RAB6A_RAT
ID RAB6A_RAT Reviewed; 208 AA.
AC Q9WVB1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Ras-related protein Rab-6A;
DE Short=Rab-6;
GN Name=Rab6a; Synonyms=Rab6;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 69-208.
RC STRAIN=Sprague-Dawley; TISSUE=Lung;
RX PubMed=11062069; DOI=10.1042/bj3520165;
RA Han S.Y., Park D.Y., Park S.D., Hong S.H.;
RT "Identification of Rab6 as an N-ethylmaleimide-sensitive fusion protein-
RT binding protein.";
RL Biochem. J. 352:165-173(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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.
CC {ECO:0000250|UniProtKB:P20340}.
CC -!- SUBUNIT: Interacts with BICDL1; leads to its accumulation in the
CC pericentrosomal region. Interacts with SCYL1BP1. Interacts with VSP52
CC and RABGAP1. Interacts with GCC2 (via its GRIP domain). Interacts with
CC RAB6IP1 (via its RUN 1 domain). Interacts with RAB6KIFL. Interacts with
CC BICD1. Interacts with BICD2. Interacts with TMF1. Interacts (GTP-bound)
CC with DYNLRB1; the interaction is direct (By similarity). Interacts with
CC PIFO (By similarity). Interacts (GTP-bound) with APBA1/MINT1 isoform 2,
CC also called Mint1_826. Interacts with RIC1 and RGP1; the interactions
CC are direct with a preference for RAB6A-GDP.
CC {ECO:0000250|UniProtKB:P20340, ECO:0000250|UniProtKB:P35279}.
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.
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; AC145474; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF148210; AAD38018.1; -; mRNA.
DR RefSeq; XP_006229856.1; XM_006229794.2.
DR AlphaFoldDB; Q9WVB1; -.
DR SMR; Q9WVB1; -.
DR BioGRID; 249922; 2.
DR IntAct; Q9WVB1; 5.
DR MINT; Q9WVB1; -.
DR STRING; 10116.ENSRNOP00000025104; -.
DR iPTMnet; Q9WVB1; -.
DR PhosphoSitePlus; Q9WVB1; -.
DR jPOST; Q9WVB1; -.
DR PaxDb; Q9WVB1; -.
DR PRIDE; Q9WVB1; -.
DR GeneID; 84379; -.
DR UCSC; RGD:619737; rat.
DR CTD; 5870; -.
DR RGD; 619737; Rab6a.
DR eggNOG; KOG0094; Eukaryota.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; Q9WVB1; -.
DR OMA; PVSNDGC; -.
DR PhylomeDB; Q9WVB1; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-6811438; Intra-Golgi traffic.
DR Reactome; R-RNO-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-RNO-8854214; TBC/RABGAPs.
DR Reactome; R-RNO-8873719; RAB geranylgeranylation.
DR Reactome; R-RNO-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR PRO; PR:Q9WVB1; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018176; Expressed in Ammon's horn and 19 other tissues.
DR ExpressionAtlas; Q9WVB1; baseline and differential.
DR Genevisible; Q9WVB1; RN.
DR GO; GO:0002080; C:acrosomal membrane; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0070381; C:endosome to plasma membrane transport vesicle; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0005802; C:trans-Golgi network; ISO:RGD.
DR GO; GO:0001671; F:ATPase activator activity; IDA:RGD.
DR GO; GO:0051117; F:ATPase binding; IPI:RGD.
DR GO; GO:0005525; F:GTP binding; IDA:RGD.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0031489; F:myosin V binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:RGD.
DR GO; GO:0019882; P:antigen processing and presentation; ISO:RGD.
DR GO; GO:0034498; P:early endosome to Golgi transport; ISO:RGD.
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:RGD.
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:0032482; P:Rab protein signal transduction; IC:RGD.
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; ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein;
KW Membrane; 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_0000121114"
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:22673903"
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"
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
