ID RAB6B_BOVIN Reviewed; 208 AA. AC A6QR46; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 27-MAR-2024, entry version 104. DE RecName: Full=Ras-related protein Rab-6B; DE EC=3.6.5.2 {ECO:0000250|UniProtKB:Q9NRW1}; GN Name=RAB6B; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Hippocampus; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The small GTPases Rab are key regulators of intracellular CC membrane trafficking, from the formation of transport vesicles to their CC fusion with membranes. Rabs cycle between active GTP-bound and inactive CC GDP-bound states. In their active state, drive transport of vesicular CC carriers from donor organelles to acceptor organelles to regulate the CC membrane traffic that maintains organelle identity and morphology. CC Recruits VPS13B to the Golgi membrane. Regulates the compacted CC morphology of the Golgi. Seems to have a role in retrograde membrane CC traffic at the level of the Golgi complex. May function in retrograde CC transport in neuronal cells. Plays a role in neuron projection CC development. {ECO:0000250|UniProtKB:Q9NRW1}. 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:Q9NRW1}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000250|UniProtKB:Q9NRW1}; CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors CC (GEFs) which promote the exchange of bound GDP for free GTP, GTPase CC activating proteins (GAPs) which increase the GTP hydrolysis activity, CC and GDP dissociation inhibitors which inhibit the dissociation of the CC nucleotide from the GTPase. {ECO:0000250|UniProtKB:Q9NRW1}. CC -!- SUBUNIT: Interacts (GTP-bound) with BICD1 (via C-terminus); the CC interaction is direct. Interacts (GDP-bound) with DYNLRB1. Interacts CC (GTP-bound) with APBA1/MINT1. Interacts (GTP-bound) with VPS13B. CC {ECO:0000250|UniProtKB:Q9NRW1}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000250|UniProtKB:Q9NRW1}; Lipid-anchor {ECO:0000305}. Endoplasmic CC reticulum-Golgi intermediate compartment CC {ECO:0000250|UniProtKB:Q9NRW1}. Cytoplasmic vesicle CC {ECO:0000250|UniProtKB:Q9NRW1}. Note=Colocalizes with BICD1 at CC vesicular structures that align along microtubules. CC {ECO:0000250|UniProtKB:Q9NRW1}. 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; BC150111; AAI50112.1; -; mRNA. DR RefSeq; NP_001094599.1; NM_001101129.1. DR AlphaFoldDB; A6QR46; -. DR SMR; A6QR46; -. DR STRING; 9913.ENSBTAP00000001199; -. DR PaxDb; 9913-ENSBTAP00000001199; -. DR GeneID; 526526; -. DR KEGG; bta:526526; -. DR CTD; 51560; -. DR eggNOG; KOG0094; Eukaryota. DR HOGENOM; CLU_041217_10_2_1; -. DR InParanoid; A6QR46; -. DR OrthoDB; 5483572at2759; -. DR TreeFam; TF300803; -. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW. DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell. DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB. DR GO; GO:1903292; P:protein localization to Golgi membrane; ISS:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central. DR CDD; cd01861; Rab6; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR001806; Small_GTPase. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR47977; RAS-RELATED PROTEIN RAB; 1. DR PANTHER; PTHR47977:SF66; RAS-RELATED PROTEIN RAB-6B ISOFORM X1; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR SMART; SM00176; RAN; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51419; RAB; 1. PE 2: Evidence at transcript level; KW Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus; GTP-binding; KW Hydrolase; Lipoprotein; Membrane; Methylation; Nucleotide-binding; KW Prenylation; Protein transport; Reference proteome; Transport. FT CHAIN 1..208 FT /note="Ras-related protein Rab-6B" FT /id="PRO_0000371507" FT MOTIF 42..50 FT /note="Effector region" FT /evidence="ECO:0000250" FT BINDING 20..27 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 45 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 68..72 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 126..129 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT MOD_RES 208 FT /note="Cysteine methyl ester" FT /evidence="ECO:0000250" FT LIPID 206 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250" FT LIPID 208 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250" SQ SEQUENCE 208 AA; 23462 MW; E81C831996E2446D CRC64; MSAGGDFGNP LRKFKLVFLG EQSVGKTSLI TRFMYDSFDN TYQATIGIDF LSKTMYLEDR TVRLQLWDTA GQERFRSLIP SYIRDSTVAV VVYDITNLNS FQQTSKWIDD VRTERGSDVI IMLVGNKTDL ADKRQITIEE GEQRAKELSV MFIETSAKTG YNVKQLFRRV ASALPGMENV QEKSKEGMID IKLDKPQEPP ASEGGCSC //