GET3_BOVIN
ID GET3_BOVIN Reviewed; 348 AA.
AC A5PJI5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) 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, CAMLG/GET2 and GET3. Within the complex,
CC CAMLG and GET1 form a heterotetramer which is stabilized by
CC phosphatidylinositol binding and which binds to the GET3 homodimer.
CC Interacts with CAMLG/GET2 (via N-terminus). GET3 shows a higher
CC affinity for CAMLG than for GET1. Interacts with SERP1 and SEC61B.
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}. Nucleus,
CC nucleolus {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; BC142125; AAI42126.1; -; mRNA.
DR RefSeq; NP_001092334.1; NM_001098864.1.
DR AlphaFoldDB; A5PJI5; -.
DR SMR; A5PJI5; -.
DR STRING; 9913.ENSBTAP00000015719; -.
DR PaxDb; A5PJI5; -.
DR PRIDE; A5PJI5; -.
DR Ensembl; ENSBTAT00000015719; ENSBTAP00000015719; ENSBTAG00000011837.
DR GeneID; 504586; -.
DR KEGG; bta:504586; -.
DR CTD; 439; -.
DR VEuPathDB; HostDB:ENSBTAG00000011837; -.
DR VGNC; VGNC:96696; GET3.
DR eggNOG; KOG2825; Eukaryota.
DR GeneTree; ENSGT00390000003817; -.
DR HOGENOM; CLU_040761_0_0_1; -.
DR InParanoid; A5PJI5; -.
DR OMA; MDAPYEF; -.
DR OrthoDB; 992208at2759; -.
DR TreeFam; TF300670; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000011837; Expressed in retina and 108 other tissues.
DR GO; GO:0043529; C:GET complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; ISS:UniProtKB.
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 Acetylation; ATP-binding; Cytoplasm; Endoplasmic reticulum; Hydrolase;
KW Metal-binding; Nucleotide-binding; Nucleus; Reference proteome; Transport;
KW Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43681"
FT CHAIN 2..348
FT /note="ATPase GET3"
FT /id="PRO_0000348229"
FT ACT_SITE 74
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 45..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 251
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 289
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 292
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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O43681"
SQ SEQUENCE 348 AA; 38793 MW; DA52C4ACC35C7A36 CRC64;
MAAGVAGWGV EAEEFEDAPD VEPLEPTLSN IIEQRSLKWI FVGGKGGVGK TTCSCSLAVQ
LSKGRESVLI ISTDPAHNIS DAFDQKFSKV PTKVKGYDNL FAMEIDPSLG VAELPDEFFE
EDNMLSMGKK MMQEAMSAFP GIDEAMSYAE VMRLVKGMNF SVVVFDTAPT GHTLRLLNFP
TIVERGLGRL MQIKNQISPF ISQMCNMLGL GDMNADQLAS KLEETLPVIR SVSEQFKDPE
QTTFICVCIA EFLSLYETER LIQELAKCKI DTHNIIVNQL VFPDPEKPCK MCEARHKIQA
KYLDQMEDLY EDFHIVKLPL LPHEVRGADK VNTFSALLLE PYKPPSAQ
