TOM40_YEAST
ID TOM40_YEAST Reviewed; 387 AA.
AC P23644; D6W028; Q6B1Q9;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Mitochondrial import receptor subunit TOM40;
DE AltName: Full=Mitochondrial import site protein ISP42;
DE AltName: Full=Translocase of outer membrane 40 kDa subunit;
GN Name=TOM40; Synonyms=ISP42, MOM38; OrderedLocusNames=YMR203W;
GN ORFNames=YM8325.04;
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 [GENOMIC DNA].
RX PubMed=2250717; DOI=10.1038/348605a0;
RA Baker K.P., Schaniel A., Vestweber D., Schatz G.;
RT "A yeast mitochondrial outer membrane protein essential for protein import
RT and cell viability.";
RL Nature 348:605-609(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP IDENTIFICATION IN THE TOM COMPLEX.
RX PubMed=9774667; DOI=10.1128/mcb.18.11.6515;
RA Dekker P.J.T., Ryan M.T., Brix J., Mueller H., Hoenlinger A., Pfanner N.;
RT "Preprotein translocase of the outer mitochondrial membrane: molecular
RT dissection and assembly of the general import pore complex.";
RL Mol. Cell. Biol. 18:6515-6524(1998).
RN [6]
RP FUNCTION.
RX PubMed=10427088; DOI=10.1083/jcb.146.2.321;
RA Rapaport D., Neupert W.;
RT "Biogenesis of Tom40, core component of the TOM complex of mitochondria.";
RL J. Cell Biol. 146:321-331(1999).
RN [7]
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 [8]
RP INTERACTION WITH FCJ1.
RX PubMed=21944719; DOI=10.1016/j.devcel.2011.08.026;
RA von der Malsburg K., Muller J.M., Bohnert M., Oeljeklaus S.,
RA Kwiatkowska P., Becker T., Loniewska-Lwowska A., Wiese S., Rao S.,
RA Milenkovic D., Hutu D.P., Zerbes R.M., Schulze-Specking A., Meyer H.E.,
RA Martinou J.C., Rospert S., Rehling P., Meisinger C., Veenhuis M.,
RA Warscheid B., van der Klei I.J., Pfanner N., Chacinska A., van der Laan M.;
RT "Dual role of mitofilin in mitochondrial membrane organization and protein
RT biogenesis.";
RL Dev. Cell 21:694-707(2011).
CC -!- FUNCTION: Channel-forming protein essential for import of protein
CC precursors into mitochondria. {ECO:0000269|PubMed:10427088}.
CC -!- SUBUNIT: Forms part of the preprotein translocase complex of the outer
CC mitochondrial membrane (TOM complex) which consists of at least 7
CC different proteins (TOM5, TOM6, TOM7, TOM20, TOM22, TOM40 and TOM70).
CC Interacts with mitochondrial targeting sequences. Interacts with FCJ1.
CC {ECO:0000269|PubMed:21944719, ECO:0000269|PubMed:9774667}.
CC -!- INTERACTION:
CC P23644; P53969: SAM50; NbExp=4; IntAct=EBI-12539, EBI-28646;
CC P23644; P35180: TOM20; NbExp=3; IntAct=EBI-12539, EBI-12522;
CC P23644; P49334: TOM22; NbExp=8; IntAct=EBI-12539, EBI-12527;
CC P23644; Q07812: BAX; Xeno; NbExp=2; IntAct=EBI-12539, EBI-516580;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the Tom40 family. {ECO:0000305}.
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DR EMBL; X56885; CAA40206.1; -; Genomic_DNA.
DR EMBL; Z48755; CAA88644.1; -; Genomic_DNA.
DR EMBL; AY693021; AAT93040.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10102.1; -; Genomic_DNA.
DR PIR; S12773; S12773.
DR RefSeq; NP_013930.1; NM_001182710.1.
DR PDB; 6JNF; EM; 3.81 A; A/F=1-387.
DR PDB; 6UCU; EM; 3.06 A; A/I=1-387.
DR PDB; 6UCV; EM; 4.10 A; A/I/a/i=1-387.
DR PDB; 7E4H; EM; 3.01 A; D=1-387.
DR PDB; 7E4I; EM; 3.05 A; D=2-387.
DR PDBsum; 6JNF; -.
DR PDBsum; 6UCU; -.
DR PDBsum; 6UCV; -.
