MGE1_ARATH
ID MGE1_ARATH Reviewed; 302 AA.
AC Q9FLP3; Q8LDE9;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=GrpE protein homolog 1, mitochondrial {ECO:0000303|PubMed:22128139};
DE Flags: Precursor;
GN Name=Mge1 {ECO:0000303|PubMed:22128139};
GN OrderedLocusNames=At5g55200 {ECO:0000312|Araport:AT5G55200};
GN ORFNames=MCO15.15 {ECO:0000312|EMBL:BAB08589.1};
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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].
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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17137349; DOI=10.1021/pr060403j;
RA Ito J., Heazlewood J.L., Millar A.H.;
RT "Analysis of the soluble ATP-binding proteome of plant mitochondria
RT identifies new proteins and nucleotide triphosphate interactions within the
RT matrix.";
RL J. Proteome Res. 5:3459-3469(2006).
RN [6]
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 [7]
RP INDUCTION BY UV-B, 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 (PubMed:17137349). Interacts with copper ions Cu(2+) (PubMed:20018591).
CC {ECO:0000250|UniProtKB:P38523, ECO:0000250|UniProtKB:Q9HAV7,
CC ECO:0000269|PubMed:17137349, ECO:0000269|PubMed:20018591}.
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:17137349}.
CC -!- INDUCTION: By UV-B. {ECO:0000269|PubMed:22128139}.
CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000305}.
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DR EMBL; AB010071; BAB08589.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96599.1; -; Genomic_DNA.
DR EMBL; AY042852; AAK68792.1; -; mRNA.
DR EMBL; AY081551; AAM10113.1; -; mRNA.
DR EMBL; AY086042; AAM63252.1; -; mRNA.
DR RefSeq; NP_200331.1; NM_124902.3.
DR AlphaFoldDB; Q9FLP3; -.
DR SMR; Q9FLP3; -.
DR IntAct; Q9FLP3; 4.
DR STRING; 3702.AT5G55200.1; -.
DR MetOSite; Q9FLP3; -.
DR PaxDb; Q9FLP3; -.
DR PRIDE; Q9FLP3; -.
DR ProteomicsDB; 250927; -.
DR EnsemblPlants; AT5G55200.1; AT5G55200.1; AT5G55200.
DR GeneID; 835613; -.
DR Gramene; AT5G55200.1; AT5G55200.1; AT5G55200.
DR KEGG; ath:AT5G55200; -.
DR Araport; AT5G55200; -.
DR TAIR; locus:2161615; AT5G55200.
DR eggNOG; KOG3003; Eukaryota.
DR HOGENOM; CLU_057217_1_0_1; -.
DR InParanoid; Q9FLP3; -.
DR OMA; MKDKFLR; -.
DR OrthoDB; 1525208at2759; -.
DR PhylomeDB; Q9FLP3; -.
DR PRO; PR:Q9FLP3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLP3; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; HDA: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; HDA:TAIR.
DR GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; HDA: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:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0009411; P:response to UV; 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 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Copper; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 40..302
FT /note="GrpE protein homolog 1, mitochondrial"
FT /id="PRO_0000441899"
FT REGION 77..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 20
FT /note="F -> L (in Ref. 4; AAM63252)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="R -> L (in Ref. 4; AAM63252)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 302 AA; 33203 MW; C57BF0D594D44726 CRC64;
MLVSRVLSRV SRSAGLRSSF SSVVTPKRNQ IPIVASRFHS LVHGTPNKLV AVPVSLRNHG
TLDLNVLQRF GFFSSSSAEP KGNESNTEVP KTGETSENVE VGKATDAEID FDDLSRDDLV
KLVSEKEDLL KVQQKDIMEM KDKFLRTYAE QQNLMDRTNR NAESAKKFAV QNFATSLLDV
ADNLERASSV VKESFSKIDT SKDLAGATPL LKNLLEGVEM TEKQLAEVFR KAGLVKEDPL
NEPFNPNRHN AVFQVPDASK PKGTIAHVLK SGYSLYDRVI RPAEVGVTCA VENQEGGKES
AA
