RAB1A_MOUSE
ID RAB1A_MOUSE Reviewed; 205 AA.
AC P62821; P11476; Q3TX44; Q811M4; Q96N61; Q9Y3T2;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Ras-related protein Rab-1A;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P62820};
DE AltName: Full=YPT1-related protein;
GN Name=Rab1A; Synonyms=Rab1;
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 [MRNA].
RX PubMed=3127202; DOI=10.1002/j.1460-2075.1987.tb02750.x;
RA Haubruck H., Disela C., Wagner P., Gallwitz D.;
RT "The ras-related ypt protein is an ubiquitous eukaryotic protein: isolation
RT and sequence analysis of mouse cDNA clones highly homologous to the yeast
RT YPT1 gene.";
RL EMBO J. 6:4049-4053(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2506528; DOI=10.1093/nar/17.16.6737;
RA Wichmann H., Disela C., Haubruck H., Gallwitz D.;
RT "Nucleotide sequence of the mouse ypt1 gene encoding a ras-related GTP-
RT binding protein.";
RL Nucleic Acids Res. 17:6737-6738(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wu G., Dorn G.W. II;
RT "Mouse Rab1A, member of RAS oncogene family mRNA.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, and Mammary gland;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [6]
RP PROTEIN SEQUENCE OF 14-24; 31-49; 62-72; 75-103; 112-125 AND 132-156, 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 [7]
RP REVIEW.
RX PubMed=19603039; DOI=10.1038/nrm2728;
RA Stenmark H.;
RT "Rab GTPases as coordinators of vesicle traffic.";
RL Nat. Rev. Mol. Cell Biol. 10:513-525(2009).
RN [8]
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 [9]
RP FUNCTION.
RX PubMed=20639577; DOI=10.1074/jbc.m110.141440;
RA Wang C., Yoo Y., Fan H., Kim E., Guan K.L., Guan J.L.;
RT "Regulation of integrin beta 1 recycling to lipid rafts by Rab1a to promote
RT cell migration.";
RL J. Biol. Chem. 285:29398-29405(2010).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22854043; DOI=10.1242/jcs.109314;
RA Ishida M., Ohbayashi N., Maruta Y., Ebata Y., Fukuda M.;
RT "Functional involvement of Rab1A in microtubule-dependent anterograde
RT melanosome transport in melanocytes.";
RL J. Cell Sci. 125:5177-5187(2012).
RN [11]
RP INTERACTION WITH C9ORF72.
RX PubMed=24549040; DOI=10.1093/hmg/ddu068;
RA Farg M.A., Sundaramoorthy V., Sultana J.M., Yang S., Atkinson R.A.,
RA Levina V., Halloran M.A., Gleeson P.A., Blair I.P., Soo K.Y., King A.E.,
RA Atkin J.D.;
RT "C9ORF72, implicated in amytrophic lateral sclerosis and frontotemporal
RT dementia, regulates endosomal trafficking.";
RL Hum. Mol. Genet. 23:3579-3595(2014).
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 (PubMed:20639577, PubMed:22854043). Rabs cycle
CC between an inactive GDP-bound form and an active GTP-bound form that is
CC able to recruit to membranes different sets of downstream effectors
CC directly responsible for vesicle formation, movement, tethering and
CC fusion (PubMed:20639577, PubMed:22854043). RAB1A regulates vesicular
CC protein transport from the endoplasmic reticulum (ER) to the Golgi
CC compartment and on to the cell surface, and plays a role in IL-8 and
CC growth hormone secretion (By similarity). Required to modulate the
CC compacted morphology of the Golgi. Regulates the level of CASR present
CC at the cell membrane (By similarity). Plays a role in cell adhesion and
CC cell migration, via its role in protein trafficking (PubMed:20639577).
CC Plays a role in autophagosome assembly and cellular defense reactions
CC against pathogenic bacteria (By similarity). Plays a role in
CC microtubule-dependent protein transport by early endosomes and in
CC anterograde melanosome transport (PubMed:22854043).
CC {ECO:0000250|UniProtKB:P62820, ECO:0000269|PubMed:20639577,
CC ECO:0000269|PubMed:22854043}.
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 -!- SUBUNIT: May interact with YIPF5 (By similarity). Interacts with
CC C9orf72; the interaction mediates recruitment of RAB1A to the ATG1/ULK1
CC kinase complex (PubMed:24549040). Interacts with GDI1; this promotes
CC dissociation from membranes (By similarity).
