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   29-MAY-2024, entry version 234.
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}.
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; 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; 319.
DR   CORUM; O14786; -.
DR   DIP; DIP-5743N; -.
DR   IntAct; O14786; 45.
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   EPD; O14786; -.
DR   jPOST; O14786; -.
DR   MassIVE; O14786; -.
DR   MaxQB; 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; 1078 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; 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; Receptor;
KW   Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW   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
//