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 27-MAR-2024, entry version 233. 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:9288753, CC PubMed:9529250, PubMed:10688880). 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:9288753, PubMed:9529250, PubMed:10688880, PubMed:19805273). 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:26503042, CC PubMed:19805273). 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; 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; 8PFE; -. DR AlphaFoldDB; O14786; -. DR SMR; O14786; -. DR BioGRID; 114356; 319. DR CORUM; O14786; -. DR DIP; DIP-5743N; -. DR IntAct; O14786; 44. 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; 1077 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:0060301; P:positive regulation of cytokine activity; TAS:BHF-UCL. 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; IMP:BHF-UCL. 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: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 GO; GO:0046718; P:viral entry into host cell; IDA:UniProtKB. 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. DR Genevisible; O14786; HS. 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 //