ID NRP1_HUMAN Reviewed; 923 AA.
AC O14786; B0LPG9; O60461; Q5T7F1; Q5T7F2; Q5T7F3; Q86T59; Q96I90; Q96IH5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 3.
DT 02-OCT-2024, entry version 236.
DE RecName: Full=Neuropilin-1 {ECO:0000305};
DE AltName: Full=Vascular endothelial cell growth factor 165 receptor;
DE AltName: CD_antigen=CD304;
DE Flags: Precursor;
GN Name=NRP1 {ECO:0000312|HGNC:HGNC:8004}; Synonyms=NRP, VEGF165R;
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 1), FUNCTION, AND VARIANT ALA-179.
RX PubMed=9288753; DOI=10.1016/s0092-8674(00)80534-6;
RA He Z., Tessier-Lavigne M.;
RT "Neuropilin is a receptor for the axonal chemorepellent semaphorin III.";
RL Cell 90:739-751(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, PROTEIN SEQUENCE OF
RP 22-39, VARIANT ALA-179, AND TISSUE SPECIFICITY.
RC TISSUE=Mammary gland;
RX PubMed=9529250; DOI=10.1016/s0092-8674(00)81402-6;
RA Soker S., Takashima S., Miao H.-Q., Neufeld G., Klagsbrun M.;
RT "Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-
RT specific receptor for vascular endothelial growth factor.";
RL Cell 92:735-745(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, PROTEIN SEQUENCE OF
RP 22-31, VARIANT ALA-179, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION
RP (ISOFORM 2).
RC TISSUE=Prostatic adenocarcinoma;
RX PubMed=10688880; DOI=10.1073/pnas.040337597;
RA Gagnon M.L., Bielenberg D.R., Gechtman Z., Miao H.-Q., Takashima S.,
RA Soker S., Klagsbrun M.;
RT "Identification of a natural soluble neuropilin-1 that binds vascular
RT endothelial growth factor: in vivo expression and antitumor activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:2573-2578(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-179.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-179.
RC TISSUE=Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-179.
RG SeattleSNPs variation discovery resource;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-179.
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP ALA-179.
RC TISSUE=Kidney, and Muscle;
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 [10]
RP INTERACTION WITH PLXNB1.
RX PubMed=10520995; DOI=10.1016/s0092-8674(00)80063-x;
RA Tamagnone L., Artigiani S., Chen H., He Z., Ming G.-L., Song H.-L.,
RA Chedotal A., Winberg M.L., Goodman C.S., Poo M.-M., Tessier-Lavigne M.,
RA Comoglio P.M.;
RT "Plexins are a large family of receptors for transmembrane, secreted and
RT GPI-anchored semaphorins in vertebrates.";
RL Cell 99:71-80(1999).
RN [11]
RP FUNCTION.
RX PubMed=10748121; DOI=10.1074/jbc.m909259199;
RA Gluzman-Poltorak Z., Cohen T., Herzog Y., Neufeld G.;
RT "Neuropilin-2 is a receptor for the vascular endothelial growth factor
RT (VEGF) forms VEGF-145 and VEGF-165.";
RL J. Biol. Chem. 275:18040-18045(2000).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-150.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [13]
RP GLYCOSYLATION AT SER-612.
RX PubMed=16763549; DOI=10.1038/sj.emboj.7601188;
RA Shintani Y., Takashima S., Asano Y., Kato H., Liao Y., Yamazaki S.,
RA Tsukamoto O., Seguchi O., Yamamoto H., Fukushima T., Sugahara K.,
RA Kitakaze M., Hori M.;
RT "Glycosaminoglycan modification of neuropilin-1 modulates VEGFR2
RT signaling.";
RL EMBO J. 25:3045-3055(2006).
RN [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-150; ASN-261 AND ASN-522.
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 [15]
RP FUNCTION, INTERACTION WITH VEGF-A165, AND DOMAIN.
RX PubMed=19805273; DOI=10.1073/pnas.0908201106;
RA Teesalu T., Sugahara K.N., Kotamraju V.R., Ruoslahti E.;
RT "C-end rule peptides mediate neuropilin-1-dependent cell, vascular, and
RT tissue penetration.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16157-16162(2009).
RN [16]
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 [17]
RP INTERACTION WITH VEGFA.
RX PubMed=26503042; DOI=10.1038/nature15510;
RA He W., Bai G., Zhou H., Wei N., White N.M., Lauer J., Liu H., Shi Y.,
RA Dumitru C.D., Lettieri K., Shubayev V., Jordanova A., Guergueltcheva V.,
RA Griffin P.R., Burgess R.W., Pfaff S.L., Yang X.L.;
RT "CMT2D neuropathy is linked to the neomorphic binding activity of glycyl-
RT tRNA synthetase.";
RL Nature 526:710-714(2015).
RN [18]
RP ERRATUM OF PUBMED:26503042.
