GET3_ASHGO
ID GET3_ASHGO Reviewed; 349 AA.
AC Q759J2;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 105.
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}; OrderedLocusNames=ADR285W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 281 AND 293.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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 -!- 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. Interacts with the
CC chloride channel protein GEF1. {ECO:0000255|HAMAP-Rule:MF_03112}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03112}.
CC Endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_03112}. Golgi
CC apparatus {ECO:0000255|HAMAP-Rule:MF_03112}. Note=GET1 and GET2 are
CC required for targeting GET3 to the endoplasmic reticulum.
CC {ECO:0000255|HAMAP-Rule:MF_03112}.
CC -!- SIMILARITY: Belongs to the arsA ATPase family. {ECO:0000255|HAMAP-
CC Rule:MF_03112}.
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DR EMBL; AE016817; AAS52205.2; -; Genomic_DNA.
DR RefSeq; NP_984381.2; NM_209734.2.
DR AlphaFoldDB; Q759J2; -.
DR SMR; Q759J2; -.
DR STRING; 33169.AAS52205; -.
DR EnsemblFungi; AAS52205; AAS52205; AGOS_ADR285W.
DR GeneID; 4620543; -.
DR KEGG; ago:AGOS_ADR285W; -.
DR eggNOG; KOG2825; Eukaryota.
DR HOGENOM; CLU_040761_0_0_1; -.
DR InParanoid; Q759J2; -.
DR OMA; MDAPYEF; -.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0043529; C:GET complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044183; F:protein folding chaperone; IEA:EnsemblFungi.
DR GO; GO:0051082; F:unfolded protein binding; IEA:EnsemblFungi.
DR GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IEA:EnsemblFungi.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0045048; P:protein insertion into ER membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0009408; P:response to heat; IEA:EnsemblFungi.
DR GO; GO:0010038; P:response to metal ion; IEA:EnsemblFungi.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Endoplasmic reticulum; Golgi apparatus; Hydrolase;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transport; Zinc.
FT CHAIN 1..349
FT /note="ATPase GET3"
FT /id="PRO_0000388186"
FT ACT_SITE 58
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 27..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 280
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 BINDING 283
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"
SQ SEQUENCE 349 AA; 38592 MW; 90DBA33D41E876AE CRC64;
MTDITPEASL RSLINSTTHK WIFVGGKGGV GKTTSSCSIA IQMALAQPTK QFLLISTDPA
HNLSDAFNEK FGKDARKVTG MDNLSCMEID PSAALKDVND MAIANGGDDD GLSGLLQGGA
LADLTGSIPG IDEALSFMEV MKHIKKQEQG DGEHFDTVIF DTAPTGHTLR FLQLPTTLTK
VLDKFGAIAG RLGPMLNSFA GNPNVDVLGK MNELKESVQK IKKQFTDPDL TTFVCVCISE
FLSLYETERL IQELISYDMD VNSIIVNQLL FAESDKEHNC KRCQARWKMQ KKYLSQIDEL
YEDFHIVKMP LCAGEIRGLE NLKKFSCFLN NKYDPETDGE LVYQLEQGL
