ID A0A091CM20_FUKDA Unreviewed; 856 AA.
AC A0A091CM20;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Neuropilin {ECO:0000256|PIRNR:PIRNR036960};
GN ORFNames=H920_19698 {ECO:0000313|EMBL:KFO18907.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO18907.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO18907.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO18907.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) 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, 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 EMBL; KN125295; KFO18907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091CM20; -.
DR STRING; 885580.ENSFDAP00000008730; -.
DR eggNOG; ENOG502QUEH; Eukaryota.
DR Proteomes; UP000028990; 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-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 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; 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 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:UP000028990};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 790..815
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..74
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 80..198
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 208..357
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 364..516
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 581..744
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT REGION 522..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..757
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-1"
FT DISULFID 15..37
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 80..106
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 139..161
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 208..357
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
FT DISULFID 364..516
FT /evidence="ECO:0000256|PIRSR:PIRSR036960-2"
SQ SEQUENCE 856 AA; 95871 MW; EDD3901B2B8FDA10 CRC64;
MINFNPHFDL EDRDCKYDYV EVIDGENENG RLWGKFCGKI APSPVVSSGP FLFIKFVSDY
ETHGAGFSIR YEIFKRGPEC SQNYTASTGV IKSPGFPEKY PNSLECTYII FAPKMSEIIL
EFESFDLELD SNNPLGMACR YDRLEFWDGF PGVGPHIGRF CGQKTPGQIR SSSGILSMVF
YTDSAIAKEG FSANYSILHS SVSEDFKCME PLGMESGEIH SDQIKASSQY STNWSAERSR
LNYPENGWTP GEDSYREWIQ VDLGLLRFVT AIGTQGAISK ETKKKYYVKT YRVDISSNED
DWITIKEGNK PVIFQGNTNP TDVAFGNFPK PLITRFIRIR PVTWETGISM RFEVYGCKIT
DYPCSGMLGI VSGLISDSQI TASNQGDRNW MPENVRLISS RSGWVLPPAP HPYNNEWLQV
DLGEETMVRG VIIQGGKHRE NKVYMRKFKV GYSNNGSDWK MIMDDSRRKA KSFEGNNNYD
TPELRTFPPI STRLIRIYPE RATHGGLGLR MELLGCDVEA PTAGPTTPNG NPVDECDDDQ
ANCHSGTGDD FQLTGGTTVL TTEKPTIIDS TIQSEFPTYG FNCEFGWGSH KTFCHWEHDS
QVQLKWSVLT SKTGPIQDHT GDGNFIYSQA DENQKGKVAR LVSPVVYSQN SAHCMTFWYH
MSGSHVGTLR VKLRYQKPEE YDQLVWMAIG HQGDHWKEGR VLLHKSLKLY QVIFEGEIGK
GNLGGIAVDD ISINNHISQE DCAKPDDLDK KNTETKIDET GSTPGYQGEG EGDKNISRKP
GNVLKTLDPI LITIIAMSAL GVLLGAVCGV VLYCACWHNG MSERNLSALE NYNFELVDGV
KLKKDKLNTQ SSYSEA
//