RX PubMed=26789244; DOI=10.1038/nature16499;
RA He W., Bai G., Zhou H., Wei N., White N.M., Lauer J., Liu H., Shi Y.,
RA Dan Dumitru C., Lettieri K., Shubayev V., Jordanova A., Guergueltcheva V.,
RA Griffin P.R., Burgess R.W., Pfaff S.L., Yang X.L.;
RT "Corrigendum: CMT2D neuropathy is linked to the neomorphic binding activity
RT of glycyl-tRNA synthetase.";
RL Nature 532:402-402(2016).
RN [19]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=30623799; DOI=10.1016/j.isci.2018.12.005;
RA Issitt T., Bosseboeuf E., De Winter N., Dufton N., Gestri G., Senatore V.,
RA Chikh A., Randi A.M., Raimondi C.;
RT "Neuropilin-1 Controls Endothelial Homeostasis by Regulating Mitochondrial
RT Function and Iron-Dependent Oxidative Stress.";
RL IScience 11:205-223(2019).
RN [20]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH SARS-COV-2 SPIKE
RP GLYCOPROTEIN (MICROBIAL INFECTION).
RX PubMed=33000221; DOI=10.3892/mmr.2020.11510;
RA Davies J., Randeva H.S., Chatha K., Hall M., Spandidos D.A., Karteris E.,
RA Kyrou I.;
RT "Neuropilin-1 as a new potential SARS-CoV-2 infection mediator implicated
RT in the neurologic features and central nervous system involvement of COVID-
RT 19.";
RL Mol. Med. Report. 22:4221-4226(2020).
RN [21]
RP TISSUE SPECIFICITY.
RX PubMed=33082293; DOI=10.1126/science.abd2985;
RA Cantuti-Castelvetri L., Ojha R., Pedro L.D., Djannatian M., Franz J.,
RA Kuivanen S., van der Meer F., Kallio K., Kaya T., Anastasina M., Smura T.,
RA Levanov L., Szirovicza L., Tobi A., Kallio-Kokko H., Oesterlund P.,
RA Joensuu M., Meunier F.A., Butcher S.J., Winkler M.S., Mollenhauer B.,
RA Helenius A., Gokce O., Teesalu T., Hepojoki J., Vapalahti O.,
RA Stadelmann C., Balistreri G., Simons M.;
RT "Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity.";
RL Science 370:856-860(2020).
RN [22]
RP TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-829.
RX PubMed=36213313; DOI=10.1007/s42485-022-00092-3;
RA Ramarajan M.G., Saraswat M., Budhraja R., Garapati K., Raymond K.,
RA Pandey A.;
RT "Mass spectrometric analysis of chondroitin sulfate-linked peptides.";
RL J. Proteins Proteom. 13:187-203(2022).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 273-427.
RX PubMed=12517344; DOI=10.1016/s0969-2126(02)00941-3;
RA Lee C.C., Kreusch A., McMullan D., Ng K., Spraggon G.;
RT "Crystal structure of the human neuropilin-1 b1 domain.";
RL Structure 11:99-108(2003).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 141-586 ALONE AND IN COMPLEX WITH
RP ANTIBODY, GLYCOSYLATION AT ASN-150 AND ASN-261, SUBUNIT, CALCIUM-BINDING
RP SITES, HEPARIN-BINDING, AND DISULFIDE BONDS.
RX PubMed=17989695; DOI=10.1038/sj.emboj.7601906;
RA Appleton B.A., Wu P., Maloney J., Yin J., Liang W.C., Stawicki S.,
RA Mortara K., Bowman K.K., Elliott J.M., Desmarais W., Bazan J.F., Bagri A.,
RA Tessier-Lavigne M., Koch A.W., Wu Y., Watts R.J., Wiesmann C.;
RT "Structural studies of neuropilin/antibody complexes provide insights into
RT semaphorin and VEGF binding.";
RL EMBO J. 26:4902-4912(2007).
RN [25] {ECO:0007744|PDB:7JJC}
RP X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 273-427 IN COMPLEX WITH
RP SARS-COV-2 SPIKE PROTEIN S1, FUNCTION (MICROBIAL INFECTION), AND
RP INTERACTION WITH SARS-COV-2 SPIKE PROTEIN S1 (MICROBIAL INFECTION).
RX PubMed=33082294; DOI=10.1126/science.abd3072;
RA Daly J.L., Simonetti B., Klein K., Chen K.E., Williamson M.K.,
RA Anton-Plagaro C., Shoemark D.K., Simon-Gracia L., Bauer M., Hollandi R.,
RA Greber U.F., Horvath P., Sessions R.B., Helenius A., Hiscox J.A.,
RA Teesalu T., Matthews D.A., Davidson A.D., Collins B.M., Cullen P.J.,
RA Yamauchi Y.;
RT "Neuropilin-1 is a host factor for SARS-CoV-2 infection.";
RL Science 370:861-865(2020).
CC -!- FUNCTION: Cell-surface receptor involved in the development of the
CC cardiovascular system, in angiogenesis, in the formation of certain
CC neuronal circuits and in organogenesis outside the nervous system.