CC {ECO:0000250|UniProtKB:P62820, ECO:0000250|UniProtKB:P62822,
CC ECO:0000269|PubMed:24549040}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:P62820}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:P62820}. Early endosome
CC {ECO:0000250|UniProtKB:P62820}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P62820}. Membrane
CC {ECO:0000250|UniProtKB:P62820}. Melanosome
CC {ECO:0000269|PubMed:22854043}. Note=Alternates between membrane-
CC associated and cytosolic forms. {ECO:0000250|UniProtKB:P62820}.
CC -!- PTM: Phosphorylated by CDK1 kinase during mitosis.
CC {ECO:0000250|UniProtKB:P62820}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; Y00094; CAA68284.1; -; mRNA.
DR EMBL; X15744; CAA33760.1; -; Genomic_DNA.
DR EMBL; X15745; CAA33760.1; JOINED; Genomic_DNA.
DR EMBL; X15746; CAA33760.1; JOINED; Genomic_DNA.
DR EMBL; X15747; CAA33760.1; JOINED; Genomic_DNA.
DR EMBL; AF226873; AAF33844.1; -; mRNA.
DR EMBL; AK034408; BAC28697.1; -; mRNA.
DR EMBL; AK159425; BAE35072.1; -; mRNA.
DR EMBL; AK166249; BAE38660.1; -; mRNA.
DR EMBL; AK167150; BAE39292.1; -; mRNA.
DR EMBL; BC002077; AAH02077.3; -; mRNA.
DR CCDS; CCDS36115.1; -.
DR PIR; S05551; TVMSYP.
DR RefSeq; NP_033022.1; NM_008996.3.
DR AlphaFoldDB; P62821; -.
DR SMR; P62821; -.
DR BioGRID; 202530; 23.
DR IntAct; P62821; 38.
DR STRING; 10090.ENSMUSP00000127330; -.
DR iPTMnet; P62821; -.
DR PhosphoSitePlus; P62821; -.
DR SwissPalm; P62821; -.
DR EPD; P62821; -.
DR jPOST; P62821; -.
DR PaxDb; P62821; -.
DR PeptideAtlas; P62821; -.
DR PRIDE; P62821; -.
DR ProteomicsDB; 300373; -.
DR Antibodypedia; 3942; 188 antibodies from 31 providers.
DR DNASU; 19324; -.
DR Ensembl; ENSMUST00000163483; ENSMUSP00000127330; ENSMUSG00000020149.
DR GeneID; 19324; -.
DR KEGG; mmu:19324; -.
DR UCSC; uc007icv.1; mouse.
DR CTD; 5861; -.
DR MGI; MGI:97842; Rab1.
DR VEuPathDB; HostDB:ENSMUSG00000020149; -.
DR eggNOG; KOG0084; Eukaryota.
DR GeneTree; ENSGT00940000154958; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; P62821; -.
DR OMA; KERMGNT; -.
DR OrthoDB; 1149105at2759; -.
DR PhylomeDB; P62821; -.
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; 19324; 6 hits in 39 CRISPR screens.
DR ChiTaRS; Rab1a; mouse.
DR PRO; PR:P62821; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P62821; protein.
DR Bgee; ENSMUSG00000020149; Expressed in vault of skull and 256 other tissues.
DR ExpressionAtlas; P62821; baseline and differential.
DR Genevisible; P62821; MM.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0001675; P:acrosome assembly; ISS:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; ISO:MGI.
DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0030252; P:growth hormone secretion; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0032402; P:melanosome transport; IMP:UniProtKB.
DR GO; GO:1903020; P:positive regulation of glycoprotein metabolic process; ISO:MGI.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR GO; GO:0047496; P:vesicle transport along microtubule; ISS:UniProtKB.
DR GO; GO:0019068; P:virion assembly; ISO:MGI.
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;
KW Endoplasmic reticulum; Endosome; ER-Golgi transport; Golgi apparatus;
KW GTP-binding; Hydrolase; Lipoprotein; Membrane; Nucleotide-binding;
KW Phosphoprotein; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT CHAIN 2..205
FT /note="Ras-related protein Rab-1A"
FT /id="PRO_0000121057"
FT REGION 178..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 40..48
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT COMPBIAS 187..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 18..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 36..43
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 66..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 154..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT MOD_RES 194
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT LIPID 204
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT LIPID 205
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62820"
SQ SEQUENCE 205 AA; 22678 MW; B2A8F4E3B0FB17D6 CRC64;
MSSMNPEYDY LFKLLLIGDS GVGKSCLLLR FADDTYTESY ISTIGVDFKI RTIELDGKTI
KLQIWDTAGQ ERFRTITSSY YRGAHGIIVV YDVTDQESFN NVKQWLQEID RYASENVNKL
LVGNKCDLTT KKVVDYTTAK EFADSLGIPF LETSAKNATN VEQSFMTMAA EIKKRMGPGA
TAGGAEKSNV KIQSTPVKQS GGGCC
