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TIM23_YEAST
ID   TIM23_YEAST             Reviewed;         222 AA.
AC   P32897; D6W1J2;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 174.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit TIM23;
DE   AltName: Full=Membrane import machinery protein MIM23;
DE   AltName: Full=Mitochondrial protein import protein 3;
DE   AltName: Full=Mitochondrial protein import protein MAS6;
GN   Name=TIM23; Synonyms=MAS6, MIM23, MPI3; OrderedLocusNames=YNR017W;
GN   ORFNames=N3180;
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=8354690; DOI=10.1083/jcb.122.5.1003;
RA   Emtage J.L.T., Jensen R.E.;
RT   "MAS6 encodes an essential inner membrane component of the yeast
RT   mitochondrial protein import pathway.";
RL   J. Cell Biol. 122:1003-1012(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8370462; DOI=10.1016/0014-5793(93)80921-g;
RA   Dekker P.J.T., Keil P., Rassow J., Maarse A.C., Pfanner N., Meijer M.;
RT   "Identification of MIM23, a putative component of the protein import
RT   machinery of the mitochondrial inner membrane.";
RL   FEBS Lett. 330:66-70(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [4]
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   [5]
RP   CHARACTERIZATION, AND TOPOLOGY.
RX   PubMed=8050570; DOI=10.1016/0014-5793(94)00670-9;
RA   Kuebrich M., Keil P., Rassow J., Dekker P.J.T., Blom J., Meijer M.,
RA   Pfanner N.;
RT   "The polytopic mitochondrial inner membrane proteins MIM17 and MIM23
RT   operate at the same preprotein import site.";
RL   FEBS Lett. 349:222-228(1994).
RN   [6]
RP   TOPOLOGY.
RX   PubMed=10830167; DOI=10.1016/s0092-8674(00)80850-8;
RA   Donzeau M., Kaldi K., Adam A., Paschen S., Wanner G., Guiard B.,
RA   Bauer M.F., Neupert W., Brunner M.;
RT   "Tim23 links the inner and outer mitochondrial membranes.";
RL   Cell 101:401-412(2000).
RN   [7]
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   [8]
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).
RN   [9]
RP   SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=18418384; DOI=10.1038/emboj.2008.79;
RA   Popov-Celeketic D., Mapa K., Neupert W., Mokranjac D.;
RT   "Active remodelling of the TIM23 complex during translocation of
RT   preproteins into mitochondria.";
RL   EMBO J. 27:1469-1480(2008).
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.
CC   -!- SUBUNIT: Component of the TIM23 complex, at least composed of TIM23,
CC       TIM17, TIM50 and TIM21. The complex interacts with the TIM44 component
CC       of the PAM complex. {ECO:0000269|PubMed:15797382}.
CC   -!- INTERACTION:
CC       P32897; P42949: PAM16; NbExp=6; IntAct=EBI-9136, EBI-26019;
CC       P32897; P39515: TIM17; NbExp=14; IntAct=EBI-9136, EBI-9127;
CC       P32897; P53220: TIM21; NbExp=16; IntAct=EBI-9136, EBI-23128;
CC       P32897; Q01852: TIM44; NbExp=8; IntAct=EBI-9136, EBI-9141;
CC       P32897; Q02776: TIM50; NbExp=13; IntAct=EBI-9136, EBI-30302;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:18418384}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:18418384}. Note=Around 20 amino acids of the N-
CC       terminus are believed to span the mitochondrial outer membrane. This
CC       association is dynamic and depends on the translocation activity of the
CC       TIM23 complex. However, this topology seems not to be critical for
CC       formation of a TOM-TIM supercomplex and preprotein import.
CC   -!- MISCELLANEOUS: Present with 1440 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the Tim17/Tim22/Tim23 family. {ECO:0000305}.
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DR   EMBL; X71633; CAA50640.1; -; Genomic_DNA.
DR   EMBL; X74161; CAA52274.1; -; Genomic_DNA.
DR   EMBL; Z71632; CAA96296.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10558.1; -; Genomic_DNA.
DR   PIR; S36139; S36139.
DR   RefSeq; NP_014414.3; NM_001183194.3.
DR   PDB; 7CLV; NMR; -; A/B=1-222.
DR   PDBsum; 7CLV; -.
DR   AlphaFoldDB; P32897; -.
DR   BMRB; P32897; -.
DR   SASBDB; P32897; -.
DR   SMR; P32897; -.
DR   BioGRID; 35842; 618.
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-2451N; -.
