniProtKB:P26453}.
CC       Basolateral cell membrane {ECO:0000269|PubMed:17267690}; Single-pass
CC       type I membrane protein {ECO:0000250|UniProtKB:P26453}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane
CC       {ECO:0000269|PubMed:21536654}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:P26453}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane
CC       {ECO:0000269|PubMed:21536654}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:P26453}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=Long, Basigin-1 {ECO:0000303|PubMed:25957687};
CC         IsoId=P35613-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short, Basigin-2 {ECO:0000303|PubMed:25957687};
CC         IsoId=P35613-2; Sequence=VSP_011501;
CC       Name=3; Synonyms=Basigin-3;
CC         IsoId=P35613-3; Sequence=VSP_043225;
CC       Name=4; Synonyms=Basigin-4;
CC         IsoId=P35613-4; Sequence=VSP_043226, VSP_043227;
CC   -!- TISSUE SPECIFICITY: [Isoform 1]: Retina-specific (PubMed:25957687).
CC       Expressed in retinal cone photoreceptors (at protein level)
CC       (PubMed:25957687). {ECO:0000269|PubMed:25957687}.
CC   -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in erythrocytes (at protein
CC       level) (PubMed:26195724, PubMed:28409866). Highly expressed in melanoma
CC       cell lines (at protein level) (PubMed:11992541). Highly expressed in
CC       the heart, kidney, skeletal muscle and testis (PubMed:21536654).
CC       {ECO:0000269|PubMed:11992541, ECO:0000269|PubMed:21536654,
CC       ECO:0000269|PubMed:26195724, ECO:0000269|PubMed:28409866}.
CC   -!- TISSUE SPECIFICITY: [Isoform 3]: Highly expressed in the bone marrow,
CC       fetal liver, lung, testis and thymus. {ECO:0000269|PubMed:21536654}.
CC   -!- TISSUE SPECIFICITY: [Isoform 4]: Highly expressed in the bone marrow,
CC       fetal liver, lung, testis and thymus. {ECO:0000269|PubMed:21536654}.
CC   -!- PTM: [Isoform 2]: N-glycosylated. {ECO:0000269|PubMed:21536654}.
CC   -!- PTM: [Isoform 3]: N-glycosylated. {ECO:0000269|PubMed:21536654}.
CC   -!- PTM: [Isoform 4]: N-glycosylated. {ECO:0000269|PubMed:21536654}.
CC   -!- BIOTECHNOLOGY: [Isoform 2]: Potential candidate for the development of
CC       parasite blood stage vaccines. In vitro and in vivo, neutralizing
CC       antibodies are capable of inhibiting merozoite invasion of host
CC       erythrocytes. {ECO:0000269|PubMed:26195724}.
CC   -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative promoter usage.
CC       {ECO:0000269|PubMed:21536654}.
CC   -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative promoter usage.
CC       {ECO:0000269|PubMed:21536654}.
CC   -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation
CC       database;
CC       URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=ok";
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DR   EMBL; X64364; CAA45716.1; -; mRNA.
DR   EMBL; D45131; BAA08109.1; -; mRNA.
DR   EMBL; L10240; AAA68936.1; -; mRNA.
DR   EMBL; M87879; AAA91084.1; -; mRNA.
DR   EMBL; L20471; AAB41120.1; -; mRNA.
DR   EMBL; AF042854; AAD10704.1; -; Genomic_DNA.
DR   EMBL; AF042848; AAD10704.1; JOINED; Genomic_DNA.
DR   EMBL; AF042849; AAD10704.1; JOINED; Genomic_DNA.
DR   EMBL; AF042850; AAD10704.1; JOINED; Genomic_DNA.
DR   EMBL; AF042851; AAD10704.1; JOINED; Genomic_DNA.
DR   EMBL; AF042852; AAD10704.1; JOINED; Genomic_DNA.
DR   EMBL; AF042853; AAD10704.1; JOINED; Genomic_DNA.
