RAB6A_MOUSE
ID RAB6A_MOUSE Reviewed; 208 AA.
AC P35279; Q542M6; Q8R2Z7; Q8VEE5; Q9JJD4;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Ras-related protein Rab-6A;
DE Short=Rab-6;
GN Name=Rab6a; Synonyms=Rab6; ORFNames=MNCb-1660;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Hippocampus, and Spinal ganglion;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-73 (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=1555775; DOI=10.1016/0378-1119(92)90387-5;
RA Chavrier P., Simons K., Zerial M.;
RT "The complexity of the Rab and Rho GTP-binding protein subfamilies revealed
RT by a PCR cloning approach.";
RL Gene 112:261-264(1992).
RN [5]
RP PROTEIN SEQUENCE OF 64-74 AND 144-158, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP MUTAGENESIS.
RX PubMed=9438855; DOI=10.1126/science.279.5350.580;
RA Echard A., Jollivet F., Martinez O., Lacapere J.-J., Rousselet A.,
RA Janoueix-Lerosey I., Goud B.;
RT "Interaction of a Golgi-associated kinesin-like protein with Rab6.";
RL Science 279:580-585(1998).
RN [7]
RP INTERACTION WITH SCYL1BP1.
RX PubMed=18997784; DOI=10.1038/ng.252;
RA Hennies H.C., Kornak U., Zhang H., Egerer J., Zhang X., Seifert W.,
RA Kuhnisch J., Budde B., Naetebus M., Brancati F., Wilcox W.R., Mueller D.,
RA Kaplan P.B., Rajab A., Zampino G., Fodale V., Dallapiccola B., Newman W.,
RA Metcalfe K., Clayton-Smith J., Tassabehji M., Steinmann B., Barr F.A.,
RA Nuernberg P., Wieacker P., Mundlos S.;
RT "Gerodermia osteodysplastica is caused by mutations in SCYL1BP1, a Rab-6
RT interacting golgin.";
RL Nat. Genet. 40:1410-1412(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION BY
RP 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 INTERACTION WITH PIFO.
RX PubMed=20643351; DOI=10.1016/j.devcel.2010.06.005;
RA Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B.,
RA Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.;
RT "Pitchfork regulates primary cilia disassembly and left-right asymmetry.";
RL Dev. Cell 19:66-77(2010).
RN [10]
RP INTERACTION WITH BICDL1.
RX PubMed=20360680; DOI=10.1038/emboj.2010.51;
RA Schlager M.A., Kapitein L.C., Grigoriev I., Burzynski G.M., Wulf P.S.,
RA Keijzer N., de Graaff E., Fukuda M., Shepherd I.T., Akhmanova A.,
RA Hoogenraad C.C.;
RT "Pericentrosomal targeting of Rab6 secretory vesicles by Bicaudal-D-related
RT protein 1 (BICDR-1) regulates neuritogenesis.";
RL EMBO J. 29:1637-1651(2010).
RN [11]
RP INTERACTION WITH APBA1.
RX PubMed=23737971; DOI=10.1371/journal.pone.0064149;
RA Thyrock A., Ossendorf E., Stehling M., Kail M., Kurtz T., Pohlentz G.,
RA Waschbusch D., Eggert S., Formstecher E., Muthing J., Dreisewerd K.,
RA Kins S., Goud B., Barnekow A.;
RT "A new Mint1 isoform, but not the conventional Mint1, interacts with the
RT small GTPase Rab6.";
RL PLoS ONE 8:E64149-E64149(2013).
CC -!- FUNCTION: Protein transport. Regulator of membrane traffic from the
CC Golgi apparatus towards the endoplasmic reticulum (ER). Involved in
CC COPI-independent retrograde transport from the Golgi to the ER (By
CC similarity). {ECO:0000250|UniProtKB:P20340}.
CC -!- SUBUNIT: Interacts with RIC1 and RGP1; the interactions are direct with
CC a preference for RAB6A-GDP. Interacts with VSP52 and RABGAP1. Interacts
CC with GCC2 (via its GRIP domain). Interacts with RAB6IP1 (via its RUN 1
CC domain). Interacts with RAB6KIFL. Interacts with BICD1. Interacts with
CC BICD2. Interacts with TMF1. Interacts (GTP-bound) with DYNLRB1; the
CC interaction is direct (By similarity). Interacts with SCYL1BP1.
CC Interacts with BICDL1; leads to its accumulation in the pericentrosomal
CC region. Interacts with PIFO. Interacts (GTP-bound) with APBA1/MINT1
CC isoform 3, also called Mint1_826. {ECO:0000250|UniProtKB:P20340,
CC ECO:0000269|PubMed:18997784, ECO:0000269|PubMed:20360680,
CC ECO:0000269|PubMed:20643351, ECO:0000269|PubMed:23737971}.
CC -!- INTERACTION:
CC P35279; Q921C5: Bicd2; NbExp=3; IntAct=EBI-444674, EBI-642984;
CC P35279; A0JNT9: Bicdl1; NbExp=6; IntAct=EBI-444674, EBI-7893170;
CC P35279; Q8TDW5: SYTL5; Xeno; NbExp=2; IntAct=EBI-444674, EBI-2939487;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P20340}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P20340}. Note=BICD2 facilitates its targeting to
CC Golgi apparatus membrane. {ECO:0000250|UniProtKB:P20340}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Rab-6a;
CC IsoId=P35279-1; Sequence=Displayed;
CC Name=2; Synonyms=Rab-6a', Rab6C;
CC IsoId=P35279-2; Sequence=VSP_005528;
CC -!- PTM: Prenylated. {ECO:0000250|UniProtKB:P20340}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AB041575; BAA95059.1; -; mRNA.