CC Mediates the chemorepulsant activity of semaphorins (PubMed:10688880,
CC PubMed:9288753, PubMed:9529250). Recognizes a C-end rule (CendR) motif
CC R/KXXR/K on its ligands which causes cellular internalization and
CC vascular leakage (PubMed:19805273). It binds to semaphorin 3A, the
CC PLGF-2 isoform of PGF, the VEGF165 isoform of VEGFA and VEGFB
CC (PubMed:10688880, PubMed:19805273, PubMed:9288753, PubMed:9529250).
CC Coexpression with KDR results in increased VEGF165 binding to KDR as
CC well as increased chemotaxis. Regulates VEGF-induced angiogenesis.
CC Binding to VEGFA initiates a signaling pathway needed for motor neuron
CC axon guidance and cell body migration, including for the caudal
CC migration of facial motor neurons from rhombomere 4 to rhombomere 6
CC during embryonic development (By similarity). Regulates mitochondrial
CC iron transport via interaction with ABCB8/MITOSUR (PubMed:30623799).
CC {ECO:0000250|UniProtKB:P97333, ECO:0000269|PubMed:10688880,
CC ECO:0000269|PubMed:19805273, ECO:0000269|PubMed:30623799,
CC ECO:0000269|PubMed:9288753, ECO:0000269|PubMed:9529250}.
CC -!- FUNCTION: (Microbial infection) Acts as a host factor for human
CC coronavirus SARS-CoV-2 infection. Recognizes and binds to CendR motif
CC RRAR on SARS-CoV-2 spike protein S1 which enhances SARS-CoV-2
CC infection. {ECO:0000269|PubMed:33082293, ECO:0000269|PubMed:33082294}.
CC -!- FUNCTION: [Isoform 2]: Binds VEGF-165 and may inhibit its binding to
CC cells (PubMed:10748121, PubMed:26503042). May induce apoptosis by
CC sequestering VEGF-165 (PubMed:10748121). May bind as well various
CC members of the semaphorin family. Its expression has an averse effect
CC on blood vessel number and integrity. {ECO:0000269|PubMed:10748121,
CC ECO:0000269|PubMed:26503042}.
CC -!- SUBUNIT: Homodimer, and heterodimer with NRP2 (PubMed:17989695).
CC Interacts with FER (By similarity). Interacts with PLXNB1
CC (PubMed:10520995). Interacts with VEGFA (PubMed:19805273,
CC PubMed:26503042). Interacts with ABCB8/MITOSUR in mitochondria
CC (PubMed:30623799). {ECO:0000250|UniProtKB:P97333,
CC ECO:0000269|PubMed:10520995, ECO:0000269|PubMed:17989695,
CC ECO:0000269|PubMed:19805273, ECO:0000269|PubMed:26503042,
CC ECO:0000269|PubMed:30623799}.
CC -!- SUBUNIT: (Microbial infection) Interacts with SARS coronavirus-2/SARS-
CC CoV-2 spike protein S1 (via the CendR motif RRAR).
CC {ECO:0000269|PubMed:33082294}.
CC -!- INTERACTION:
CC O14786; P21333: FLNA; NbExp=2; IntAct=EBI-1187100, EBI-350432;
CC O14786; P08648: ITGA5; NbExp=2; IntAct=EBI-1187100, EBI-1382311;
CC O14786; P35968: KDR; NbExp=2; IntAct=EBI-1187100, EBI-1005487;
CC O14786; P15692: VEGFA; NbExp=4; IntAct=EBI-1187100, EBI-1026643;
CC O14786; P0DTC2: S; Xeno; NbExp=9; IntAct=EBI-1187100, EBI-25474821;
CC O14786-2; P15692-4: VEGFA; NbExp=4; IntAct=EBI-6285281, EBI-1026691;
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted
CC {ECO:0000269|PubMed:10688880}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000305|PubMed:30623799}; Single-pass type I membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:30623799}; Single-pass
CC type I membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000269|PubMed:30623799}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Membrane-bound;
CC IsoId=O14786-1; Sequence=Displayed;
CC Name=2; Synonyms=Soluble {ECO:0000303|PubMed:10688880}, SNRP1;
CC IsoId=O14786-2; Sequence=VSP_004339, VSP_004340;
CC Name=3;
CC IsoId=O14786-3; Sequence=VSP_053498, VSP_004339, VSP_004340;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: The expression of isoforms 1 and 2
CC does not seem to overlap. Expressed in olfactory epithelium (at protein
CC level) (PubMed:33082293). Expressed in fibroblasts (at protein level)
CC (PubMed:36213313). Expressed by the blood vessels of different tissues.
CC In the developing embryo it is found predominantly in the nervous
CC system. In adult tissues, it is highly expressed in heart and placenta;
CC moderately in lung, liver, skeletal muscle, kidney and pancreas; and
CC low in adult brain (PubMed:10688880, PubMed:9529250). Expressed in the
CC central nervous system, including olfactory related regions such as the
CC olfactory tubercles and paraolfactory gyri (PubMed:33082293).
