NRP1_XENLA
ID NRP1_XENLA Reviewed; 928 AA.
AC P28824;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Neuropilin-1;
DE AltName: Full=A5 antigen;
DE AltName: Full=A5 protein;
DE Flags: Precursor;
GN Name=nrp1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1908252; DOI=10.1016/0896-6273(91)90268-5;
RA Takagi S., Hirata T., Agata K., Mochii M., Eguchi G., Fujisawa H.;
RT "The A5 antigen, a candidate for the neuronal recognition molecule, has
RT homologies to complement components and coagulation factors.";
RL Neuron 7:295-307(1991).
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: Retinal ganglion cells and visual center neurons.
CC -!- SIMILARITY: Belongs to the neuropilin family. {ECO:0000305}.
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DR EMBL; D10467; BAA01260.1; -; mRNA.
DR PIR; JH0466; JQ0948.
DR AlphaFoldDB; P28824; -.
DR SMR; P28824; -.
DR PRIDE; P28824; -.
DR Proteomes; UP000186698; Genome assembly.
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; IEA:UniProtKB-SubCell.
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:0035767; P:endothelial cell chemotaxis; IEA:InterPro.
DR GO; GO:0120035; P:regulation of plasma membrane bounded cell projection organization; IEA:UniProt.
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 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..928
FT /note="Neuropilin-1"
FT /id="PRO_0000021862"
FT TOPO_DOM 22..860
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 861..883
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 884..928
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..584
FT /note="F5/8 type C 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 646..812
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT REGION 624..645
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:0000250|UniProtKB:O14786"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 613
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine;
FT alternate"
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT CARBOHYD 613
FT /note="O-linked (Xyl...) (heparan sulfate) serine;
FT alternate"
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT CARBOHYD 844
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..54
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT DISULFID 82..104
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT DISULFID 147..173
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT DISULFID 206..228
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT DISULFID 275..424
FT /evidence="ECO:0000250|UniProtKB:O14786"
FT DISULFID 431..584
FT /evidence="ECO:0000250|UniProtKB:O14786"
SQ SEQUENCE 928 AA; 103416 MW; AF6B323B0A4C789D CRC64;
MLLRLLSCCC WLLCSLRSSW ASRNDKCGDT IKITSPSYLT SAGYPHSYPP SQRCEWLIQA
PEHYQRIMIN FNPHFDLEDR ECKYDYVEVI DGDNANGQLL GKYCGKIAPS PLVSTGPSIF
IRFVSDYETP GAGFSIRYEV FKTGPECSRN FTSSNGVIKS PKYPEKYPNA LECTYIIFAP
KMQEIVLEFE SFELEADSNA PGGQTCRYDW LGIWDGFPGV GPHIGRYCGQ NTPGRVRSFT
GILSMIFHTD SAIAKEGFFA NFSVVQSNTD EDFQCKEALG MESGEIHFDQ ISVSSQYSMN
WSAERSRLNY VENGWTPGED TVKEWIQVDL ENLRFVSGIG TQGAISKETK KKYFVKSYKV
DISSNGEDWI TLKDGNKHLV FTGNTDATDV VYRPFSKPVI TRFVRLRPVT WENGISLRFE
LYGCKITDYP CSRMLGMVSG LISDSQITAS SQVDRNWVPE LARLVTSRSG WALPPSNTHP
YTKEWLQIDL AEEKIVRGVI IQGGKHKENK VFMRKFKIGY SNNGTEWEMI MDSSKNKPKT
FEGNTNYDTP ELRTFAHITT GFIRIIPERA SASGLALRLE LLGCEVETPT SIPTTPEVNG
GDECEGDLAN CHSGTDEGFK LTVGATGQST ETPTVEASPE EPDMTHSDLD CKFGWGSQKT
VCNWQHDISS DLKWAVLNSK TGPVQDHTGD GNFIYSEADE RHEGRAARLM SPVVSSSRSA
HCLTFWYHMD GSHVGTLSIK LKYEMEEDFD QTLWTVSGNQ GDQWKEARVV LHKTMKQYQV
IVEGTVGKGS AGGIAVDDII IANHISPSQC RAPEIDDSAN KIGEEDSEID KTGSTPNYAL
NEFNESISKK PGNVLKTLDP ILITIIAMSA LGVLLGAICG VVLYCACWHN GMSERNLSAL
ENYNFELVDG VKLKKDKLNT QNSYSEAS
