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Q12328

- TIM22_YEAST

UniProt

Q12328 - TIM22_YEAST

Protein

Mitochondrial import inner membrane translocase subunit TIM22

Gene

TIM22

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Essential core component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins, such as mitochondrial carrier family members, into the mitochondrial inner membrane. In the TIM22 complex, it constitutes the voltage-activated and signal-gated channel. Forms a twin-pore translocase that uses the membrane potential as external driving force in 2 voltage-dependent steps. Mediates the insertion of precursor proteins in a 3 step process. After the precursor is tethered to the translocase without losing energy from the Delta(psi), 2 energy-requiring steps are needed. First, Delta(psi) acts on the precursor protein and promotes its docking in the translocase complex. Then, Delta(psi) and an internal signal peptide together induce rapid gating transitions in one pore and closing of the other pore and drive membrane insertion to completion.3 Publications

    GO - Molecular functioni

    1. mitochondrion targeting sequence binding Source: SGD
    2. protein binding Source: IntAct
    3. protein channel activity Source: SGD

    GO - Biological processi

    1. protein import into mitochondrial inner membrane Source: SGD

    Keywords - Biological processi

    Protein transport, Translocation, Transport

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29598-MONOMER.
    ReactomeiREACT_189012. Mitochondrial protein import.

    Protein family/group databases

    TCDBi3.A.8.1.1. the mitochondrial protein translocase (mpt) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitochondrial import inner membrane translocase subunit TIM22
    Gene namesi
    Name:TIM22
    Ordered Locus Names:YDL217C
    ORF Names:D0884
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDL217c.
    SGDiS000002376. TIM22.

    Subcellular locationi

    Mitochondrion inner membrane 2 Publications; Multi-pass membrane protein 2 Publications
    Note: Import into inner membrane protein requires TOM20 function.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. integral component of membrane Source: UniProtKB-KW
    3. mitochondrial inner membrane Source: Reactome
    4. mitochondrial inner membrane protein insertion complex Source: SGD
    5. mitochondrial intermembrane space Source: Reactome

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 207207Mitochondrial import inner membrane translocase subunit TIM22PRO_0000210301Add
    BLAST

    Proteomic databases

    MaxQBiQ12328.
    PaxDbiQ12328.

    Expressioni

    Gene expression databases

    GenevestigatoriQ12328.

    Interactioni

    Subunit structurei

    Component of the TIM22 complex, whose core is composed of TIM18, TIM22 and TIM54, associated with the peripheral proteins MRS5/TIM12 and the 70 kDa heterohexamer composed of TIM9 and TIM10 (or TIM8 and TIM13).2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TIM21P532202EBI-9132,EBI-23128

    Protein-protein interaction databases

    BioGridi31828. 60 interactions.
    DIPiDIP-1142N.
    IntActiQ12328. 7 interactions.
    MINTiMINT-513851.
    STRINGi4932.YDL217C.

    Structurei

    3D structure databases

    ProteinModelPortaliQ12328.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei47 – 6721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei152 – 17221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei173 – 19321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the Tim17/Tim22/Tim23 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5596.
    GeneTreeiENSGT00390000016067.
    HOGENOMiHOG000161169.
    KOiK17790.
    OMAiNFGYIGM.
    OrthoDBiEOG7F7WN2.

    Family and domain databases

    InterProiIPR003397. Tim17/Tim22/Tim23/PMP24.
    [Graphical view]
    PfamiPF02466. Tim17. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q12328-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVYTGFGLEQ ISPAQKKPYN ELTPEEQGER GAEMIMNFMT SCPGKSVVSG    50
    VTGFALGGVL GLFMASMAYD TPLHTPTPAN TAATATAGNI GVGGISRTVQ 100
    QISDLPFRQQ MKLQFTDMGK KSYSSAKNFG YIGMIYAGVE CVIESLRAKN 150
    DIYNGVTAGF FTGAGLAYKA GPQAALMGGA GFAAFSAAID LYMKSEDGRP 200
    PQNDFKE 207
    Length:207
    Mass (Da):21,864
    Last modified:November 1, 1997 - v1
    Checksum:i3C94DBF31F413968
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X99000 Genomic DNA. Translation: CAA67473.1.
    Z74265 Genomic DNA. Translation: CAA98795.1.
    AY558171 Genomic DNA. Translation: AAS56497.1.
    BK006938 Genomic DNA. Translation: DAA11647.1.
    PIRiS67776.
    RefSeqiNP_010064.1. NM_001180277.1.

