ID TOM71_YEAST Reviewed; 639 AA.
AC P38825; D3DL67;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 27-MAR-2024, entry version 186.
DE RecName: Full=Protein TOM71;
DE AltName: Full=71 kDa mitochondrial outer membrane protein;
GN Name=TOM71; Synonyms=TOM72; OrderedLocusNames=YHR117W;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 SUBCELLULAR LOCATION.
RX PubMed=8612740; DOI=10.1016/0014-5793(96)00156-1;
RA Boemer U., Pfanner N., Dietmeier K.;
RT "Identification of a third yeast mitochondrial Tom protein with tetratrico
RT peptide repeats.";
RL FEBS Lett. 382:153-158(1996).
RN [4]
RP INTERACTION WITH TOM40 AND TOM70, AND SUBCELLULAR LOCATION.
RX PubMed=8663394; DOI=10.1074/jbc.271.30.17890;
RA Schlossmann J., Lill R., Neupert W., Court D.A.;
RT "Tom71, a novel homologue of the mitochondrial preprotein receptor Tom70.";
RL J. Biol. Chem. 271:17890-17895(1996).
RN [5]
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 [6]
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 [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [8]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16689936; DOI=10.1111/j.1742-4658.2006.05171.x;
RA Burri L., Vascotto K., Gentle I.E., Chan N.C., Beilharz T., Stapleton D.I.,
RA Ramage L., Lithgow T.;
RT "Integral membrane proteins in the mitochondrial outer membrane of
RT Saccharomyces cerevisiae.";
RL FEBS J. 273:1507-1515(2006).
RN [9]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16407407; DOI=10.1091/mbc.e05-08-0740;
RA Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N.,
RA Schoenfisch B., Guiard B., Pfanner N., Meisinger C.;
RT "Proteomic analysis of the yeast mitochondrial outer membrane reveals
RT accumulation of a subclass of preproteins.";
RL Mol. Biol. Cell 17:1436-1450(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [12]
RP FUNCTION, AND INTERACTION WITH MBF1.
RX PubMed=18007655; DOI=10.1038/sj.embor.7401113;
RA Kondo-Okamoto N., Shaw J.M., Okamoto K.;
RT "Tetratricopeptide repeat proteins Tom70 and Tom71 mediate yeast
RT mitochondrial morphogenesis.";
RL EMBO Rep. 9:63-69(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Involved in MBF1-mediated mitochondrial morphogenesis.
CC {ECO:0000269|PubMed:18007655}.
CC -!- SUBUNIT: Interacts with TOM40, TOM70 and MBF1.
CC {ECO:0000269|PubMed:18007655, ECO:0000269|PubMed:8663394}.
CC -!- INTERACTION:
CC P38825; P11484: SSB1; NbExp=2; IntAct=EBI-24694, EBI-8627;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:16407407, ECO:0000269|PubMed:16689936,
CC ECO:0000269|PubMed:8612740, ECO:0000269|PubMed:8663394}; Single-pass
CC membrane protein {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16407407,
CC ECO:0000269|PubMed:16689936, ECO:0000269|PubMed:8612740,
CC ECO:0000269|PubMed:8663394}.
CC -!- MISCELLANEOUS: Present with 4110 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the Tom70 family. {ECO:0000305}.
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DR EMBL; U00059; AAB68868.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06811.1; -; Genomic_DNA.
DR PIR; S48959; S48959.
DR RefSeq; NP_011985.1; NM_001179247.1.
DR PDB; 3FP2; X-ray; 1.98 A; A=107-639.
DR PDB; 3FP3; X-ray; 1.98 A; A=107-639.
DR PDB; 3FP4; X-ray; 2.14 A; A=107-639.
DR PDB; 3LCA; X-ray; 2.19 A; A=107-639.
DR PDBsum; 3FP2; -.
DR PDBsum; 3FP3; -.
DR PDBsum; 3FP4; -.
DR PDBsum; 3LCA; -.
DR AlphaFoldDB; P38825; -.
DR SMR; P38825; -.
DR BioGRID; 36550; 91.
DR DIP; DIP-5618N; -.
DR IntAct; P38825; 23.
DR STRING; 4932.YHR117W; -.
DR iPTMnet; P38825; -.
DR MaxQB; P38825; -.
DR PaxDb; 4932-YHR117W; -.
DR PeptideAtlas; P38825; -.
DR EnsemblFungi; YHR117W_mRNA; YHR117W; YHR117W.
