GRPE1_RAT
ID GRPE1_RAT Reviewed; 217 AA.
AC P97576; Q4QRA3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=GrpE protein homolog 1, mitochondrial;
DE AltName: Full=Mt-GrpE#1;
DE Flags: Precursor;
GN Name=Grpel1; Synonyms=Grepel1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 28-54; 65-72; 110-120;
RP 170-196 AND 205-215.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8914984; DOI=10.1016/0014-5793(96)01100-3;
RA Naylor D.J., Hoogenraad N.J., Hoej P.B.;
RT "Isolation and characterisation of a cDNA encoding rat mitochondrial GrpE,
RT a stress-inducible nucleotide-exchange factor of ubiquitous appearance in
RT mammalian organs.";
RL FEBS Lett. 396:181-188(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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).
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.
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.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Particularly abundant in heart, kidney
CC and liver.
CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000305}.
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DR EMBL; U62940; AAC53534.1; -; mRNA.
DR EMBL; BC097312; AAH97312.1; -; mRNA.
DR RefSeq; NP_077813.1; NM_024487.4.
DR AlphaFoldDB; P97576; -.
DR SMR; P97576; -.
DR BioGRID; 249476; 3.
DR STRING; 10116.ENSRNOP00000008930; -.
DR iPTMnet; P97576; -.
DR PhosphoSitePlus; P97576; -.
DR SwissPalm; P97576; -.
DR jPOST; P97576; -.
DR PaxDb; P97576; -.
DR PRIDE; P97576; -.
DR Ensembl; ENSRNOT00000008932; ENSRNOP00000008930; ENSRNOG00000006593.
DR GeneID; 79563; -.
DR KEGG; rno:79563; -.
DR CTD; 80273; -.
DR RGD; 70947; Grpel1.
DR eggNOG; KOG3003; Eukaryota.
DR GeneTree; ENSGT00390000005589; -.
DR HOGENOM; CLU_057217_0_1_1; -.
DR InParanoid; P97576; -.
DR PhylomeDB; P97576; -.
DR TreeFam; TF105284; -.
DR PRO; PR:P97576; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000006593; Expressed in heart and 19 other tissues.
DR ExpressionAtlas; P97576; baseline and differential.
DR Genevisible; P97576; RN.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0051117; F:ATPase binding; IPI:RGD.
DR GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; ISO:RGD.
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; Direct protein sequencing; Mitochondrion;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:8914984"
FT CHAIN 28..217
FT /note="GrpE protein homolog 1, mitochondrial"
FT /id="PRO_0000013051"
FT MOD_RES 94
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LP6"
FT MOD_RES 94
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LP6"
FT MOD_RES 100
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LP6"
FT MOD_RES 120
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LP6"
FT MOD_RES 215
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9HAV7"
FT MOD_RES 215
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99LP6"
SQ SEQUENCE 217 AA; 24297 MW; 59A30DA6FC54C6B5 CRC64;
MAARCVRLAR RSLPALALSF RPSPRLLCTA TKQKNNGQNL EEDLGHCEPK TDPSSADKTL
LEEKVKLEEQ LKETMEKYKR ALADTENLRQ RSQKLVEEAK LYGIQGFCKD LLEVADILEK
ATQSVPKEEV SNNNPHLKSL YEGLVMTEVQ IQKVFTKHGL LRLDPIGAKF DPYEHEALFH
TPVEGKEPGT VALVSKVGYK LHGRTLRPAL VGVVKDA
