ID M3Z444_MUSPF Unreviewed; 216 AA.
AC M3Z444;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=GrpE protein homolog {ECO:0000256|RuleBase:RU000640};
GN Name=LOC101690198 {ECO:0000313|RefSeq:XP_044925567.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000018356.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000018356.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_044925567.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_044925567.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|RuleBase:RU000640}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|RuleBase:RU000640}.
CC -!- SIMILARITY: Belongs to the GrpE family. {ECO:0000256|ARBA:ARBA00009054,
CC ECO:0000256|RuleBase:RU004478}.
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DR EMBL; AEYP01054464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_044925567.1; XM_045069632.1.
DR STRING; 9669.ENSMPUP00000018356; -.
DR Ensembl; ENSMPUT00000018626.1; ENSMPUP00000018356.1; ENSMPUG00000018474.1.
DR eggNOG; KOG3003; Eukaryota.
DR GeneTree; ENSGT00390000005589; -.
DR HOGENOM; CLU_057217_0_1_1; -.
DR OMA; MKMLANR; -.
DR OrthoDB; 151932at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd00446; GrpE; 1.
DR Gene3D; 3.90.20.20; -; 1.
DR Gene3D; 2.30.22.10; Head domain of nucleotide exchange factor GrpE; 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; GRPE PROTEIN; 1.
DR PANTHER; PTHR21237:SF25; GRPE PROTEIN HOMOLOG 1, MITOCHONDRIAL; 1.
DR Pfam; PF01025; GrpE; 1.
DR PRINTS; PR00773; GRPEPROTEIN.
DR SUPFAM; SSF58014; Coiled-coil domain of nucleotide exchange factor GrpE; 1.
DR SUPFAM; SSF51064; Head domain of nucleotide exchange factor GrpE; 1.
DR PROSITE; PS01071; GRPE; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU000640};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU000640};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT COILED 56..97
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 216 AA; 24179 MW; 4ECAC8765A19156E CRC64;
MAARCVRLAG QSLPAYLSLR PSPRLLCTAT KQKNSGQNLE EVVSQNEQKT DTPSPEKILL
DEKVKLEEQL KETVEKYKRA LADTENLRQR SQKLVEEAKL YGIQGFCKDL LEVADILEKA
TQSVPKEEVR DDNPHLKNLY EGLLMTEVQI QKVFTKHGLL LLNPVGARFD PYEHEALFHT
PVEGKEPGTV ALVSKVGYKL HGRTLRPALV GVVKAA
//