DR   EMBL; AB072923; BAB88938.1; -; mRNA.
DR   EMBL; AB085790; BAC76828.1; -; mRNA.
DR   EMBL; AF548371; AAN40694.1; -; mRNA.
DR   EMBL; GU557064; ADD31881.1; -; mRNA.
DR   EMBL; GU557065; ADD31882.1; -; mRNA.
DR   EMBL; AY358113; AAQ88480.1; -; mRNA.
DR   EMBL; AY942196; AAX20110.1; -; Genomic_DNA.
DR   EMBL; AC005559; AAC33279.1; -; Genomic_DNA.
DR   EMBL; CH471242; EAW61181.1; -; Genomic_DNA.
DR   EMBL; CH471242; EAW61185.1; -; Genomic_DNA.
DR   EMBL; BC009040; AAH09040.1; -; mRNA.
DR   CCDS; CCDS12033.1; -. [P35613-1]
DR   CCDS; CCDS12034.1; -. [P35613-2]
DR   CCDS; CCDS58635.1; -. [P35613-3]
DR   PIR; A46506; A46506.
DR   RefSeq; NP_001309172.1; NM_001322243.1. [P35613-2]
DR   RefSeq; NP_001719.2; NM_001728.3. [P35613-1]
DR   RefSeq; NP_940991.1; NM_198589.2. [P35613-2]
DR   RefSeq; NP_940992.1; NM_198590.2. [P35613-3]
DR   RefSeq; NP_940993.1; NM_198591.2. [P35613-3]
DR   RefSeq; XP_016882662.1; XM_017027173.1.
DR   PDB; 3B5H; X-ray; 2.80 A; A/B/C/D=140-321.
DR   PDB; 3I84; X-ray; 2.00 A; A/B=13-219.
DR   PDB; 3I85; X-ray; 2.50 A; A/B=13-219.
DR   PDB; 3QQN; X-ray; 2.31 A; A/B=23-138.
DR   PDB; 3QR2; X-ray; 2.30 A; A/B=23-138.
DR   PDB; 4U0Q; X-ray; 3.10 A; B/D=1-385.
DR   PDB; 5X0T; X-ray; 2.50 A; E/F=138-217.
DR   PDB; 5XF0; NMR; -; A=215-321.
DR   PDB; 6LYY; EM; 3.60 A; B=140-385.
DR   PDB; 6LZ0; EM; 3.60 A; B=140-385.
DR   PDB; 7CKO; EM; 2.95 A; B=140-385.
DR   PDB; 7CKR; EM; 3.00 A; B=140-385.
DR   PDB; 7DA5; EM; 3.30 A; B=140-385.
DR   PDB; 7DAA; X-ray; 2.51 A; A=219-385.
DR   PDB; 7DCE; EM; 3.80 A; B=219-385.
DR   PDB; 7XY8; X-ray; 2.30 A; A/B=138-321.
DR   PDB; 8XEJ; EM; 3.66 A; B=219-385.
DR   PDBsum; 3B5H; -.
DR   PDBsum; 3I84; -.
DR   PDBsum; 3I85; -.
DR   PDBsum; 3QQN; -.
DR   PDBsum; 3QR2; -.
DR   PDBsum; 4U0Q; -.
DR   PDBsum; 5X0T; -.
DR   PDBsum; 5XF0; -.
DR   PDBsum; 6LYY; -.
DR   PDBsum; 6LZ0; -.
DR   PDBsum; 7CKO; -.
DR   PDBsum; 7CKR; -.
DR   PDBsum; 7DA5; -.
DR   PDBsum; 7DAA; -.
DR   PDBsum; 7DCE; -.
DR   PDBsum; 7XY8; -.
DR   PDBsum; 8XEJ; -.
DR   AlphaFoldDB; P35613; -.
DR   BMRB; P35613; -.
DR   EMDB; EMD-30019; -.
DR   EMDB; EMD-30020; -.
DR   EMDB; EMD-30389; -.
