ID A0A3Q2D258_CYPVA Unreviewed; 876 AA.
AC A0A3Q2D258;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Neuropilin {ECO:0000256|PIRNR:PIRNR036960};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000012566.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000012566.1}
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; A0A3Q2D258; -.
DR Ensembl; ENSCVAT00000030386.1; ENSCVAP00000012566.1; ENSCVAG00000015007.1.
DR GeneTree; ENSGT00940000155270; -.
DR Proteomes; UP000265020; 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:InterPro.
DR GO; GO:0007411; P:axon guidance; IEA:InterPro.
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:SF2; NEUROPILIN-2; 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; 2.
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; PS50060; MAM_2; 1.
PE 3: Inferred from homology;
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 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}; Receptor {ECO:0000256|PIRNR:PIRNR036960};
KW Reference proteome {ECO:0000313|Proteomes:UP000265020};
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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..876
FT /note="Neuropilin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018633865"
FT TRANSMEM 810..835
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 32..146
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 153..271
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 281..431
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 438..598
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 618..768
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT DISULFID 32..59
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2,
FT ECO:0000256|PROSITE-ProRule:PRU00059"
FT DISULFID 87..109
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 153..179
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 212..234
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 281..431
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 438..598
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
SQ SEQUENCE 876 AA; 98397 MW; 5DC448005511775F CRC64;
HPPYPLNFSF LITFSSPHLI CLCSLAPTDS ECGGILDASK PGYITSPGYP TEYPPHQNCH
WVIQAPEPSQ RIVLNFNPHF EIERLDCKYD FIEIRDGTSD TADVLGRHCS NIAPPPIISS
GSSIQIRFVS DYAHQGAGFS LRYEIFKTGS EFCFRNFTSP SGMIESPGFP DKYPHNLECS
YMIMAPPHMD ITLTFLTFDL ENDPLMVGEG DCKYDWLEVW DGLPQASPLI GRYCGTKIPP
EIQSSSGLLS LSFHTDMAVA KDGFSARYNI THKKVSDSFH CSLALGMESG KISDDQISAS
TTFYDNRWLP RQARLNNDDN AWTPAEDSNK EFIQVDLHFL KVLTGISTQG AISKETQKSY
YVTTFKLEVS TNGEDWMVYR HGKNHKIFHA NTDPAEVVLN RIPQPLLARF VRIRPQTWKN
GIALRFELYG CQITDTRCSD LQGLMSGLLP DAQISVSSSR EVVWNPSSAR LVASRSGWFP
APTQPLAGEE WLQVDLGLPK TVRGVITQGA RGGDPGSGPA TDNRAFVRKY KVAYSLNAKD
WNFIMDFRTS QPKIFEGNTQ YDTPELRHFE ETVAQYIRLY PERWSPGGIG MRVEIIGCDL
PGRTHIMSYD DKSSRCGRGC SYDAALNLIW MPFWGFVNFN RVSFFSALNS YLYLDVSMKT
EQQRARLVSP VVPADAGPLC LLFSYQMWGE AKGHLRIFVR DSLNDESLLW SLHDNHTTVW
REGRTIVPRS PKEFQVVIEG FFEHNTRGHI WIDNIHMSAS SPLKECTGRS HNALGGLQYP
EWNTASPSSH PAVTLTPEKD NSWLYTLDPI LVTIIVMSSL GVLLGAVCAG LLLYCTCSYS
GLSSRSSTTL ENYNFELYDG LKHKVKLNQQ RCCTEA
//
