TIM50_MOUSE
ID TIM50_MOUSE Reviewed; 353 AA.
AC Q9D880; Q8R3A7; Q91Z17;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM50;
DE Flags: Precursor;
GN Name=Timm50; Synonyms=Tim50;
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].
RC STRAIN=C57BL/6J;
RX PubMed=15044455; DOI=10.1074/jbc.m402049200;
RA Guo Y., Cheong N., Zhang Z., De Rose R., Deng Y., Farber S.A.,
RA Fernandes-Alnemri T., Alnemri E.S.;
RT "Tim50, a component of the mitochondrial translocator, regulates
RT mitochondrial integrity and cell death.";
RL J. Biol. Chem. 279:24813-24825(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Placenta, and Small intestine;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-353.
RC STRAIN=FVB/N, and FVB/N-3; TISSUE=Mammary gland;
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 PROTEIN SEQUENCE OF 48-64 AND 275-284, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
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).
CC -!- FUNCTION: Essential component of the TIM23 complex, a complex that
CC mediates the translocation of transit peptide-containing proteins
CC across the mitochondrial inner membrane. Has some phosphatase activity
CC in vitro; however such activity may not be relevant in vivo.
CC {ECO:0000250|UniProtKB:Q3ZCQ8}.
CC -!- SUBUNIT: Component of the TIM23 complex at least composed of TIMM23,
CC TIMM17 (TIMM17A or TIMM17B) and TIMM50; within this complex, directly
CC interacts with TIMM23. The complex interacts with the TIMM44 component
CC of the PAM complex and with DNAJC15. {ECO:0000250|UniProtKB:Q3ZCQ8}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q3ZCQ8}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q3ZCQ8}.
CC -!- SIMILARITY: Belongs to the TIM50 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH10303.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY551342; AAT01209.1; -; mRNA.
DR EMBL; AK008340; BAB25615.1; -; mRNA.
DR EMBL; AK167473; BAE39556.1; -; mRNA.
DR EMBL; BC010303; AAH10303.1; ALT_INIT; mRNA.
DR EMBL; BC025844; AAH25844.1; -; mRNA.
DR CCDS; CCDS21039.1; -.
DR RefSeq; NP_079892.1; NM_025616.3.
DR AlphaFoldDB; Q9D880; -.
DR SMR; Q9D880; -.
DR BioGRID; 211535; 7.
DR IntAct; Q9D880; 1.
DR STRING; 10090.ENSMUSP00000080614; -.
DR iPTMnet; Q9D880; -.
DR PhosphoSitePlus; Q9D880; -.
DR SwissPalm; Q9D880; -.
DR EPD; Q9D880; -.
DR jPOST; Q9D880; -.
DR MaxQB; Q9D880; -.
DR PaxDb; Q9D880; -.
DR PeptideAtlas; Q9D880; -.
DR PRIDE; Q9D880; -.
DR ProteomicsDB; 259509; -.
DR Antibodypedia; 30377; 187 antibodies from 32 providers.
DR DNASU; 66525; -.
DR Ensembl; ENSMUST00000081946; ENSMUSP00000080614; ENSMUSG00000003438.
DR GeneID; 66525; -.
DR KEGG; mmu:66525; -.
DR UCSC; uc009fyg.1; mouse.
DR CTD; 92609; -.
DR MGI; MGI:1913775; Timm50.
DR VEuPathDB; HostDB:ENSMUSG00000003438; -.
DR eggNOG; KOG2832; Eukaryota.
DR GeneTree; ENSGT01040000240503; -.
DR HOGENOM; CLU_048293_1_1_1; -.
DR InParanoid; Q9D880; -.
DR OMA; FSFWAIY; -.
DR OrthoDB; 648380at2759; -.
DR PhylomeDB; Q9D880; -.
DR TreeFam; TF106198; -.
DR BioGRID-ORCS; 66525; 29 hits in 72 CRISPR screens.
DR ChiTaRS; Timm50; mouse.
DR PRO; PR:Q9D880; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9D880; protein.
DR Bgee; ENSMUSG00000003438; Expressed in dorsal pancreas and 263 other tissues.
DR Genevisible; Q9D880; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; ISS:UniProtKB.
DR GO; GO:0005134; F:interleukin-2 receptor binding; ISO:MGI.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; ISO:MGI.
DR GO; GO:0007006; P:mitochondrial membrane organization; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; ISO:MGI.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR027111; Tim50.
DR PANTHER; PTHR12210:SF3; PTHR12210:SF3; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transit peptide; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 22..353
FT /note="Mitochondrial import inner membrane translocase
FT subunit TIM50"
FT /id="PRO_0000043116"
FT TOPO_DOM 22..65
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..353
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 143..286
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT REGION 23..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3ZCQ8"
SQ SEQUENCE 353 AA; 39776 MW; 1BAC1FD183C532F4 CRC64;
MAASAALFSR LRSGLRVGAR GLCTRLAPPP PRTPEQVTEI ANRGGSKAQG PQHQPGSEGP
SYAKKIALWI AGLLGAGGTV SIVYIFGNNP VDENGTKIPD EFDSDPILVQ QLRRTYKYFK
DYRQMIIEPT SPCLLPDPLR EPYYQPPYTL VLELTGVLLH PEWSLATGWR FKKRPGIETL
FQQLAPLYEI VIFTSETGMT AFPLIDSVDP HGFISYRLFR DATRYMEGHH VKDISCLNRD
PARVVVVDCK KEAFRLQPFN GVALRPWDGN SDDRVLLDLS AFLKTIALNQ VEDVRTVLEH
YALEDDPLEA FKQRQSRLEQ EEQQRLAELS KSNRQGLSFG SLASRLWPRS KQP
