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Protein

Thimet oligopeptidase

Gene

THOP1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 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. Able to degrade the beta-amyloid precursor protein and generate amyloidogenic fragments (By similarity).By similarity

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

Zn2+By similarityNote: 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: Ensembl

GO - Biological processi

  1. intracellular signal transduction Source: Ensembl
  2. peptide metabolic process Source: Ensembl
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)
Gene namesi
Name:THOP1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 7

Subcellular locationi

Cytoplasm By similarity

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_0000263069Add
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

PaxDbiQ1JPJ8.
PRIDEiQ1JPJ8.

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ1JPJ8.
SMRiQ1JPJ8. Positions 24-677.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M3 family.Curated

Phylogenomic databases

eggNOGiCOG0339.
GeneTreeiENSGT00550000074738.
HOGENOMiHOG000245985.
HOVERGENiHBG000238.
InParanoidiQ1JPJ8.
KOiK01392.
OrthoDBiEOG7SR4KW.
TreeFamiTF300459.

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.

Q1JPJ8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKPPAACTGD ALDVVAPCSA VNHLRWDLSA QQIAELTTEL IEQTKRVYDC
60 70 80 90 100
VGAQEPQDVS YENTLKALAD VEVSYTVQRN ILDFPQHVSP SKDIRTASTE
110 120 130 140 150
ADKKLSEFDV EMSMRQDVYQ RIVWLQEKVQ KDSLRPEASR YLERLIKLGR
160 170 180 190 200
RNGLHLPEET QEKIKSIKKK LSLLCIDFNK NLNEDTTFLP FTREELGGLP
210 220 230 240 250
EDFLNSLEKT EDEKLKVTLK YPHYFPLLKK CHVPETRRKV EEAFNCRCKE
260 270 280 290 300
ENCAILRELV RLRAQKSRLL GFSTHADYVL EMNMAKTSQV VATFLDELAQ
310 320 330 340 350
KLKPLGEQER AVILELKRAE CEQRGLAFDG RINAWDMRYY MNQVEETRYR
360 370 380 390 400
VDQNLLKEYF PMQVVTRGLL GIYQELLGLS FQLEEGAAVW HEDVALYAVR
410 420 430 440 450
DAASGKLIGK FYLDLYPREG KYGHAACFGL QPGCLRKDGS RQIAIAAMVA
460 470 480 490 500
NFTKPTPDAP SLLQHDEVET YFHEFGHVMH QLCSQAEFAM FSGTHVERDF
510 520 530 540 550
VEAPSQMLEN WVWEAEPLLR MSQHYRTGSS IPQELLDKLI KSRQANTGLF
560 570 580 590 600
NLRQIVLAKV DQALHTQTAA DPAKEYARLC QEILGVPATP GTNMPATFGH
610 620 630 640 650
LAGGYDAQYY GYLWSEVYSA DMFHTRFKQE GVLSGKVGMD YRSCILRPGG
660 670 680
SEDASVMLKL FLGRDPKQDA FLLSKGLQVE GCEPPAC
Length:687
Mass (Da):78,139
Last modified:January 23, 2007 - v3
Checksum:i70627C332F5A7B8B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501C → R in AAI49984. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT025355 mRNA. Translation: ABF57311.1.
BC149983 mRNA. Translation: AAI49984.1.
RefSeqiNP_001029163.2. NM_001033991.3.
UniGeneiBt.21827.

Genome annotation databases

EnsembliENSBTAT00000027246; ENSBTAP00000027246; ENSBTAG00000020446.
GeneIDi510889.
KEGGibta:510889.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT025355 mRNA. Translation: ABF57311.1.
BC149983 mRNA. Translation: AAI49984.1.
RefSeqiNP_001029163.2. NM_001033991.3.
UniGeneiBt.21827.

3D structure databases

ProteinModelPortaliQ1JPJ8.
SMRiQ1JPJ8. Positions 24-677.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM03.001.

Proteomic databases

PaxDbiQ1JPJ8.
PRIDEiQ1JPJ8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000027246; ENSBTAP00000027246; ENSBTAG00000020446.
GeneIDi510889.
KEGGibta:510889.

Organism-specific databases

CTDi7064.

Phylogenomic databases

eggNOGiCOG0339.
GeneTreeiENSGT00550000074738.
HOGENOMiHOG000245985.
HOVERGENiHBG000238.
InParanoidiQ1JPJ8.
KOiK01392.
OrthoDBiEOG7SR4KW.
TreeFamiTF300459.

Miscellaneous databases

NextBioi20869665.

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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Thymus.

Entry informationi

Entry nameiTHOP1_BOVIN
AccessioniPrimary (citable) accession number: Q1JPJ8
Secondary accession number(s): A6QQT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 64 of the entry and version 3 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.