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Protein

Thimet oligopeptidase

Gene

Thop1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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

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

  • metal ion binding Source: UniProtKB-KW
  • metalloendopeptidase activity Source: RGD
  • peptidase activity Source: RGD
  • peptide binding Source: RGD

GO - Biological processi

  • proteolysis Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.15. 5301.

Protein family/group databases

MEROPSiM03.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Thimet oligopeptidase (EC:3.4.24.15)
Alternative name(s):
Endo-oligopeptidase A
Endopeptidase 24.15
PZ-peptidase
Soluble metallo-endopeptidase
Gene namesi
Name:Thop1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi68330. Thop1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 687687Thimet oligopeptidasePRO_0000078155Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei257 – 2571N6-acetyllysineBy similarity
Modified residuei278 – 2781PhosphotyrosineBy similarity
Modified residuei538 – 5381N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP24155.
PRIDEiP24155.

PTM databases

PhosphoSiteiP24155.

Expressioni

Tissue specificityi

Expressed abundantly in the testis. It is also found in the liver, lung and kidney.

Gene expression databases

GenevisibleiP24155. RN.

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
Calm3P621612EBI-6372841,EBI-397530

Protein-protein interaction databases

BioGridi249102. 1 interaction.
IntActiP24155. 2 interactions.
STRINGi10116.ENSRNOP00000027045.

Structurei

3D structure databases

ProteinModelPortaliP24155.
SMRiP24155. Positions 24-677.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M3 family.Curated

Phylogenomic databases

eggNOGiCOG0339.
GeneTreeiENSGT00550000074738.
HOGENOMiHOG000245985.
HOVERGENiHBG000238.
InParanoidiP24155.
KOiK01392.
OMAiGCEPPAC.
OrthoDBiEOG7SR4KW.
PhylomeDBiP24155.
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.

P24155-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPPAACAGD VVDTVSPCST VNHLRWDLSA QQIRALTTQL IEQTKCVYDR
60 70 80 90 100
VGAQDFEDVS YESTLKALAD VEVTYTVQRN ILDFPQHVSP NKDIRAASTE
110 120 130 140 150
ADKKLSEFDV EMSMRQDVYQ RVVWLQEKIP KDSLKPEAAR YLERLIKLGR
160 170 180 190 200
RNGLHLPQDT QEKIKNIKKR LSLLCIDFNK NLNEDTTFLP FTREELGGLP
210 220 230 240 250
EDFLNSLEKT EDGKLKVTLK YPHYFPLLKK CHVPETRRLL EEAFNCRCKE
260 270 280 290 300
ENCAILKELV SLRAQKSNLL GFRTHADYVL EMNMAKTSQT VATFLDELAR
310 320 330 340 350
KLKPLGEQER AVILELKEAE CAKRGLPFDG RIHAWDMRYY MNQVEETRYR
360 370 380 390 400
VDQNLLKEYF PMQVVTRGLL AIYQELLGLT FTLEEGAAAW HEDVRLYSVR
410 420 430 440 450
DAASGEEIGK FYLDLYPREG KYGHAACFGL QPGCLRQDGS RQLAIAAMVA
460 470 480 490 500
NFTKPTPDVP SLLQHDEVET YFHEFGHVMH QLCSQAEFAM FSGTHVERDF
510 520 530 540 550
VEAPSQMLEN WVWEKEPLMR MSQHYRTGGE APEDLLEKLI KSRQANAGLF
560 570 580 590 600
NLRQIVLAKV DQVLHTQTDV DPAEEYARLC QEILGVPATP GTNMPATFGH
610 620 630 640 650
LAGGYDAQYY GYLWSEVYSM DMFHTRFKQE GVLSPKVGMD YRTSILRPGG
660 670 680
SEDASTMLKQ FLGRDPKQDA FLLSKGLQVE GCEPPAC
Length:687
Mass (Da):78,385
Last modified:February 26, 2008 - v4
Checksum:iA0B399AF61B60F81
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti321 – 3211C → S in AAA41586 (PubMed:2261476).Curated
Sequence conflicti347 – 3482TR → DS in AAA41586 (PubMed:2261476).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61142 mRNA. Translation: AAA41586.1.
BC081706 mRNA. Translation: AAH81706.1.
PIRiS38760. HYRTTH.
RefSeqiNP_742072.2. NM_172075.2.
UniGeneiRn.9490.

Genome annotation databases

EnsembliENSRNOT00000027045; ENSRNOP00000027045; ENSRNOG00000019924.
GeneIDi64517.
KEGGirno:64517.
UCSCiRGD:68330. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61142 mRNA. Translation: AAA41586.1.
BC081706 mRNA. Translation: AAH81706.1.
PIRiS38760. HYRTTH.
RefSeqiNP_742072.2. NM_172075.2.
UniGeneiRn.9490.

3D structure databases

ProteinModelPortaliP24155.
SMRiP24155. Positions 24-677.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249102. 1 interaction.
IntActiP24155. 2 interactions.
STRINGi10116.ENSRNOP00000027045.

Protein family/group databases

MEROPSiM03.001.

PTM databases

PhosphoSiteiP24155.

Proteomic databases

PaxDbiP24155.
PRIDEiP24155.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000027045; ENSRNOP00000027045; ENSRNOG00000019924.
GeneIDi64517.
KEGGirno:64517.
UCSCiRGD:68330. rat.

Organism-specific databases

CTDi7064.
RGDi68330. Thop1.

Phylogenomic databases

eggNOGiCOG0339.
GeneTreeiENSGT00550000074738.
HOGENOMiHOG000245985.
HOVERGENiHBG000238.
InParanoidiP24155.
KOiK01392.
OMAiGCEPPAC.
OrthoDBiEOG7SR4KW.
PhylomeDBiP24155.
TreeFamiTF300459.

Enzyme and pathway databases

BRENDAi3.4.24.15. 5301.

Miscellaneous databases

NextBioi613318.
PROiP24155.

Gene expression databases

GenevisibleiP24155. RN.

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

« Hide 'large scale' publications
  1. "Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15."
    Pierotti A., Dong K.-W., Glucksman M.J., Orlowski M., Roberts J.L.
    Biochemistry 29:10323-10329(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Testis.
  2. "Thimet oligopeptidase: similarity to 'soluble angiotensin II-binding protein' and some corrections to the published amino acid sequence of the rat testis enzyme."
    McKie N., Dando P.M., Rawlings N.D., Barrett A.J.
    Biochem. J. 295:57-60(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  4. Lubec G., Chen W.-Q.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 35-45; 267-273; 311-317; 351-357; 411-418 AND 560-578, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.

Entry informationi

Entry nameiTHOP1_RAT
AccessioniPrimary (citable) accession number: P24155
Secondary accession number(s): Q66HS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: February 26, 2008
Last modified: July 22, 2015
This is version 124 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.