GET3_YEAST
ID GET3_YEAST Reviewed; 354 AA.
AC Q12154; D6VRQ0; Q6B1B6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=ATPase GET3 {ECO:0000255|HAMAP-Rule:MF_03112};
DE EC=3.6.-.- {ECO:0000255|HAMAP-Rule:MF_03112};
DE AltName: Full=Arsenical pump-driving ATPase {ECO:0000255|HAMAP-Rule:MF_03112};
DE AltName: Full=Arsenite-stimulated ATPase {ECO:0000255|HAMAP-Rule:MF_03112};
DE AltName: Full=Golgi to ER traffic protein 3 {ECO:0000255|HAMAP-Rule:MF_03112};
DE AltName: Full=Guided entry of tail-anchored proteins 3 {ECO:0000255|HAMAP-Rule:MF_03112};
GN Name=GET3 {ECO:0000255|HAMAP-Rule:MF_03112}; Synonyms=ARR4;
GN OrderedLocusNames=YDL100C; ORFNames=D2371;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8923743;
RX DOI=10.1002/(sici)1097-0061(199610)12:13%3c1377::aid-yea35%3e3.0.co;2-r;
RA Boskovic J., Soler-Mira A., Garcia-Cantalejo J.M., Ballesta J.P.G.,
RA Jimenez A., Remacha M.A.;
RT "The sequence of a 16,691 bp segment of Saccharomyces cerevisiae chromosome
RT IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open
RT reading frames.";
RL Yeast 12:1377-1384(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP IDENTIFICATION IN GET COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11805837; DOI=10.1038/415180a;
RA Ho Y., Gruhler A., Heilbut A., Bader G.D., Moore L., Adams S.-L.,
RA Millar A., Taylor P., Bennett K., Boutilier K., Yang L., Wolting C.,
RA Donaldson I., Schandorff S., Shewnarane J., Vo M., Taggart J.,
RA Goudreault M., Muskat B., Alfarano C., Dewar D., Lin Z., Michalickova K.,
RA Willems A.R., Sassi H., Nielsen P.A., Rasmussen K.J., Andersen J.R.,
RA Johansen L.E., Hansen L.H., Jespersen H., Podtelejnikov A., Nielsen E.,
RA Crawford J., Poulsen V., Soerensen B.D., Matthiesen J., Hendrickson R.C.,
RA Gleeson F., Pawson T., Moran M.F., Durocher D., Mann M., Hogue C.W.V.,
RA Figeys D., Tyers M.;
RT "Systematic identification of protein complexes in Saccharomyces cerevisiae
RT by mass spectrometry.";
RL Nature 415:180-183(2002).
RN [6]
RP FUNCTION, MUTAGENESIS OF GLY-30, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=12680698; DOI=10.1023/a:1022504311669;
RA Shen J., Hsu C.-M., Kang B.-K., Rosen B.P., Bhattacharjee H.;
RT "The Saccharomyces cerevisiae Arr4p is involved in metal and heat
RT tolerance.";
RL BioMetals 16:369-378(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP FUNCTION, IDENTIFICATION IN GET COMPLEX, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH GET1.
RX PubMed=16269340; DOI=10.1016/j.cell.2005.08.031;
RA Schuldiner M., Collins S.R., Thompson N.J., Denic V., Bhamidipati A.,
RA Punna T., Ihmels J., Andrews B., Boone C., Greenblatt J.F., Weissman J.S.,
RA Krogan N.J.;
RT "Exploration of the function and organization of the yeast early secretory
RT pathway through an epistatic miniarray profile.";
RL Cell 123:507-519(2005).
RN [10]
RP INTERACTION WITH GET1 AND GET2, AND SUBCELLULAR LOCATION.
RX PubMed=16816426; DOI=10.1534/genetics.106.058362;
RA Auld K.L., Hitchcock A.L., Doherty H.K., Frietze S., Huang L.S.,
RA Silver P.A.;
RT "The conserved ATPase Get3/Arr4 modulates the activity of membrane-
RT associated proteins in Saccharomyces cerevisiae.";
RL Genetics 174:215-227(2006).
RN [11]
RP INTERACTION WITH GEF1, AND SUBUNIT.
