ID RAB1B_RAT Reviewed; 201 AA. AC P10536; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 02-SEP-2026, entry version 177. DE RecName: Full=Ras-related protein Rab-1B; DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P62820}; GN Name=Rab1b; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2493636; DOI=10.1093/nar/17.4.1770; RA Zahraoui A., Touchot N., Chardin P., Tavitian A.; RT "Nucleotide sequence of a rat cDNA: rab1B, encoding a rab1-YPT related RT protein."; RL Nucleic Acids Res. 17:1770-1770(1989). RN [2] RP CHARACTERIZATION, AND MUTAGENESIS OF LYS-21 AND ALA-65. RX PubMed=2509243; DOI=10.1016/0014-5793(89)81722-3; RA Touchot N., Zahraoui A., Vielh E., Tavitian A.; RT "Biochemical properties of the YPT-related rab1B protein. Comparison with RT rab1A."; RL FEBS Lett. 256:79-84(1989). RN [3] RP SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=1918138; DOI=10.1083/jcb.115.1.31; RA Plutner H., Cox A.D., Pind S., Khosravi-Far R., Bourne J.R., RA Schwaninger R., Der C.J., Balch W.E.; RT "Rab1b regulates vesicular transport between the endoplasmic reticulum and RT successive Golgi compartments."; RL J. Cell Biol. 115:31-43(1991). RN [4] RP ISOPRENYLATION AT CYS-200 AND CYS-201. RX PubMed=1648736; DOI=10.1073/pnas.88.14.6264; RA Khosravi-Far R., Lutz R.J., Cox A.D., Conroy L., Bourne J.R., Sinensky M., RA Balch W.E., Buss J.E., Der C.J.; RT "Isoprenoid modification of rab proteins terminating in CC or CXC motifs."; RL Proc. Natl. Acad. Sci. U.S.A. 88:6264-6268(1991). RN [5] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=23188820; DOI=10.1074/jbc.m112.395087; RA Mochizuki Y., Ohashi R., Kawamura T., Iwanari H., Kodama T., Naito M., RA Hamakubo T.; RT "Phosphatidylinositol 3-phosphatase myotubularin-related protein 6 (MTMR6) RT is regulated by small GTPase Rab1B in the early secretory and autophagic RT pathways."; RL J. Biol. Chem. 288:1009-1021(2013). 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 an inactive GDP-bound form CC and an active GTP-bound form that is able to recruit to membranes CC different set of downstream effectors directly responsible for vesicle CC formation, movement, tethering and fusion (By similarity). Plays a role CC in the initial events of the autophagic vacuole development which take CC place at specialized regions of the endoplasmic reticulum (By CC similarity). Regulates vesicular transport between the endoplasmic CC reticulum and successive Golgi compartments (PubMed:1918138). Required CC to modulate the compacted morphology of the Golgi. Promotes the CC recruitment of lipid phosphatase MTMR6 to the endoplasmic reticulum- CC Golgi intermediate compartment (PubMed:23188820). CC {ECO:0000250|UniProtKB:Q9H0U4, ECO:0000269|PubMed:1918138, CC ECO:0000269|PubMed:23188820}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + phosphate + H(+); 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:P62820}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000250|UniProtKB:P62820}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:Q9H0U4}; CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors CC (GEFs) which promote the exchange of bound GDP for free GTP. Regulated CC by GTPase activating proteins (GAPs) including TBC1D20 which increases CC the GTP hydrolysis activity. Inhibited by GDP dissociation inhibitors CC (GDIs). {ECO:0000250|UniProtKB:Q9H0U4}. CC -!- SUBUNIT: Interacts with MICAL1 and MICAL2. Interacts (in GTP-bound CC form) with MICALCL, MICAL1 and MILCAL3. Interacts with GDI1; the CC interaction requires the GDP-bound state. Interacts with CHM/REP1; the CC interaction requires the GDP-bound form and is necessary for CC prenylation by GGTase II. Interacts with RabGAP TBC1D20. Interacts (in CC GDP-bound form) with lipid phosphatase MTMR6 (via GRAM domain); the CC interaction regulates MTMR6 recruitment to the endoplasmic reticulum- CC Golgi intermediate compartment (By similarity). Interacts (in GDP-bound CC form) with lipid phosphatase MTMR7 (By similarity). CC {ECO:0000250|UniProtKB:Q9D1G1, ECO:0000250|UniProtKB:Q9H0U4}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1918138, CC ECO:0000269|PubMed:23188820}. Membrane {ECO:0000269|PubMed:1918138}; CC Lipid-anchor {ECO:0000269|PubMed:1918138}; Cytoplasmic side CC {ECO:0000269|PubMed:1918138}. Preautophagosomal structure membrane CC {ECO:0000250|UniProtKB:Q9H0U4}; Lipid-anchor {ECO:0000305}; Cytoplasmic CC side {ECO:0000305}. Cytoplasm, perinuclear region CC {ECO:0000269|PubMed:23188820}. Note=Targeted by REP1 to membranes of CC specific subcellular compartments including endoplasmic reticulum, CC Golgi apparatus, and intermediate vesicles between these two CC compartments. In the GDP-form, colocalizes with GDI in the cytoplasm CC (By similarity). Co-localizes with MTMR6 to the endoplasmic reticulum- CC Golgi intermediate compartment and to the peri-Golgi region CC (PubMed:23188820). {ECO:0000250|UniProtKB:Q9H0U4, CC ECO:0000269|PubMed:23188820}. CC -!- DOMAIN: Switch I, switch II and the interswitch regions are CC characteristic of Rab GTPases and mediate the interactions with Rab CC downstream effectors. The switch regions undergo conformational changes CC upon nucleotide binding which drives interaction with specific sets of CC effector proteins, with most effectors only binding to GTP-bound Rab. CC {ECO:0000250|UniProtKB:Q9H0U4}. CC -!- PTM: Prenylated; by GGTase II, only after interaction of the substrate CC with Rab escort protein 1 (REP1). {ECO:0000250|UniProtKB:Q9H0U4}. CC -!- MISCELLANEOUS: Rab-1B binds GTP and GDP and possesses intrinsic GTPase CC activity. {ECO:0000250|UniProtKB:Q9H0U4}. 