ID TIM44_MOUSE Reviewed; 452 AA. AC O35857; Q2NLC5; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 22-FEB-2023, entry version 155. DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM44; DE Flags: Precursor; GN Name=Timm44; Synonyms=Mimt44, Tim44; 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 [MRNA], AND SUBCELLULAR LOCATION. RC STRAIN=CD-1; TISSUE=Kidney; RX PubMed=9419343; DOI=10.1073/pnas.95.1.144; RA Wada J., Kanwar Y.S.; RT "Characterization of mammalian translocase of inner mitochondrial membrane RT (Tim44) isolated from diabetic newborn mouse kidney."; RL Proc. Natl. Acad. Sci. U.S.A. 95:144-149(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NMRI; 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 [4] 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 [5] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-177 AND LYS-217, 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 [6] RP FUNCTION, INTERACTION WITH TIMM23; SLC25A4 AND SLC25A5, AND MUTAGENESIS OF RP LYS-282. RX PubMed=31618756; DOI=10.1038/s41586-019-1667-4; RA Hoshino A., Wang W.J., Wada S., McDermott-Roe C., Evans C.S., Gosis B., RA Morley M.P., Rathi K.S., Li J., Li K., Yang S., McManus M.J., Bowman C., RA Potluri P., Levin M., Damrauer S., Wallace D.C., Holzbaur E.L.F., Arany Z.; RT "The ADP/ATP translocase drives mitophagy independent of nucleotide RT exchange."; RL Nature 575:375-379(2019). 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 (PubMed:31618756). Recruits mitochondrial HSP70 to drive protein CC translocation into the matrix using ATP as an energy source (By CC similarity). {ECO:0000250|UniProtKB:Q01852, CC ECO:0000269|PubMed:31618756}. 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 (PubMed:31618756). Interacts with CC SLC25A4/ANT1 and SLC25A5/ANT2; leading to inhibit the presequence CC translocase TIMM23, thereby promoting stabilization of PINK1 CC (PubMed:31618756). {ECO:0000250|UniProtKB:Q01852, CC ECO:0000269|PubMed:31618756}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000269|PubMed:9419343}; Peripheral membrane protein CC {ECO:0000269|PubMed:9419343}; Matrix side {ECO:0000269|PubMed:9419343}. CC -!- SIMILARITY: Belongs to the Tim44 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; U69898; AAB97624.1; -; mRNA. DR EMBL; CH466566; EDL21992.1; -; Genomic_DNA. DR EMBL; BC110677; AAI10678.1; -; mRNA. DR EMBL; BC117523; AAI17524.1; -; mRNA. DR EMBL; BC117524; AAI17525.1; -; mRNA. DR CCDS; CCDS22083.1; -. DR RefSeq; NP_035722.2; NM_011592.2. DR AlphaFoldDB; O35857; -. DR SMR; O35857; -. DR BioGRID; 204201; 41. DR IntAct; O35857; 2. DR MINT; O35857; -. DR STRING; 10090.ENSMUSP00000003029; -. DR iPTMnet; O35857; -. DR PhosphoSitePlus; O35857; -. DR SwissPalm; O35857; -. DR REPRODUCTION-2DPAGE; O35857; -. DR EPD; O35857; -. DR jPOST; O35857; -. DR MaxQB; O35857; -. DR PaxDb; O35857; -. DR PeptideAtlas; O35857; -. DR ProteomicsDB; 259508; -. DR Antibodypedia; 24720; 63 antibodies from 22 providers. DR DNASU; 21856; -. DR Ensembl; ENSMUST00000003029.14; ENSMUSP00000003029.8; ENSMUSG00000002949.16. DR GeneID; 21856; -. DR KEGG; mmu:21856; -. DR UCSC; uc009ktq.2; mouse. DR AGR; MGI:1343262; -. DR CTD; 10469; -. DR MGI; MGI:1343262; Timm44. DR VEuPathDB; HostDB:ENSMUSG00000002949; -. DR eggNOG; KOG2580; Eukaryota. DR GeneTree; ENSGT00390000000051; -. DR HOGENOM; CLU_020932_1_1_1; -. DR InParanoid; O35857; -. DR OMA; PVFVVTC; -. DR OrthoDB; 2873015at2759; -. DR PhylomeDB; O35857; -. DR TreeFam; TF106197; -. DR BioGRID-ORCS; 21856; 27 hits in 76 CRISPR screens. DR ChiTaRS; Timm44; mouse. DR PRO; PR:O35857; -. DR Proteomes; UP000000589; Chromosome 8. DR RNAct; O35857; protein. DR Bgee; ENSMUSG00000002949; Expressed in ciliary body and 259 other tissues. DR Genevisible; O35857; MM. DR GO; GO:0001650; C:fibrillar center; ISO:MGI. DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI. DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI. DR GO; GO:0005739; C:mitochondrion; HDA:MGI. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0051087; F:chaperone binding; ISO:MGI. DR GO; GO:0019899; F:enzyme binding; ISO:MGI. DR GO; GO:0006886; P:intracellular protein transport; ISO:MGI. DR GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central. DR Gene3D; 3.10.450.240; -; 1. 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; MITOCHONDRIAL IMPORT INNER MEMBRANE TRANSLOCASE SUBUNIT TIM44; 1. DR PANTHER; PTHR10721:SF1; MITOCHONDRIAL IMPORT INNER MEMBRANE TRANSLOCASE SUBUNIT TIM44; 1. DR Pfam; PF04280; Tim44; 1. DR PIRSF; PIRSF037871; TIM44; 1. DR SMART; SM00978; Tim44; 1. DR SUPFAM; SSF54427; NTF2-like; 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 ?..452 FT /note="Mitochondrial import inner membrane translocase FT subunit TIM44" FT /id="PRO_0000034315" FT BINDING 166..173 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT MOD_RES 128 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:O43615" FT MOD_RES 177 FT /note="N6-succinyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 180 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O43615" FT MOD_RES 217 FT /note="N6-succinyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MUTAGEN 282 FT /note="K->D: Abolished interaction with SLC25A4/ANT1." FT /evidence="ECO:0000269|PubMed:31618756" FT CONFLICT 5 FT /note="A -> R (in Ref. 1; AAB97624)" FT /evidence="ECO:0000305" SQ SEQUENCE 452 AA; 51091 MW; DC3E5F4E43972D2F CRC64; MAAAALRGGW CRCPRRCLGS GIQFLSSHNL PHGSSYQISR PGRELTLTKS YSSGSRKGFL SGLLDNIKQE LAKNKEMKES IKKFRDEAKK LEESDALQEA RRKYKSIESE TVRTSEAIKK KLGELTGTVK ESLDEVSKSD LGRKIKEGVE EAARTAKQSA ESVSKSGEKL GKTAAFKAIS QGVESVKKEL DESVLGQTGP YRRPERLRKR TEFAGAKFKE SKVFEANEEA LGVVLHKDSK WYQQWKDFKD NNVVFNRFFE MKMKYDESDN VLIRASRALT DKVTDLLGGL FSKTEMSEVL TEILRVDPTF DKDHFLHQCE TDIIPNILEA MISGELDILK DWCYEATYSQ LAHPIQQAKA LGFQFHSRIL DISNVDLAMG KMMEQGPVLI VTFQAQVVMV IKNSKGEVYD GDPDKVQRML YVWALCRDQE ELNPYAAWRL LDISASSTEQ IL //