DR PDBsum; 7E4H; -.
DR PDBsum; 7E4I; -.
DR AlphaFoldDB; P23644; -.
DR SMR; P23644; -.
DR BioGRID; 35381; 63.
DR ComplexPortal; CPX-473; TOM40 mitochondrial outer membrane translocase core complex.
DR ComplexPortal; CPX-474; TOM40 mitochondrial outer membrane translocase holocomplex.
DR DIP; DIP-2540N; -.
DR IntAct; P23644; 17.
DR MINT; P23644; -.
DR STRING; 4932.YMR203W; -.
DR TCDB; 1.B.8.2.1; the mitochondrial and plastid porin (mpp) family.
DR TCDB; 3.A.8.1.1; the mitochondrial protein translocase (mpt) family.
DR iPTMnet; P23644; -.
DR MaxQB; P23644; -.
DR PaxDb; P23644; -.
DR PRIDE; P23644; -.
DR EnsemblFungi; YMR203W_mRNA; YMR203W; YMR203W.
DR GeneID; 855243; -.
DR KEGG; sce:YMR203W; -.
DR SGD; S000004816; TOM40.
DR VEuPathDB; FungiDB:YMR203W; -.
DR eggNOG; KOG3296; Eukaryota.
DR GeneTree; ENSGT00390000003308; -.
DR HOGENOM; CLU_042174_0_0_1; -.
DR InParanoid; P23644; -.
DR OMA; SHQFAMG; -.
DR BioCyc; YEAST:G3O-32889-MON; -.
DR PRO; PR:P23644; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P23644; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:ComplexPortal.
DR GO; GO:0005742; C:mitochondrial outer membrane translocase complex; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IDA:SGD.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IMP:SGD.
DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IDA:ComplexPortal.
DR CDD; cd07305; Porin3_Tom40; 1.
DR Gene3D; 2.40.160.10; -; 1.
DR InterPro; IPR023614; Porin_dom_sf.
DR InterPro; IPR027246; Porin_Euk/Tom40.
DR InterPro; IPR037930; Tom40.
DR InterPro; IPR005686; Tom40_fungi.
DR PANTHER; PTHR10802; PTHR10802; 1.
DR Pfam; PF01459; Porin_3; 1.
DR TIGRFAMs; TIGR00989; 3a0801s07tom40; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Porin; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane beta strand; Transport.
FT CHAIN 1..387
FT /note="Mitochondrial import receptor subunit TOM40"
FT /id="PRO_0000051535"
FT CONFLICT 387
FT /note="L -> M (in Ref. 4; AAT93040)"
FT /evidence="ECO:0000305"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:7E4H"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:7E4H"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:7E4H"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:7E4H"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:7E4H"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 97..107
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 113..121
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 123..132
FT /evidence="ECO:0007829|PDB:7E4H"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 145..157
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 164..172
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 174..184
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 195..203
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 205..224
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 227..237
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 241..249
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 255..262
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 264..275
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 299..308
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 310..319
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 322..331
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 333..345
FT /evidence="ECO:0007829|PDB:7E4H"
FT TURN 346..349
FT /evidence="ECO:0007829|PDB:7E4H"
FT STRAND 352..362
FT /evidence="ECO:0007829|PDB:7E4H"
FT HELIX 365..372
FT /evidence="ECO:0007829|PDB:7E4H"
SQ SEQUENCE 387 AA; 42038 MW; 6436FBBA4020464B CRC64;
MSAPTPLAEA SQIPTIPALS PLTAKQSKGN FFSSNPISSF VVDTYKQLHS HRQSLELVNP
GTVENLNKEV SRDVFLSQYF FTGLRADLNK AFSMNPAFQT SHTFSIGSQA LPKYAFSALF
ANDNLFAQGN IDNDLSVSGR LNYGWDKKNI SKVNLQISDG QPTMCQLEQD YQASDFSVNV
KTLNPSFSEK GEFTGVAVAS FLQSVTPQLA LGLETLYSRT DGSAPGDAGV SYLTRYVSKK
QDWIFSGQLQ ANGALIASLW RKVAQNVEAG IETTLQAGMV PITDPLMGTP IGIQPTVEGS
TTIGAKYEYR QSVYRGTLDS NGKVACFLER KVLPTLSVLF CGEIDHFKND TKIGCGLQFE
TAGNQELLML QQGLDADGNP LQALPQL