DR   EMDB; EMD-30391; -.
DR   EMDB; EMD-30623; -.
DR   EMDB; EMD-30636; -.
DR   EMDB; EMD-38291; -.
DR   SMR; P35613; -.
DR   BioGRID; 107147; 649.
DR   CORUM; P35613; -.
DR   DIP; DIP-50310N; -.
DR   IntAct; P35613; 246.
DR   MINT; P35613; -.
DR   STRING; 9606.ENSP00000333769; -.
DR   ChEMBL; CHEMBL3580492; -.
DR   TCDB; 8.A.23.1.1; the basigin (basigin) family.
DR   GlyConnect; 1027; 9 N-Linked glycans (2 sites).
DR   GlyCosmos; P35613; 4 sites, 10 glycans.
DR   GlyGen; P35613; 11 sites, 8 N-linked glycans (2 sites), 4 O-linked glycans (8 sites).
DR   iPTMnet; P35613; -.
DR   MetOSite; P35613; -.
DR   PhosphoSitePlus; P35613; -.
DR   SwissPalm; P35613; -.
DR   BioMuta; BSG; -.
DR   DMDM; 51704273; -.
DR   CPTAC; CPTAC-319; -.
DR   CPTAC; CPTAC-320; -.
DR   jPOST; P35613; -.
DR   MassIVE; P35613; -.
DR   PaxDb; 9606-ENSP00000333769; -.
DR   PeptideAtlas; P35613; -.
DR   ProteomicsDB; 55113; -. [P35613-1]
DR   ProteomicsDB; 55114; -. [P35613-2]
DR   ProteomicsDB; 55115; -. [P35613-3]
DR   ProteomicsDB; 55116; -. [P35613-4]
DR   Pumba; P35613; -.
DR   TopDownProteomics; P35613-1; -. [P35613-1]
DR   TopDownProteomics; P35613-2; -. [P35613-2]
DR   TopDownProteomics; P35613-3; -. [P35613-3]
DR   ABCD; P35613; 89 sequenced antibodies.
DR   Antibodypedia; 3719; 2435 antibodies from 48 providers.
DR   DNASU; 682; -.
DR   Ensembl; ENST00000333511.9; ENSP00000333769.3; ENSG00000172270.22. [P35613-1]
DR   Ensembl; ENST00000346916.9; ENSP00000344707.4; ENSG00000172270.22. [P35613-3]
DR   Ensembl; ENST00000353555.9; ENSP00000343809.4; ENSG00000172270.22. [P35613-2]
DR   Ensembl; ENST00000545507.6; ENSP00000473664.1; ENSG00000172270.22. [P35613-3]
DR   Ensembl; ENST00000573784.6; ENSP00000473393.2; ENSG00000172270.22. [P35613-3]
DR   Ensembl; ENST00000576984.3; ENSP00000473528.2; ENSG00000172270.22. [P35613-3]
DR   Ensembl; ENST00000680065.1; ENSP00000506020.1; ENSG00000172270.22. [P35613-3]
DR   GeneID; 682; -.
DR   KEGG; hsa:682; -.
DR   MANE-Select; ENST00000333511.9; ENSP00000333769.3; NM_001728.4; NP_001719.2.
DR   UCSC; uc002loy.5; human. [P35613-1]
DR   AGR; HGNC:1116; -.
DR   CTD; 682; -.
DR   DisGeNET; 682; -.
DR   GeneCards; BSG; -.
DR   HGNC; HGNC:1116; BSG.
DR   HPA; ENSG00000172270; Low tissue specificity.
DR   MIM; 109480; gene.
DR   MIM; 111380; phenotype.
DR   neXtProt; NX_P35613; -.
DR   OpenTargets; ENSG00000172270; -.
DR   PharmGKB; PA25433; -.
DR   VEuPathDB; HostDB:ENSG00000172270; -.
DR   eggNOG; ENOG502QPKN; Eukaryota.
DR   GeneTree; ENSGT00940000159142; -.
