GET3_DANRE
ID GET3_DANRE Reviewed; 341 AA.
AC Q6IQE5; B8A663;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
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};
GN ORFNames=si:dkey-121b10.2, zgc:86799;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
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; BC071461; AAH71461.1; -; mRNA.
DR EMBL; BX901942; CAX14558.1; -; Genomic_DNA.
DR RefSeq; NP_001002298.1; NM_001002298.2.
DR PDB; 7RU9; EM; 3.30 A; A/B=1-341.
DR PDB; 7RUA; EM; 3.40 A; A/B=1-341.
DR PDB; 7RUC; EM; 3.60 A; A/B=1-341.
DR PDBsum; 7RU9; -.
DR PDBsum; 7RUA; -.
DR PDBsum; 7RUC; -.
DR AlphaFoldDB; Q6IQE5; -.
DR SMR; Q6IQE5; -.
DR STRING; 7955.ENSDARP00000018158; -.
DR iPTMnet; Q6IQE5; -.
DR PaxDb; Q6IQE5; -.
DR DNASU; 325704; -.
DR Ensembl; ENSDART00000007079; ENSDARP00000018158; ENSDARG00000018190.
DR GeneID; 325704; -.
DR KEGG; dre:325704; -.
DR CTD; 439; -.
DR ZFIN; ZDB-GENE-040625-120; get3.
DR eggNOG; KOG2825; Eukaryota.
DR GeneTree; ENSGT00390000003817; -.
DR HOGENOM; CLU_040761_0_0_1; -.
DR InParanoid; Q6IQE5; -.
DR OMA; MDAPYEF; -.
DR OrthoDB; 992208at2759; -.
DR PhylomeDB; Q6IQE5; -.
DR TreeFam; TF300670; -.
DR PRO; PR:Q6IQE5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 1.
DR Bgee; ENSDARG00000018190; Expressed in swim bladder and 29 other tissues.
DR ExpressionAtlas; Q6IQE5; baseline.
DR GO; GO:0043529; C:GET complex; IBA:GO_Central.
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; IDA:MGI.
DR GO; GO:0045048; P:protein insertion into ER membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0007416; P:synapse assembly; IMP:ZFIN.
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; Hydrolase;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transport; Zinc.
FT CHAIN 1..341
FT /note="ATPase GET3"
FT /id="PRO_0000348230"
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"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT HELIX 23..27
FT /evidence="ECO:0007829|PDB:7RU9"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:7RU9"
FT HELIX 44..56
FT /evidence="ECO:0007829|PDB:7RU9"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:7RU9"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:7RU9"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:7RU9"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:7RU9"
FT HELIX 117..132
FT /evidence="ECO:0007829|PDB:7RU9"
FT HELIX 136..151
FT /evidence="ECO:0007829|PDB:7RU9"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:7RU9"
FT HELIX 164..186
FT /evidence="ECO:0007829|PDB:7RU9"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:7RU9"
FT HELIX 210..230
FT /evidence="ECO:0007829|PDB:7RU9"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:7RU9"
FT STRAND 236..245
FT /evidence="ECO:0007829|PDB:7RU9"
FT HELIX 246..262
FT /evidence="ECO:0007829|PDB:7RU9"
FT STRAND 268..274
FT /evidence="ECO:0007829|PDB:7RU9"
FT HELIX 284..303
FT /evidence="ECO:0007829|PDB:7RU9"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:7RUA"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:7RU9"
FT HELIX 322..333
FT /evidence="ECO:0007829|PDB:7RU9"
SQ SEQUENCE 341 AA; 38339 MW; D66174356B02E21F CRC64;
MAASVEDEFE DAPDVEPLEP TLKNIIEQKS LKWIFVGGKG GVGKTTCSCS LAVQLAAVRE
SVLIISTDPA HNISDAFDQK FSKVPTKVKG YDNLFAMEID PSLGVAELPD EFFEEDNMLS
MGKKMMQEAM SAFPGIDEAM SYAEVMRLVK GMNFSVVVFD TAPTGHTLRL LNFPTIVERG
LGRLMQIKNQ ISPFISQMCN MLGLGDMNAD QLASKLEETL PVIRSVSEQF KDPEQTTFIC
VCIAEFLSLY ETERLIQELA KCRIDTHNII VNQLVFPDNE RPCKMCEARH KIQSKYLDQM
EDLYEDFHIV KLPLLPHEVR GADKVNTFSK QLLEPYSPPK K
