GET3_VANPO
ID GET3_VANPO Reviewed; 352 AA.
AC A7TH32;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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}; ORFNames=Kpol_1032p81;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480389; EDO18484.1; -; Genomic_DNA.
DR RefSeq; XP_001646342.1; XM_001646292.1.
DR AlphaFoldDB; A7TH32; -.
DR SMR; A7TH32; -.
DR STRING; 436907.A7TH32; -.
DR EnsemblFungi; EDO18484; EDO18484; Kpol_1032p81.
DR GeneID; 5546771; -.
DR KEGG; vpo:Kpol_1032p81; -.
DR eggNOG; KOG2825; Eukaryota.
DR HOGENOM; CLU_040761_0_0_1; -.
DR InParanoid; A7TH32; -.
DR OMA; MDAPYEF; -.
DR OrthoDB; 992208at2759; -.
DR PhylomeDB; A7TH32; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
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 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..352
FT /note="ATPase GET3"
FT /id="PRO_0000388236"
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 /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 270
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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 286
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 352 AA; 38992 MW; 374DDF80E0166DE8 CRC64;
MDLTVDPNLH SLINSTTHRW IFVGGKGGVG KTTSSCSIAI QMALSQPSKQ FLLISTDPAH
NLSDAFGEKF GKDARKVTGM DNLSCMEIDP SAALNDMNDM AVSRANENGN GGDGLSDILQ
GGALADLTGS IPGIDEALSF MEVMKHIKNQ ENGEGDRYDT VIFDTAPTGH TLRFLQLPNT
LSKLLEKFGE ITGKLGPMLN SLAGAGNVDI SGKLNELKEN VEKIRQQFTD PDLTTFVCVC
ISEFLSLYET ERLIQELISY DMDVNSIIVN QLLFAEYDAE HNCKRCQARW KMQKKYLDQI
DELYEDFHVV KMPLCAGEIR GLNNLKKFSA FLNKEYDPVA DGKVIYELEE KN
