GET3_DEBHA
ID GET3_DEBHA Reviewed; 348 AA.
AC Q6BSM0;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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};
GN OrderedLocusNames=DEHA2D07832g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ADP.
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).
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; CR382136; CAG86944.1; -; Genomic_DNA.
DR RefSeq; XP_458800.1; XM_458800.1.
DR PDB; 3IO3; X-ray; 1.80 A; A=1-348.
DR PDBsum; 3IO3; -.
DR AlphaFoldDB; Q6BSM0; -.
DR SMR; Q6BSM0; -.
DR STRING; 4959.XP_458800.1; -.
DR EnsemblFungi; CAG86944; CAG86944; DEHA2D07832g.
DR GeneID; 2900983; -.
DR KEGG; dha:DEHA2D07832g; -.
DR VEuPathDB; FungiDB:DEHA2D07832g; -.
DR eggNOG; KOG2825; Eukaryota.
DR HOGENOM; CLU_040761_0_0_1; -.
DR InParanoid; Q6BSM0; -.
DR OMA; MDAPYEF; -.
DR OrthoDB; 992208at2759; -.
DR Proteomes; UP000000599; Chromosome D.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045048; P:protein insertion into ER membrane; IEA:UniProtKB-UniRule.
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; ATP-binding; Cytoplasm; Endoplasmic reticulum;
KW Golgi apparatus; Hydrolase; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transport; Zinc.
FT CHAIN 1..348
FT /note="ATPase GET3"
FT /id="PRO_0000388206"
FT ACT_SITE 57
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 26..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 268
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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"
FT BINDING 310..312
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:3IO3"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:3IO3"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:3IO3"
FT HELIX 31..45
FT /evidence="ECO:0007829|PDB:3IO3"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:3IO3"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:3IO3"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:3IO3"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:3IO3"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:3IO3"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:3IO3"
FT HELIX 221..226
FT /evidence="ECO:0007829|PDB:3IO3"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:3IO3"
FT STRAND 232..241
FT /evidence="ECO:0007829|PDB:3IO3"
FT HELIX 242..257
FT /evidence="ECO:0007829|PDB:3IO3"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:3IO3"
FT HELIX 281..300
FT /evidence="ECO:0007829|PDB:3IO3"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:3IO3"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:3IO3"
FT HELIX 319..330
FT /evidence="ECO:0007829|PDB:3IO3"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:3IO3"
FT HELIX 339..343
FT /evidence="ECO:0007829|PDB:3IO3"
SQ SEQUENCE 348 AA; 39212 MW; B96EB93AB6B2D230 CRC64;
MDLELEPTLE SIVQHDSLKW IFVGGKGGVG KTTTSSSVAV QLALAQPNEQ FLLISTDPAH
NLSDAFCQKF GKDARKVEGL PNLSCMEIDP EAAMSDLQQQ ASQYNNDPND PLKSMMSDMT
GSIPGIDEAL SFMEVLKHIK NQKVLEGEDN SNAISYKTII FDTAPTGHTL RFLQLPSTLE
KLLSKFKDLS GKLGPMLSMM GGGQQQDIFE KLNEVQKNVS EVNEQFTNPE LTTFICVCIS
EFLSLYETER MIQELMSYNM DVNSIVVNQL LFAEGDDHSC KRCESRWKMQ KKYLDQMGEL
YEDYHLVKMP LLGCEIRGVE NLKKFSKFLL KPYDPKADSD IVFDLEEK
