GRPE2_MOUSE
ID GRPE2_MOUSE Reviewed; 224 AA.
AC O88396; Q3ULH8; Q9CQ97;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=GrpE protein homolog 2, mitochondrial;
DE AltName: Full=Mt-GrpE#2;
DE Flags: Precursor;
GN Name=Grpel2; Synonyms=Mt-grpel2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, Embryo, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-224.
RX PubMed=9694873; DOI=10.1074/jbc.273.33.21169;
RA Naylor D.J., Stines A.P., Hoogenraad N.J., Hoej P.B.;
RT "Evidence for the existence of distinct mammalian cytosolic, microsomal,
RT and two mitochondrial GrpE-like proteins, the co-chaperones of specific
RT Hsp70 members.";
RL J. Biol. Chem. 273:21169-21177(1998).
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
CC manner. Seems to control the nucleotide-dependent binding of
CC mitochondrial HSP70 to substrate proteins. Stimulates ATPase activity
CC of mt-HSP70. May also serve to modulate the interconversion of
CC oligomeric (inactive) and monomeric (active) forms of mt-HSP70.
CC -!- SUBUNIT: Probable component of the PAM complex at least composed of a
CC mitochondrial HSP70 protein, GRPEL1 or GRPEL2, TIMM44, TIMM16/PAM16 and
CC TIMM14/DNAJC19. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000305}.
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DR EMBL; AK003011; BAB22511.1; -; mRNA.
DR EMBL; AK012634; BAB28371.1; -; mRNA.
DR EMBL; AK082983; BAC38720.1; -; mRNA.
DR EMBL; AK145493; BAE26470.1; -; mRNA.
DR EMBL; AF041060; AAC31364.1; -; mRNA.
DR CCDS; CCDS29288.1; -.
DR RefSeq; NP_067271.1; NM_021296.2.
DR AlphaFoldDB; O88396; -.
DR SMR; O88396; -.
DR BioGRID; 201546; 4.
DR STRING; 10090.ENSMUSP00000053440; -.
DR PhosphoSitePlus; O88396; -.
DR EPD; O88396; -.
DR PaxDb; O88396; -.
DR PeptideAtlas; O88396; -.
DR PRIDE; O88396; -.
DR ProteomicsDB; 271337; -.
DR Antibodypedia; 3037; 122 antibodies from 20 providers.
DR DNASU; 17714; -.
DR Ensembl; ENSMUST00000062991; ENSMUSP00000053440; ENSMUSG00000024580.
DR GeneID; 17714; -.
DR KEGG; mmu:17714; -.
DR UCSC; uc008fco.1; mouse.
DR CTD; 134266; -.
DR MGI; MGI:1334416; Grpel2.
DR VEuPathDB; HostDB:ENSMUSG00000024580; -.
DR eggNOG; KOG3003; Eukaryota.
DR GeneTree; ENSGT00390000005589; -.
DR HOGENOM; CLU_057217_0_1_1; -.
DR InParanoid; O88396; -.
DR OMA; ICHVPAD; -.
DR OrthoDB; 1525208at2759; -.
DR PhylomeDB; O88396; -.
DR TreeFam; TF105284; -.
DR BioGRID-ORCS; 17714; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Grpel2; mouse.
DR PRO; PR:O88396; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; O88396; protein.
DR Bgee; ENSMUSG00000024580; Expressed in ear vesicle and 255 other tissues.
DR ExpressionAtlas; O88396; baseline and differential.
DR Genevisible; O88396; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
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:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IDA:MGI.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
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 Acetylation; Chaperone; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 32..224
FT /note="GrpE protein homolog 2, mitochondrial"
FT /id="PRO_0000013053"
FT MOD_RES 141
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8TAA5"
SQ SEQUENCE 224 AA; 25030 MW; ADCD75FA05C7B892 CRC64;
MAARSLWAVQ RLQRLLASGA MSESRGWLHP FSTATQRTAG EDCSSEDPPD GLGPSLAEQA
LRLKAVKLEK EVQDLTLRYQ RAVADCENIR RRTQRCVEDA KIFGIQSFCK DLVEVADILE
KTAKCCSEGA EPEDHRRTLE KVFQGLSLLE ARLKSVFTKH GLEKMTPIGD KYDPHEHELI
CHMPAGVGVQ PGTVALVRQD GYKLHGRTIR LAQVEVAVES QRRL
