ID A0A093CGE9_TAUER Unreviewed; 840 AA.
AC A0A093CGE9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Neuropilin-1 {ECO:0000313|EMBL:KFV13528.1};
DE Flags: Fragment;
GN ORFNames=N340_10125 {ECO:0000313|EMBL:KFV13528.1};
OS Tauraco erythrolophus (Red-crested turaco).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Musophagiformes; Musophagidae; Tauraco.
OX NCBI_TaxID=121530 {ECO:0000313|EMBL:KFV13528.1, ECO:0000313|Proteomes:UP000053661};
RN [1] {ECO:0000313|EMBL:KFV13528.1, ECO:0000313|Proteomes:UP000053661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N340 {ECO:0000313|EMBL:KFV13528.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL461810; KFV13528.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093CGE9; -.
DR Proteomes; UP000053661; Unassembled WGS sequence.
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-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:0007411; P:axon guidance; IEA:InterPro.
DR GO; GO:0120035; P:regulation of plasma membrane bounded cell projection organization; 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 PRINTS; PR00020; MAMDOMAIN.
DR SMART; SM00042; CUB; 1.
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 Angiogenesis {ECO:0000256|ARBA:ARBA00022657};
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR036960-1};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
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|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036960-1};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000053661};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 774..799
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..59
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 65..183
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 193..342
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 349..501
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 566..728
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT BINDING 127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT DISULFID 65..91
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 124..146
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 193..342
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 349..501
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV13528.1"
FT NON_TER 840
FT /evidence="ECO:0000313|EMBL:KFV13528.1"
SQ SEQUENCE 840 AA; 94032 MW; B2C5D0B03686EEC1 CRC64;
RYDYVEVIDG DNAEGRLWGK YCGKIAPPPL VSSGPYLFIK FVSDYETHGA GFSIRYEVFK
RGPECSRNFT SSSGAIKSPG FPEKYPNSLE CTYIIFAPKM SEIILEFESF ELEPDSNTPG
GAFCRYDRLE IWDGFPDVGP HIGRYCGQNN PGRVRSSTGI LSMVFYTDSA IAKEGFSANY
SVSQSSVSED FQCMEPLGME SGEIHSDQIT VSSQYSAIWS SERSRLNYPE NGWTPGEDSS
REWIQVDLGL LRFVSGIGTQ GAISKETKKE YYLKTYRVDV SSNGEDWITL KEGNKPVVFQ
GNSNPTEVVY RPFAKPVLTR FVRIRPLSWE NGVSLRFEVY GCKITDYPCS GMLGMVSGLI
PDSQITASTQ VDRNWIPENA RLITSRSGWA LPPTTHPYTN EWLQIDLGEE KKVRGIIVQG
GKHRENKVFM KKFKIGYSNN GSDWKMIMDS SKKKIKTFEG NTNYDTPELR TFEPLSTRFI
RVYPERATHG GLGLRMELLG CELEAPTAVP TVSEGKPVDE CDDDQANCHS GTGDDYQLTG
GTTVLNTEKP TVIDNTLQPE LPLYNFNCAF GWGSQKTLCH WEHDNQVDLK WAILTSKTGP
IQDHTGDGNF IYSQADESQK GKVARLLSPV IYSQNSAHCM TFWYHMSGAH VGTLKIKLRY
QKPDEYDQVL WTLSGHQANC WKEGRVLLHK SVKHYQVVIE GEIGKGTGGI AVDDIKIDNH
VAQEDCRILT RIGSENFAIL YSILGFTPPY HTGEDYDDNI SRKPGNVLKT LDPILITIIA
MSALGVLLGA ICGVVLYCAC WHNGMSERNL SALENYNFEL VDGVKLKKDK LNTQNSYSEA
//