DR EMBL; AK051246; BAC34572.1; -; mRNA.
DR EMBL; AK083262; BAC38834.1; -; mRNA.
DR EMBL; AK084131; BAC39121.1; -; mRNA.
DR EMBL; AK160134; BAE35649.1; -; mRNA.
DR EMBL; AK160866; BAE36058.1; -; mRNA.
DR EMBL; AK169842; BAE41406.1; -; mRNA.
DR EMBL; BC019118; AAH19118.1; -; mRNA.
DR EMBL; BC026915; AAH26915.1; -; mRNA.
DR EMBL; M79313; AAK14837.1; -; mRNA.
DR CCDS; CCDS21503.1; -. [P35279-1]
DR CCDS; CCDS52323.1; -. [P35279-2]
DR PIR; A38883; A38883.
DR RefSeq; NP_001157135.1; NM_001163663.1. [P35279-2]
DR RefSeq; NP_077249.1; NM_024287.4. [P35279-1]
DR AlphaFoldDB; P35279; -.
DR SMR; P35279; -.
DR BioGRID; 202550; 14.
DR DIP; DIP-120N; -.
DR IntAct; P35279; 26.
DR MINT; P35279; -.
DR STRING; 10090.ENSMUSP00000032946; -.
DR iPTMnet; P35279; -.
DR PhosphoSitePlus; P35279; -.
DR SwissPalm; P35279; -.
DR EPD; P35279; -.
DR jPOST; P35279; -.
DR PaxDb; P35279; -.
DR PeptideAtlas; P35279; -.
DR PRIDE; P35279; -.
DR ProteomicsDB; 253150; -. [P35279-1]
DR ProteomicsDB; 253151; -. [P35279-2]
DR TopDownProteomics; P35279-1; -. [P35279-1]
DR ABCD; P35279; 39 sequenced antibodies.
DR Antibodypedia; 4093; 301 antibodies from 33 providers.
DR DNASU; 19346; -.
DR Ensembl; ENSMUST00000032946; ENSMUSP00000032946; ENSMUSG00000030704. [P35279-1]
DR Ensembl; ENSMUST00000098252; ENSMUSP00000095852; ENSMUSG00000030704. [P35279-2]
DR GeneID; 19346; -.
DR KEGG; mmu:19346; -.
DR UCSC; uc009ini.2; mouse. [P35279-1]
DR CTD; 5870; -.
DR MGI; MGI:894313; Rab6a.
DR VEuPathDB; HostDB:ENSMUSG00000030704; -.
DR eggNOG; KOG0094; Eukaryota.
DR GeneTree; ENSGT00940000154769; -.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; P35279; -.
DR OMA; PVSNDGC; -.
DR PhylomeDB; P35279; -.
DR TreeFam; TF300803; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-6811438; Intra-Golgi traffic.
DR Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-MMU-8854214; TBC/RABGAPs.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 19346; 14 hits in 73 CRISPR screens.
DR ChiTaRS; Rab6a; mouse.
DR PRO; PR:P35279; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P35279; protein.
DR Bgee; ENSMUSG00000030704; Expressed in primary motor cortex and 268 other tissues.
DR ExpressionAtlas; P35279; baseline and differential.
DR Genevisible; P35279; MM.
DR GO; GO:0002080; C:acrosomal membrane; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0070381; C:endosome to plasma membrane transport vesicle; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0001671; F:ATPase activator activity; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0031489; F:myosin V binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0019882; P:antigen processing and presentation; ISO:MGI.
DR GO; GO:0034498; P:early endosome to Golgi transport; ISO:MGI.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0018125; P:peptidyl-cysteine methylation; ISO:MGI.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; ISS:UniProtKB.
DR GO; GO:1903292; P:protein localization to Golgi membrane; ISS:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; ISS:UniProtKB.
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; Alternative splicing; Direct protein sequencing;
KW ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P20340"
FT CHAIN 2..208
FT /note="Ras-related protein Rab-6A"
FT /id="PRO_0000121113"
FT MOTIF 42..50
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 20..28
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 BINDING 156..158
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P20340"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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"
FT VAR_SEQ 62..88
FT /note="VRLQLWDTAGQERFRSLIPSYIRDSTV -> IRLQLWDTAGQERFRSLIPSY
FT IRDSAA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:1555775"
FT /id="VSP_005528"
FT MUTAGEN 22
FT /note="Q->V: Loss of binding to rabkinesin-6."
FT /evidence="ECO:0000269|PubMed:9438855"
FT MUTAGEN 27
FT /note="T->N: Loss of binding to rabkinesin-6; when
FT associated with L-73."
FT /evidence="ECO:0000269|PubMed:9438855"
FT MUTAGEN 46
FT /note="I->E: Loss of binding to rabkinesin-6."
FT /evidence="ECO:0000269|PubMed:9438855"
FT MUTAGEN 72
FT /note="Q->L: Loss of binding to rabkinesin-6; when
FT associated with N-28."
FT /evidence="ECO:0000269|PubMed:9438855"
SQ SEQUENCE 208 AA; 23590 MW; DD08CC2914668FD4 CRC64;
MSAGGDFGNP LRKFKLVFLG EQSVGKTSLI TRFMYDSFDN TYQATIGIDF LSKTMYLEDR
TVRLQLWDTA GQERFRSLIP SYIRDSTVAV VVYDITNVNS FQQTTKWIDD VRTERGSDVI
IMLVGNKTDL ADKRQVSIEE GERKAKELNV MFIETSAKAG YNVKQLFRRV AAALPGMEST
QDRSREDMID IKLEKPQEQP VNEGGCSC
