ID A0A3B3YLB8_9TELE Unreviewed; 919 AA.
AC A0A3B3YLB8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Neuropilin {ECO:0000256|PIRNR:PIRNR036960};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000028142.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000028142.1}
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_014855412.1; XM_014999926.1.
DR STRING; 48701.ENSPMEP00000011003; -.
DR Ensembl; ENSPMET00000018003.1; ENSPMEP00000028142.1; ENSPMEG00000013020.1.
DR Ensembl; ENSPMET00000018009.1; ENSPMEP00000011003.1; ENSPMEG00000013020.1.
DR GeneID; 106925524; -.
DR CTD; 353246; -.
DR OrthoDB; 5293253at2759; -.
DR Proteomes; UP000261480; 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}; 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..919
FT /note="Neuropilin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040590482"
FT TRANSMEM 853..878
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 586..623
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 919 AA; 102233 MW; 2393F17E024A8DEB CRC64;
MHCGLVFVLF MGILVVLEAF KNDKCGGNIR ISSASYLTSP GYPMSYPPSQ RCMWVISAPG
PHQRILINFN PHFDLEDREC KYDYVEVRDG VDENGQLVGK YCGKIAPSAV VSSGNQLFIK
FVSDYETHGA GFSIRYEIFK TGPECSKNFT SNSGVIKSPG FPEKYPNNLD CTFMIFAPKM
SEIILEFESF ELEPDTTPPT GVFCRYDRLE IWDGFPGVGP YIGRYCGQNT PGRIISYTGI
LALTINTDSA IAKEGFSANF TVLDRTVPED FDCSDPLGME SGEITSDQIM ASSQYNPSWS
PERSRLNYYE NAWTPAEDSN KEWIQVDLGF LRFISAIGTQ GAISQETHKI YFVKSYKVDV
SSNGEDWITL KEGSKQKIFQ GNTNPTDVTK TKLPKPTLTR FLRIRPVTWE TGIALRFEVY
GCKISEYPCS GMLGMVSGLI TDNQITASSH TDRSWVPENA RLLTSRTGWT LLPQPQPFTN
EWLQVDLGEE KLVKGFIIQG GKYRENKVFM KKFRLGYSNN GSDWRVVSDT SGNKPKIFEG
NSNYDTPELR TVEPLLTRFI RIYPERATPA GMGLRLELLG CEIEAPTFPP TTPAPSTTPS
DECDDDQASC HSGTGGTTMP ETTTLKVDPI PAFLWFACDF GWPNDPSFCR WTSEDTGSRW
QIQSSGTPTL NTGPNMDHTG GSGNFIYTLA TGLQESEVAR LVSPMVSSED SDLCVSFWYH
MHGSHIGTLH IKQREQTEEG TADILLWTVS GHQGNRWREG RVLVPRISKP YQVVIEGLVQ
RKSWGDIAVD DIKVLDGLGK SDCEDPDVPT EPMLPEDNNN EIFEVEDITD YPDLVETNQI
SGAGNMLKTL NPILITIIAM SALGVFLGAI CGVVLYCACS HGGMSERNLS ALENYNFELV
DGVKLKKDKL NVQNSYSEA
//
