ID   THOP1_RAT               Reviewed;         687 AA.
AC   P24155; Q66HS4;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 4.
DT   16-JUN-2009, entry version 79.
DE   RecName: Full=Thimet oligopeptidase;
DE            EC=3.4.24.15;
DE   AltName: Full=Endo-oligopeptidase A;
DE   AltName: Full=Endopeptidase 24.15;
DE   AltName: Full=PZ-peptidase;
DE   AltName: Full=Soluble metallo-endopeptidase;
GN   Name=Thop1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Testis;
RX   MEDLINE=91084500; PubMed=2261476; DOI=10.1021/bi00497a006;
RA   Pierotti A., Dong K.-W., Glucksman M.J., Orlowski M., Roberts J.L.;
RT   "Molecular cloning and primary structure of rat testes
RT   metalloendopeptidase EC 3.4.24.15.";
RL   Biochemistry 29:10323-10329(1990).
RN   [2]
RP   SEQUENCE REVISION.
RX   MEDLINE=94029935; PubMed=8216239;
RA   McKie N., Dando P.M., Rawlings N.D., Barrett A.J.;
RT   "Thimet oligopeptidase: similarity to 'soluble angiotensin II-binding
RT   protein' and some corrections to the published amino acid sequence of
RT   the rat testis enzyme.";
RL   Biochem. J. 295:57-60(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 35-45; 267-273; 311-317; 351-357; 411-418 AND
RP   560-578, AND MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA   Lubec G., Chen W.-Q.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Involved in the metabolism of neuropeptides under 20
CC       amino acid residues long. Involved in cytoplasmic peptide
CC       degradation.
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage of bonds with
CC       hydrophobic residues at P1, P2 and P3' and a small residue at P1'
CC       in substrates of 5 to 15 residues.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Expressed abundantly in the testis. It is also
CC       found in the liver, lung and kidney.
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
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DR   EMBL; M61142; AAA41586.1; -; mRNA.
DR   EMBL; BC081706; AAH81706.1; -; mRNA.
DR   IPI; IPI00211777; -.
DR   PIR; S38760; HYRTTH.
DR   RefSeq; NP_742072.2; -.
DR   UniGene; Rn.9490; -.
DR   HSSP; P42676; 1I1I.
DR   SMR; P24155; 24-677.
DR   MEROPS; M03.001; -.
DR   PhosphoSite; P24155; -.
DR   Ensembl; ENSRNOG00000019924; Rattus norvegicus.
DR   GeneID; 64517; -.
DR   KEGG; rno:64517; -.
DR   RGD; 68330; Thop1.
DR   HOVERGEN; P24155; -.
DR   OMA; P24155; EQTKCVY.
DR   BRENDA; 3.4.24.15; 248.
DR   NextBio; 613318; -.
DR   ArrayExpress; P24155; -.
DR   GermOnline; ENSRNOG00000019924; Rattus norvegicus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005625; C:soluble fraction; IDA:RGD.
DR   GO; GO:0004222; F:metalloendopeptidase activity; TAS:RGD.
DR   GO; GO:0042277; F:peptide binding; IDA:RGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; TAS:RGD.
DR   InterPro; IPR001567; Pept_M3A_M3B.
DR   InterPro; IPR006025; Pept_M_Zn_BS.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Hydrolase; Metal-binding;
KW   Metalloprotease; Phosphoprotein; Protease; Zinc.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    687       Thimet oligopeptidase.
FT                                /FTId=PRO_0000078155.
FT   ACT_SITE    474    474       By similarity.
FT   METAL       473    473       Zinc; catalytic (By similarity).
FT   METAL       477    477       Zinc; catalytic (By similarity).
FT   METAL       480    480       Zinc; catalytic (By similarity).
FT   MOD_RES     278    278       Phosphotyrosine (By similarity).
FT   CONFLICT    321    321       C -> S (in Ref. 1; AAA41586).
FT   CONFLICT    347    348       TR -> DS (in Ref. 1; AAA41586).
SQ   SEQUENCE   687 AA;  78385 MW;  A0B399AF61B60F81 CRC64;
     MKPPAACAGD VVDTVSPCST VNHLRWDLSA QQIRALTTQL IEQTKCVYDR VGAQDFEDVS
     YESTLKALAD VEVTYTVQRN ILDFPQHVSP NKDIRAASTE ADKKLSEFDV EMSMRQDVYQ
     RVVWLQEKIP KDSLKPEAAR YLERLIKLGR RNGLHLPQDT QEKIKNIKKR LSLLCIDFNK
     NLNEDTTFLP FTREELGGLP EDFLNSLEKT EDGKLKVTLK YPHYFPLLKK CHVPETRRLL
     EEAFNCRCKE ENCAILKELV SLRAQKSNLL GFRTHADYVL EMNMAKTSQT VATFLDELAR
     KLKPLGEQER AVILELKEAE CAKRGLPFDG RIHAWDMRYY MNQVEETRYR VDQNLLKEYF
     PMQVVTRGLL AIYQELLGLT FTLEEGAAAW HEDVRLYSVR DAASGEEIGK FYLDLYPREG
     KYGHAACFGL QPGCLRQDGS RQLAIAAMVA NFTKPTPDVP SLLQHDEVET YFHEFGHVMH
     QLCSQAEFAM FSGTHVERDF VEAPSQMLEN WVWEKEPLMR MSQHYRTGGE APEDLLEKLI
     KSRQANAGLF NLRQIVLAKV DQVLHTQTDV DPAEEYARLC QEILGVPATP GTNMPATFGH
     LAGGYDAQYY GYLWSEVYSM DMFHTRFKQE GVLSPKVGMD YRTSILRPGG SEDASTMLKQ
     FLGRDPKQDA FLLSKGLQVE GCEPPAC
//