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; X13905; CAA32105.1; -; mRNA. DR PIR; S06147; S06147. DR AlphaFoldDB; P10536; -. DR SMR; P10536; -. DR FunCoup; P10536; 2476. DR IntAct; P10536; 2. DR MINT; P10536; -. DR STRING; 10116.ENSRNOP00000067788; -. DR GlyGen; P10536; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P10536; -. DR PhosphoSitePlus; P10536; -. DR SwissPalm; P10536; -. DR jPOST; P10536; -. DR PaxDb; 10116-ENSRNOP00000067788; -. DR AGR; RGD:1642882; -. DR AGR; RGD:619736; -. DR RGD; 1642882; Rab1b. DR eggNOG; KOG0084; Eukaryota. DR InParanoid; P10536; -. DR PhylomeDB; P10536; -. DR Reactome; R-RNO-162658; Golgi Cisternae Pericentriolar Stack Reorganization. DR Reactome; R-RNO-204005; COPII-mediated vesicle transport. DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport. DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic. DR Reactome; R-RNO-8873719; RAB geranylgeranylation. DR Reactome; R-RNO-8876198; RAB GEFs exchange GTP for GDP on RABs. DR PRO; PR:P10536; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0005737; C:cytoplasm; EXP:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD. DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:RGD. DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD. DR GO; GO:0016020; C:membrane; EXP:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0034045; C:phagophore assembly site membrane; ISS:UniProtKB. DR GO; GO:0045202; C:synapse; IDA:SynGO. DR GO; GO:0003925; F:G protein activity; ISS:UniProtKB. DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB. DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB. DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:RGD. DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB. DR GO; GO:1903020; P:positive regulation of glycoprotein metabolic process; ISO:RGD. DR GO; GO:0032482; P:Rab protein signal transduction; IEA:UniProtKB-ARBA. DR GO; GO:2000785; P:regulation of autophagosome assembly; ISO:RGD. DR CDD; cd01869; Rab1_Ypt1; 1. DR FunFam; 3.40.50.300:FF:000069; Ras GTP-binding protein YPT1; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR050227; Rab. DR InterPro; IPR057289; Rab1/Ypt1. DR InterPro; IPR005225; Small_GTP-bd. DR InterPro; IPR001806; Small_GTPase. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR47977; RAS-RELATED PROTEIN RAB; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00177; ARF; 1. 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 1: Evidence at protein level; KW Acetylation; Autophagy; Cytoplasm; GTP-binding; Hydrolase; Lipoprotein; KW Magnesium; Membrane; Metal-binding; Methylation; Nucleotide-binding; KW Phosphoprotein; Prenylation; Protein transport; Reference proteome; KW Transport. FT CHAIN 1..201 FT /note="Ras-related protein Rab-1B" FT /id="PRO_0000121063" FT REGION 35..43 FT /note="Switch-I" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00753" FT REGION 66..82 FT /note="Switch-II; required for interaction with REP1/CHM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00753" FT REGION 173..201 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 17 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9H0U4" FT BINDING 18 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9H0U4" FT BINDING 19 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9H0U4" FT BINDING 20 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9H0U4" FT BINDING 21 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9H0U4" FT BINDING 22 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9H0U4" FT BINDING 22 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q9H0U4" FT BINDING 23 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9H0U4" FT BINDING 33 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9H0U4" FT BINDING 34 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9H0U4" FT BINDING 35 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9H0U4" FT BINDING 36 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9H0U4" FT BINDING 39 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9H0U4" FT BINDING 40 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9H0U4" FT BINDING 40 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q9H0U4" FT BINDING 63 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q9H0U4" FT BINDING 66 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9H0U4" FT BINDING 121 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9H0U4" FT BINDING 122 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9H0U4" FT BINDING 124 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9H0U4" FT BINDING 151 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9H0U4" FT BINDING 152 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9H0U4" FT BINDING 153 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9H0U4" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:Q9H0U4" FT MOD_RES 201 FT /note="Cysteine methyl ester" FT /evidence="ECO:0000255" FT LIPID 200 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000269|PubMed:1648736" FT LIPID 201 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000269|PubMed:1648736" FT MUTAGEN 21 FT /note="K->M: Abolishes GTP-binding." FT /evidence="ECO:0000269|PubMed:2509243" FT MUTAGEN 65 FT /note="A->T: Reduced GTPase activity." FT /evidence="ECO:0000269|PubMed:2509243" SQ SEQUENCE 201 AA; 22163 MW; 8D3EEDC2AEF4A2FE CRC64; MNPEYDYLFK LLLIGDSGVG KSCLLLRFAD DTYTESYIST IGVDFKIRTI ELDGKTIKLQ IWDTAGQERF RTVTSSYYRG AHGIIVVYDV TDQESYANVK QWLQEIDRYA SENVNKLLVG NKSDLTTKKV VDNTTAKEFA DSLGVPFLET SAKNATNVEQ AFMTMAAEIK KRMGPGAASG GERPNLKIDS TPVKSASGGC C //