ID A0A2K6D1I2_MACNE Unreviewed; 925 AA.
AC A0A2K6D1I2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Neuropilin {ECO:0000256|PIRNR:PIRNR036960};
GN Name=NRP1 {ECO:0000313|Ensembl:ENSMNEP00000029768.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000029768.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000029768.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the neuropilin family.
CC {ECO:0000256|ARBA:ARBA00006078, ECO:0000256|PIRNR:PIRNR036960}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR RefSeq; XP_011736548.1; XM_011738246.1.
DR AlphaFoldDB; A0A2K6D1I2; -.
DR STRING; 9545.ENSMNEP00000029768; -.
DR Ensembl; ENSMNET00000054182.1; ENSMNEP00000029768.1; ENSMNEG00000038208.1.
DR GeneID; 105479920; -.
DR KEGG; mni:105479920; -.
DR CTD; 8829; -.
DR GeneTree; ENSGT00940000157169; -.
DR OrthoDB; 5293253at2759; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000038208; Expressed in spleen and 11 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0017154; F:semaphorin receptor activity; IEA:InterPro.
DR GO; GO:0038085; F:vascular endothelial growth factor binding; IEA:Ensembl.
DR GO; GO:0005021; F:vascular endothelial growth factor receptor activity; IEA:InterPro.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IEA:InterPro.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IEA:Ensembl.
DR GO; GO:0035767; P:endothelial cell chemotaxis; IEA:Ensembl.
DR GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IEA:Ensembl.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IEA:Ensembl.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IEA:Ensembl.
DR GO; GO:0006930; P:substrate-dependent cell migration, cell extension; IEA:Ensembl.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0038190; P:VEGF-activated neuropilin signaling pathway; IEA:Ensembl.
DR GO; GO:0046718; P:viral entry into host cell; 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 3: Inferred from homology;
KW Angiogenesis {ECO:0000256|ARBA:ARBA00022657};
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRNR:PIRNR036960};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473,
KW ECO:0000256|PIRNR:PIRNR036960};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782,
KW ECO:0000256|PIRNR:PIRNR036960};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR036960-2};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022974};
KW Heparan sulfate {ECO:0000256|ARBA:ARBA00023207};
KW Heparin-binding {ECO:0000256|ARBA:ARBA00022674};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR036960};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036960-1};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902,
KW ECO:0000256|PIRNR:PIRNR036960};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Receptor {ECO:0000256|PIRNR:PIRNR036960};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..925
FT /note="Neuropilin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014399326"
FT TRANSMEM 859..884
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..143
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 149..267
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 277..426
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 433..585
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 650..813
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT REGION 822..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT DISULFID 29..56
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2,
FT ECO:0000256|PROSITE-ProRule:PRU00059"
FT DISULFID 84..106
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 149..175
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 208..230
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 277..426
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 433..585
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
SQ SEQUENCE 925 AA; 103244 MW; 5B2FF9138B79DBB3 CRC64;
MEKGLPLLCA ALALALALAP AGAFRNDKCG DTIKIESPGY LTSPGYPHSY HPSEKCEWLI
QAPDPYQRIM INFNPHFDLE DRDCKYDYVE VFDGENENGR LWGKFCGKIA PPPVVSSGQF
LFIKFVSDYE THGAGFSIRY EIFKRGPECS QNYTTSSGVI KSPGFPEKYP NSLECTYIVF
APKMSEIILE FESFDLEPDS NPPGGMFCRY DRLEIWDGFP DVGPHIGRYC GQKTPGRIRS
SSGILSMVFY TDSAIAKEGF SANYSVLQSS VSEDFKCMEA MGMESGEIHS DQITASSQYS
TNWSAERSRL NYPENGWTPG EDSYREWIQV DLGLLRFVTA VGTQGAISKE TKKKYYVKTY
KIDISSNGED WITIKEGNKP VLFQGNTNPT DVVVAVFPKP LITRFVRIKP ATWETGISMR
FEVYGCKITD YPCSGMLGMV SGLISDSQIT SSNQGDRNWM PENIRLVTSR SGWALPPAPH
SYVNEWLQID LGEEKIVRGI IIQGGKHREN KVFMRKFKIG YSNNGSDWKM IMDDSKRKAK
SFEGNNNYDT PELRTFPALS TRFIRIYPER ATHGGLGLRM ELLGCEVEAP TAGPTTPNGN
PVDECDDDQA NCHSGTGDDF QLTGGTTVLA TEKPTVIDST IQSEFPTYGF NCEFGWGSHK
TFCHWEHDNH VQLKWSVLTS KTGPIQDHTG DGNFIYSQAD ENQKGKVARL VSPVVYSQNS
AHCMTFWYHM SGSHVGTLRV KLRYQKPEEY DQLVWMAIGH QGDHWKEGRV LLHKSLKLYQ
VIFEGEIGKG NLGGIAVDDI SINNHISQED CAKPADLDKK NPEIKIDETG STPGYEGEGE
GDKNISRKPG NVLKTLDPIL ITIIAMSALG VLLGAVCGVV LYCACWHNGM SERNLSALEN
YNFELVDGVK LKKDKLNTQS TYSEA
//
