GET3_XENLA
ID GET3_XENLA Reviewed; 342 AA.
AC Q6GNQ1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Guided entry of tail-anchored proteins factor 3, ATPase {ECO:0000255|HAMAP-Rule:MF_03112};
GN Name=get3 {ECO:0000255|HAMAP-Rule:MF_03112};
GN Synonyms=asna1 {ECO:0000255|HAMAP-Rule:MF_03112};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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/WRB and CAMLG/GET2, where the tail-
CC anchored protein is released for insertion. This process is regulated
CC by ATP binding and hydrolysis. ATP binding drives the homodimer towards
CC the closed dimer state, facilitating recognition of newly synthesized
CC TA membrane proteins. ATP hydrolysis is required for insertion.
CC Subsequently, the homodimer reverts towards the open dimer state,
CC lowering its affinity for the GET1-CAMLG receptor, and returning it to
CC the cytosol to initiate a new round of targeting. {ECO:0000255|HAMAP-
CC Rule:MF_03112}.
CC -!- SUBUNIT: Homodimer. Component of the Golgi to ER traffic (GET) complex,
CC which is composed of GET1/WRB, CAMLG/GET2 and GET3/TRC40. Within the
CC complex, CAMLG and GET1 form a heterotetramer which is stabilized by
CC phosphatidylinositol binding and which binds to the GET3 homodimer.
CC {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}.
CC -!- SIMILARITY: Belongs to the arsA ATPase family. {ECO:0000255|HAMAP-
CC Rule:MF_03112}.
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DR EMBL; BC073453; AAH73453.1; -; mRNA.
DR RefSeq; NP_001085870.1; NM_001092401.1.
DR AlphaFoldDB; Q6GNQ1; -.
DR SMR; Q6GNQ1; -.
DR BioGRID; 102460; 1.
DR DNASU; 444297; -.
DR GeneID; 444297; -.
DR KEGG; xla:444297; -.
DR CTD; 444297; -.
DR Xenbase; XB-GENE-1013231; get3.S.
DR OrthoDB; 992208at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 444297; Expressed in brain and 19 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; 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 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Endoplasmic reticulum; Hydrolase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transport; Zinc.
FT CHAIN 1..342
FT /note="ATPase GET3"
FT /id="PRO_0000348231"
FT ACT_SITE 68
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 272
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 342 AA; 38316 MW; 00CCC2BF7D1C18B2 CRC64;
MAAPVDDEFE DAPDVEPLEP TLSNVIDQRS LRWIFVGGKG GVGKTTCSCS LAVQLSLVRD
SVLIISTDPA HNISDAFDQK FSKVPTKVRG YDNLFAMEID PSLGVAELPD EIFEEDNMLS
MGKKMMQEAM SAFPGIDEAM SYAEVMRLVK GMNFSVVVFD TAPTGHTLRL LNFPTIVERG
LGRLMQIKNQ ISPFISQMCN MLGLGDMNAD QLASKLEETL PVIRSVSEQF KDPEQTTFIC
VCIAEFLSLY ETERLIQELA KCSIDTHNII VNQLVFPDPE KPCRMCEARH KIQSKYLDQM
EDLYEDFHIA KLPLLPHEVR GVENVNTFSK LLLEPYKPPS GK