DR GeneID; 856517; -.
DR KEGG; sce:YHR117W; -.
DR AGR; SGD:S000001159; -.
DR SGD; S000001159; TOM71.
DR VEuPathDB; FungiDB:YHR117W; -.
DR eggNOG; KOG0547; Eukaryota.
DR GeneTree; ENSGT00940000176538; -.
DR HOGENOM; CLU_017516_1_0_1; -.
DR InParanoid; P38825; -.
DR OMA; PTYYHRG; -.
DR OrthoDB; 1083789at2759; -.
DR BioCyc; YEAST:G3O-31159-MONOMER; -.
DR BioGRID-ORCS; 856517; 10 hits in 10 CRISPR screens.
DR EvolutionaryTrace; P38825; -.
DR PRO; PR:P38825; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38825; Protein.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0030943; F:mitochondrion targeting sequence binding; IBA:GO_Central.
DR GO; GO:0008320; F:protein transmembrane transporter activity; ISS:SGD.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0006626; P:protein targeting to mitochondrion; IMP:SGD.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR46208; MITOCHONDRIAL IMPORT RECEPTOR SUBUNIT TOM70; 1.
DR PANTHER; PTHR46208:SF1; MITOCHONDRIAL IMPORT RECEPTOR SUBUNIT TOM70; 1.
DR Pfam; PF00515; TPR_1; 2.
DR Pfam; PF14559; TPR_19; 1.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF48452; TPR-like; 3.
DR PROSITE; PS50005; TPR; 7.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..639
FT /note="Protein TOM71"
FT /id="PRO_0000106420"
FT TOPO_DOM 1..14
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT TRANSMEM 15..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..639
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REPEAT 127..160
FT /note="TPR 1"
FT REPEAT 162..194
FT /note="TPR 2"
FT REPEAT 345..378
FT /note="TPR 3"
FT REPEAT 379..411
FT /note="TPR 4"
FT REPEAT 412..445
FT /note="TPR 5"
FT REPEAT 447..479
FT /note="TPR 6"
FT REPEAT 480..513
FT /note="TPR 7"
FT REPEAT 530..563
FT /note="TPR 8"
FT REPEAT 565..597
FT /note="TPR 9"
FT REGION 45..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 120..139
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 147..156
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 161..174
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 177..190
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 195..208
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 211..221
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 235..251
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 266..274
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 278..283
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 295..306
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 310..331
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 338..357
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 361..374
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 378..387
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 395..407
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 412..424
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 428..441
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 447..458
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 462..475
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 481..492
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 496..512
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 521..534
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 543..559
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 564..576
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 580..593
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 598..617
FT /evidence="ECO:0007829|PDB:3FP2"
FT HELIX 620..626
FT /evidence="ECO:0007829|PDB:3FP3"
SQ SEQUENCE 639 AA; 71856 MW; B4AD583BB6CB466B CRC64;
MAENSLLRFI TKNKVAILAT VSAGTAAVGA YVYYQQIKQQ QQQQLKGTKD NRRQSEAFAG
QNEDEADLKD DGSVVSGSNK RKKKKNKRKR NNKAKSGEGF DYPSLPNGEP DIAQLKGLSP
SQRQAYAVQL KNRGNHFFTA KNFNEAIKYY QYAIELDPNE PVFYSNISAC YISTGDLEKV
IEFTTKALEI KPDHSKALLR RASANESLGN FTDAMFDLSV LSLNGDFDGA SIEPMLERNL
NKQAMKVLNE NLSKDEGRGS QVLPSNTSLA SFFGIFDSHL EVSSVNTSSN YDTAYALLSD
ALQRLYSATD EGYLVANDLL TKSTDMYHSL LSANTVDDPL RENAALALCY TGIFHFLKNN
LLDAQVLLQE SINLHPTPNS YIFLALTLAD KENSQEFFKF FQKAVDLNPE YPPTYYHRGQ
MYFILQDYKN AKEDFQKAQS LNPENVYPYI QLACLLYKQG KFTESEAFFN ETKLKFPTLP
EVPTFFAEIL TDRGDFDTAI KQYDIAKRLE EVQEKIHVGI GPLIGKATIL ARQSSQDPTQ
LDEEKFNAAI KLLTKACELD PRSEQAKIGL AQLKLQMEKI DEAIELFEDS AILARTMDEK
LQATTFAEAA KIQKRLRADP IISAKMELTL ARYRAKGML
//
