ID A0A3B3CCZ1_ORYME Unreviewed; 868 AA.
AC A0A3B3CCZ1;
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 Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000015178.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000015178.1}
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 AlphaFoldDB; A0A3B3CCZ1; -.
DR STRING; 30732.ENSOMEP00000015178; -.
DR PaxDb; 30732-ENSOMEP00000015178; -.
DR Ensembl; ENSOMET00000033868.1; ENSOMEP00000015178.1; ENSOMEG00000016727.1.
DR GeneTree; ENSGT00940000155270; -.
DR OMA; XYDFIEI; -.
DR Proteomes; UP000261560; 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:SF11; NEUROPILIN; 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; PS00740; MAM_1; 1.
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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 802..827
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..134
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 140..258
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 268..418
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 425..583
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 597..759
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT BINDING 243
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT DISULFID 20..47
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2,
FT ECO:0000256|PROSITE-ProRule:PRU00059"
FT DISULFID 75..97
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 140..166
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 199..221
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 268..418
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 425..583
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
SQ SEQUENCE 868 AA; 96605 MW; 0E377A939AF2CD22 CRC64;
SSLFPVSWSS CFSLDSPEPC GGYLDASDAG YITTPGYPHE YPANQNCRWI ITAPEPSQRI
ILNFNPHFEI EKLDCRYDYV EIHDGNSESA DLLGKHCSNI APAPIISSGP SLLIKFVSDY
AQHGAGFSLR YEIYKTGSDC SRNFTSHSGL IESPGFPDKY PHNLECFFII VVPPSMDVTL
NFLTFDLEND PLPGGEGECK YDWLEVWDGL PAVGPLIGRY CGTRVPPEIH SSTGILSLAF
HTDMAVAKDG FSARYNMTHK EVSETFHCSN PFGMESGKIT DEQITASSTF EEGHWLPRQA
RLNCNDNAWT PNEDSVREYI QVDLHTVKVL TGIATQGAIS KETQKTYYVT TFKLEISTNG
EDWMIYRHSK NHKIFHGNTD ATEVVLNRIP QPVLARFVRI RPQTWKNGIA LRFELYGCQI
TDAPCSELQG MLSGLLPDSQ ISASSMRDIH GSMGAARLVA SRSGWFPNPT QPIVGEEWLQ
VDLGVPKMVR GVITQGARGL EGSTSAENRA FVRKYKLAHS LSGKDWSYIL DSKTGFAKVF
EGNSHYDTPE VRRFDEIVAQ YIRIFPERWS PAGIGMRMEV LGCDLPGEQT TTPSLSAVCD
FEQSLCGWSA DPHSGASWSL TTAAHSSLTS FSASFPDFSG NYLNLDAGSH SQQKKARLLS
PEVEPERGPL CLQFHYQLQG EAQGSLRVLL RDSDLDETLL WELRGDQGPH WREGRTILPQ
SPKEYQVVFE GFFENPTRGH IRIDNIHMSD SIQLEQCARE SLRLLTNSKN FIISLVSVRS
LPLPTSSFVS KDNAWLYTLD PILLTIIVMS SLGVLLGAVC AGLLLYCTCS YGGLSSRSST
TLENYNFELY DGIKHKVKIN QQRCCSEA
//