DR   IntAct; P32897; 16.
DR   MINT; P32897; -.
DR   STRING; 4932.YNR017W; -.
DR   BindingDB; P32897; -.
DR   ChEMBL; CHEMBL1741180; -.
DR   TCDB; 3.A.8.1.1; the mitochondrial protein translocase (mpt) family.
DR   MaxQB; P32897; -.
DR   PaxDb; P32897; -.
DR   PRIDE; P32897; -.
DR   EnsemblFungi; YNR017W_mRNA; YNR017W; YNR017W.
DR   GeneID; 855751; -.
DR   KEGG; sce:YNR017W; -.
DR   SGD; S000005300; TIM23.
DR   VEuPathDB; FungiDB:YNR017W; -.
DR   eggNOG; KOG3324; Eukaryota.
DR   GeneTree; ENSGT00390000001094; -.
DR   HOGENOM; CLU_063935_1_1_1; -.
DR   InParanoid; P32897; -.
DR   OMA; GVRPMMI; -.
DR   BioCyc; YEAST:G3O-33332-MON; -.
DR   Reactome; R-SCE-1268020; Mitochondrial protein import.
DR   PRO; PR:P32897; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P32897; protein.
DR   GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IPI:SGD.
DR   GO; GO:0030943; F:mitochondrion targeting sequence binding; IDA:SGD.
DR   GO; GO:0008320; F:protein transmembrane transporter activity; 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   InterPro; IPR005681; Tim23.
DR   InterPro; IPR045238; Tim23-like.
DR   PANTHER; PTHR15371; PTHR15371; 1.
DR   TIGRFAMs; TIGR00983; 3a0801s02tim23; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Protein transport; Reference proteome; Translocation; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..222
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit TIM23"
FT                   /id="PRO_0000210307"
FT   TRANSMEM        1..?
FT                   /note="Helical; Note=Outer membrane"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        ?..96
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..118
FT                   /note="Helical; Note=Inner membrane"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        119..144
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..166
FT                   /note="Helical; Note=Inner membrane"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        167..174
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..189
FT                   /note="Helical; Note=Inner membrane"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        190..196
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..215
FT                   /note="Helical; Note=Inner membrane"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        216..222
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   TURN            4..6
FT                   /evidence="ECO:0007829|PDB:7CLV"
FT   HELIX           12..16
FT                   /evidence="ECO:0007829|PDB:7CLV"
FT   HELIX           30..33
FT                   /evidence="ECO:0007829|PDB:7CLV"
FT   HELIX           39..43
FT                   /evidence="ECO:0007829|PDB:7CLV"
FT   TURN            56..58
FT                   /evidence="ECO:0007829|PDB:7CLV"
FT   HELIX           63..82
FT                   /evidence="ECO:0007829|PDB:7CLV"
FT   TURN            91..93
FT                   /evidence="ECO:0007829|PDB:7CLV"
FT   HELIX           95..98
FT                   /evidence="ECO:0007829|PDB:7CLV"
FT   HELIX           103..123
FT                   /evidence="ECO:0007829|PDB:7CLV"
FT   HELIX           135..139
FT                   /evidence="ECO:0007829|PDB:7CLV"
FT   TURN            151..154
FT                   /evidence="ECO:0007829|PDB:7CLV"
FT   HELIX           155..168
FT                   /evidence="ECO:0007829|PDB:7CLV"
FT   TURN            177..183
FT                   /evidence="ECO:0007829|PDB:7CLV"
FT   HELIX           184..188
FT                   /evidence="ECO:0007829|PDB:7CLV"
FT   STRAND          193..195
FT                   /evidence="ECO:0007829|PDB:7CLV"
FT   HELIX           198..213
FT                   /evidence="ECO:0007829|PDB:7CLV"
FT   HELIX           218..221
FT                   /evidence="ECO:0007829|PDB:7CLV"
SQ   SEQUENCE   222 AA;  23244 MW;  08E5AB4F400F675B CRC64;
     MSWLFGDKTP TDDANAAVGG QDTTKPKELS LKQSLGFEPN INNIISGPGG MHVDTARLHP
     LAGLDKGVEY LDLEEEQLSS LEGSQGLIPS RGWTDDLCYG TGAVYLLGLG IGGFSGMMQG
     LQNIPPNSPG KLQLNTVLNH ITKRGPFLGN NAGILALSYN IINSTIDALR GKHDTAGSIG
     AGALTGALFK SSKGLKPMGY SSAMVAAACA VWCSVKKRLL EK
 
 
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