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RAB5C_CHICK
ID   RAB5C_CHICK             Reviewed;         216 AA.
AC   Q98932;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Ras-related protein Rab-5C;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P20339};
DE   AltName: Full=Rab5C-like protein;
GN   Name=RAB5C;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC   TISSUE=Liver;
RX   PubMed=9602038; DOI=10.1016/s0167-4781(98)00053-0;
RA   Bojer C.D.A., Wohlrab F., Ivessa N.E.;
RT   "Molecular cloning and expression of an avian rab5 homolog.";
RL   Biochim. Biophys. Acta 1398:25-31(1998).
CC   -!- FUNCTION: Protein transport. Probably involved in vesicular traffic.
CC       {ECO:0000250|UniProtKB:P20339}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC         Evidence={ECO:0000250|UniProtKB:P20339};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000250|UniProtKB:P20339};
CC   -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC       (GEFs) which promote the exchange of bound GDP for free GTP.
CC       {ECO:0000250|UniProtKB:P18066}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20339};
CC       Lipid-anchor {ECO:0000250|UniProtKB:P20339}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P20339}. Early endosome membrane
CC       {ECO:0000250|UniProtKB:P20339}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P20339}.
CC   -!- TISSUE SPECIFICITY: Detected in brain, ovary, rectum, small intestine,
CC       large intestine, liver, spleen, follicle and kidney (at protein level).
CC       {ECO:0000269|PubMed:9602038}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; Y07811; CAA69142.1; -; mRNA.
DR   RefSeq; NP_989856.1; NM_204525.1.
DR   RefSeq; XP_015155054.1; XM_015299568.1.
DR   AlphaFoldDB; Q98932; -.
DR   SMR; Q98932; -.
DR   STRING; 9031.ENSGALP00000005302; -.
DR   PaxDb; Q98932; -.
DR   Ensembl; ENSGALT00000005312; ENSGALP00000005302; ENSGALG00000003359.
DR   Ensembl; ENSGALT00000061358; ENSGALP00000044276; ENSGALG00000003359.
DR   Ensembl; ENSGALT00000078413; ENSGALP00000045206; ENSGALG00000003359.
DR   GeneID; 395197; -.
DR   KEGG; gga:395197; -.
DR   CTD; 5878; -.
DR   VEuPathDB; HostDB:geneid_395197; -.
DR   eggNOG; KOG0092; Eukaryota.
DR   GeneTree; ENSGT00940000154971; -.
DR   HOGENOM; CLU_041217_10_2_1; -.
DR   InParanoid; Q98932; -.
DR   OMA; TYAEEES; -.
DR   OrthoDB; 1340129at2759; -.
DR   PhylomeDB; Q98932; -.
DR   Reactome; R-GGA-432722; Golgi Associated Vesicle Biogenesis.
DR   Reactome; R-GGA-6798695; Neutrophil degranulation.
DR   Reactome; R-GGA-8854214; TBC/RABGAPs.
DR   Reactome; R-GGA-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-GGA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   PRO; PR:Q98932; -.
DR   Proteomes; UP000000539; Chromosome 27.
DR   Bgee; ENSGALG00000003359; Expressed in lung and 13 other tissues.
DR   ExpressionAtlas; Q98932; baseline and differential.
DR   GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0005811; C:lipid droplet; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR   GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0048227; P:plasma membrane to endosome transport; IEA:Ensembl.
DR   GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Endosome; GTP-binding; Hydrolase; Lipoprotein; Membrane;
KW   Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..216
FT                   /note="Ras-related protein Rab-5C"
FT                   /id="PRO_0000276769"
FT   REGION          184..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           50..58
FT                   /note="Effector region"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        200..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         28..36
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   BINDING         47..53
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   BINDING         76..80
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   BINDING         134..137
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   BINDING         164..166
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   LIPID           213
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   LIPID           214
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
SQ   SEQUENCE   216 AA;  23554 MW;  4EF604EE314FE6C7 CRC64;
     MAGRGGAARP NGPAAGNKIC QFKLVLLGES AVGKSSLVLR FVKGQFHEYQ ESTIGAAFLT
     QTVCLDDTTV KFEIWDTAGQ ERYHSLAPMY YRGAQAAIVV YDITNTDTFV RAKNWVKELQ
     RQASPNIVIA LAGNKADLAT KRAVDFQDAQ TYADDNSLLF METSAKTAMN VNEIFMAIAK
     KLPKNEPQNA PGGPGRNRVV DLQESSQPSR SQCCSN
 
 
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