CC {ECO:0000269|PubMed:10688880, ECO:0000269|PubMed:33082293,
CC ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:9529250}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: The expression of isoforms 1 and 2
CC does not seem to overlap. Found in liver hepatocytes, kidney distal and
CC proximal tubules. {ECO:0000269|PubMed:10688880}.
CC -!- DOMAIN: The tandem CUB domains mediate binding to semaphorin, while the
CC tandem F5/8 domains are responsible for heparin and VEGF binding. F5/8
CC domains mediate the recognition and binding to R/KXXR/K CendR motifs
CC (PubMed:19805273, PubMed:33082294). {ECO:0000269|PubMed:19805273,
CC ECO:0000269|PubMed:33082294}.
CC -!- SIMILARITY: Belongs to the neuropilin family. {ECO:0000305}.
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DR EMBL; AF018956; AAC51759.1; -; mRNA.
DR EMBL; AF016050; AAC12921.1; -; mRNA.
DR EMBL; AF145712; AAF44344.1; -; mRNA.
DR EMBL; BT006995; AAP35641.1; -; mRNA.
DR EMBL; BX510902; CAD91133.1; -; mRNA.
DR EMBL; EU332859; ABY87548.1; -; Genomic_DNA.
DR EMBL; AL353600; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW85942.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW85944.1; -; Genomic_DNA.
DR EMBL; BC007533; AAH07533.1; -; mRNA.
DR EMBL; BC007737; AAH07737.1; -; mRNA.
DR CCDS; CCDS31179.1; -. [O14786-3]
DR CCDS; CCDS31180.1; -. [O14786-2]
DR CCDS; CCDS7177.1; -. [O14786-1]
DR RefSeq; NP_001019799.1; NM_001024628.2. [O14786-2]
DR RefSeq; NP_001019800.1; NM_001024629.2. [O14786-3]
DR RefSeq; NP_001316997.1; NM_001330068.1.
DR RefSeq; NP_003864.4; NM_003873.5. [O14786-1]
DR PDB; 1KEX; X-ray; 1.90 A; A=273-427.
DR PDB; 2QQI; X-ray; 1.80 A; A=273-586.
DR PDB; 2QQM; X-ray; 2.00 A; A=141-586.
DR PDB; 2QQN; X-ray; 2.20 A; A=273-427.
DR PDB; 3I97; X-ray; 2.90 A; A/B=273-427.
DR PDB; 4DEQ; X-ray; 2.65 A; A/B=274-429.
DR PDB; 4RN5; X-ray; 1.73 A; A=273-427.
DR PDB; 5C7G; X-ray; 1.45 A; A=273-427.
DR PDB; 5IJR; X-ray; 1.52 A; A/B=273-427.
DR PDB; 5IYY; X-ray; 1.60 A; A/B=273-427.
DR PDB; 5J1X; X-ray; 2.10 A; A/B/C/D=273-427.
DR PDB; 5JGI; X-ray; 1.38 A; A/B=273-427.
DR PDB; 5JGQ; X-ray; 1.60 A; A/B=273-427.
DR PDB; 5JHK; X-ray; 1.80 A; A/B=273-427.
DR PDB; 5L73; X-ray; 2.24 A; A/B=628-813.
DR PDB; 6FMC; X-ray; 0.90 A; A=273-427.
DR PDB; 6FMF; X-ray; 2.81 A; A=273-427.
DR PDB; 6TKK; X-ray; 1.06 A; A=273-427.
DR PDB; 7JJC; X-ray; 2.36 A; A/B/C/D=273-427.
DR PDB; 7O1N; X-ray; 1.56 A; A=273-427.
DR PDB; 7P5U; X-ray; 1.60 A; AAA/BBB=273-427.
DR PDB; 8C5G; X-ray; 2.70 A; A/B=271-586.
DR PDB; 8PFE; X-ray; 1.35 A; A/C=273-427.
DR PDBsum; 1KEX; -.
DR PDBsum; 2QQI; -.
DR PDBsum; 2QQM; -.
DR PDBsum; 2QQN; -.
DR PDBsum; 3I97; -.
DR PDBsum; 4DEQ; -.
DR PDBsum; 4RN5; -.
DR PDBsum; 5C7G; -.
DR PDBsum; 5IJR; -.
DR PDBsum; 5IYY; -.
DR PDBsum; 5J1X; -.
DR PDBsum; 5JGI; -.
DR PDBsum; 5JGQ; -.
DR PDBsum; 5JHK; -.
DR PDBsum; 5L73; -.
DR PDBsum; 6FMC; -.
DR PDBsum; 6FMF; -.
DR PDBsum; 6TKK; -.
DR PDBsum; 7JJC; -.
DR PDBsum; 7O1N; -.
DR PDBsum; 7P5U; -.
DR PDBsum; 8C5G; -.
DR PDBsum; 8PFE; -.
DR AlphaFoldDB; O14786; -.
DR SMR; O14786; -.
DR BioGRID; 114356; 320.
DR CORUM; O14786; -.
DR DIP; DIP-5743N; -.
DR IntAct; O14786; 57.
DR MINT; O14786; -.
DR STRING; 9606.ENSP00000265371; -.
