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P35999

- PMIP_YEAST

UniProt

P35999 - PMIP_YEAST

Protein

Mitochondrial intermediate peptidase

Gene

OCT1

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 126 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Cleaves proteins, imported into the mitochondrion, to their mature size. While most mitochondrial precursor proteins are processed to the mature form in one step by mitochondrial processing peptidase (MPP), the sequential cleavage by MIP of an octapeptide after initial processing by MPP is a required step for a subgroup of nuclear-encoded precursor proteins destined for the matrix or the inner membrane. Cleaves precursor proteins of respiratory components, including subunits of the electron transport chain and tricarboxylic acid cycle enzymes, and components of the mitochondrial genetic machinery, including ribosomal proteins, translation factors, and proteins required for mitochondrial DNA metabolism.2 Publications

    Catalytic activityi

    Release of an N-terminal octapeptide as second stage of processing of some proteins imported into the mitochondrion.

    Cofactori

    Binds 1 zinc ion.By similarity

    Enzyme regulationi

    Stimulated by Fe2+.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi558 – 5581Zinc; catalyticPROSITE-ProRule annotation
    Active sitei559 – 5591PROSITE-ProRule annotation
    Metal bindingi562 – 5621Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi565 – 5651Zinc; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. metalloendopeptidase activity Source: SGD

    GO - Biological processi

    1. cellular iron ion homeostasis Source: SGD
    2. protein processing involved in protein targeting to mitochondrion Source: SGD
    3. protein stabilization Source: SGD

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:YKL134C-MONOMER.

    Protein family/group databases

    MEROPSiM03.006.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitochondrial intermediate peptidase (EC:3.4.24.59)
    Short name:
    MIP
    Gene namesi
    Name:OCT1
    Synonyms:MIP1
    Ordered Locus Names:YKL134C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XI

    Organism-specific databases

    SGDiS000001617. OCT1.

    Subcellular locationi

    Mitochondrion matrix 3 Publications

    GO - Cellular componenti

    1. mitochondrial matrix Source: SGD

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi131 – 1311C → S or V: Affects protein stability, but has no effect on peptidase activity. 1 Publication
    Mutagenesisi557 – 5571F → R: Affects protein stability. 1 Publication
    Mutagenesisi558 – 5581H → R: Abolishes proteolytic activity. 1 Publication
    Mutagenesisi559 – 5591E → D: Abolishes proteolytic activity. 1 Publication
    Mutagenesisi561 – 5611G → L: Affects protein stability. 1 Publication
    Mutagenesisi562 – 5621H → R: Abolishes proteolytic activity. 1 Publication
    Mutagenesisi565 – 5651H → R: Temperature sensitive; abolishes proteolytic activity for RIP1, but not for COX4. 1 Publication
    Mutagenesisi578 – 5781G → L: Temperature sensitive; abolishes proteolytic activity for RIP1, but not for COX4. 1 Publication
    Mutagenesisi581 – 5811C → S or V: Affects protein stability, but has no effect on peptidase activity. 1 Publication
    Mutagenesisi584 – 5841D → E: No effect. 1 Publication
    Mutagenesisi587 – 5871E → D: Abolishes proteolytic activity. 1 Publication
    Mutagenesisi589 – 5891P → L: No effect. 1 Publication
    Mutagenesisi590 – 5901S → Y: Affects protein stability. 1 Publication
    Mutagenesisi594 – 5941E → D: No effect. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3737MitochondrionSequence AnalysisAdd
    BLAST
    Chaini38 – 772735Mitochondrial intermediate peptidasePRO_0000028583Add
    BLAST

    Proteomic databases

    MaxQBiP35999.
    PaxDbiP35999.
    PRIDEiP35999.

    Expressioni

    Gene expression databases

    GenevestigatoriP35999.

    Interactioni

    Protein-protein interaction databases

    BioGridi34002. 60 interactions.
    DIPiDIP-2670N.
    IntActiP35999. 1 interaction.
    MINTiMINT-497669.
    STRINGi4932.YKL134C.

    Structurei

    3D structure databases

    ProteinModelPortaliP35999.
    SMRiP35999. Positions 123-751.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M3 family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0339.
    GeneTreeiENSGT00550000075047.
    HOGENOMiHOG000076521.
    KOiK01410.
    OMAiLQVFYSA.
    OrthoDBiEOG71GB4R.

