[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. TISSUE=Testis; DOI=10.1021/bi00497a006; PubMed=2261476 [NCBI, ExPASy, EBI, Israel, Japan] Pierotti A., Dong K.-W., Glucksman M.J., Orlowski M., Roberts J.L.; "Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15."; Biochemistry 29:10323-10329(1990).
[2]	SEQUENCE REVISION. PubMed=8216239 [NCBI, ExPASy, EBI, Israel, Japan] McKie N., Dando P.M., Rawlings N.D., Barrett A.J.; "Thimet oligopeptidase: similarity to 'soluble angiotensin II-binding protein' and some corrections to the published amino acid sequence of the rat testis enzyme."; Biochem. J. 295:57-60(1993).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Testis; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	PROTEIN SEQUENCE OF 35-45; 267-273; 311-317; 351-357; 411-418 AND 560-578, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Hippocampus; Lubec G., Chen W.-Q.; Submitted (APR-2007) to UniProtKB.

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: Monomer.
SUBCELLULAR LOCATION: Cytoplasm.
TISSUE SPECIFICITY: Expressed abundantly in the testis. It is also found in the liver, lung and kidney.
SIMILARITY: Belongs to the peptidase M3 family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M61142; AAA41586.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC081706; AAH81706.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S38760; HYRTTH.

NP_742072.2; -.

3D structure databases

HSSP

P42676; 1I1I. [HSSP ENTRY / PDB]

SMR

P24155; 24-677.

ModBase

P24155.

Protein family/group databases

MEROPS

M03.001; -.

PTM databases

PhosphoSite

P24155; -.

Organism-specific databases

RGD

68330; Thop1.

Gene expression databases

ArrayExpress

P24155; -.

GermOnline

ENSRNOG00000019924; Rattus norvegicus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004222;	Molecular function: metalloendopeptidase activity (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001567; Pept_M3A_M3B.
IPR006025; Pept_M_Zn_BS.
Graphical view of domain structure.

Pfam

PF01432; Peptidase_M3; 1.
Pfam graphical view of domain structure.

PROSITE

PS00142; ZINC_PROTEASE; 1.

Genome annotation databases

Ensembl

ENSRNOG00000019924; Rattus norvegicus. [Contig view]

GeneID

64517; -.

KEGG

rno:64517; -.

Phylogenomic databases

HOVERGEN

P24155; -.

Other

613318; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease; Phosphoprotein; Protease; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 687`	`686`	`Thimet oligopeptidase.`	`PRO_0000078155`
`ACT_SITE`	`474 474`		`By similarity.`
`METAL`	`473 473`		`Zinc; catalytic (By similarity).`
`METAL`	`477 477`		`Zinc; catalytic (By similarity).`
`METAL`	`480 480`		`Zinc; catalytic (By similarity).`
`MOD_RES`	`278 278`		`Phosphotyrosine (By similarity).`
`CONFLICT`	`321 321`		`C -> S (in Ref. 1; AAA41586).`
`CONFLICT`	`347 348`		`TR -> DS (in Ref. 1; AAA41586).`

Sequence information

Length: 687 AA [This is the length of the unprocessed precursor]

Molecular weight: 78385 Da [This is the MW of the unprocessed precursor]

CRC64: A0B399AF61B60F81 [This is a checksum on the sequence]

        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

P24155 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools