Reviewed, UniProtKB/Swiss-Prot P24155 (THOP1_RAT)

Names and origin

Protein names

Recommended name:
    Thimet oligopeptidase
    EC=3.4.24.15
Alternative name(s):
    Endo-oligopeptidase A
    Endopeptidase 24.15
    PZ-peptidase
    Soluble metallo-endopeptidase

Gene names

Name:

Thop1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	687 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in the metabolism of neuropeptides under 20 amino acid residues long. Involved in cytoplasmic peptide degradation.
Catalytic activity	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.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Monomer.
Subcellular location	Cytoplasm.
Tissue specificity	Expressed abundantly in the testis. It is also found in the liver, lung and kidney.
Sequence similarities	Belongs to the peptidase M3 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Traceable author statement. Source: RGD
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell soluble fraction Inferred from direct assay. Source: RGD
Molecular function	metalloendopeptidase activity Traceable author statement. Source: RGD peptide binding Inferred from direct assay. Source: RGD zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 687	686	Thimet oligopeptidase		PRO_0000078155
Sites
	Active site	474	1	By similarity
	Metal binding	473	1	Zinc; catalytic By similarity
	Metal binding	477	1	Zinc; catalytic By similarity
	Metal binding	480	1	Zinc; catalytic By similarity
Amino acid modifications
	Modified residue	278	1	Phosphotyrosine By similarity
Experimental info
	Sequence conflict	321	1	C → S in AAA41586. Ref.1
	Sequence conflict	347 – 348	2	TR → DS in AAA41586. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P24155-1 [UniParc]. Last modified February 26, 2008. Version 4. Checksum: A0B399AF61B60F81	FASTA	687	78,385
	10 20 30 40 50 60 MKPPAACAGD VVDTVSPCST VNHLRWDLSA QQIRALTTQL IEQTKCVYDR VGAQDFEDVS 70 80 90 100 110 120 YESTLKALAD VEVTYTVQRN ILDFPQHVSP NKDIRAASTE ADKKLSEFDV EMSMRQDVYQ 130 140 150 160 170 180 RVVWLQEKIP KDSLKPEAAR YLERLIKLGR RNGLHLPQDT QEKIKNIKKR LSLLCIDFNK 190 200 210 220 230 240 NLNEDTTFLP FTREELGGLP EDFLNSLEKT EDGKLKVTLK YPHYFPLLKK CHVPETRRLL 250 260 270 280 290 300 EEAFNCRCKE ENCAILKELV SLRAQKSNLL GFRTHADYVL EMNMAKTSQT VATFLDELAR 310 320 330 340 350 360 KLKPLGEQER AVILELKEAE CAKRGLPFDG RIHAWDMRYY MNQVEETRYR VDQNLLKEYF 370 380 390 400 410 420 PMQVVTRGLL AIYQELLGLT FTLEEGAAAW HEDVRLYSVR DAASGEEIGK FYLDLYPREG 430 440 450 460 470 480 KYGHAACFGL QPGCLRQDGS RQLAIAAMVA NFTKPTPDVP SLLQHDEVET YFHEFGHVMH 490 500 510 520 530 540 QLCSQAEFAM FSGTHVERDF VEAPSQMLEN WVWEKEPLMR MSQHYRTGGE APEDLLEKLI 550 560 570 580 590 600 KSRQANAGLF NLRQIVLAKV DQVLHTQTDV DPAEEYARLC QEILGVPATP GTNMPATFGH 610 620 630 640 650 660 LAGGYDAQYY GYLWSEVYSM DMFHTRFKQE GVLSPKVGMD YRTSILRPGG SEDASTMLKQ 670 680 FLGRDPKQDA FLLSKGLQVE GCEPPAC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2261476] [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: 8216239] [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: 15489334] [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, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M61142 mRNA. Translation: AAA41586.1. BC081706 mRNA. Translation: AAH81706.1.
IPI	IPI00211777.
PIR	HYRTTH. S38760.
RefSeq	NP_742072.2.
UniGene	Rn.9490
3D structure databases
HSSP	HSSP built from PDB template 1I1I based on UniProtKB P42676.
SMR	P24155. Positions 24-677.
ModBase	Search...
Protein family/group databases
MEROPS	M03.001.
PTM databases
PhosphoSite	P24155.
Genome annotation databases
Ensembl	ENSRNOG00000019924. Rattus norvegicus. [Contig view]
GeneID	64517.
KEGG	rno:64517.
Organism-specific databases
RGD	68330. Thop1.
Phylogenomic databases
HOVERGEN	P24155.
OMA	P24155. EQTKCVY.
Enzyme and pathway databases
BRENDA	3.4.24.15. 248.
Gene expression databases
ArrayExpress	P24155.
GermOnline	ENSRNOG00000019924. Rattus norvegicus.
Family and domain databases
InterPro	IPR001567. Pept_M3A_M3B. IPR006025. Pept_M_Zn_BS. [Graphical view]
Pfam	PF01432. Peptidase_M3. 1 hit. [Graphical view]
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	613318.

Entry information

Entry name

THOP1_RAT

Accession

Primary (citable) accession number: P24155
Secondary accession number(s): Q66HS4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	February 26, 2008
Last modified:	June 16, 2009
This is version 79 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)