RAB1B_MOUSE
ID RAB1B_MOUSE Reviewed; 201 AA.
AC Q9D1G1; Q3U0N1;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Ras-related protein Rab-1B;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P62820};
GN Name=Rab1b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 11-21; 59-69; 72-100; 109-122; 138-153 AND 173-187, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP INTERACTION WITH MTMR6 AND MTMR7, AND MUTAGENESIS OF SER-22 AND GLN-67.
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. Required to modulate the
CC compacted morphology of the Golgi. Promotes the recruitment of lipid
CC phosphatase MTMR6 to the endoplasmic reticulum-Golgi intermediate
CC compartment (By similarity). {ECO:0000250|UniProtKB:P10536,
CC ECO:0000250|UniProtKB:Q9H0U4}.
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 (GTP-bound form)
CC with MICALCL, MICAL1 and MILCAL3. Interacts with GDI1; the interaction
CC requires the GDP-bound state. Interacts with CHM/REP1; the interaction
CC requires the GDP-bound form and is necessary for prenylation by GGTase
CC II. Interacts with RabGAP TBC1D20 (By similarity). Interacts (in GDP-
CC bound form) with lipid phosphatase MTMR6 (via GRAM domain); the
CC interaction regulates MTMR6 recruitment to the endoplasmic reticulum-
CC Golgi intermediate compartment (PubMed:23188820). Interacts (in GDP-
CC bound form) with lipid phosphatase MTMR7 (PubMed:23188820).
CC {ECO:0000250|UniProtKB:Q9H0U4, ECO:0000269|PubMed:23188820}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H0U4}.
CC Membrane {ECO:0000250|UniProtKB:Q9H0U4}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9H0U4}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9H0U4}. Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:Q9H0U4}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9H0U4}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9H0U4}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P10536}. 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 (By
CC similarity). {ECO:0000250|UniProtKB:P10536,
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}.
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DR EMBL; AK003609; BAB22888.1; -; mRNA.
DR EMBL; AK156726; BAE33821.1; -; mRNA.
DR EMBL; BC016408; AAH16408.1; -; mRNA.
DR CCDS; CCDS29452.1; -.
DR RefSeq; NP_083852.1; NM_029576.3.
DR AlphaFoldDB; Q9D1G1; -.
DR SMR; Q9D1G1; -.
DR BioGRID; 218071; 7.
DR IntAct; Q9D1G1; 16.
DR MINT; Q9D1G1; -.
DR STRING; 10090.ENSMUSP00000025804; -.
DR iPTMnet; Q9D1G1; -.
DR PhosphoSitePlus; Q9D1G1; -.
DR SwissPalm; Q9D1G1; -.
DR EPD; Q9D1G1; -.
DR jPOST; Q9D1G1; -.
DR MaxQB; Q9D1G1; -.
DR PaxDb; Q9D1G1; -.
DR PRIDE; Q9D1G1; -.
DR ProteomicsDB; 253142; -.
DR Antibodypedia; 4132; 314 antibodies from 32 providers.
DR DNASU; 76308; -.
DR Ensembl; ENSMUST00000025804; ENSMUSP00000025804; ENSMUSG00000024870.
DR GeneID; 76308; -.
DR KEGG; mmu:76308; -.
DR UCSC; uc008gcf.1; mouse.
DR CTD; 81876; -.
DR MGI; MGI:1923558; Rab1b.
DR VEuPathDB; HostDB:ENSMUSG00000024870; -.
DR eggNOG; KOG0084; Eukaryota.
DR GeneTree; ENSGT00940000155078; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; Q9D1G1; -.
DR OMA; QRYACDS; -.
DR OrthoDB; 1149105at2759; -.
DR PhylomeDB; Q9D1G1; -.
DR TreeFam; TF300097; -.
DR Reactome; R-MMU-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 76308; 6 hits in 71 CRISPR screens.
DR ChiTaRS; Rab1b; mouse.
DR PRO; PR:Q9D1G1; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9D1G1; protein.
DR Bgee; ENSMUSG00000024870; Expressed in lip and 246 other tissues.
DR ExpressionAtlas; Q9D1G1; baseline and differential.
DR Genevisible; Q9D1G1; MM.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0034045; C:phagophore assembly site membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
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:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; 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 1: Evidence at protein level;
KW Acetylation; Autophagy; Cytoplasm; Direct protein sequencing; GTP-binding;
KW Hydrolase; Lipoprotein; Membrane; 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_0000121062"
FT REGION 64..83
FT /note="Switch 2 region; required for interaction with
FT REP1/CHM"
FT /evidence="ECO:0000250|UniProtKB:Q9H0U4"
FT REGION 174..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:0000250"
FT LIPID 201
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 22
FT /note="S->N: Increases the interaction with MTMR6."
FT /evidence="ECO:0000269|PubMed:23188820"
FT MUTAGEN 67
FT /note="Q->L: No effect on the interaction with MTMR6."
FT /evidence="ECO:0000269|PubMed:23188820"
SQ SEQUENCE 201 AA; 22187 MW; 870DFF52AEF4B2BE CRC64;
MNPEYDYLFK LLLIGDSGVG KSCLLLRFAD DTYTESYIST IGVDFKIRTI ELDGKTIKLQ
IWDTAGQERF RTITSSYYRG AHGIIVVYDV TDQESYANVK QWLQEIDRYA SENVNKLLVG
NKSDLTTKKV VDNTTAKEFA DSLGVPFLET SAKNATNVEQ AFMTMAAEIK KRMGPGAASG
GERPNLKIDS TPVKPASGGC C
