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 24-JUL-2024, entry version 237. 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"; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/bsg/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 646. DR CORUM; P35613; -. DR DIP; DIP-50310N; -. DR IntAct; P35613; 175. 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; 2315 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: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 Receptor; Reference proteome; Signal; 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 //