DR   HOGENOM; CLU_058449_0_0_1; -.
DR   InParanoid; P35613; -.
DR   OMA; TITGHKW; -.
DR   OrthoDB; 4092110at2759; -.
DR   PhylomeDB; P35613; -.
DR   TreeFam; TF326759; -.
DR   PathwayCommons; P35613; -.
DR   Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-HSA-210991; Basigin interactions.
DR   Reactome; R-HSA-216083; Integrin cell surface interactions.
DR   Reactome; R-HSA-433692; Proton-coupled monocarboxylate transport.
DR   Reactome; R-HSA-5619070; Defective SLC16A1 causes symptomatic deficiency in lactate transport (SDLT).
DR   Reactome; R-HSA-9749641; Aspirin ADME.
DR   SignaLink; P35613; -.
DR   SIGNOR; P35613; -.
DR   BioGRID-ORCS; 682; 68 hits in 1156 CRISPR screens.
DR   ChiTaRS; BSG; human.
DR   EvolutionaryTrace; P35613; -.
DR   GeneWiki; Basigin; -.
DR   GenomeRNAi; 682; -.
DR   Pharos; P35613; Tbio.
DR   PRO; PR:P35613; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P35613; protein.
DR   Bgee; ENSG00000172270; Expressed in apex of heart and 193 other cell types or tissues.
DR   ExpressionAtlas; P35613; baseline and differential.
DR   GO; GO:0002080; C:acrosomal membrane; IEA:Ensembl.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; HDA:UniProtKB.
DR   GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB.
DR   GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR   GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR   GO; GO:0005537; F:D-mannose binding; IEA:UniProtKB-KW.
DR   GO; GO:0038023; F:signaling receptor activity; IDA:UniProtKB.
DR   GO; GO:0001618; F:virus receptor activity; IMP:UniProtKB.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR   GO; GO:0046697; P:decidualization; IEA:Ensembl.
DR   GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR   GO; GO:0061154; P:endothelial tube morphogenesis; IDA:UniProtKB.
DR   GO; GO:0003407; P:neural retina development; ISS:UniProtKB.
DR   GO; GO:0030593; P:neutrophil chemotaxis; IMP:UniProtKB.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR   GO; GO:0045494; P:photoreceptor cell maintenance; IDA:UniProtKB.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:UniProtKB.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:UniProtKB.
DR   GO; GO:1904466; P:positive regulation of matrix metallopeptidase secretion; IDA:UniProtKB.
DR   GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IDA:UniProtKB.
DR   GO; GO:0046598; P:positive regulation of viral entry into host cell; IDA:UniProtKB.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IMP:ARUK-UCL.
DR   GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR   GO; GO:0046689; P:response to mercury ion; IEA:Ensembl.
DR   GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR   CDD; cd20940; Ig0_BSG1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   PANTHER; PTHR10075:SF112; BASIGIN; 1.
DR   PANTHER; PTHR10075; BASIGIN RELATED; 1.
