NRP1_CHICK
ID NRP1_CHICK Reviewed; 914 AA.
AC P79795;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Neuropilin-1;
DE AltName: Full=A5 protein;
DE Flags: Precursor;
GN Name=NRP1; Synonyms=NRP;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn; TISSUE=Embryonic brain;
RX PubMed=7601310; DOI=10.1006/dbio.1995.1208;
RA Takagi S., Kasuya Y., Shimizu M., Matsuura T., Tsuboi M., Kawakami A.,
RA Fujisawa H.;
RT "Expression of a cell adhesion molecule, neuropilin, in the developing
RT chick nervous system.";
RL Dev. Biol. 170:207-222(1995).
CC -!- FUNCTION: Receptor involved in the development of the cardiovascular
CC system, in angiogenesis, in the formation of certain neuronal circuits
CC and in organogenesis outside the nervous system (By similarity).
CC Mediates the chemorepulsant activity of semaphorins. Binding to VEGFA
CC initiates a signaling pathway needed for motor neuron axon guidance and
CC cell body migration, including for the caudal migration of facial motor
CC neurons from rhombomere 4 to rhombomere 6 during embryonic development
CC (By similarity). Regulates mitochondrial iron transport via interaction
CC (By similarity). {ECO:0000250|UniProtKB:O14786,
CC ECO:0000250|UniProtKB:P97333}.
CC -!- SUBUNIT: Homodimer, and heterodimer. {ECO:0000250|UniProtKB:O14786}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000250|UniProtKB:O14786}; Single-pass type I membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:O14786}; Single-
CC pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Developing nervous system; optic tectum (layers D
CC and E of SGFS), amacrine cells of retina, neurites of dorsal root
CC ganglia. Also expressed in non-neuronal cells, e.g. blood vessels in
CC the entire embryo.
CC -!- SIMILARITY: Belongs to the neuropilin family. {ECO:0000305}.
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DR EMBL; D45416; BAA08256.1; -; mRNA.
DR RefSeq; NP_990113.1; NM_204782.1.
DR AlphaFoldDB; P79795; -.
DR SMR; P79795; -.
DR STRING; 9031.ENSGALP00000011550; -.
DR PaxDb; P79795; -.
DR GeneID; 395560; -.
DR KEGG; gga:395560; -.
DR CTD; 8829; -.
DR VEuPathDB; HostDB:geneid_395560; -.
DR eggNOG; ENOG502QUEH; Eukaryota.
DR InParanoid; P79795; -.
DR OrthoDB; 124611at2759; -.
DR PhylomeDB; P79795; -.
DR PRO; PR:P79795; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0030424; C:axon; IDA:AgBase.
DR GO; GO:0043679; C:axon terminus; IDA:AgBase.
DR GO; GO:0044295; C:axonal growth cone; IDA:AgBase.
DR GO; GO:0070852; C:cell body fiber; IDA:AgBase.
DR GO; GO:0032584; C:growth cone membrane; IDA:AgBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR GO; GO:0019838; F:growth factor binding; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017154; F:semaphorin receptor activity; IEA:InterPro.
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:0009887; P:animal organ morphogenesis; IEA:InterPro.
DR GO; GO:0007411; P:axon guidance; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0098743; P:cell aggregation; IDA:AgBase.
DR GO; GO:0035767; P:endothelial cell chemotaxis; IEA:InterPro.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:AgBase.
DR GO; GO:0022035; P:rhombomere cell migration; IMP:AgBase.
DR GO; GO:0048729; P:tissue morphogenesis; IMP:AgBase.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IEA:InterPro.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00057; FA58C; 2.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.120.290; -; 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; IPR027146; NRP1.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR46806:SF4; PTHR46806:SF4; 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; SSF49785; SSF49785; 2.
DR SUPFAM; SSF49854; SSF49854; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
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 2: Evidence at transcript level;
KW Angiogenesis; Calcium; Cell adhesion; Cell membrane; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein; Heparan sulfate;
KW Heparin-binding; Membrane; Metal-binding; Mitochondrion; Neurogenesis;
KW Proteoglycan; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..914
FT /note="Neuropilin-1"
FT /id="PRO_0000021858"
FT TOPO_DOM 20..847
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 848..870
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 871..914
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..139
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 145..263
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 273..422
FT /note="F5/8 type C 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 429..581
FT /note="F5/8 type C 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 636..801
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT REGION 809..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 610
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine;
FT alternate"
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT CARBOHYD 610
FT /note="O-linked (Xyl...) (heparan sulfate) serine;
FT alternate"
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT CARBOHYD 817
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 25..52
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT DISULFID 80..102
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT DISULFID 145..171
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT DISULFID 204..226
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT DISULFID 273..422
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT DISULFID 429..581
FT /evidence="ECO:0000250|UniProtKB:O14786"
SQ SEQUENCE 914 AA; 102480 MW; DD2EE6D6F0CBB68C CRC64;
MDWGLFLHCA ALTFTLSRAL RSDKCGDTIK ILSPGYLTSP GYPQSYHPSQ KCEWLIQAPE
PYQRIMINFN PHFDLEDRDC KYDYVEVIDG DNAEGRLWGK YCGKIAPPPL VSSGPYLFIK
FVSDYETHGA GFSIRYEVFK RGPECSRNFT SSSGMIKSPG FPEKYPNSLE CTYIIFAPKM
SEIILEFESF ELEPDSNTPG GAFCRYDRLE IWDGFPDVGP HIGRYCGQNN PGRVRSSTGI
LSMVFYTDSA IAKEGFSANY SVSQSSVSED FQCMEPLGME SGEIHSDQIT VSSQYSAIWS
SERSRLNYPE NGWTPGEDSV REWIQVDLGL LRFVSGIGTQ GAISKETKKE YYLKTYRVDV
SSNGEDWITL KEGNKPVVFQ GNSNPTDVVY RPFPKPVLTR FVRIKPVSWE NGVSLRFEVY
GCKITDYPCS GMLGMVSGLI PDSQITASTQ VDRNWIPENA RLITSRSGWA LPPTTHPYTN
EWLQIDLGEE KIVRGIIVQG GKHRENKVFM KKFKIGYSNN GSDWKMIMDS SKKKIKTFEG
NTNYDTPELR TFEPVSTRII RVYPERATHA GLGLRMELLG CELEAPTAVP TVSEGKPVDE
CDDDQANCHS GTGGTTVLNT EKPTVIDNTV QPELPPYNLN CGFGWGSHKT LCQWEHDNQV
DLKWAILTSK TGPIQDHTGD GNFIYSQADE SQKGKVARLL SPIIYSQNSA HCMTFWYHMS
GPHVGTLKIK LRYQKPDEYD QVLLSLNGHQ ANCWQEGRVL LHKSVKLYQV VIEGEIGKGN
GGIAVDDINI DNHISQEDCQ KSTDVESEIV EEDPESNQTG FTPSYRTDED YDDISRKPGN
VLKTLDPILI TIIAMSALGV LLGAICGVVL YCACWHNGMS ERNLSALENY NFELVDGVKL
KKDKLNTQNS YSEA
