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RAB5B_CHICK
ID   RAB5B_CHICK             Reviewed;         215 AA.
AC   Q5ZHW4;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Ras-related protein Rab-5B;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P20339};
GN   Name=RAB5B; ORFNames=RCJMB04_32j11;
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 [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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:P61020};
CC       Lipid-anchor {ECO:0000250|UniProtKB:P61020}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P61020}. Early endosome membrane
CC       {ECO:0000250|UniProtKB:P61020}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P61020}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; AJ721020; CAG32679.1; -; mRNA.
DR   RefSeq; NP_001186777.1; NM_001199848.1.
DR   AlphaFoldDB; Q5ZHW4; -.
DR   SMR; Q5ZHW4; -.
DR   STRING; 9031.ENSGALP00000041857; -.
DR   Ensembl; ENSGALT00000058623; ENSGALP00000056524; ENSGALG00000042482.
DR   GeneID; 100529061; -.
DR   KEGG; gga:100529061; -.
DR   CTD; 5869; -.
DR   VEuPathDB; HostDB:geneid_100529061; -.
DR   eggNOG; KOG0092; Eukaryota.
DR   GeneTree; ENSGT00940000160756; -.
DR   InParanoid; Q5ZHW4; -.
DR   OMA; AVHFDIW; -.
DR   PhylomeDB; Q5ZHW4; -.
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:Q5ZHW4; -.
DR   Proteomes; UP000000539; Unplaced.
DR   Bgee; ENSGALG00000042482; Expressed in skeletal muscle tissue and 12 other tissues.
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: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: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   2: Evidence at transcript level;
KW   Cell membrane; Endosome; GTP-binding; Hydrolase; Lipoprotein; Membrane;
KW   Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..215
FT                   /note="Ras-related protein Rab-5B"
FT                   /id="PRO_0000260744"
FT   REGION          184..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           49..57
FT                   /note="Effector region"
FT                   /evidence="ECO:0000255"
FT   BINDING         27..35
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   BINDING         46..52
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   BINDING         75..79
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   BINDING         133..136
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   BINDING         163..165
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   LIPID           212
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
FT   LIPID           213
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P20339"
SQ   SEQUENCE   215 AA;  23615 MW;  00C89A390443B49B CRC64;
     MTSRGAARPN GQSQASKICQ FKLVLLGESA VGKSSLVLRF VKGQFHEYQE STIGAAFLTQ
     SVCLDDTTVK FEIWDTAGQE RYHSLAPMYY RGAQAAIVVY DITNQETFAR AKTWVKELQR
     QASPSIVIAL AGNKADLASK RMVEYEEAQA YADDNSLLFM ETSAKTAMNV NDLFLAIAKK
     LPKSEPQSTS GAAGRSRGVD LHEQTQQNKS QCCSN
 
 
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