DR BindingDB; O14786; -.
DR ChEMBL; CHEMBL5174; -.
DR GuidetoPHARMACOLOGY; 2998; -.
DR TCDB; 8.A.47.1.5; the neuropilin and tolloid-like (neto) family.
DR GlyConnect; 1557; 7 N-Linked glycans (4 sites).
DR GlyCosmos; O14786; 11 sites, 10 glycans.
DR GlyGen; O14786; 16 sites, 7 N-linked glycans (4 sites), 4 O-linked glycans (8 sites).
DR iPTMnet; O14786; -.
DR PhosphoSitePlus; O14786; -.
DR SwissPalm; O14786; -.
DR BioMuta; NRP1; -.
DR jPOST; O14786; -.
DR MassIVE; O14786; -.
DR PaxDb; 9606-ENSP00000265371; -.
DR PeptideAtlas; O14786; -.
DR ProteomicsDB; 48233; -. [O14786-1]
DR ProteomicsDB; 48234; -. [O14786-2]
DR ProteomicsDB; 64659; -.
DR Pumba; O14786; -.
DR ABCD; O14786; 26 sequenced antibodies.
DR Antibodypedia; 3859; 1024 antibodies from 42 providers.
DR DNASU; 8829; -.
DR Ensembl; ENST00000265371.8; ENSP00000265371.3; ENSG00000099250.18. [O14786-1]
DR Ensembl; ENST00000374821.9; ENSP00000363954.5; ENSG00000099250.18. [O14786-3]
DR Ensembl; ENST00000374822.8; ENSP00000363955.4; ENSG00000099250.18. [O14786-2]
DR Ensembl; ENST00000374867.7; ENSP00000364001.2; ENSG00000099250.18. [O14786-1]
DR GeneID; 8829; -.
DR KEGG; hsa:8829; -.
DR MANE-Select; ENST00000374867.7; ENSP00000364001.2; NM_003873.7; NP_003864.5.
DR UCSC; uc001iwx.5; human. [O14786-1]
DR AGR; HGNC:8004; -.
DR CTD; 8829; -.
DR DisGeNET; 8829; -.
DR GeneCards; NRP1; -.
DR HGNC; HGNC:8004; NRP1.
DR HPA; ENSG00000099250; Low tissue specificity.
DR MIM; 602069; gene.
DR neXtProt; NX_O14786; -.
DR OpenTargets; ENSG00000099250; -.
DR PharmGKB; PA31783; -.
DR VEuPathDB; HostDB:ENSG00000099250; -.
DR eggNOG; ENOG502QUEH; Eukaryota.
DR GeneTree; ENSGT00940000157169; -.
DR HOGENOM; CLU_015228_6_1_1; -.
DR InParanoid; O14786; -.
DR OMA; QEDCTKP; -.
DR OrthoDB; 5293253at2759; -.
DR PhylomeDB; O14786; -.
DR TreeFam; TF316506; -.
DR PathwayCommons; O14786; -.
DR Reactome; R-HSA-194306; Neurophilin interactions with VEGF and VEGFR.
DR Reactome; R-HSA-376176; Signaling by ROBO receptors.
DR Reactome; R-HSA-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-HSA-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-HSA-399956; CRMPs in Sema3A signaling.
DR Reactome; R-HSA-445144; Signal transduction by L1.
DR Reactome; R-HSA-447041; CHL1 interactions.
DR Reactome; R-HSA-9694614; Attachment and Entry.
DR SignaLink; O14786; -.
DR SIGNOR; O14786; -.
DR BioGRID-ORCS; 8829; 19 hits in 1158 CRISPR screens.
DR ChiTaRS; NRP1; human.
DR EvolutionaryTrace; O14786; -.
DR GeneWiki; Neuropilin_1; -.
DR GenomeRNAi; 8829; -.
DR Pharos; O14786; Tchem.
DR PRO; PR:O14786; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O14786; protein.
DR Bgee; ENSG00000099250; Expressed in stromal cell of endometrium and 195 other cell types or tissues.
DR ExpressionAtlas; O14786; baseline and differential.
DR GO; GO:0030424; C:axon; ISS:BHF-UCL.
DR GO; GO:0031410; C:cytoplasmic vesicle; TAS:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0005769; C:early endosome; ISS:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IDA:BHF-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005883; C:neurofilament; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; ISS:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0043235; C:receptor complex; TAS:BHF-UCL.
DR GO; GO:0002116; C:semaphorin receptor complex; NAS:BHF-UCL.
DR GO; GO:0097443; C:sorting endosome; ISS:BHF-UCL.
DR GO; GO:0015026; F:coreceptor activity; TAS:BHF-UCL.
DR GO; GO:0019955; F:cytokine binding; NAS:BHF-UCL.
DR GO; GO:0019838; F:growth factor binding; IPI:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IMP:BHF-UCL.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0017154; F:semaphorin receptor activity; IBA:GO_Central.
DR GO; GO:0038085; F:vascular endothelial growth factor binding; IPI:BHF-UCL.
