TIM50_YEAST
ID TIM50_YEAST Reviewed; 476 AA.
AC Q02776; D6W3V2;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM50;
DE Flags: Precursor;
GN Name=TIM50; OrderedLocusNames=YPL063W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE TIM23 COMPLEX,
RP TRANSIT PEPTIDE CLEAVAGE SITE, LACK OF PHOSPHATASE ACTIVITY, FUNCTION,
RP SUBCELLULAR LOCATION, TOPOLOGY, AND INTERACTION WITH TIM23.
RX PubMed=12437924; DOI=10.1016/s0092-8674(02)01073-5;
RA Geissler A., Chacinska A., Truscott K.N., Wiedemann N., Brandner K.,
RA Sickmann A., Meyer H.E., Meisinger C., Pfanner N., Rehling P.;
RT "The mitochondrial presequence translocase: an essential role of Tim50 in
RT directing preproteins to the import channel.";
RL Cell 111:507-518(2002).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE TIM23 COMPLEX,
RP TRANSIT PEPTIDE CLEAVAGE SITE, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY,
RP AND INTERACTION WITH TIM23.
RX PubMed=12437925; DOI=10.1016/s0092-8674(02)01053-x;
RA Yamamoto H., Esaki M., Kanamori T., Tamura Y., Nishikawa S., Endo T.;
RT "Tim50 is a subunit of the TIM23 complex that links protein translocation
RT across the outer and inner mitochondrial membranes.";
RL Cell 111:519-528(2002).
RN [5]
RP FUNCTION, AND DOMAIN INTERMEMBRANE.
RX PubMed=14532110; DOI=10.1093/emboj/cdg532;
RA Chacinska A., Rehling P., Guiard B., Frazier A.E., Schulze-Specking A.,
RA Pfanner N., Voos W., Meisinger C.;
RT "Mitochondrial translocation contact sites: separation of dynamic and
RT stabilizing elements in formation of a TOM-TIM-preprotein supercomplex.";
RL EMBO J. 22:5370-5381(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP IDENTIFICATION IN THE TIM23 COMPLEX.
RX PubMed=15797382; DOI=10.1016/j.cell.2005.01.011;
RA Chacinska A., Lind M., Frazier A.E., Dudek J., Meisinger C., Geissler A.,
RA Sickmann A., Meyer H.E., Truscott K.N., Guiard B., Pfanner N., Rehling P.;
RT "Mitochondrial presequence translocase: switching between TOM tethering and
RT motor recruitment involves Tim21 and Tim17.";
RL Cell 120:817-829(2005).
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. Required to direct preproteins
CC in transit and direct them to the channel protein TIM23, and possibly
CC facilitates transfer of the translocating proteins from the TOM complex
CC to the TIM23 complex. Does not act as a structural subunit of the TIM23
CC complex but plays a dynamic role in protein import. Has no phosphatase
CC activity. {ECO:0000269|PubMed:12437924, ECO:0000269|PubMed:12437925,
CC ECO:0000269|PubMed:14532110}.
CC -!- SUBUNIT: Component of the TIM23 complex, at least composed of TIM23,
CC TIM17, TIM50 and TIM21. Interacts directly with TIM23. Interacts with
CC preproteins in transit. {ECO:0000269|PubMed:12437924,
CC ECO:0000269|PubMed:12437925, ECO:0000269|PubMed:15797382}.
CC -!- INTERACTION:
CC Q02776; P53220: TIM21; NbExp=10; IntAct=EBI-30302, EBI-23128;
CC Q02776; P32897: TIM23; NbExp=13; IntAct=EBI-30302, EBI-9136;
CC Q02776; Q02776: TIM50; NbExp=2; IntAct=EBI-30302, EBI-30302;
CC Q02776; P11884: Aldh2; Xeno; NbExp=3; IntAct=EBI-30302, EBI-916402;
CC Q02776; P00842: oli; Xeno; NbExp=5; IntAct=EBI-30302, EBI-9084292;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:12437924, ECO:0000269|PubMed:12437925,
CC ECO:0000269|PubMed:14562095}; Single-pass membrane protein
CC {ECO:0000269|PubMed:12437924, ECO:0000269|PubMed:12437925,
CC ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The mitochondrial intermembrane region is required for
CC generation but not stabilization of the TIM23 complex.
CC {ECO:0000269|PubMed:14532110}.
CC -!- DOMAIN: The FCP1 homology domain does not contain the canonical D-x-D-
CC x-[TV] active site, suggesting that it probably does not display
CC phosphatase activity. {ECO:0000269|PubMed:14532110}.
