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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; 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
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-KW
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 – 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.
InParanoidiP47788.
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

« Hide

        10         20         30         40         50
MKPPAACAGD ALDVAAPCSA VNYLRWDLSA QQIGELTTEL IEQTKRVYDR
60 70 80 90 100
VGTQELQDVS YENTLKALAD VEVSYTVQRN ILDFPQHVSP CKDIRTASTE
110 120 130 140 150
ADKKLSEFDV EMSMRQDVYQ RIVWLQEKVQ KDSLRPEAAR YLERLIKLGR
160 170 180 190 200
RNGLHLPKET QEKIKSIKKK LSLLCIDFNK NLNEDTTFLP VTREELGGLP
210 220 230 240 250
EDFLNSLEKT EDEKLKVTLK YPHYFPLLKK CHVPETRRKV EEAFNCRCKE
260 270 280 290 300
ENCAILRELV RLRAQKSSLL GFSTHADYVL EMNMAKTSQV VATFLDELAQ
310 320 330 340 350
KLKPLGEQER AVILELKKAE CTKRGLDFDG RINAWDMRYY MNQVEETRYR
360 370 380 390 400
VDQNLLKEYF PMQVVTRGLL GIYQELLGLT FHLEEGAAVW HEDVMLYSVR
410 420 430 440 450
DAASGKVIGK FYLDLYPREG KYGHAACFGL QPGCLRQDGS RQIAIAAMVA
460 470 480 490 500
NFTKPTPDAP SLLQHDEVET YFHEFGHVMH QLCSQAEFAM FSGTHVERDF
510 520 530 540 550
VEAPSQMLEN WVWEAEPLLR MSQHYRTGSA IPQELLEKLI KSRQANTGLF
560 570 580 590 600
NLRQIVLAKV DQALHTQTAA DPAEEYARLC QEILGVPATP GTNMPATFGH
610 620 630 640 650
LAGGYDAQYY GYLWSEVYSA DMFHTRFKQE GILSGKVGMD YRSCILRPGG
660 670 680
SEDASVMLKL FLGRDPKQDA FLLSKGLQVE GCEPPAS
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.
InParanoidi P47788.
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 29, 2014
This is version 92 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