RX PubMed=16260785; DOI=10.1074/jbc.m507481200;
RA Metz J., Waechter A., Schmidt B., Bujnicki J.M., Schwappach B.;
RT "The yeast Arr4p ATPase binds the chloride transporter Gef1p when copper is
RT available in the cytosol.";
RL J. Biol. Chem. 281:410-417(2006).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18724936; DOI=10.1016/j.cell.2008.06.025;
RA Schuldiner M., Metz J., Schmid V., Denic V., Rakwalska M., Schmitt H.D.,
RA Schwappach B., Weissman J.S.;
RT "The GET complex mediates insertion of tail-anchored proteins into the ER
RT membrane.";
RL Cell 134:634-645(2008).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=24392163; DOI=10.1371/journal.pone.0085033;
RA Vilardi F., Stephan M., Clancy A., Janshoff A., Schwappach B.;
RT "WRB and CAML are necessary and sufficient to mediate tail-anchored protein
RT targeting to the ER membrane.";
RL PLoS ONE 9:e85033-e85033(2014).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) IN COMPLEX WITH ADP AND ZINC,
RP SUBUNIT, AND MUTAGENESIS OF ASP-57; CYS-285 AND CYS-288.
RX PubMed=19675567; DOI=10.1038/nature08319;
RA Mateja A., Szlachcic A., Downing M.E., Dobosz M., Mariappan M., Hegde R.S.,
RA Keenan R.J.;
RT "The structural basis of tail-anchored membrane protein recognition by
RT Get3.";
RL Nature 461:361-366(2009).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=19956640; DOI=10.1371/journal.pone.0008061;
RA Hu J., Li J., Qian X., Denic V., Sha B.;
RT "The crystal structures of yeast Get3 suggest a mechanism for tail-anchored
RT protein membrane insertion.";
RL PLoS ONE 4:E8061-E8061(2009).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF GLY-30.
RX PubMed=19706470; DOI=10.1073/pnas.0907522106;
RA Suloway C.J.M., Chartron J.W., Zaslaver M., Clemons W.M. Jr.;
RT "Model for eukaryotic tail-anchored protein binding based on the structure
RT of Get3.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:14849-14854(2009).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH ADP.
RX PubMed=20015340; DOI=10.1111/j.1365-2443.2009.01362.x;
RA Yamagata A., Mimura H., Sato Y., Yamashita M., Yoshikawa A., Fukai S.;
RT "Structural insight into the membrane insertion of tail-anchored proteins
RT by Get3.";
RL Genes Cells 15:29-41(2010).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH GET2, FUNCTION, AND
RP SUBUNIT.
RX PubMed=21866104; DOI=10.1038/nature10362;
RA Mariappan M., Mateja A., Dobosz M., Bove E., Hegde R.S., Keenan R.J.;
RT "The mechanism of membrane-associated steps in tail-anchored protein
RT insertion.";
RL Nature 477:61-66(2011).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH GET1, FUNCTION, AND
RP SUBUNIT.
RX PubMed=21719644; DOI=10.1126/science.1207125;
RA Stefer S., Reitz S., Wang F., Wild K., Pang Y.Y., Schwarz D., Bomke J.,
RA Hein C., Lohr F., Bernhard F., Denic V., Dotsch V., Sinning I.;
RT "Structural basis for tail-anchored membrane protein biogenesis by the
RT Get3-receptor complex.";
RL Science 333:758-762(2011).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=22684149; DOI=10.1016/j.jmb.2012.05.045;
RA Kubota K., Yamagata A., Sato Y., Goto-Ito S., Fukai S.;
RT "Get1 stabilizes an open dimer conformation of get3 ATPase by binding two
RT distinct interfaces.";
RL J. Mol. Biol. 422:366-375(2012).
RN [21]
RP STRUCTURE BY ELECTRON MICROSCOPY (14 ANGSTROMS) OF THE GET COMPLEX.
RX PubMed=32910895; DOI=10.1016/j.molcel.2020.08.012;
RA McDowell M.A., Heimes M., Fiorentino F., Mehmood S., Farkas A.,
RA Coy-Vergara J., Wu D., Bolla J.R., Schmid V., Heinze R., Wild K.,
RA Flemming D., Pfeffer S., Schwappach B., Robinson C.V., Sinning I.;
RT "Structural Basis of Tail-Anchored Membrane Protein Biogenesis by the GET
RT Insertase Complex.";
RL Mol. Cell 80:72-86(2020).
