(data stored in SCRATCH zone)

SWISSPROT: MGE2_ARATH

ID   MGE2_ARATH              Reviewed;         327 AA.
AC   Q8LB47; Q96515; Q9SZ18;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   11-DEC-2019, entry version 138.
DE   RecName: Full=GrpE protein homolog 2, mitochondrial {ECO:0000303|PubMed:22128139};
DE   Flags: Precursor;
GN   Name=Mge2 {ECO:0000303|PubMed:22128139};
GN   Synonyms=AR192 {ECO:0000303|PubMed:9287109};
GN   OrderedLocusNames=At4g26780 {ECO:0000312|Araport:AT4G26780};
GN   ORFNames=F10M23.120 {ECO:0000312|EMBL:CAB36524.1};
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 43-327.
RX   PubMed=9287109; DOI=10.1016/s0014-5793(97)00871-5;
RA   Hirayama T., Ishida C., Kuromori T., Obata S., Shimoda C., Yamamoto M.,
RA   Shinozaki K., Ohto C.;
RT   "Functional cloning of a cDNA encoding Mei2-like protein from Arabidopsis
RT   thaliana using a fission yeast pheromone receptor deficient mutant.";
RL   FEBS Lett. 413:16-20(1997).
RN   [7]
RP   FUNCTION.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=20018591; DOI=10.1104/pp.109.147942;
RA   Tan Y.-F., O'Toole N., Taylor N.L., Millar A.H.;
RT   "Divalent metal ions in plant mitochondria and their role in interactions
RT   with proteins and oxidative stress-induced damage to respiratory
RT   function.";
RL   Plant Physiol. 152:747-761(2010).
RN   [8]
RP   FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY HEAT, SUBCELLULAR LOCATION,
RP   GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=22128139; DOI=10.1104/pp.111.187674;
RA   Hu C., Lin S.Y., Chi W.T., Charng Y.Y.;
RT   "Recent gene duplication and subfunctionalization produced a mitochondrial
RT   GrpE, the nucleotide exchange factor of the Hsp70 complex, specialized in
RT   thermotolerance to chronic heat stress in Arabidopsis.";
RL   Plant Physiol. 158:747-758(2012).
CC   -!- FUNCTION: Essential component of the PAM complex, a complex required
CC       for the translocation of transit peptide-containing proteins from the
CC       inner membrane into the mitochondrial matrix in an ATP-dependent manner
CC       (By similarity). Seems to control the nucleotide-dependent binding of
CC       mitochondrial HSP70 to substrate proteins (By similarity). Binds ATP
CC       (By similarity). Interacts with copper ions Cu(2+) (PubMed:20018591).
CC       Confers thermotolerance to long-term exposure at moderately high
CC       temperature (TMHT at 35 degrees Celsius) (PubMed:22128139).
CC       {ECO:0000250|UniProtKB:P38523, ECO:0000250|UniProtKB:Q9FLP3,
CC       ECO:0000250|UniProtKB:Q9HAV7, ECO:0000269|PubMed:20018591,
CC       ECO:0000269|PubMed:22128139}.
CC   -!- SUBUNIT: Probable component of the PAM complex, at least composed of
CC       SSC1 (mtHsp70), MGE1, TIM44, PAM16/TIM16, PAM17 and PAM18/TIM14.
CC       Interacts with SSQ1. {ECO:0000250|UniProtKB:P38523}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000269|PubMed:22128139}.
CC   -!- INDUCTION: Induced by heat treatment at 38 degrees Celsius in a HSFA1-
CC       dependent manner (at protein level). {ECO:0000269|PubMed:22128139}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype in normal conditions.
CC       Defective for thermotolerance to moderately high temperature (TMHT at
CC       35 degrees Celsius), but normal basal thermotolerance (BT), short-term
