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   24-JAN-2024, entry version 142.
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,
RC   Pancreas, 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; 11.
DR   IntAct; Q9D880; 1.
DR   STRING; 10090.ENSMUSP00000080614; -.
DR   GlyGen; Q9D880; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9D880; -.
DR   PhosphoSitePlus; Q9D880; -.
DR   SwissPalm; Q9D880; -.
DR   EPD; Q9D880; -.
DR   jPOST; Q9D880; -.
DR   MaxQB; Q9D880; -.
DR   PaxDb; 10090-ENSMUSP00000080614; -.
DR   PeptideAtlas; Q9D880; -.
DR   ProteomicsDB; 259509; -.
DR   Pumba; Q9D880; -.
DR   Antibodypedia; 30377; 214 antibodies from 32 providers.
DR   DNASU; 66525; -.
DR   Ensembl; ENSMUST00000081946.5; ENSMUSP00000080614.5; ENSMUSG00000003438.18.
DR   GeneID; 66525; -.
DR   KEGG; mmu:66525; -.
DR   UCSC; uc009fyg.1; mouse.
DR   AGR; MGI:1913775; -.
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; WKSLHYY; -.
DR   OrthoDB; 11362at2759; -.
DR   PhylomeDB; Q9D880; -.
DR   TreeFam; TF106198; -.
DR   BioGRID-ORCS; 66525; 29 hits in 77 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 266 other cell types or tissues.
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   CDD; cd07521; HAD_FCP1-like; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR004274; FCP1_dom.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR12210:SF3; MITOCHONDRIAL IMPORT INNER MEMBRANE TRANSLOCASE SUBUNIT TIM50; 1.
DR   Pfam; PF03031; NIF; 1.
DR   SMART; SM00577; CPDc; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS50969; FCP1; 1.
DR   Genevisible; Q9D880; MM.
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
//