CC -!- FUNCTION: ATPase required for the post-translational delivery of tail-
CC anchored (TA) proteins to the endoplasmic reticulum. Recognizes and
CC selectively binds the transmembrane domain of TA proteins in the
CC cytosol. This complex then targets to the endoplasmic reticulum by
CC membrane-bound receptors GET1 and GET2, where the tail-anchored protein
CC is released for insertion. This process is regulated by ATP binding and
CC hydrolysis. ATP binding drives the homodimer towards the closed dimer
CC state, facilitating recognition of newly synthesized TA membrane
CC proteins. ATP hydrolysis is required for insertion. Subsequently, the
CC homodimer reverts towards the open dimer state, lowering its affinity
CC for the GET1-GET2 receptor, and returning it to the cytosol to initiate
CC a new round of targeting. Cooperates with the HDEL receptor ERD2 to
CC mediate the ATP-dependent retrieval of resident ER proteins that
CC contain a C-terminal H-D-E-L retention signal from the Golgi to the ER.
CC Involved in low-level resistance to the oxyanions arsenite and
CC arsenate, and in heat tolerance. {ECO:0000255|HAMAP-Rule:MF_03112,
CC ECO:0000269|PubMed:12680698, ECO:0000269|PubMed:16269340,
CC ECO:0000269|PubMed:18724936, ECO:0000269|PubMed:21719644,
CC ECO:0000269|PubMed:21866104}.
CC -!- SUBUNIT: Homodimer. Component of the Golgi to ER traffic (GET) complex,
CC which is composed of GET1, GET2 and GET3. Within the complex, GET1 and
CC GET2 form a heterotetramer which is stabilized by phosphatidylinositol
CC binding and which binds to the GET3 homodimer (PubMed:32910895).
CC Interacts with the chloride channel protein GEF1. {ECO:0000255|HAMAP-
CC Rule:MF_03112, ECO:0000269|PubMed:11805837,
CC ECO:0000269|PubMed:12680698, ECO:0000269|PubMed:16260785,
CC ECO:0000269|PubMed:16269340, ECO:0000269|PubMed:16816426,
CC ECO:0000269|PubMed:19675567, ECO:0000269|PubMed:19706470,
CC ECO:0000269|PubMed:20015340, ECO:0000269|PubMed:21719644,
CC ECO:0000269|PubMed:21866104, ECO:0000269|PubMed:32910895}.
CC -!- INTERACTION:
CC Q12154; P37020: GEF1; NbExp=6; IntAct=EBI-2989, EBI-7552;
CC Q12154; P53192: GET1; NbExp=12; IntAct=EBI-2989, EBI-23722;
CC Q12154; P40056: GET2; NbExp=9; IntAct=EBI-2989, EBI-22604;
CC Q12154; Q12154: GET3; NbExp=12; IntAct=EBI-2989, EBI-2989;
CC Q12154; Q12125: GET4; NbExp=11; IntAct=EBI-2989, EBI-36940;
CC Q12154; Q12285: MDY2; NbExp=10; IntAct=EBI-2989, EBI-34904;
CC Q12154; Q12255: NYV1; NbExp=3; IntAct=EBI-2989, EBI-35465;
CC Q12154; P32854: PEP12; NbExp=5; IntAct=EBI-2989, EBI-13098;
CC Q12154; P22214: SEC22; NbExp=7; IntAct=EBI-2989, EBI-16577;
CC Q12154; P60468: SEC61B; Xeno; NbExp=4; IntAct=EBI-2989, EBI-1788819;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum
CC {ECO:0000269|PubMed:24392163}. Golgi apparatus. Note=GET1 and GET2 are
CC required for targeting GET3 to the endoplasmic reticulum.
CC -!- MISCELLANEOUS: Present with 17300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the arsA ATPase family. {ECO:0000255|HAMAP-
CC Rule:MF_03112}.
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DR EMBL; X95644; CAA64913.1; -; Genomic_DNA.
DR EMBL; Z74148; CAA98667.1; -; Genomic_DNA.
DR EMBL; AY693164; AAT93183.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11760.1; -; Genomic_DNA.
DR PIR; S67642; S67642.
DR RefSeq; NP_010183.1; NM_001180159.1.
DR PDB; 2WOJ; X-ray; 1.99 A; A/B/C/D=1-354.