CC       acquired thermotolerance (SAT) and long-term acquired thermotolerance
CC       (LAT) at 37 and 44 degrees Celsius. {ECO:0000269|PubMed:22128139}.
CC   -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA13686.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAA13686.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAB36524.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79533.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AL035440; CAB36524.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161565; CAB79533.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE85251.1; -; Genomic_DNA.
DR   EMBL; AK118205; BAC42827.1; -; mRNA.
DR   EMBL; BT006047; AAP04032.1; -; mRNA.
DR   EMBL; AY087425; AAM64973.1; -; mRNA.
DR   EMBL; D88745; BAA13686.1; ALT_SEQ; mRNA.
DR   PIR; T04801; T04801.
DR   RefSeq; NP_567757.1; NM_118812.4.
DR   SMR; Q8LB47; -.
DR   IntAct; Q8LB47; 1.
DR   STRING; 3702.AT4G26780.1; -.
DR   PaxDb; Q8LB47; -.
DR   PRIDE; Q8LB47; -.
DR   EnsemblPlants; AT4G26780.1; AT4G26780.1; AT4G26780.
DR   GeneID; 828785; -.
DR   Gramene; AT4G26780.1; AT4G26780.1; AT4G26780.
DR   KEGG; ath:AT4G26780; -.
DR   Araport; AT4G26780; -.
DR   TAIR; locus:2116277; AT4G26780.
DR   eggNOG; KOG3003; Eukaryota.
DR   eggNOG; COG0576; LUCA.
DR   HOGENOM; HOG000252083; -.
DR   InParanoid; Q8LB47; -.
DR   KO; K03687; -.
DR   OMA; KNEKCNT; -.
DR   OrthoDB; 1525208at2759; -.
DR   PhylomeDB; Q8LB47; -.
DR   PRO; PR:Q8LB47; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8LB47; baseline and differential.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0001405; C:PAM complex, Tim23 associated import motor; IBA:GO_Central.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR   GO; GO:0005507; F:copper ion binding; IDA:TAIR.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0010286; P:heat acclimation; IMP:UniProtKB.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0009408; P:response to heat; IEP:TAIR.
DR   CDD; cd00446; GrpE; 1.
DR   Gene3D; 2.30.22.10; -; 1.
DR   Gene3D; 3.90.20.20; -; 1.
DR   HAMAP; MF_01151; GrpE; 1.
DR   InterPro; IPR000740; GrpE.
DR   InterPro; IPR013805; GrpE_coiled_coil.
DR   InterPro; IPR009012; GrpE_head.
DR   PANTHER; PTHR21237; PTHR21237; 1.
DR   Pfam; PF01025; GrpE; 1.
DR   PRINTS; PR00773; GRPEPROTEIN.
DR   SUPFAM; SSF51064; SSF51064; 1.
DR   SUPFAM; SSF58014; SSF58014; 1.
DR   PROSITE; PS01071; GRPE; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q8LB47.
DR   SWISS-2DPAGE; Q8LB47.
KW   ATP-binding; Chaperone; Copper; Metal-binding; Mitochondrion;
KW   Nucleotide-binding; Reference proteome; Stress response; Transit peptide.
FT   TRANSIT         1..39
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..327
FT                   /note="GrpE protein homolog 2, mitochondrial"
FT                   /id="PRO_0000441900"
SQ   SEQUENCE   327 AA;  36116 MW;  DEE814C6BEF552F8 CRC64;
     MLVLRILSRV TRNAGIRSSL SAVTLPARNQ TPVFSSRFHS LAHDFSHKLV PAQMSMMDSF
     ALQRFNFSSS TSPESDEKKT HTEASKTSEE KPTAEANQPG LDSESKDSVT DSAKRKRKGA
     KGAASSSSES DSESDDDELS ADDLVKLVAE KEELLSEKEE EIKQLKDKVL RTYAEMENVM
     DRTRRDAENT KKYAVQNFAK SLLDVADNLG RASSVVKESF SKLDTSEDSA GAAPLLKTLL
     EGVEMTEKQL AEVFKKFGME KYDPINEPFD PNRHNAVFQV PDASKPEGTV AHVLKSGYTL
     YDRVIRPAEV GVTQGGENQE EKKESDA
//

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