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P47788

- THOP1_PIG

UniProt

P47788 - THOP1_PIG

Protein

Thimet oligopeptidase

Gene

THOP1

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Involved in the metabolism of neuropeptides under 20 amino acid residues long. Involved in cytoplasmic peptide degradation.

    Catalytic activityi

    Preferential cleavage of bonds with hydrophobic residues at P1, P2 and P3' and a small residue at P1' in substrates of 5 to 15 residues.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi473 – 4731Zinc; catalyticPROSITE-ProRule annotation
    Active sitei474 – 4741PROSITE-ProRule annotation
    Metal bindingi477 – 4771Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi480 – 4801Zinc; 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

    MEROPSiM03.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thimet oligopeptidase (EC:3.4.24.15)
    Alternative name(s):
    Endopeptidase 24.15
    Gene namesi
    Name:THOP1
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 687687Thimet oligopeptidasePRO_0000078154Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei278 – 2781PhosphotyrosineBy similarity
    Modified residuei538 – 5381N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP47788.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000014316.

    Structurei

    3D structure databases

    ProteinModelPortaliP47788.
    SMRiP47788. Positions 24-677.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M3 family.Curated

    Phylogenomic databases

    eggNOGiCOG0339.
    HOGENOMiHOG000245985.
    HOVERGENiHBG000238.
    KOiK01392.

    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.

    P47788-1 [UniParc]FASTAAdd to Basket

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    MKPPAACAGD ALDVAAPCSA VNYLRWDLSA QQIGELTTEL IEQTKRVYDR    50
    VGTQELQDVS YENTLKALAD VEVSYTVQRN ILDFPQHVSP CKDIRTASTE 100
    ADKKLSEFDV EMSMRQDVYQ RIVWLQEKVQ KDSLRPEAAR YLERLIKLGR 150
    RNGLHLPKET QEKIKSIKKK LSLLCIDFNK NLNEDTTFLP VTREELGGLP 200
    EDFLNSLEKT EDEKLKVTLK YPHYFPLLKK CHVPETRRKV EEAFNCRCKE 250
    ENCAILRELV RLRAQKSSLL GFSTHADYVL EMNMAKTSQV VATFLDELAQ 300
    KLKPLGEQER AVILELKKAE CTKRGLDFDG RINAWDMRYY MNQVEETRYR 350
    VDQNLLKEYF PMQVVTRGLL GIYQELLGLT FHLEEGAAVW HEDVMLYSVR 400
    DAASGKVIGK FYLDLYPREG KYGHAACFGL QPGCLRQDGS RQIAIAAMVA 450
    NFTKPTPDAP SLLQHDEVET YFHEFGHVMH QLCSQAEFAM FSGTHVERDF 500
    VEAPSQMLEN WVWEAEPLLR MSQHYRTGSA IPQELLEKLI KSRQANTGLF 550
    NLRQIVLAKV DQALHTQTAA DPAEEYARLC QEILGVPATP GTNMPATFGH 600
    LAGGYDAQYY GYLWSEVYSA DMFHTRFKQE GILSGKVGMD YRSCILRPGG 650
    SEDASVMLKL FLGRDPKQDA FLLSKGLQVE GCEPPAS 687
    Length:687
    Mass (Da):78,144
    Last modified:January 23, 2007 - v2
    Checksum:i70AEF85C6C466929
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D21871 mRNA. Translation: BAA04882.1.
    AB000438 Genomic DNA. Translation: BAA19107.1.
    PIRiS43250.
    RefSeqiNP_999388.1. NM_214223.2.
    UniGeneiSsc.16161.

    Genome annotation databases

    GeneIDi397442.
    KEGGissc:397442.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D21871 mRNA. Translation: BAA04882.1 .
    AB000438 Genomic DNA. Translation: BAA19107.1 .
    PIRi S43250.
    RefSeqi NP_999388.1. NM_214223.2.
    UniGenei Ssc.16161.

    3D structure databases

    ProteinModelPortali P47788.
    SMRi P47788. Positions 24-677.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9823.ENSSSCP00000014316.

    Protein family/group databases

    MEROPSi M03.001.

    Proteomic databases

    PaxDbi P47788.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 397442.
    KEGGi ssc:397442.

    Organism-specific databases

    CTDi 7064.

    Phylogenomic databases

    eggNOGi COG0339.
    HOGENOMi HOG000245985.
    HOVERGENi HBG000238.
    KOi K01392.

    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. "Cloning, amino acid sequence and tissue distribution of porcine thimet oligopeptidase. A comparison with soluble angiotensin-binding protein."
      Kato A., Sugiura N., Hagiwara H., Hirose S.
      Eur. J. Biochem. 221:159-165(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Targeting of endopeptidase 24.16 to different subcellular compartments by alternative promoter usage."
      Kato A., Sugiura N., Saruta Y., Hosoiri T., Yasue H., Hirose S.
      J. Biol. Chem. 272:15313-15322(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Liver.

    Entry informationi

    Entry nameiTHOP1_PIG
    AccessioniPrimary (citable) accession number: P47788
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 91 of the entry and version 2 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