DR   Pfam; PF13927; Ig_3; 2.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
DR   PROSITE; PS50835; IG_LIKE; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative promoter usage; Alternative splicing;
KW   Angiogenesis; Blood group antigen; Cell membrane; Cell projection;
KW   Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; Endosome;
KW   Glycoprotein; Host cell receptor for virus entry; Host-virus interaction;
KW   Immunoglobulin domain; Lectin; Mannose-binding; Membrane; Phosphoprotein;
KW   Proteomics identification; Receptor; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT   CHAIN           22..385
FT                   /note="Basigin"
FT                   /id="PRO_0000014518"
FT   TOPO_DOM        138..323
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P26453"
FT   TRANSMEM        324..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        345..385
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P26453"
FT   DOMAIN          37..120
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DOMAIN          138..219
FT                   /note="Ig-like C2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DOMAIN          221..315
FT                   /note="Ig-like V-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   REGION          353..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         362
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         368
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   CARBOHYD        160
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754519,
FT                   ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973"
FT   CARBOHYD        268
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754519,
FT                   ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        44..108
FT                   /evidence="ECO:0000269|PubMed:21620857,
FT                   ECO:0007744|PDB:3QQN, ECO:0007744|PDB:3QR2"
FT   DISULFID        157..203
FT                   /evidence="ECO:0000269|PubMed:18430721,
FT                   ECO:0000269|PubMed:19768682, ECO:0000269|PubMed:25132548,
FT                   ECO:0000269|Ref.60, ECO:0007744|PDB:3B5H,
FT                   ECO:0007744|PDB:3I84, ECO:0007744|PDB:4U0Q,
FT                   ECO:0007744|PDB:5X0T"
FT   DISULFID        242..301
FT                   /evidence="ECO:0000269|PubMed:18430721,
FT                   ECO:0000269|PubMed:25132548, ECO:0007744|PDB:3B5H,
FT                   ECO:0007744|PDB:4U0Q"
FT   VAR_SEQ         1..209
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:21536654"
FT                   /id="VSP_043225"
FT   VAR_SEQ         1..11
FT                   /note="MAAALFVLLGF -> MKQSDASPQER (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:21536654"
FT                   /id="VSP_043226"
FT   VAR_SEQ         12..191
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:21536654"
FT                   /id="VSP_043227"
FT   VAR_SEQ         24..139
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:1634773, ECO:0000303|PubMed:7812975"
FT                   /id="VSP_011501"
FT   VARIANT         13
FT                   /note="L -> V (in dbSNP:rs201850688)"
FT                   /evidence="ECO:0000269|PubMed:32867305"
FT                   /id="VAR_084546"
FT   VARIANT         16
FT                   /note="T -> A (in dbSNP:rs11551906)"
FT                   /evidence="ECO:0000269|PubMed:32867305"
FT                   /id="VAR_084547"
FT   VARIANT         26
FT                   /note="V -> F (in dbSNP:rs144824657)"
FT                   /evidence="ECO:0000269|PubMed:32867305"
FT                   /id="VAR_084548"
FT   VARIANT         152
FT                   /note="K -> N (no effect on the interaction with
FT                   P.falciparum RH5; dbSNP:rs14704)"
FT                   /evidence="ECO:0000269|PubMed:22080952"
FT                   /id="VAR_082637"
FT   VARIANT         176
FT                   /note="V -> L (no effect on the interaction with
FT                   P.falciparum RH5; dbSNP:rs2229662)"
FT                   /evidence="ECO:0000269|PubMed:22080952"
FT                   /id="VAR_082638"
FT   VARIANT         206
FT                   /note="L -> P (loss of interaction with P.falciparum RH5;
FT                   dbSNP:rs55911144)"
FT                   /evidence="ECO:0000269|PubMed:22080952"
FT                   /id="VAR_082639"
FT   VARIANT         208
FT                   /note="E -> K (in Ok(A-); 2-fold reduction in the binding
FT                   affinity for P.falciparum RH5 with reduced erythrocyte
FT                   invasion by P.falciparum isolates 3D7 and Dd2;
FT                   dbSNP:rs104894669)"
FT                   /evidence="ECO:0000269|PubMed:22080952,
FT                   ECO:0000269|PubMed:9130641"
FT                   /id="VAR_013574"
FT   VARIANT         269
FT                   /note="G -> V (loss of interaction with P.falciparum RH5;
FT                   dbSNP:rs1803203)"
FT                   /evidence="ECO:0000269|PubMed:22080952"
FT                   /id="VAR_011720"
FT   MUTAGEN         67
FT                   /note="C->M: Loss of ability to stimulate interleukin-6
FT                   secretion."
FT                   /evidence="ECO:0000269|PubMed:21620857"
FT   MUTAGEN         160
FT                   /note="N->D: No effect on the interaction with P.falciparum
FT                   RH5; when associated with D-268 and D-302."
