|NRP1_HUMAN » Neuropilin-1 » Vascular endothelial cell growth factor 165 receptor;|
|Hydrophobic Thickness||36.4 ± 3.8 Å|
|Tilt Angle||8 ± 6°|
|Links||UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, Reactome|
|TM Segments||856-880 (856-888)|
Axon guidance (KEGG)
Developmental Biology (Reactome)
HTLV-I infection (KEGG)
Signal Transduction (Reactome)
|PDB||1kex (273-427), 3i97 (273-427), 2qqi (273-586), 4deq (A/B=274-429), 2qqm (A=141-586), 2qqn (A=273-427)|
ITB1, Complex: ITB1:NRP1
PLVAP, Complex: PLVAP:NRP1
PLXD1, Complex: PLXD1:NRP1
TGBR3, Complex: TGBR3:NRP1
TGFR1, Complex: TGFR1:NRP1
TGFR2, Complex: TGFR2:NRP1
AA: 842-923, C-terminal domain of neuropilin glycoprotein
|UniProt annotation for NRP1_HUMAN » Neuropilin-1|
|FUNCTION: The membrane-bound isoform 1 is a receptor involved in the development of the cardiovascular system, in angiogenesis, in the formation of certain neuronal circuits and in organogenesis outside the nervous system. It mediates the chemorepulsant activity of semaphorins. It binds to semaphorin 3A, The PLGF-2 isoform of PGF, The VEGF-165 isoform of VEGF and VEGF-B. Coexpression with KDR results in increased VEGF-165 binding to KDR as well as increased chemotaxis. It may regulate VEGF-induced angiogenesis. FUNCTION: The soluble isoform 2 binds VEGF-165 and appears to inhibit its binding to cells. It may also induce apoptosis by sequestering VEGF-165. May bind as well various members of the semaphorin family. Its expression has an averse effect on blood vessel number and integrity. SUBUNIT: Homodimer, and heterodimer with NRP2. Interacts with FER (By similarity). Binds PLXNB1. TISSUE SPECIFICITY: The expression of isoforms 1 and 2 does not seem to overlap. Isoform 1 is expressed by the blood vessels of different tissues. In the developing embryo it is found predominantly in the nervous system. In adult tissues, it is highly expressed in heart and placenta; moderately in lung, liver, skeletal muscle, kidney and pancreas; and low in adult brain. Isoform 2 is found in liver hepatocytes, kidney distal and proximal tubules. DOMAIN: The tandem CUB domains mediate binding to semaphorin, while the tandem F5/8 domains are responsible for heparin and VEGF binding.|
|UniProt features for NRP1_HUMAN » Neuropilin-1|
SIGNAL 1 21 |
CHAIN 22 923 Neuropilin-1.
DOMAIN 27 141 CUB 1.
DOMAIN 147 265 CUB 2.
DOMAIN 275 424 F5/8 type C 1.
DOMAIN 431 583 F5/8 type C 2.
DOMAIN 645 811 MAM.
DISULFID 27 54 Probable.
DISULFID 82 104 Probable.
DISULFID 147 173
DISULFID 206 228
DISULFID 275 424
DISULFID 431 583
|Amino Acid Sequence for NRP1_HUMAN » Neuropilin-1|
|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|