RAB1B_RAT
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 03-AUG-2022, entry version 163.
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 + 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:P62820};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P62820};
CC -!- ACTIVITY REGULATION: Rab activation is generally mediated by a guanine
CC exchange factor (GEF), while inactivation through hydrolysis of bound
CC GTP is catalyzed by a GTPase activating protein (GAP). {ECO:0000305}.
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 -!- 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 IntAct; P10536; 2.
DR MINT; P10536; -.
DR STRING; 10116.ENSRNOP00000067788; -.
DR iPTMnet; P10536; -.
DR PhosphoSitePlus; P10536; -.
DR SwissPalm; P10536; -.
DR jPOST; P10536; -.
DR PaxDb; P10536; -.
DR PRIDE; P10536; -.
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:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0034045; C:phagophore assembly site membrane; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
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:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:1903020; P:positive regulation of glycoprotein metabolic process; ISO:RGD.
DR GO; GO:2000785; P:regulation of autophagosome assembly; ISO:RGD.
DR GO; GO:0019068; P:virion assembly; ISO:RGD.
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 Acetylation; Autophagy; Cytoplasm; GTP-binding; Hydrolase; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..201
FT /note="Ras-related protein Rab-1B"
FT /id="PRO_0000121063"
FT REGION 64..83
FT /note="Switch 2 region; required for interaction with
FT REP1/CHM"
FT /evidence="ECO:0000250|UniProtKB:Q9H0U4"
FT REGION 173..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 15..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 33..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9H0U4"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9H0U4"
FT BINDING 151..153
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
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