FT                   /evidence="ECO:0000269|PubMed:22080952"
FT   MUTAGEN         268
FT                   /note="N->D: No effect on the interaction with P.falciparum
FT                   RH5; when associated with D-160 and D-302."
FT                   /evidence="ECO:0000269|PubMed:22080952"
FT   MUTAGEN         302
FT                   /note="N->D: No effect on the interaction with P.falciparum
FT                   RH5; when associated with D-160 and D-268."
FT                   /evidence="ECO:0000269|PubMed:22080952"
FT   CONFLICT        328
FT                   /note="F -> L (in Ref. 2; BAC76828)"
FT                   /evidence="ECO:0000305"
FT   STRAND          24..27
FT                   /evidence="ECO:0007829|PDB:3QR2"
FT   STRAND          32..35
FT                   /evidence="ECO:0007829|PDB:3QR2"
FT   STRAND          40..47
FT                   /evidence="ECO:0007829|PDB:3QR2"
FT   STRAND          53..62
FT                   /evidence="ECO:0007829|PDB:3QR2"
FT   HELIX           74..77
FT                   /evidence="ECO:0007829|PDB:3QR2"
FT   STRAND          79..95
FT                   /evidence="ECO:0007829|PDB:3QR2"
FT   HELIX           100..102
FT                   /evidence="ECO:0007829|PDB:3QR2"
FT   STRAND          104..111
FT                   /evidence="ECO:0007829|PDB:3QR2"
FT   STRAND          116..118
FT                   /evidence="ECO:0007829|PDB:3QR2"
FT   STRAND          128..137
FT                   /evidence="ECO:0007829|PDB:3QR2"
FT   STRAND          142..149
FT                   /evidence="ECO:0007829|PDB:3I84"
FT   STRAND          152..159
FT                   /evidence="ECO:0007829|PDB:3I84"
FT   STRAND          166..173
FT                   /evidence="ECO:0007829|PDB:3I84"
FT   STRAND          176..181
FT                   /evidence="ECO:0007829|PDB:3I84"
FT   STRAND          186..192
FT                   /evidence="ECO:0007829|PDB:3I84"
FT   HELIX           194..196
FT                   /evidence="ECO:0007829|PDB:3I84"
FT   STRAND          199..207
FT                   /evidence="ECO:0007829|PDB:3I84"
FT   STRAND          210..217
FT                   /evidence="ECO:0007829|PDB:3I84"
FT   STRAND          224..226
FT                   /evidence="ECO:0007829|PDB:7XY8"
FT   STRAND          228..232
FT                   /evidence="ECO:0007829|PDB:7XY8"
FT   STRAND          234..236
FT                   /evidence="ECO:0007829|PDB:7DAA"
FT   STRAND          238..243
FT                   /evidence="ECO:0007829|PDB:7XY8"
FT   STRAND          250..258
FT                   /evidence="ECO:0007829|PDB:7XY8"
FT   STRAND          260..262
FT                   /evidence="ECO:0007829|PDB:3B5H"
FT   STRAND          263..265
FT                   /evidence="ECO:0007829|PDB:7XY8"
FT   HELIX           270..272
FT                   /evidence="ECO:0007829|PDB:7XY8"
FT   STRAND          274..278
FT                   /evidence="ECO:0007829|PDB:7XY8"
FT   STRAND          280..287
FT                   /evidence="ECO:0007829|PDB:7XY8"
FT   TURN            292..294
FT                   /evidence="ECO:0007829|PDB:7XY8"
FT   STRAND          297..305
FT                   /evidence="ECO:0007829|PDB:7XY8"
FT   STRAND          308..318
FT                   /evidence="ECO:0007829|PDB:7XY8"
FT   TURN            323..325
FT                   /evidence="ECO:0007829|PDB:7CKO"
FT   HELIX           326..353
FT                   /evidence="ECO:0007829|PDB:7CKO"
FT   REGION          P35613-2:195..199
FT                   /note="Essential for interaction with KDR/VEGFR2"
FT                   /evidence="ECO:0000269|PubMed:25825981"
FT   MUTAGEN         P35613-2:27
FT                   /note="F->L: Severe reduction in the interaction with
FT                   P.falciparum RH5."