DR GO; GO:0005021; F:vascular endothelial growth factor receptor activity; ISS:BHF-UCL.
DR GO; GO:0001525; P:angiogenesis; IMP:BHF-UCL.
DR GO; GO:0060978; P:angiogenesis involved in coronary vascular morphogenesis; ISS:BHF-UCL.
DR GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
DR GO; GO:0048844; P:artery morphogenesis; ISS:BHF-UCL.
DR GO; GO:0048846; P:axon extension involved in axon guidance; ISS:BHF-UCL.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007413; P:axonal fasciculation; IEA:Ensembl.
DR GO; GO:0060385; P:axonogenesis involved in innervation; ISS:BHF-UCL.
DR GO; GO:0150020; P:basal dendrite arborization; ISS:ARUK-UCL.
DR GO; GO:0150018; P:basal dendrite development; ISS:ARUK-UCL.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISS:BHF-UCL.
DR GO; GO:0021785; P:branchiomotor neuron axon guidance; ISS:ParkinsonsUK-UCL.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISS:BHF-UCL.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IMP:BHF-UCL.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISS:BHF-UCL.
DR GO; GO:0071679; P:commissural neuron axon guidance; ISS:BHF-UCL.
DR GO; GO:0060982; P:coronary artery morphogenesis; IEA:Ensembl.
DR GO; GO:0060666; P:dichotomous subdivision of terminal units involved in salivary gland branching; IEA:Ensembl.
DR GO; GO:1904835; P:dorsal root ganglion morphogenesis; IEA:Ensembl.
DR GO; GO:0035767; P:endothelial cell chemotaxis; IMP:BHF-UCL.
DR GO; GO:0097102; P:endothelial tip cell fate specification; ISS:BHF-UCL.
DR GO; GO:0021612; P:facial nerve structural organization; ISS:ParkinsonsUK-UCL.
DR GO; GO:1903375; P:facioacoustic ganglion development; IEA:Ensembl.
DR GO; GO:0021828; P:gonadotrophin-releasing hormone neuronal migration to the hypothalamus; IEA:Ensembl.
DR GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:BHF-UCL.
DR GO; GO:0008045; P:motor neuron axon guidance; ISS:ParkinsonsUK-UCL.
DR GO; GO:0097475; P:motor neuron migration; ISS:UniProtKB.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IEA:Ensembl.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0001755; P:neural crest cell migration; IBA:GO_Central.
DR GO; GO:1901166; P:neural crest cell migration involved in autonomic nervous system development; ISS:BHF-UCL.
DR GO; GO:0001764; P:neuron migration; ISS:BHF-UCL.
DR GO; GO:0038189; P:neuropilin signaling pathway; IMP:BHF-UCL.
DR GO; GO:1905040; P:otic placode development; IEA:Ensembl.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; ISS:BHF-UCL.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0050918; P:positive chemotaxis; ISS:BHF-UCL.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; ISS:BHF-UCL.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IEA:Ensembl.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:BHF-UCL.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; TAS:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:BHF-UCL.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:BHF-UCL.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IDA:BHF-UCL.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; TAS:BHF-UCL.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:BHF-UCL.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:BHF-UCL.
DR GO; GO:0099173; P:postsynapse organization; IEA:Ensembl.
DR GO; GO:1902946; P:protein localization to early endosome; ISS:BHF-UCL.
DR GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IMP:BHF-UCL.
DR GO; GO:0030947; P:regulation of vascular endothelial growth factor receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; TAS:BHF-UCL.
DR GO; GO:0061441; P:renal artery morphogenesis; IEA:Ensembl.
DR GO; GO:0009611; P:response to wounding; IBA:GO_Central.
DR GO; GO:0061299; P:retina vasculature morphogenesis in camera-type eye; ISS:BHF-UCL.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; ISS:BHF-UCL.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; ISS:BHF-UCL.
DR GO; GO:0097374; P:sensory neuron axon guidance; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0002040; P:sprouting angiogenesis; ISS:BHF-UCL.
DR GO; GO:0006930; P:substrate-dependent cell migration, cell extension; IMP:BHF-UCL.
DR GO; GO:0046718; P:symbiont entry into host cell; IDA:UniProtKB.
DR GO; GO:0061549; P:sympathetic ganglion development; ISS:BHF-UCL.
DR GO; GO:0097490; P:sympathetic neuron projection extension; ISS:BHF-UCL.
DR GO; GO:0097491; P:sympathetic neuron projection guidance; ISS:BHF-UCL.
DR GO; GO:0061551; P:trigeminal ganglion development; IEA:Ensembl.
DR GO; GO:0021637; P:trigeminal nerve structural organization; ISS:ParkinsonsUK-UCL.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0001570; P:vasculogenesis; IBA:GO_Central.
DR GO; GO:0038190; P:VEGF-activated neuropilin signaling pathway; IMP:BHF-UCL.
DR GO; GO:0036486; P:ventral trunk neural crest cell migration; IEA:Ensembl.
DR GO; GO:0021649; P:vestibulocochlear nerve structural organization; IEA:Ensembl.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00057; FA58C; 2.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR014648; Neuropilin.
