GRPE1_MOUSE
ID GRPE1_MOUSE Reviewed; 217 AA.
AC Q99LP6; Q3TSZ3;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=GrpE protein homolog 1, mitochondrial;
DE AltName: Full=Mt-GrpE#1;
DE Flags: Precursor;
GN Name=Grpel1;
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, and NOD; TISSUE=Cerebellum, Liver, and Thymus;
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 [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-94; LYS-120 AND LYS-215, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-94; LYS-100 AND LYS-215, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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 (By similarity).
CC {ECO:0000250}.
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. Binds to HSP70, HSC70 and HSJ1B (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK048732; BAC33437.1; -; mRNA.
DR EMBL; AK050445; BAC34257.1; -; mRNA.
DR EMBL; AK089113; BAC40758.1; -; mRNA.
DR EMBL; AK161688; BAE36532.1; -; mRNA.
DR EMBL; BC002284; AAH02284.1; -; mRNA.
DR CCDS; CCDS19238.1; -.
DR RefSeq; NP_077798.1; NM_024478.2.
DR AlphaFoldDB; Q99LP6; -.
DR SMR; Q99LP6; -.
DR BioGRID; 201545; 10.
DR IntAct; Q99LP6; 3.
DR STRING; 10090.ENSMUSP00000031099; -.
DR iPTMnet; Q99LP6; -.
DR PhosphoSitePlus; Q99LP6; -.
DR SwissPalm; Q99LP6; -.
DR UCD-2DPAGE; Q99LP6; -.
DR EPD; Q99LP6; -.
DR jPOST; Q99LP6; -.
DR MaxQB; Q99LP6; -.
DR PaxDb; Q99LP6; -.
DR PeptideAtlas; Q99LP6; -.
DR PRIDE; Q99LP6; -.
DR ProteomicsDB; 271101; -.
DR Antibodypedia; 22707; 155 antibodies from 24 providers.
DR DNASU; 17713; -.
DR Ensembl; ENSMUST00000031099; ENSMUSP00000031099; ENSMUSG00000029198.
DR GeneID; 17713; -.
DR KEGG; mmu:17713; -.
DR UCSC; uc008xep.1; mouse.
DR CTD; 80273; -.
DR MGI; MGI:1334417; Grpel1.
DR VEuPathDB; HostDB:ENSMUSG00000029198; -.
DR eggNOG; KOG3003; Eukaryota.
DR GeneTree; ENSGT00390000005589; -.
DR HOGENOM; CLU_057217_0_1_1; -.
DR InParanoid; Q99LP6; -.
DR OMA; YAYEKIA; -.
DR OrthoDB; 1525208at2759; -.
DR PhylomeDB; Q99LP6; -.
DR TreeFam; TF105284; -.
DR BioGRID-ORCS; 17713; 28 hits in 74 CRISPR screens.
DR ChiTaRS; Grpel1; mouse.
DR PRO; PR:Q99LP6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q99LP6; protein.
DR Bgee; ENSMUSG00000029198; Expressed in facial nucleus and 266 other tissues.
DR Genevisible; Q99LP6; MM.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO: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:0001671; F:ATPase activator activity; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; ISO: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 1: Evidence at protein level;
KW Acetylation; Chaperone; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 28..217
FT /note="GrpE protein homolog 1, mitochondrial"
FT /id="PRO_0000013050"
FT REGION 37..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 94
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 94
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 100
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 120
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 215
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 215
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 217 AA; 24307 MW; BE7A6D26A9C5B329 CRC64;
MAARCVRLAR RSLPALALSF RPSPRLLCTA TKQKNNGQNL DEDLGHCEPK TDPPSADKTL
LEEKAKLEEQ LRETMEKYKR ALADTENLRQ RSQKLVEEAK LYGIQGFCKD LLEVADILEK
ATQSVPKEEI SNNNPHLKSL YEGLVMTEVQ IQKVFTKHGL LRLDPIGAKF DPYEHEALFH
TPVEGKEPGT VALVSKVGYK LHGRTLRPAL VGVVKDA
