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Q5RF14

- MIPEP_PONAB

UniProt

Q5RF14 - MIPEP_PONAB

Protein

Mitochondrial intermediate peptidase

Gene

MIPEP

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
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    Functioni

    Cleaves proteins, imported into the mitochondrion, to their mature size.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

    Enzyme regulationi

    Activity is divalent cation-dependent. It is stimulated by manganese, magnesium or calcium ions and reversibly inhibited by zinc, cobalt and iron By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi495 – 4951Zinc; catalyticPROSITE-ProRule annotation
    Active sitei496 – 4961PROSITE-ProRule annotation
    Metal bindingi499 – 4991Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi502 – 5021Zinc; 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

    Calcium, Cobalt, Iron, Magnesium, Manganese, Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM03.A05.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitochondrial intermediate peptidase (EC:3.4.24.59)
    Short name:
    MIP
    Gene namesi
    Name:MIPEP
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Unplaced

    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 – 3535MitochondrionBy similarityAdd
    BLAST
    Chaini36 – 713678Mitochondrial intermediate peptidasePRO_0000319049Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei126 – 1261N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ5RF14.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M3 family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    HOGENOMiHOG000230535.
    HOVERGENiHBG008215.
    InParanoidiQ5RF14.
    KOiK01410.

    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.

    Q5RF14-1 [UniParc]FASTAAdd to Basket

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    MLCVGRLGGL GARAAALPPR RAGRGILEAG IRARRVSTSW SPVGAAFNVK    50
    PQGSRLDLFG ERRGLFGVPE LSAPEGFHAA QEKALRKAEL LVGRACSTPP 100
    GPQTVLIFDE LSDSLCRVAD LADFVKIAHP EPAFREAAEE ACRSIGTMVE 150
    KLNTNVDLYQ SLRKLLADKK LVDSLDPETR RVAELFMFDF EISGIHLDKE 200
    KRKRAVDLNV KILDLSSTFL MGANFPNKIE KHLLPEHIRR NFTSAGDHII 250
    IDGLHAESPD DLVREAAYKI FLYPNAGQLK CLEELLSSRD LLAKLVGYST 300
    FSHRALQGTI AKNPETVMQF LEKLSDKLSE RTLKDFEMIR GMKMKLNPQN 350
    SEVMPWDPPY YSGVIRAERY NIEPSLYCPF FSLGACMEGL NILLNRLLGI 400
    SLYAEQPAKG EVWSEDVRKL AVVHESEGLL GYIYCDFFQR ADKPHQDCHF 450
    TIRGGRLKED GDYQLPVVVL MLNLPRSSRS SPTLLTPGMM ENLFHEMGHA 500
    MHSMLGRTRY QHVTGTRCPT DFAEVPSILM EYFANDYRVV NQFARHYQTG 550
    QPLPKNMVSR LCESKKVCAA ADMQLQVFYA TLDQIYHGKH PLRNSTTDIL 600
    KETQEKFYGL PYVPDTAWQL RFSHLVGYGA KYYSYLMSRA VASMVWKECF 650
    LQDPFNRAAG ERYRREMLAH GGGREPMLMV EGMLQKCPSV DDFVSALVSD 700
    LDLDFETFLM DSE 713
    Length:713
    Mass (Da):80,478
    Last modified:December 21, 2004 - v1
    Checksum:i32FB7C32F5BD1FF9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR857347 mRNA. Translation: CAH89643.1.
    RefSeqiNP_001124737.1. NM_001131265.1.

    Genome annotation databases

    GeneIDi100171586.
    KEGGipon:100171586.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR857347 mRNA. Translation: CAH89643.1 .
    RefSeqi NP_001124737.1. NM_001131265.1.

    3D structure databases

    ProteinModelPortali Q5RF14.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M03.A05.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100171586.
    KEGGi pon:100171586.

    Organism-specific databases

    CTDi 4285.

    Phylogenomic databases

    HOGENOMi HOG000230535.
    HOVERGENi HBG008215.
    InParanoidi Q5RF14.
    KOi K01410.

    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. The German cDNA consortium
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.

    Entry informationi

    Entry nameiMIPEP_PONAB
    AccessioniPrimary (citable) accession number: Q5RF14
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 56 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata 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