    Genome annotation databases

    EnsemblFungiiYDL217C; YDL217C; YDL217C.
    GeneIDi851309.
    KEGGisce:YDL217C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X99000 Genomic DNA. Translation: CAA67473.1 .
    Z74265 Genomic DNA. Translation: CAA98795.1 .
    AY558171 Genomic DNA. Translation: AAS56497.1 .
    BK006938 Genomic DNA. Translation: DAA11647.1 .
    PIRi S67776.
    RefSeqi NP_010064.1. NM_001180277.1.

    3D structure databases

    ProteinModelPortali Q12328.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31828. 60 interactions.
    DIPi DIP-1142N.
    IntActi Q12328. 7 interactions.
    MINTi MINT-513851.
    STRINGi 4932.YDL217C.

    Protein family/group databases

    TCDBi 3.A.8.1.1. the mitochondrial protein translocase (mpt) family.

    Proteomic databases

    MaxQBi Q12328.
    PaxDbi Q12328.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDL217C ; YDL217C ; YDL217C .
    GeneIDi 851309.
    KEGGi sce:YDL217C.

    Organism-specific databases

    CYGDi YDL217c.
    SGDi S000002376. TIM22.

    Phylogenomic databases

    eggNOGi COG5596.
    GeneTreei ENSGT00390000016067.
    HOGENOMi HOG000161169.
    KOi K17790.
    OMAi NFGYIGM.
    OrthoDBi EOG7F7WN2.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29598-MONOMER.
    Reactomei REACT_189012. Mitochondrial protein import.

    Miscellaneous databases

    NextBioi 968328.
    PROi Q12328.

    Gene expression databases

    Genevestigatori Q12328.

    Family and domain databases

    InterProi IPR003397. Tim17/Tim22/Tim23/PMP24.
    [Graphical view ]
    Pfami PF02466. Tim17. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of a 39 kb segment of yeast chromosome IV: 12 new open reading frames, nine known genes and one gene for Gly-tRNA."
      Bahr A., Moeller-Rieker S., Hankeln T., Kraemer C., Protin U., Schmidt E.R.
      Yeast 13:163-169(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "Import of carrier proteins into the mitochondrial inner membrane mediated by Tim22."
      Sirrenberg C., Bauer M.D., Guiard B., Neupert W., Brunner M.
      Nature 384:582-585(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TIM10 AND TIM12.
    6. "Carrier protein import into mitochondria mediated by the intermembrane proteins Tim10/Mrs11 and Tim12/Mrs5."
      Sirrenberg C., Endres M., Foelsch H., Stuart R.A., Neupert W., Brunner M.
      Nature 391:912-915(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TIM10 AND TIM12.
    7. "Import of mitochondrial carriers mediated by essential proteins of the intermembrane space."
      Koehler C.M., Jarosch E., Tokatlidis K., Schmid K., Schweyen R.J., Schatz G.
      Science 279:369-373(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TIM10 AND TIM12.
    8. "Biogenesis of Tim proteins of the mitochondrial carrier import pathway: differential targeting mechanisms and crossing over with the main import pathway."
      Kurz M., Martin H., Rassow J., Pfanner N., Ryan M.T.
      Mol. Biol. Cell 10:2461-2474(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "Tim18p, a new subunit of the TIM22 complex that mediates insertion of imported proteins into the yeast mitochondrial inner membrane."
      Koehler C.M., Murphy M.P., Bally N.A., Leuenberger D., Oppliger W., Dolfini L., Junne T., Schatz G., Or E.
      Mol. Cell. Biol. 20:1187-1193(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A THE TIM22 COMPLEX WITH TIM12; TIM18 AND TIM54.
    10. "Tim22, the essential core of the mitochondrial protein insertion complex, forms a voltage-activated and signal-gated channel."
      Kovermann P., Truscott K.N., Guiard B., Rehling P., Sepuri N.B., Mueller H., Jensen R.E., Wagner R., Pfanner N.
      Mol. Cell 9:363-373(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Protein insertion into the mitochondrial inner membrane by a twin-pore translocase."
      Rehling P., Model K., Brandner K., Kovermann P., Sickmann A., Meyer H.E., Kuehlbrandt W., Wagner R., Truscott K.N., Pfanner N.
      Science 299:1747-1751(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE TIM22 COMPLEX WITH TIM10; TIM12; TIM18 AND TIM54.

    Entry informationi

    Entry nameiTIM22_YEAST
    AccessioniPrimary (citable) accession number: Q12328
    Secondary accession number(s): D6VRD7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3