ID   TIM23_HUMAN             Reviewed;         209 AA.
AC   O14925; Q53FF8; Q5T1E6; Q6P5S5;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit Tim23;
GN   Name=TIMM23; Synonyms=TIM23;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10339406; DOI=10.1006/jmbi.1999.2751;
RA   Bauer M.F., Gempel K., Reichert A.S., Rappold G.A., Lichtner P.,
RA   Gerbitz K.-D., Neupert W., Brunner M., Hofmann S.;
RT   "Genetic and structural characterization of the human mitochondrial inner
RT   membrane translocase.";
RL   J. Mol. Biol. 289:69-82(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Cao X., Li Q., Jin K., Liu L., Dai S., Wu G., Dong C.;
RT   "Cloning of Homo sapiens translocase of inner mitochondrial membrane 23
RT   (Tim23) mRNA.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   INTERACTION WITH TIMM50.
RX   PubMed=15044455; DOI=10.1074/jbc.m402049200;
RA   Guo Y., Cheong N., Zhang Z., De Rose R., Deng Y., Farber S.A.,
RA   Fernandes-Alnemri T., Alnemri E.S.;
RT   "Tim50, a component of the mitochondrial translocator, regulates
RT   mitochondrial integrity and cell death.";
RL   J. Biol. Chem. 279:24813-24825(2004).
RN   [7]
RP   INTERACTION WITH DNAJC15.
RX   PubMed=23263864; DOI=10.1093/hmg/dds541;
RA   Schusdziarra C., Blamowska M., Azem A., Hell K.;
RT   "Methylation-controlled J-protein MCJ acts in the import of proteins into
RT   human mitochondria.";
RL   Hum. Mol. Genet. 22:1348-1357(2013).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=25997101; DOI=10.7554/elife.06265;
RA   Guarani V., McNeill E.M., Paulo J.A., Huttlin E.L., Froehlich F.,
RA   Gygi S.P., Van Vactor D., Harper J.W.;
RT   "QIL1 is a novel mitochondrial protein required for MICOS complex stability
RT   and cristae morphology.";
RL   Elife 4:0-0(2015).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
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. {ECO:0000305|PubMed:10339406}.
CC   -!- SUBUNIT: Component of the TIM23 complex at least composed of TIMM23,
CC       TIMM17 (TIMM17A or TIMM17B) and TIMM50; within this complex, directly
CC       interacts with TIMM50. The complex interacts with the TIMM44 component
CC       of the PAM complex and with DNAJC15. {ECO:0000269|PubMed:15044455,
CC       ECO:0000269|PubMed:23263864}.
CC   -!- INTERACTION:
CC       O14925; Q13520: AQP6; NbExp=3; IntAct=EBI-1047996, EBI-13059134;
CC       O14925; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-1047996, EBI-6942903;
CC       O14925; Q15125: EBP; NbExp=3; IntAct=EBI-1047996, EBI-3915253;
CC       O14925; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-1047996, EBI-18938272;
CC       O14925; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-1047996, EBI-12175685;
CC       O14925; Q6ZVE7: GOLT1A; NbExp=3; IntAct=EBI-1047996, EBI-17231387;
CC       O14925; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-1047996, EBI-18053395;
CC       O14925; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-1047996, EBI-10266796;
CC       O14925; P13473-2: LAMP2; NbExp=3; IntAct=EBI-1047996, EBI-21591415;
CC       O14925; Q6P5S7: RNASEK; NbExp=3; IntAct=EBI-1047996, EBI-18397230;
CC       O14925; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-1047996, EBI-17247926;
CC       O14925; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-1047996, EBI-2623095;
CC       O14925; O60669: SLC16A7; NbExp=3; IntAct=EBI-1047996, EBI-3921243;
CC       O14925; O60830: TIMM17B; NbExp=4; IntAct=EBI-1047996, EBI-2372529;
CC       O14925; Q9BVV7: TIMM21; NbExp=3; IntAct=EBI-1047996, EBI-6570759;
CC       O14925; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-1047996, EBI-12947623;
CC       O14925; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-1047996, EBI-8638294;
CC       O14925; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-1047996, EBI-2548832;
CC       O14925; Q6PEY1: TMEM88; NbExp=3; IntAct=EBI-1047996, EBI-17198826;
CC       O14925; P19075: TSPAN8; NbExp=3; IntAct=EBI-1047996, EBI-4289938;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:25997101}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the Tim17/Tim22/Tim23 family. {ECO:0000305}.
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DR   EMBL; AF030162; AAB84060.1; -; mRNA.
DR   EMBL; AY442341; AAR14723.1; -; mRNA.