    Family and domain databases

    Gene3Di1.10.1370.10. 2 hits.
    1.20.1050.40. 1 hit.
    3.40.390.10. 1 hit.
    InterProiIPR024079. MetalloPept_cat_dom.
    IPR024077. Neurolysin/TOP_dom2.
    IPR024080. Neurolysin/TOP_N.
    IPR001567. Pept_M3A_M3B.
    [Graphical view]
    PfamiPF01432. Peptidase_M3. 1 hit.
    [Graphical view]
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P35999-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRTIILKAG SNASIPSPSR QNKLLRFFAT AGAVSRTSPG SIKKIFDDNS    50
    YWRNINGQDA NNSKISQYLF KKNKTGLFKN PYLTSPDGLR KFSQVSLQQA 100
    QELLDKMRND FSESGKLTYI MNLDRLSDTL CRVIDLCEFI RSTHPDDAFV 150
    RAAQDCHEQM FEFMNVLNTD VSLCNILKSV LNNPEVSSKL SAEELKVGKI 200
    LLDDFEKSGI YMNPDVREKF IQLSQEISLV GQEFINHTDY PGSNSVKIPC 250
    KDLDNSKVST FLLKQLNKDV KGQNYKVPTF GYAAYALLKS CENEMVRKKL 300
    WTALHSCSDK QVKRLSHLIK LRAILANLMH KTSYAEYQLE GKMAKNPKDV 350
    QDFILTLMNN TIEKTANELK FIAELKAKDL KKPLTTNTDE ILKLVRPWDR 400
    DYYTGKYFQL NPSNSPNAKE ISYYFTLGNV IQGLSDLFQQ IYGIRLEPAI 450
    TDEGETWSPD VRRLNVISEE EGIIGIIYCD LFERNGKTSN PAHFTVCCSR 500
    QIYPSETDFS TIQVGENPDG TYFQLPVISL VCNFSPILIA SKKSLCFLQL 550
    SEVETLFHEM GHAMHSMLGR THMQNISGTR CATDFVELPS ILMEHFAKDI 600
    RILTKIGKHY GTGETIQADM LQRFMKSTNF LQNCETYSQA KMAMLDQSFH 650
    DEKIISDIDN FDVVENYQAL ERRLKVLVDD QSNWCGRFGH LFGYGATYYS 700
    YLFDRTIASK IWYALFEDDP YSRKNGDKFK KHLLKWGGLK DPWKCIADVL 750
    ECPMLEKGGS DAMEFIAQSH KS 772
    Length:772
    Mass (Da):88,183
    Last modified:November 1, 1997 - v2
    Checksum:i1C19A0655FAAE7CA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti343 – 3508MAKNPKDV → WQDRRC in CAA81975. (PubMed:8196765)Curated
    Sequence conflicti694 – 7029YGATYYSYL → SGQLITATY in CAA81975. (PubMed:8196765)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10243 Genomic DNA. Translation: AAA21278.1.
    Z28134 Genomic DNA. Translation: CAA81975.1.
    BK006944 Genomic DNA. Translation: DAA09028.2.
    PIRiS37963.
    RefSeqiNP_012788.2. NM_001179700.2.

    Genome annotation databases

    EnsemblFungiiYKL134C; YKL134C; YKL134C.
    GeneIDi853724.
    KEGGisce:YKL134C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10243 Genomic DNA. Translation: AAA21278.1 .
    Z28134 Genomic DNA. Translation: CAA81975.1 .
    BK006944 Genomic DNA. Translation: DAA09028.2 .
    PIRi S37963.
    RefSeqi NP_012788.2. NM_001179700.2.

    3D structure databases

    ProteinModelPortali P35999.
    SMRi P35999. Positions 123-751.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34002. 60 interactions.
    DIPi DIP-2670N.
    IntActi P35999. 1 interaction.
    MINTi MINT-497669.
    STRINGi 4932.YKL134C.

    Protein family/group databases

    MEROPSi M03.006.

    Proteomic databases

    MaxQBi P35999.
    PaxDbi P35999.
    PRIDEi P35999.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YKL134C ; YKL134C ; YKL134C .
    GeneIDi 853724.
    KEGGi sce:YKL134C.

    Organism-specific databases

    SGDi S000001617. OCT1.

    Phylogenomic databases

    eggNOGi COG0339.
    GeneTreei ENSGT00550000075047.
    HOGENOMi HOG000076521.
    KOi K01410.
    OMAi LQVFYSA.
    OrthoDBi EOG71GB4R.

    Enzyme and pathway databases

    BioCyci YEAST:YKL134C-MONOMER.

    Miscellaneous databases

    NextBioi 974752.
    PROi P35999.

    Gene expression databases

    Genevestigatori P35999.

    Family and domain databases

    Gene3Di 1.10.1370.10. 2 hits.
    1.20.1050.40. 1 hit.
    3.40.390.10. 1 hit.
    InterProi IPR024079. MetalloPept_cat_dom.
    IPR024077. Neurolysin/TOP_dom2.
    IPR024080. Neurolysin/TOP_N.
    IPR001567. Pept_M3A_M3B.
    [Graphical view ]
    Pfami PF01432. Peptidase_M3. 1 hit.
    [Graphical view ]
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "MIP1, a new yeast gene homologous to the rat mitochondrial intermediate peptidase gene, is required for oxidative metabolism in Saccharomyces cerevisiae."
      Isaya G., Miklos D., Rollins R.A.
      Mol. Cell. Biol. 14:5603-5616(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    2. "Complete DNA sequence of yeast chromosome XI."
      Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
      , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
      Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 343-350 AND 694-702.
      Strain: ATCC 204508 / S288c.
    4. "Prediction and identification of new natural substrates of the yeast mitochondrial intermediate peptidase."
      Branda S.S., Isaya G.
      J. Biol. Chem. 270:27366-27373(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Mutations in a putative zinc-binding domain inactivate the mitochondrial intermediate peptidase."
      Chew A., Rollins R.A., Sakati W.R., Isaya G.
      Biochem. Biophys. Res. Commun. 226:822-829(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-131; PHE-557; HIS-558; GLE-559; GLY-561; HIS-562; HIS-565; GLY-578; CYS-581; ASP-584; GLU-587; PRO-589; SER-590 AND GLU-594, SUBCELLULAR LOCATION.
    6. "Mitochondrial intermediate peptidase and the yeast frataxin homolog together maintain mitochondrial iron homeostasis in Saccharomyces cerevisiae."
      Branda S.S., Yang Z.Y., Chew A., Isaya G.
      Hum. Mol. Genet. 8:1099-1110(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics."
      Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.
      J. Proteome Res. 5:1543-1554(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPMIP_YEAST
    AccessioniPrimary (citable) accession number: P35999
    Secondary accession number(s): D6VX62, P51980
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 126 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 2690 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3