ID A0A3Q1CNW0_AMPOC Unreviewed; 917 AA.
AC A0A3Q1CNW0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Neuropilin {ECO:0000256|PIRNR:PIRNR036960};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000027483.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000027483.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 AlphaFoldDB; A0A3Q1CNW0; -.
DR STRING; 80972.ENSAOCP00000027483; -.
DR Ensembl; ENSAOCT00000019597.1; ENSAOCP00000027483.1; ENSAOCG00000016425.1.
DR GeneTree; ENSGT00940000157169; -.
DR Proteomes; UP000257160; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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: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:0120035; P:regulation of plasma membrane bounded cell projection organization; IEA:UniProt.
DR GO; GO:0032101; P:regulation of response to external stimulus; IEA:UniProt.
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 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; 1.
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:UP000257160};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..917
FT /note="Neuropilin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018663726"
FT TRANSMEM 851..876
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 25..139
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 145..263
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 273..422
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 429..581
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 636..805
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT REGION 597..617
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:0000256|PIRSR:PIRSR036960-1"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT DISULFID 25..52
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2,
FT ECO:0000256|PROSITE-ProRule:PRU00059"
FT DISULFID 80..102
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 145..171
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 204..226
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 273..422
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 429..581
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
SQ SEQUENCE 917 AA; 101903 MW; 34BDF583FA90F8DE CRC64;
MHCGLVFILF MGILLVVKAF KNDKCGGNIR ISTANYLTSP GYPMSYPPSQ RCVWVISAPG
PHQRILINFN PHFDLEDREC KYDYVEVRDG VDESGQLVGK YCGKIAPSPV VSSGNQLFIK
FVSDYETHGA GFSIRYEIFK TGPECSRNFT SNSGVIKSPG FPEKYPNNLD CTFMIFAPKM
SEIILEFESF ELEPDTTPPT GVFCRYDRLE IWDGFPGVGP YIGRYCGQNT PGRIISYTGI
LALTINTDSA IAKEGFSANF TVIERTVPED FDCSDPLGME SGEITSDQIM ASSQYNPSWS
PERSRLNYYE NAWTPAEDSN KEWIQVDLGF LRFVSAIGTQ GAISQETRRV YFVKSYKVDV
SSNGEDWITL KEGSKQKVFQ GNTNPTDVAK TMLPKPTLTR FVRIRPVTWE TGIALRFEVY
GCKISEYPCS GMLGMVSGLI TDNQITASSH TDRSWVPENA RLLTSRTGWT LLPQPQPFTN
EWLQVDLGEE KLLKGLIIQG GKHRENKVFM KKFRLGYSNN GSDWRMVLDT NGNKPKIFEG
NSNYDTPELR TVEPLLTRFI RIYPERATPA GMGLRIELLG CEIEAPTLPP ITVVPSTTPS
DECDDDQASC HSGTGGTVMP ETTTAEVDTI PAFLWFACDF GWANDPSFCS WTSEDTGSRW
QIQSSGTPTL NTGPNMDHTG GSGNFIYTLA TGPQETEVAR LVSPVVSSTD SDLCVSFWYH
MFGSHIGTLH IKQRKQTVDG PADILLWTVS GHQGNRWREG RVLVPRTNKP YQVVIEGMVE
RKSWGDIAVD DIKVLNGLSM SDCKDPDVPT EPMLPEDSFN EILEEITEYP DFVETNQISG
AGNMLKTLDP ILITIIAMSA LGVFLGAICG VVLYCACSHG GMSDRNLSAL ENYNFELVDG
VKLKKDKLNV QSSYSEA
//
