RAB5B_PONAB
ID RAB5B_PONAB Reviewed; 215 AA.
AC Q5RBG1;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Ras-related protein Rab-5B;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P20339};
GN Name=RAB5B;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Binds EEA1. Interacts with RIN2 and RIN3, which probably
CC regulate its pathway, possibly by acting as GEFs (By similarity).
CC Interacts with GDI1, GDI2, CHML and CHM; phosphorylation at Ser-84
CC disrupts this interaction (By similarity).
CC {ECO:0000250|UniProtKB:P61020}.
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}. Melanosome
CC {ECO:0000250|UniProtKB:P61020}.
CC -!- PTM: Phosphorylation of Ser-84 in the switch II region by LRRK2
CC prevents the association of RAB regulatory proteins, including CHM,
CC CHML and RAB GDP dissociation inhibitors GDI1 and GDI2.
CC {ECO:0000250|UniProtKB:P61020}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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; CR858688; CAH90899.1; -; mRNA.
DR RefSeq; NP_001125512.1; NM_001132040.1.
DR AlphaFoldDB; Q5RBG1; -.
DR SMR; Q5RBG1; -.
DR STRING; 9601.ENSPPYP00000005284; -.
DR Ensembl; ENSPPYT00000005492; ENSPPYP00000005284; ENSPPYG00000004639.
DR GeneID; 100172422; -.
DR KEGG; pon:100172422; -.
DR CTD; 5869; -.
DR eggNOG; KOG0092; Eukaryota.
DR GeneTree; ENSGT00940000160756; -.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; Q5RBG1; -.
DR OrthoDB; 1340129at2759; -.
DR Proteomes; UP000001595; Chromosome 12.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
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 Acetylation; Cell membrane; Endosome; GTP-binding; Hydrolase; Lipoprotein;
KW Membrane; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P61020"
FT CHAIN 2..215
FT /note="Ras-related protein Rab-5B"
FT /id="PRO_0000260743"
FT REGION 186..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 49..57
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT COMPBIAS 200..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:P61020"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61020"
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; 23707 MW; D47AD834BCF8B591 CRC64;
MTSRSTARPN GQPQASKICQ FKLVLLGESA VGKSSLVLRF VKGQFHEYQE STIGAAFLTQ
SVCLDDTTVK FEIWDTAGQE RYHSLAPMYY RGAQAAIVVY DITNQETFAR AKTWVKELQR
QASPSIVIAL AGNKADLANK RMVEYEEAQA YADDNSLLFM ETSAKTAMNV NDLFLAIAKK
LPKSEPQNLG GAAGRSRGVD LHEQSQQNKS QCCSN
