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 27-MAR-2024, entry version 181. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 637. 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; 4932-YNR017W; -. DR PeptideAtlas; P32897; -. DR EnsemblFungi; YNR017W_mRNA; YNR017W; YNR017W. DR GeneID; 855751; -. DR KEGG; sce:YNR017W; -. DR AGR; SGD:S000005300; -. 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; AWCGIKR; -. DR OrthoDB; 1382000at2759; -. DR BioCyc; YEAST:G3O-33332-MONOMER; -. DR Reactome; R-SCE-1268020; Mitochondrial protein import. DR BioGRID-ORCS; 855751; 4 hits in 10 CRISPR screens. DR PRO; PR:P32897; -. DR Proteomes; UP000002311; Chromosome XIV. DR RNAct; P32897; Protein. 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; NAS:ComplexPortal. DR GO; GO:0030150; P:protein import into mitochondrial matrix; IMP:SGD. DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; NAS:ComplexPortal. DR InterPro; IPR005681; Tim23. DR InterPro; IPR045238; Tim23-like. DR NCBIfam; TIGR00983; 3a0801s02tim23; 1. DR PANTHER; PTHR15371:SF0; MITOCHONDRIAL IMPORT INNER MEMBRANE TRANSLOCASE SUBUNIT TIM23-RELATED; 1. DR PANTHER; PTHR15371; TIM23; 1. DR Pfam; PF02466; Tim17; 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 //