FT                   /evidence="ECO:0000269|PubMed:24297912"
FT   MUTAGEN         P35613-2:32
FT                   /note="D->E: No effect on the interaction with P.falciparum
FT                   RH5."
FT                   /evidence="ECO:0000269|PubMed:24297912"
FT   MUTAGEN         P35613-2:75
FT                   /note="K->E: No effect on the interaction with P.falciparum
FT                   RH5."
FT                   /evidence="ECO:0000269|PubMed:24297912"
FT   MUTAGEN         P35613-2:100
FT                   /note="Q->K: Severe reduction in the interaction with
FT                   P.falciparum RH5."
FT                   /evidence="ECO:0000269|PubMed:24297912"
FT   MUTAGEN         P35613-2:102
FT                   /note="H->HH: Severe reduction in the interaction with
FT                   P.falciparum RH5."
FT                   /evidence="ECO:0000269|PubMed:24297912"
FT   MUTAGEN         P35613-2:144
FT                   /note="D->A: Reduced interaction with KDR/VEGFR2."
FT                   /evidence="ECO:0000269|PubMed:25825981"
FT   MUTAGEN         P35613-2:180..181
FT                   /note="PG->AA: Loss of its ability to mediate chemotactic
FT                   activity of PPIA/CYPA."
FT                   /evidence="ECO:0000269|PubMed:11943775"
FT   MUTAGEN         P35613-2:182
FT                   /note="Q->A: Reduced interaction with KDR/VEGFR2.
FT                   Significant loss of interaction with KDR/VEGFR2; when
FT                   associated with A-184."
FT                   /evidence="ECO:0000269|PubMed:25825981"
FT   MUTAGEN         P35613-2:184
FT                   /note="R->A: Reduced interaction with KDR/VEGFR2.
FT                   Significant loss of interaction with KDR/VEGFR2; when
FT                   associated with A-182."
FT                   /evidence="ECO:0000269|PubMed:25825981"
FT   MUTAGEN         P35613-2:195
FT                   /note="Q->A: Reduced interaction with KDR/VEGFR2. Complete
FT                   loss of interaction with KDR/VEGFR2 when associated with A-
FT                   199."
FT                   /evidence="ECO:0000269|PubMed:25825981"
FT   MUTAGEN         P35613-2:199
FT                   /note="T->A: Reduced interaction with KDR/VEGFR2. Complete
FT                   loss of interaction with KDR/VEGFR2; when associated with
FT                   A-195."
FT                   /evidence="ECO:0000269|PubMed:25825981"
FT   MUTAGEN         P35613-2:211
FT                   /note="P->A: Loss of interaction with PPIL2."
FT                   /evidence="ECO:0000269|PubMed:15946952"
SQ   SEQUENCE   385 AA;  42200 MW;  D74C37455BF26685 CRC64;
     MAAALFVLLG FALLGTHGAS GAAGFVQAPL SQQRWVGGSV ELHCEAVGSP VPEIQWWFEG
     QGPNDTCSQL WDGARLDRVH IHATYHQHAA STISIDTLVE EDTGTYECRA SNDPDRNHLT
     RAPRVKWVRA QAVVLVLEPG TVFTTVEDLG SKILLTCSLN DSATEVTGHR WLKGGVVLKE
     DALPGQKTEF KVDSDDQWGE YSCVFLPEPM GTANIQLHGP PRVKAVKSSE HINEGETAML
     VCKSESVPPV TDWAWYKITD SEDKALMNGS ESRFFVSSSQ GRSELHIENL NMEADPGQYR
     CNGTSSKGSD QAIITLRVRS HLAALWPFLG IVAEVLVLVT IIFIYEKRRK PEDVLDDDDA
     GSAPLKSSGQ HQNDKGKNVR QRNSS
//