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P47788

- THOP1_PIG

UniProt

P47788 - THOP1_PIG

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Protein

Thimet oligopeptidase

Gene
THOP1
Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

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; catalytic By similarity
Active sitei474 – 4741 By similarity
Metal bindingi477 – 4771Zinc; catalytic By similarity
Metal bindingi480 – 4801Zinc; catalytic By similarity

GO - Molecular functioni

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

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
Complete GO annotation...

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 – 2781Phosphotyrosine By similarity
Modified residuei538 – 5381N6-acetyllysine By 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.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M3 family.

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: May 14, 2014
This is version 90 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

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