GET3A_ARATH
ID GET3A_ARATH Reviewed; 353 AA.
AC Q949M9; Q56ZR6;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=ATPase GET3A {ECO:0000305};
DE Short=AtGET3A {ECO:0000303|PubMed:28096354};
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 3 homolog A {ECO:0000305};
GN Name=GET3A {ECO:0000303|PubMed:28096354};
GN OrderedLocusNames=At1g01910 {ECO:0000312|Araport:AT1G01910};
GN ORFNames=F22M8.4 {ECO:0000312|EMBL:AEE27348.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 281-353.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [6]
RP INTERACTION WITH GET1 AND GET4, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF GLY-28.
RX PubMed=28096354; DOI=10.1073/pnas.1619525114;
RA Xing S., Mehlhorn D.G., Wallmeroth N., Asseck L.Y., Kar R., Voss A.,
RA Denninger P., Schmidt V.A., Schwarzlaender M., Stierhof Y.D., Grossmann G.,
RA Grefen C.;
RT "Loss of GET pathway orthologs in Arabidopsis thaliana causes root hair
RT growth defects and affects SNARE abundance.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E1544-E1553(2017).
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, where the tail-anchored protein is released
CC for insertion. This process is regulated by ATP binding and hydrolysis.
CC ATP binding drives the homodimer towards the closed dimer state,
CC facilitating recognition of newly synthesized TA membrane proteins. ATP
CC hydrolysis is required for insertion. Subsequently, the homodimer
CC reverts towards the open dimer state, lowering its affinity for the
CC membrane-bound receptor, and returning it to the cytosol to initiate a
CC new round of targeting (By similarity). Involved in the control of root
CC hair growth through the regulation of syntaxin SYP123 expression
CC (PubMed:28096354). {ECO:0000255|HAMAP-Rule:MF_03112,
CC ECO:0000269|PubMed:28096354}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with GET1 and GET4
CC (PubMed:28096354). {ECO:0000255|HAMAP-Rule:MF_03112,
CC ECO:0000269|PubMed:28096354}.
CC -!- INTERACTION:
CC Q949M9; Q9LFR3: GASA14; NbExp=2; IntAct=EBI-4426052, EBI-2293075;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:28096354}.
CC Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03112}. Endoplasmic reticulum
CC {ECO:0000255|HAMAP-Rule:MF_03112}.
CC -!- DISRUPTION PHENOTYPE: Strong reduction of root hair length.
CC {ECO:0000269|PubMed:28096354}.
CC -!- SIMILARITY: Belongs to the arsA ATPase family. {ECO:0000255|HAMAP-
CC Rule:MF_03112}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94314.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC020622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE27348.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27349.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27351.1; -; Genomic_DNA.
DR EMBL; AY051004; AAK93681.1; -; mRNA.
DR EMBL; AY122993; AAM67526.1; -; mRNA.
DR EMBL; AK220895; BAD94314.1; ALT_INIT; mRNA.
DR RefSeq; NP_001077445.1; NM_001083976.2.
DR RefSeq; NP_563640.1; NM_100071.3.
DR RefSeq; NP_849575.1; NM_179244.2.
DR AlphaFoldDB; Q949M9; -.
DR SMR; Q949M9; -.
DR IntAct; Q949M9; 42.
DR STRING; 3702.AT1G01910.4; -.
DR PaxDb; Q949M9; -.
DR ProteomicsDB; 191808; -.
DR EnsemblPlants; AT1G01910.1; AT1G01910.1; AT1G01910.
DR EnsemblPlants; AT1G01910.2; AT1G01910.2; AT1G01910.
DR EnsemblPlants; AT1G01910.4; AT1G01910.4; AT1G01910.
DR GeneID; 839305; -.
DR Gramene; AT1G01910.1; AT1G01910.1; AT1G01910.
DR Gramene; AT1G01910.2; AT1G01910.2; AT1G01910.
DR Gramene; AT1G01910.4; AT1G01910.4; AT1G01910.
DR KEGG; ath:AT1G01910; -.
DR Araport; AT1G01910; -.
DR TAIR; locus:2025467; AT1G01910.
DR eggNOG; KOG2825; Eukaryota.
DR InParanoid; Q949M9; -.
DR OMA; MDAPYEF; -.
DR OrthoDB; 992208at2759; -.
DR PhylomeDB; Q949M9; -.
DR PRO; PR:Q949M9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q949M9; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0043529; C:GET complex; IPI:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0043621; F:protein self-association; IPI:TAIR.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0045048; P:protein insertion into ER membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0048767; P:root hair elongation; IMP:TAIR.
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 ATP-binding; Coiled coil; Cytoplasm; Endoplasmic reticulum; Hydrolase;
KW Nucleotide-binding; Reference proteome; Transport.
FT CHAIN 1..353
FT /note="ATPase GET3A"
FT /id="PRO_0000449808"
FT COILED 320..353
FT /evidence="ECO:0000255"
FT ACT_SITE 56
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 27..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT BINDING 253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03112"
FT MUTAGEN 28
FT /note="G->A: Unable to complement get3a-1 mutant
FT phenotype."
FT /evidence="ECO:0000269|PubMed:28096354"
FT CONFLICT 319
FT /note="P -> T (in Ref. 4; BAD94314)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 39670 MW; B52CB9920F67CB7A CRC64;
MAADLPEATV QNILDQESLK WVFVGGKGGV GKTTCSSILA ICLASVRSSV LIISTDPAHN
LSDAFQQRFT KSPTLVQGFS NLFAMEVDPT VETDDMAGTD GMDGLFSDLA NAIPGIDEAM
SFAEMLKLVQ TMDYATIVFD TAPTGHTLRL LQFPATLEKG LSKLMSLKSR FGGLMTQMSR
MFGMEDEFGE DALLGRLEGL KDVIEQVNRQ FKDPDMTTFV CVCIPEFLSL YETERLVQEL
AKFEIDTHNI IINQVLYDDE DVESKLLRAR MRMQQKYLDQ FYMLYDDFNI TKLPLLPEEV
TGVEALKAFS HKFLTPYHPT TSRSNVEELE RKVHTLRLQL KTAEEELERV KSG