DR InterPro; IPR022579; Neuropilin_C.
DR InterPro; IPR050633; Neuropilin_MCO_CoagFactor.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR46806; F5/8 TYPE C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46806:SF4; NEUROPILIN-1; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF11980; DUF3481; 1.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR Pfam; PF00629; MAM; 1.
DR PIRSF; PIRSF036960; Neuropilin; 1.
DR PRINTS; PR00020; MAMDOMAIN.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00231; FA58C; 2.
DR SMART; SM00137; MAM; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01285; FA58C_1; 2.
DR PROSITE; PS01286; FA58C_2; 2.
DR PROSITE; PS50022; FA58C_3; 2.
DR PROSITE; PS00740; MAM_1; 1.
DR PROSITE; PS50060; MAM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Angiogenesis; Calcium; Cell membrane;
KW Cytoplasm; Developmental protein; Differentiation;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Heparan sulfate;
KW Heparin-binding; Host-virus interaction; Membrane; Metal-binding;
KW Mitochondrion; Neurogenesis; Phosphoprotein; Proteoglycan;
KW Proteomics identification; Receptor; Reference proteome; Repeat; Secreted;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:10688880,
FT ECO:0000269|PubMed:9529250"
FT CHAIN 22..923
FT /note="Neuropilin-1"
FT /id="PRO_0000021859"
FT TOPO_DOM 22..856
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 857..879
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 880..923
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..141
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 147..265
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 275..424
FT /note="F5/8 type C 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 431..583
FT /note="F5/8 type C 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 645..811
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT REGION 820..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17989695,
FT ECO:0007744|PDB:2QQM"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17989695,
FT ECO:0007744|PDB:2QQM"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17989695,
FT ECO:0007744|PDB:2QQM"
FT MOD_RES 894
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97333"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:17989695, ECO:0000269|PubMed:19159218"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17989695,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 612
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:16763549"
FT CARBOHYD 612
FT /note="O-linked (Xyl...) (heparan sulfate) serine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:16763549"
FT CARBOHYD 829
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000269|PubMed:36213313"
FT CARBOHYD 842
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..54
FT /evidence="ECO:0000305|PubMed:17989695"
FT DISULFID 82..104
FT /evidence="ECO:0000305|PubMed:17989695"
FT DISULFID 147..173
FT /evidence="ECO:0000269|PubMed:17989695"
FT DISULFID 206..228
FT /evidence="ECO:0000269|PubMed:17989695"
FT DISULFID 275..424
FT /evidence="ECO:0000269|PubMed:17989695"
FT DISULFID 431..583
FT /evidence="ECO:0000269|PubMed:17989695"
FT VAR_SEQ 587..621
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_053498"
FT VAR_SEQ 642..644
FT /note="EFP -> GIK (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10688880,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_004339"
FT VAR_SEQ 645..923
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10688880,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_004340"
FT VARIANT 179
FT /note="V -> A (in dbSNP:rs7079053)"
FT /evidence="ECO:0000269|PubMed:10688880,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:9288753, ECO:0000269|PubMed:9529250,
FT ECO:0000269|Ref.4, ECO:0000269|Ref.6, ECO:0000269|Ref.8"
FT /id="VAR_046536"
FT VARIANT 561
FT /note="F -> L (in dbSNP:rs2228637)"
FT /id="VAR_046537"
FT VARIANT 733
FT /note="V -> I (in dbSNP:rs2228638)"
FT /id="VAR_056957"
FT CONFLICT 26
FT /note="K -> E (in Ref. 1; AAC51759)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="D -> G (in Ref. 5; CAD91133)"
FT /evidence="ECO:0000305"
FT CONFLICT 749
FT /note="D -> H (in Ref. 2; AAC12921)"
FT /evidence="ECO:0000305"
FT CONFLICT 855
FT /note="D -> E (in Ref. 1; AAC51759)"
FT /evidence="ECO:0000305"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:2QQM"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:2QQM"
FT TURN 161..164
