TIM44_RAT
ID TIM44_RAT Reviewed; 453 AA.
AC O35094;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM44;
DE Flags: Precursor;
GN Name=Timm44; Synonyms=Mimt44, Tim44;
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 SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=9538267; DOI=10.1093/oxfordjournals.jbchem.a021997;
RA Ishihara N., Mihara K.;
RT "Identification of the protein import components of the rat mitochondrial
RT inner membrane, rTIM17, rTIM23, and rTIM44.";
RL J. Biochem. 123:722-732(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
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). Recruits mitochondrial HSP70 to drive protein
CC translocation into the matrix using ATP as an energy source (By
CC similarity). {ECO:0000250|UniProtKB:O35857,
CC ECO:0000250|UniProtKB:Q01852}.
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 (By similarity). The complex interacts with the TIMM23
CC component of the TIM23 complex. Interacts with SLC25A4/ANT1 and
CC SLC25A5/ANT2; leading to inhibit the presequence translocase TIMM23,
CC thereby promoting stabilization of PINK1 (By similarity).
CC {ECO:0000250|UniProtKB:O35857, ECO:0000250|UniProtKB:Q01852}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:9538267}; Peripheral membrane protein
CC {ECO:0000269|PubMed:9538267}; Matrix side {ECO:0000269|PubMed:9538267}.
CC Mitochondrion matrix {ECO:0000269|PubMed:9538267}.
CC -!- SIMILARITY: Belongs to the Tim44 family. {ECO:0000305}.
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DR EMBL; AB006452; BAA21820.1; -; mRNA.
DR PIR; JE0155; JE0155.
DR RefSeq; NP_058963.1; NM_017267.1.
DR AlphaFoldDB; O35094; -.
DR SMR; O35094; -.
DR BioGRID; 248258; 2.
DR CORUM; O35094; -.
DR IntAct; O35094; 4.
DR STRING; 10116.ENSRNOP00000001409; -.
DR iPTMnet; O35094; -.
DR PhosphoSitePlus; O35094; -.
DR jPOST; O35094; -.
DR PaxDb; O35094; -.
DR PRIDE; O35094; -.
DR GeneID; 29635; -.
DR KEGG; rno:29635; -.
DR UCSC; RGD:3864; rat.
DR CTD; 10469; -.
DR RGD; 3864; Timm44.
DR eggNOG; KOG2580; Eukaryota.
DR InParanoid; O35094; -.
DR OrthoDB; 1041560at2759; -.
DR PhylomeDB; O35094; -.
DR PRO; PR:O35094; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051087; F:chaperone binding; IPI:RGD.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; IEP:RGD.
DR GO; GO:0006886; P:intracellular protein transport; IMP:RGD.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR GO; GO:1905242; P:response to 3,3',5-triiodo-L-thyronine; IEP:RGD.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR017303; Tim44.
DR InterPro; IPR039544; Tim44-like.
DR InterPro; IPR007379; Tim44-like_dom.
DR PANTHER; PTHR10721; PTHR10721; 1.
DR Pfam; PF04280; Tim44; 1.
DR PIRSF; PIRSF037871; TIM44; 1.
DR SMART; SM00978; Tim44; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR TIGRFAMs; TIGR00984; 3a0801s03tim44; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Nucleotide-binding; Phosphoprotein; Protein transport; Reference proteome;
KW Transit peptide; Translocation; Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..453
FT /note="Mitochondrial import inner membrane translocase
FT subunit TIM44"
FT /id="PRO_0000034316"
FT BINDING 167..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 129
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43615"
FT MOD_RES 178
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35857"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43615"
FT MOD_RES 218
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35857"
SQ SEQUENCE 453 AA; 51060 MW; 387C685147C577A0 CRC64;
MAAAALRGGW CRCPRRCLGS GIQFLSSHNL PRGGSSYQIS RPGGELTLTK SYSSGSRKGF
LSGLLDNIKQ ELAQNKEMKE SIKKFRDEAK KLEESDALQE ARRKYKTIES ETVRTSEAIK
KKLGELTGTV KESLDEVSKS DLGRKIKEGV EEAARTAKQS AESVSKGGEK LGKTAAFKAI
SQGVESVKKE IDESVLGHTG TYRRPERLRK RTEFAGAKFK ESKVFEANEE ALGVVLHKDS
KWYQQWKDFK DNNVVFNRFF EMKMKYDESD NVLIRASRAL TDKVTDLLGG LFSKTEMSEV
LTEILRVDPT FDKDRFLHQC ETDIIPNILE AMISGELDIL KDWCYEATYN QLAHSIQQAK
ALGLQFHSRI LDISNVDLAM GKMMEQGPVL IVTFQAQLVM VIKNPKGEVF DGDPDKVLRM
LYVWALCRDQ EELNPYAAWR LLDISASSTE QIL