DR PDB; 3A36; X-ray; 2.80 A; A/B=1-354.
DR PDB; 3A37; X-ray; 3.00 A; A/B=1-354.
DR PDB; 3B2E; X-ray; 3.00 A; A/B/C/D=1-354.
DR PDB; 3H84; X-ray; 2.30 A; A/B=1-354.
DR PDB; 3IDQ; X-ray; 3.70 A; A=1-354.
DR PDB; 3SJA; X-ray; 3.00 A; A/B/E/F/I=1-354.
DR PDB; 3SJB; X-ray; 3.30 A; A/B=1-354.
DR PDB; 3SJC; X-ray; 3.20 A; A/B/E/F=1-354.
DR PDB; 3SJD; X-ray; 4.60 A; A/B/C=1-354.
DR PDB; 3VLC; X-ray; 4.50 A; A=1-354.
DR PDB; 3ZS8; X-ray; 3.00 A; A/B=1-354.
DR PDB; 3ZS9; X-ray; 2.10 A; A/B=1-354.
DR PDB; 4PWX; X-ray; 5.40 A; A/B=2-354.
DR PDB; 4XTR; X-ray; 2.05 A; A/B=1-354.
DR PDB; 4XVU; X-ray; 2.35 A; A/B/G/H=1-354.
DR PDB; 4XWO; X-ray; 2.75 A; A/B/G/H/M/N/S/T=1-354.
DR PDB; 5BW8; X-ray; 2.80 A; A/B=2-354.
DR PDB; 5BWK; X-ray; 6.00 A; A/B/C/D/M/N/O/P=2-354.
DR PDBsum; 2WOJ; -.
DR PDBsum; 3A36; -.
DR PDBsum; 3A37; -.
DR PDBsum; 3B2E; -.
DR PDBsum; 3H84; -.
DR PDBsum; 3IDQ; -.
DR PDBsum; 3SJA; -.
DR PDBsum; 3SJB; -.
DR PDBsum; 3SJC; -.
DR PDBsum; 3SJD; -.
DR PDBsum; 3VLC; -.
DR PDBsum; 3ZS8; -.
DR PDBsum; 3ZS9; -.
DR PDBsum; 4PWX; -.
DR PDBsum; 4XTR; -.
DR PDBsum; 4XVU; -.
DR PDBsum; 4XWO; -.
DR PDBsum; 5BW8; -.
DR PDBsum; 5BWK; -.
DR AlphaFoldDB; Q12154; -.
DR SMR; Q12154; -.
DR BioGRID; 31962; 467.
DR ComplexPortal; CPX-956; GET complex.
DR DIP; DIP-3908N; -.
DR IntAct; Q12154; 60.
DR MINT; Q12154; -.
DR STRING; 4932.YDL100C; -.
DR TCDB; 3.A.21.1.1; the c-terminal tail-anchored membrane protein biogenesis/ insertion complex (tamp-b) family.
DR iPTMnet; Q12154; -.
DR MaxQB; Q12154; -.
DR PaxDb; Q12154; -.
DR PRIDE; Q12154; -.
DR ABCD; Q12154; 1 sequenced antibody.
DR EnsemblFungi; YDL100C_mRNA; YDL100C; YDL100C.
DR GeneID; 851458; -.
DR KEGG; sce:YDL100C; -.
DR SGD; S000002258; GET3.
DR VEuPathDB; FungiDB:YDL100C; -.
DR eggNOG; KOG2825; Eukaryota.
DR GeneTree; ENSGT00390000003817; -.
DR HOGENOM; CLU_040761_0_0_1; -.
DR InParanoid; Q12154; -.
DR OMA; MDAPYEF; -.
DR BioCyc; YEAST:G3O-29503-MON; -.
DR EvolutionaryTrace; Q12154; -.
DR PRO; PR:Q12154; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12154; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0043529; C:GET complex; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044183; F:protein folding chaperone; IDA:SGD.
DR GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
DR GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0045048; P:protein insertion into ER membrane; IDA:ComplexPortal.
DR GO; GO:0046685; P:response to arsenic-containing substance; IEA:UniProtKB-KW.
DR GO; GO:0009408; P:response to heat; IMP:SGD.
DR GO; GO:0010038; P:response to metal ion; IMP:SGD.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IDA:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03112; Asna1_Get3; 1.
