GET3B_ARATH
ID GET3B_ARATH Reviewed; 411 AA.
AC A1L4Y1; Q9SS46;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=ATPase GET3B {ECO:0000305};
DE Short=AtGET3B {ECO:0000303|PubMed:28096354};
DE EC=3.6.-.- {ECO:0000305};
DE AltName: Full=Guided entry of tail-anchored proteins 3 homolog B {ECO:0000305};
DE Flags: Precursor;
GN Name=GET3B {ECO:0000303|PubMed:28096354};
GN OrderedLocusNames=At3g10350 {ECO:0000312|Araport:AT3G10350};
GN ORFNames=F14P13.5 {ECO:0000312|EMBL:AAF02825.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 [MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:28096354}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:28096354}.
CC -!- SIMILARITY: Belongs to the arsA ATPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF02825.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009400; AAF02825.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74894.1; -; Genomic_DNA.
DR EMBL; BT029768; ABM06038.1; -; mRNA.
DR RefSeq; NP_187646.2; NM_111870.3.
DR AlphaFoldDB; A1L4Y1; -.
DR SMR; A1L4Y1; -.
DR PRIDE; A1L4Y1; -.
DR ProteomicsDB; 181222; -.
DR EnsemblPlants; AT3G10350.1; AT3G10350.1; AT3G10350.
DR GeneID; 820197; -.
DR Gramene; AT3G10350.1; AT3G10350.1; AT3G10350.
DR KEGG; ath:AT3G10350; -.
DR Araport; AT3G10350; -.
DR HOGENOM; CLU_040761_2_1_1; -.
DR OMA; DAMMLDM; -.
DR PhylomeDB; A1L4Y1; -.
DR PRO; PR:A1L4Y1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; A1L4Y1; baseline and differential.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR025723; Anion-transp_ATPase-like_dom.
DR InterPro; IPR016300; ATPase_ArsA/GET3.
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; Chloroplast; Hydrolase; Nucleotide-binding; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..67
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 68..411
FT /note="ATPase GET3B"
FT /id="PRO_0000449809"
FT ACT_SITE 124
FT /evidence="ECO:0000250|UniProtKB:Q949M9"
FT BINDING 95..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q949M9"
FT BINDING 348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q949M9"
SQ SEQUENCE 411 AA; 44754 MW; 13CE776D5FC6D7D5 CRC64;
MATLSSYLLS SPPLCKSRFS ATSLVSGIDF ISFSPRTTLS SSSTVLPAIL SLSVKHNRRR
NSLQVKSVAS PTETISEFDE MVSGTKRKYY MLGGKGGVGK TSCAASLAVR FANNGHPTLV
VSTDPAHSLS DSFAQDLTGG MLVPVEGPEA PLFALEINPE KAREEFRSAS QMNGGTGVKD
FMDGMGLGML VEQLGELKLG ELLDTPPPGL DEAIAISKVI QFLESPEYNM FTRIVFDTAP
TGHTLRLLSL PDFLDASIGK ILKLRQKITS ATSAIKSVFG KEEKGPDAAD KLEKLRERMV
KVRELFRDTE STEFVIVTIP TVMAVSESSR LSASLKKESV PVKRLIVNQL LPPSSSDCKF
CSIKRKDQMR ALDMIREDSE LSALTLMEAP LVDMEIRGVP ALRFLGDIIW K
