ID   THOP1_BOVIN             Reviewed;         687 AA.
AC   Q1JPJ8; A6QQT3;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=Thimet oligopeptidase;
DE            EC=3.4.24.15;
GN   Name=THOP1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the metabolism of neuropeptides under 20
CC       amino acid residues long. Involved in cytoplasmic peptide
CC       degradation. Able to degrade the beta-amyloid precursor protein
CC       and generate amyloidogenic fragments (By similarity).
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 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
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DR   EMBL; BT025355; ABF57311.1; -; mRNA.
DR   EMBL; BC149983; AAI49984.1; -; mRNA.
DR   IPI; IPI00867151; -.
DR   RefSeq; NP_001029163.2; -.
DR   UniGene; Bt.21827; -.
DR   SMR; Q1JPJ8; 24-677.
DR   MEROPS; M03.001; -.
DR   Ensembl; ENSBTAG00000020446; Bos taurus.
DR   GeneID; 510889; -.
DR   KEGG; bta:510889; -.
DR   HOVERGEN; Q1JPJ8; -.
DR   BRENDA; 3.4.24.15; 251.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; Phosphoprotein;
KW   Protease; Zinc.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    687       Thimet oligopeptidase.
FT                                /FTId=PRO_0000263069.
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     50     50       C -> R (in Ref. 2; AAI49984).
SQ   SEQUENCE   687 AA;  78139 MW;  70627C332F5A7B8B CRC64;
     MKPPAACTGD ALDVVAPCSA VNHLRWDLSA QQIAELTTEL IEQTKRVYDC VGAQEPQDVS
     YENTLKALAD VEVSYTVQRN ILDFPQHVSP SKDIRTASTE ADKKLSEFDV EMSMRQDVYQ
     RIVWLQEKVQ KDSLRPEASR YLERLIKLGR RNGLHLPEET QEKIKSIKKK LSLLCIDFNK
     NLNEDTTFLP FTREELGGLP EDFLNSLEKT EDEKLKVTLK YPHYFPLLKK CHVPETRRKV
     EEAFNCRCKE ENCAILRELV RLRAQKSRLL GFSTHADYVL EMNMAKTSQV VATFLDELAQ
     KLKPLGEQER AVILELKRAE CEQRGLAFDG RINAWDMRYY MNQVEETRYR VDQNLLKEYF
     PMQVVTRGLL GIYQELLGLS FQLEEGAAVW HEDVALYAVR DAASGKLIGK FYLDLYPREG
     KYGHAACFGL QPGCLRKDGS RQIAIAAMVA NFTKPTPDAP SLLQHDEVET YFHEFGHVMH
     QLCSQAEFAM FSGTHVERDF VEAPSQMLEN WVWEAEPLLR MSQHYRTGSS IPQELLDKLI
     KSRQANTGLF NLRQIVLAKV DQALHTQTAA DPAKEYARLC QEILGVPATP GTNMPATFGH
     LAGGYDAQYY GYLWSEVYSA DMFHTRFKQE GVLSGKVGMD YRSCILRPGG SEDASVMLKL
     FLGRDPKQDA FLLSKGLQVE GCEPPAC
//