FT /evidence="ECO:0007829|PDB:2QQM"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:2QQM"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:2QQM"
FT STRAND 185..193
FT /evidence="ECO:0007829|PDB:2QQM"
FT STRAND 208..217
FT /evidence="ECO:0007829|PDB:2QQM"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:2QQM"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:2QQM"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:2QQM"
FT STRAND 240..248
FT /evidence="ECO:0007829|PDB:2QQM"
FT STRAND 257..264
FT /evidence="ECO:0007829|PDB:2QQM"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:4RN5"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:6FMC"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:5JGI"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:6FMC"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:6FMC"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:6FMC"
FT HELIX 303..306
FT /evidence="ECO:0007829|PDB:6FMC"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:6TKK"
FT STRAND 326..342
FT /evidence="ECO:0007829|PDB:6FMC"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:6FMC"
FT STRAND 352..368
FT /evidence="ECO:0007829|PDB:6FMC"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:1KEX"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:5C7G"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:6FMC"
FT STRAND 391..414
FT /evidence="ECO:0007829|PDB:6FMC"
FT STRAND 417..424
FT /evidence="ECO:0007829|PDB:6FMC"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:2QQI"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:2QQI"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:2QQI"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:2QQI"
FT TURN 450..453
FT /evidence="ECO:0007829|PDB:2QQI"
FT HELIX 459..462
FT /evidence="ECO:0007829|PDB:2QQI"
FT TURN 464..466
FT /evidence="ECO:0007829|PDB:2QQM"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:2QQM"
FT STRAND 485..502
FT /evidence="ECO:0007829|PDB:2QQI"
FT TURN 506..508
FT /evidence="ECO:0007829|PDB:2QQM"
FT STRAND 515..525
FT /evidence="ECO:0007829|PDB:2QQI"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:2QQI"
FT STRAND 544..547
FT /evidence="ECO:0007829|PDB:2QQI"
FT STRAND 550..566
FT /evidence="ECO:0007829|PDB:2QQI"
FT STRAND 570..572
FT /evidence="ECO:0007829|PDB:2QQI"
FT STRAND 576..584
FT /evidence="ECO:0007829|PDB:2QQI"
FT HELIX 643..645
FT /evidence="ECO:0007829|PDB:5L73"
FT TURN 646..648
FT /evidence="ECO:0007829|PDB:5L73"
FT STRAND 667..671
FT /evidence="ECO:0007829|PDB:5L73"
FT STRAND 674..677
FT /evidence="ECO:0007829|PDB:5L73"
FT STRAND 680..682
FT /evidence="ECO:0007829|PDB:5L73"
FT TURN 686..689
FT /evidence="ECO:0007829|PDB:5L73"
FT STRAND 690..696
FT /evidence="ECO:0007829|PDB:5L73"
FT HELIX 699..701
FT /evidence="ECO:0007829|PDB:5L73"
FT STRAND 705..713
FT /evidence="ECO:0007829|PDB:5L73"
FT STRAND 720..728
FT /evidence="ECO:0007829|PDB:5L73"
FT STRAND 733..742
FT /evidence="ECO:0007829|PDB:5L73"
FT STRAND 744..746
FT /evidence="ECO:0007829|PDB:5L73"
FT STRAND 749..757
FT /evidence="ECO:0007829|PDB:5L73"
FT STRAND 761..770
FT /evidence="ECO:0007829|PDB:5L73"
FT STRAND 777..785
FT /evidence="ECO:0007829|PDB:5L73"
FT STRAND 792..800
FT /evidence="ECO:0007829|PDB:5L73"
FT TURN 806..808
FT /evidence="ECO:0007829|PDB:5L73"
FT STRAND 809..811
FT /evidence="ECO:0007829|PDB:5L73"
SQ SEQUENCE 923 AA; 103134 MW; 1EAC2FA6C8FD6A0B CRC64;
MERGLPLLCA VLALVLAPAG AFRNDKCGDT IKIESPGYLT SPGYPHSYHP SEKCEWLIQA
PDPYQRIMIN FNPHFDLEDR DCKYDYVEVF DGENENGHFR GKFCGKIAPP PVVSSGPFLF
IKFVSDYETH GAGFSIRYEI FKRGPECSQN YTTPSGVIKS PGFPEKYPNS LECTYIVFVP
KMSEIILEFE SFDLEPDSNP PGGMFCRYDR LEIWDGFPDV GPHIGRYCGQ KTPGRIRSSS
GILSMVFYTD SAIAKEGFSA NYSVLQSSVS EDFKCMEALG MESGEIHSDQ ITASSQYSTN
WSAERSRLNY PENGWTPGED SYREWIQVDL GLLRFVTAVG TQGAISKETK KKYYVKTYKI
DVSSNGEDWI TIKEGNKPVL FQGNTNPTDV VVAVFPKPLI TRFVRIKPAT WETGISMRFE
VYGCKITDYP CSGMLGMVSG LISDSQITSS NQGDRNWMPE NIRLVTSRSG WALPPAPHSY
INEWLQIDLG EEKIVRGIII QGGKHRENKV FMRKFKIGYS NNGSDWKMIM DDSKRKAKSF
EGNNNYDTPE LRTFPALSTR FIRIYPERAT HGGLGLRMEL LGCEVEAPTA GPTTPNGNLV
DECDDDQANC HSGTGDDFQL TGGTTVLATE KPTVIDSTIQ SEFPTYGFNC EFGWGSHKTF
CHWEHDNHVQ LKWSVLTSKT GPIQDHTGDG NFIYSQADEN QKGKVARLVS PVVYSQNSAH
CMTFWYHMSG SHVGTLRVKL RYQKPEEYDQ LVWMAIGHQG DHWKEGRVLL HKSLKLYQVI
FEGEIGKGNL GGIAVDDISI NNHISQEDCA KPADLDKKNP EIKIDETGST PGYEGEGEGD
KNISRKPGNV LKTLDPILIT IIAMSALGVL LGAVCGVVLY CACWHNGMSE RNLSALENYN
FELVDGVKLK KDKLNTQSTY SEA
//