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A7TSL2

- PMIP_VANPO

UniProt

A7TSL2 - PMIP_VANPO

Protein

Mitochondrial intermediate peptidase

Gene

OCT1

Organism
Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294) (Kluyveromyces polysporus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 36 (01 Oct 2014)
      Sequence version 1 (02 Oct 2007)
      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 By similarity.By similarity

    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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi573 – 5731Zinc; catalyticPROSITE-ProRule annotation
    Active sitei574 – 5741PROSITE-ProRule annotation
    Metal bindingi577 – 5771Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi580 – 5801Zinc; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

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

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM03.006.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitochondrial intermediate peptidase (EC:3.4.24.59)
    Short name:
    MIP
    Alternative name(s):
    Octapeptidyl aminopeptidase
    Gene namesi
    Name:OCT1
    ORF Names:Kpol_297p8
    OrganismiVanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294) (Kluyveromyces polysporus)
    Taxonomic identifieri436907 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeVanderwaltozyma
    ProteomesiUP000000267: Unassembled WGS sequence

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3636MitochondrionSequence AnalysisAdd
    BLAST
    Chaini37 – 787751Mitochondrial intermediate peptidasePRO_0000338596Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi436907.A7TSL2.

    Structurei

    3D structure databases

    ProteinModelPortaliA7TSL2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M3 family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0339.
    KOiK01410.
    OrthoDBiEOG71GB4R.

    Family and domain databases

    Gene3Di1.10.1370.10. 2 hits.
    3.40.390.10. 1 hit.
    InterProiIPR024079. MetalloPept_cat_dom.
    IPR024077. Neurolysin/TOP_dom2.
    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.

    A7TSL2-1 [UniParc]FASTAAdd to Basket

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    MQNKVLRGIL FKNVPLGYSY NRSIRHPTFG NSIIRWASTQ VKTSSDVLQR    50
    SFDDHLYWTE INKQNYSSKE GWGSITKRLK GNKLTTNRSG LFNNEYLTSP 100
    EGLKLFSQVS LEKSQKIVDK LRSDRTPEGL RLYVQNLDLL SDTLCRVIDL 150
    CEFIRSSHPD YKFVEAAQDC YEEMFEFMNM LNTDVNLCFT LKHVLENKEI 200
    ASKLSEEELR VGRILLEDFE KSGIYMKPEV REQFITLSQS ISVIGQEFIS 250
    NTDFVKDNNV VVSCNQLDSL GIDPELLSQI EKDIAGKNYK IPTYGYIPFA 300
    LLKSCPSEEI REKIWVAVHN CSNEQIKRLT DLVKLRAVLS QLLGKKSYAE 350
    YQLEGKMAKN PKEVIEFIKT LMDFTKPMAA KELDGIAEKK LTIKSNGSNL 400
    SVCDILKTVR PWDRDYYSAI EREQTSAKNL YGSEEVLKYF TLGNVMQGLS 450
    NLFQKIYGIK LELDVPKIGE TWSPEVRKIN VISEDEGLIG IIYCDLFERS 500
    GKTSNAAHFT ICCSRDISPY ETEDSTTQIA IDSKGTRFQL PIISLVCNFS 550
    KTMISETDSV CFLHLPEVET LFHEMGHAMH SMLGRTKLQN ISGTRCATDF 600
    VELPSILMEY FARDPRVLET IGKHYLTKET VKREMLEPHL QDLKYLQHCE 650
    TYSQAKMAML DQTLHGETIS SHLDHLDVVK LYQDLERQLG VLVDDKSNWC 700
    GKFGHLFGYS AVYYSYLFDR AIASKIWGAL FERNPFSRAS GDKYRNSVLQ 750
    WGGSRDPWHC IASALDKPEL AKGDDEAIKY IGSTNQL 787
    Length:787
    Mass (Da):90,031
    Last modified:October 2, 2007 - v1
    Checksum:i478D339F977CF096
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS480515 Genomic DNA. Translation: EDO14747.1.
    RefSeqiXP_001642605.1. XM_001642555.1.

    Genome annotation databases

    GeneIDi5542774.
    KEGGivpo:Kpol_297p8.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DS480515 Genomic DNA. Translation: EDO14747.1 .
    RefSeqi XP_001642605.1. XM_001642555.1.

    3D structure databases

    ProteinModelPortali A7TSL2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 436907.A7TSL2.

    Protein family/group databases

    MEROPSi M03.006.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 5542774.
    KEGGi vpo:Kpol_297p8.

    Phylogenomic databases

    eggNOGi COG0339.
    KOi K01410.
    OrthoDBi EOG71GB4R.

    Family and domain databases

    Gene3Di 1.10.1370.10. 2 hits.
    3.40.390.10. 1 hit.
    InterProi IPR024079. MetalloPept_cat_dom.
    IPR024077. Neurolysin/TOP_dom2.
    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. "Independent sorting-out of thousands of duplicated gene pairs in two yeast species descended from a whole-genome duplication."
      Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.
      Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 22028 / DSM 70294.

    Entry informationi

    Entry nameiPMIP_VANPO
    AccessioniPrimary (citable) accession number: A7TSL2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: October 2, 2007
    Last modified: October 1, 2014
    This is version 36 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. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3