DR InterPro; IPR025723; Anion-transp_ATPase-like_dom.
DR InterPro; IPR016300; ATPase_ArsA/GET3.
DR InterPro; IPR027542; ATPase_ArsA/GET3_euk.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10803; PTHR10803; 1.
DR Pfam; PF02374; ArsA_ATPase; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00345; GET3_arsA_TRC40; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Arsenical resistance; ATP-binding; Cytoplasm;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Hydrolase;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transport; Zinc.
FT CHAIN 1..354
FT /note="ATPase GET3"
FT /id="PRO_0000152256"
FT ACT_SITE 57
FT BINDING 26..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112,
FT ECO:0000269|PubMed:19675567"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112,
FT ECO:0000269|PubMed:19675567"
FT BINDING 315..322
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MUTAGEN 30
FT /note="G->R: Abolishes ATPase activity, leading to
FT secretion of resident ER proteins."
FT /evidence="ECO:0000269|PubMed:12680698,
FT ECO:0000269|PubMed:19706470"
FT MUTAGEN 57
FT /note="D->N: Abolishes ATP hydrolysis."
FT /evidence="ECO:0000269|PubMed:19675567"
FT MUTAGEN 285
FT /note="C->S: Prevents dimerization; when associated with S-
FT 288."
FT /evidence="ECO:0000269|PubMed:19675567"
FT MUTAGEN 288
FT /note="C->S: Prevents dimerization; when associated with S-
FT 285."
FT /evidence="ECO:0000269|PubMed:19675567"
FT CONFLICT 43
FT /note="A -> T (in Ref. 4; AAT93183)"
FT /evidence="ECO:0000305"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:4XWO"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:2WOJ"
FT STRAND 20..26
FT /evidence="ECO:0007829|PDB:2WOJ"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:3H84"
FT HELIX 31..45
FT /evidence="ECO:0007829|PDB:2WOJ"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:3B2E"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:2WOJ"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:4XVU"
FT HELIX 62..66
FT /evidence="ECO:0007829|PDB:2WOJ"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:2WOJ"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:2WOJ"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:3B2E"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:3H84"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:3H84"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:3H84"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:2WOJ"
FT HELIX 136..153
FT /evidence="ECO:0007829|PDB:2WOJ"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:3H84"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:2WOJ"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:2WOJ"
FT HELIX 179..188
FT /evidence="ECO:0007829|PDB:2WOJ"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:3H84"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:3B2E"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:3H84"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:3H84"
FT HELIX 213..230
FT /evidence="ECO:0007829|PDB:2WOJ"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:2WOJ"
FT STRAND 236..245
FT /evidence="ECO:0007829|PDB:2WOJ"
FT HELIX 246..261
FT /evidence="ECO:0007829|PDB:2WOJ"
FT STRAND 268..274
FT /evidence="ECO:0007829|PDB:2WOJ"
FT TURN 277..281
FT /evidence="ECO:0007829|PDB:3H84"
FT HELIX 286..305
FT /evidence="ECO:0007829|PDB:2WOJ"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:2WOJ"
FT STRAND 309..315
FT /evidence="ECO:0007829|PDB:2WOJ"
FT HELIX 323..335
FT /evidence="ECO:0007829|PDB:2WOJ"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:2WOJ"
FT HELIX 344..350
FT /evidence="ECO:0007829|PDB:2WOJ"
SQ SEQUENCE 354 AA; 39354 MW; F795C359B5A4A461 CRC64;
MDLTVEPNLH SLITSTTHKW IFVGGKGGVG KTTSSCSIAI QMALSQPNKQ FLLISTDPAH
NLSDAFGEKF GKDARKVTGM NNLSCMEIDP SAALKDMNDM AVSRANNNGS DGQGDDLGSL
LQGGALADLT GSIPGIDEAL SFMEVMKHIK RQEQGEGETF DTVIFDTAPT GHTLRFLQLP
NTLSKLLEKF GEITNKLGPM LNSFMGAGNV DISGKLNELK ANVETIRQQF TDPDLTTFVC
VCISEFLSLY ETERLIQELI SYDMDVNSII VNQLLFAEND QEHNCKRCQA RWKMQKKYLD
QIDELYEDFH VVKMPLCAGE IRGLNNLTKF SQFLNKEYNP ITDGKVIYEL EDKE