CC -!- MISCELLANEOUS: Present with 2400 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TIM50 family. {ECO:0000305}.
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DR EMBL; U39205; AAB68302.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11368.1; -; Genomic_DNA.
DR PIR; S60927; S60927.
DR RefSeq; NP_015262.1; NM_001183877.1.
DR PDB; 4QQF; X-ray; 2.67 A; A/B/C/D/E/F=164-361.
DR PDBsum; 4QQF; -.
DR AlphaFoldDB; Q02776; -.
DR BMRB; Q02776; -.
DR SMR; Q02776; -.
DR BioGRID; 36116; 238.
DR ComplexPortal; CPX-539; TIM23 mitochondrial inner membrane pre-sequence translocase complex, motor variant.
DR ComplexPortal; CPX-6127; TIM23 mitochondrial inner membrane pre-sequence translocase complex, sort variant.
DR DIP; DIP-8544N; -.
DR IntAct; Q02776; 21.
DR MINT; Q02776; -.
DR STRING; 4932.YPL063W; -.
DR TCDB; 3.A.8.1.1; the mitochondrial protein translocase (mpt) family.
DR MaxQB; Q02776; -.
DR PaxDb; Q02776; -.
DR PRIDE; Q02776; -.
DR EnsemblFungi; YPL063W_mRNA; YPL063W; YPL063W.
DR GeneID; 856042; -.
DR KEGG; sce:YPL063W; -.
DR SGD; S000005984; TIM50.
DR VEuPathDB; FungiDB:YPL063W; -.
DR eggNOG; KOG2832; Eukaryota.
DR GeneTree; ENSGT01040000240503; -.
DR HOGENOM; CLU_023309_1_2_1; -.
DR InParanoid; Q02776; -.
DR OMA; LGRNWDT; -.
DR BioCyc; YEAST:G3O-33972-MON; -.
DR PRO; PR:Q02776; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02776; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030943; F:mitochondrion targeting sequence binding; IDA:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IC:ComplexPortal.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IMP:SGD.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IC:ComplexPortal.
DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IDA:SGD.
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 3D-structure; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Protein transport; Reference proteome; Transit peptide; Translocation;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..43
FT /note="Mitochondrion"
FT /evidence="ECO:0000305|PubMed:12437924,
FT ECO:0000305|PubMed:12437925"
FT CHAIN 44..476
FT /note="Mitochondrial import inner membrane translocase
FT subunit TIM50"
FT /id="PRO_0000043139"
FT TOPO_DOM 44..114
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..476
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 187..330
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT REGION 67..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:4QQF"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:4QQF"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:4QQF"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:4QQF"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:4QQF"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:4QQF"
FT HELIX 221..228
FT /evidence="ECO:0007829|PDB:4QQF"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:4QQF"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:4QQF"
FT HELIX 242..248
FT /evidence="ECO:0007829|PDB:4QQF"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:4QQF"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:4QQF"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:4QQF"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:4QQF"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:4QQF"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:4QQF"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:4QQF"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:4QQF"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:4QQF"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:4QQF"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:4QQF"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:4QQF"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:4QQF"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:4QQF"
FT HELIX 324..332
FT /evidence="ECO:0007829|PDB:4QQF"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:4QQF"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:4QQF"
FT HELIX 351..354
FT /evidence="ECO:0007829|PDB:4QQF"
SQ SEQUENCE 476 AA; 55099 MW; 778D54F5C4ED27C8 CRC64;
MLSILRNSVR LNSRALRVVP SAANTLTSVQ ASRRLLTSYS SFLQKETKDD KPKSILTDDM
LFKAGVDVDE KGQGKNEETS GEGGEDKNEP SSKSEKSRRK RQTSTDIKRE KYANWFYIFS
LSALTGTAIY MARDWEPQES EELKKDIDNG YTLSLMYKRF KARFNSMFTY FQEPPFPDLL
PPPPPPPYQR PLTLVITLED FLVHSEWSQK HGWRTAKRPG ADYFLGYLSQ YYEIVLFSSN
YMMYSDKIAE KLDPIHAFVS YNLFKEHCVY KDGVHIKDLS KLNRDLSKVI IIDTDPNSYK
LQPENAIPME PWNGEADDKL VRLIPFLEYL ATQQTKDVRP ILNSFEDKKN LAEEFDHRVK
KLKDKFYGDH KSGGNWAMTA LGLGNSLGGS TKFPLDLIHE EGQKNYLMFM KMIEEEKEKI
RIQQEQMGGQ TFTLKDYVEG NLPSPEEQMK IQLEKQKEVD ALFEEEKKKK KIAESK