DR   EMBL; AK223331; BAD97051.1; -; mRNA.
DR   EMBL; AL450342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC062707; AAH62707.1; -; mRNA.
DR   EMBL; BC066951; AAH66951.1; -; mRNA.
DR   CCDS; CCDS73091.1; -.
DR   RefSeq; NP_006318.1; NM_006327.3.
DR   AlphaFoldDB; O14925; -.
DR   SMR; O14925; -.
DR   BioGRID; 939591; 85.
DR   ComplexPortal; CPX-6129; TIM23 mitochondrial inner membrane pre-sequence translocase complex, TIM17A variant.
DR   ComplexPortal; CPX-6130; TIM23 mitochondrial inner membrane pre-sequence translocase complex, TIM17B variant.
DR   CORUM; O14925; -.
DR   IntAct; O14925; 60.
DR   MINT; O14925; -.
DR   STRING; 9606.ENSP00000464522; -.
DR   GlyGen; O14925; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O14925; -.
DR   PhosphoSitePlus; O14925; -.
DR   SwissPalm; O14925; -.
DR   BioMuta; TIMM23; -.
DR   EPD; O14925; -.
DR   jPOST; O14925; -.
DR   MassIVE; O14925; -.
DR   MaxQB; O14925; -.
DR   PaxDb; 9606-ENSP00000464522; -.
DR   PeptideAtlas; O14925; -.
DR   ProteomicsDB; 48306; -.
DR   Pumba; O14925; -.
DR   TopDownProteomics; O14925; -.
DR   Antibodypedia; 73127; 135 antibodies from 25 providers.
DR   DNASU; 100287932; -.
DR   Ensembl; ENST00000580018.4; ENSP00000464522.3; ENSG00000265354.4.
DR   GeneID; 100287932; -.
DR   KEGG; hsa:100287932; -.
DR   MANE-Select; ENST00000580018.4; ENSP00000464522.3; NM_006327.4; NP_006318.1.
DR   UCSC; uc001jiu.5; human.
DR   AGR; HGNC:17312; -.
DR   CTD; 100287932; -.
DR   DisGeNET; 100287932; -.
DR   GeneCards; TIMM23; -.
DR   HGNC; HGNC:17312; TIMM23.
DR   HPA; ENSG00000265354; Low tissue specificity.
DR   MIM; 605034; gene.
DR   neXtProt; NX_O14925; -.
DR   OpenTargets; ENSG00000265354; -.
DR   PharmGKB; PA38227; -.
DR   VEuPathDB; HostDB:ENSG00000265354; -.
DR   eggNOG; KOG3324; Eukaryota.
DR   GeneTree; ENSGT00390000001094; -.
DR   HOGENOM; CLU_063935_2_0_1; -.
DR   InParanoid; O14925; -.
DR   OMA; QYIMPEG; -.
DR   OrthoDB; 5355126at2759; -.
DR   PhylomeDB; O14925; -.
DR   TreeFam; TF106196; -.
DR   PathwayCommons; O14925; -.
DR   Reactome; R-HSA-1268020; Mitochondrial protein import.
DR   SignaLink; O14925; -.
DR   SIGNOR; O14925; -.
DR   BioGRID-ORCS; 100287932; 539 hits in 1148 CRISPR screens.
DR   ChiTaRS; TIMM23; human.
DR   GenomeRNAi; 100287932; -.
DR   Pharos; O14925; Tbio.
DR   PRO; PR:O14925; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; O14925; Protein.
DR   Bgee; ENSG00000265354; Expressed in gingival epithelium and 208 other cell types or tissues.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IDA:BHF-UCL.
DR   GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; NAS:ComplexPortal.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0006626; P:protein targeting to mitochondrion; TAS:ProtInc.
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.
DR   Genevisible; O14925; HS.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Protein transport;
KW   Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..209
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit Tim23"
FT                   /id="PRO_0000210302"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        27
FT                   /note="S -> P (in Ref. 3; BAD97051)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        62
FT                   /note="Missing (in Ref. 5; AAH62707)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   209 AA;  21943 MW;  C9A1BBEC703B6838 CRC64;
     MEGGGGSGNK TTGGLAGFFG AGGAGYSHAD LAGVPLTGMN PLSPYLNVDP RYLVQDTDEF
     ILPTGANKTR GRFELAFFTI GGCCMTGAAF GAMNGLRLGL KETQNMAWSK PRNVQILNMV
     TRQGALWANT LGSLALLYSA FGVIIEKTRG AEDDLNTVAA GTMTGMLYKC TGGLRGIARG
     GLTGLTLTSL YALYNNWEHM KGSLLQQSL
//