THOP1_BOVIN
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 03-AUG-2022, entry version 96.
DE RecName: Full=Thimet oligopeptidase;
DE EC=3.4.24.15 {ECO:0000250|UniProtKB:P52888};
GN Name=THOP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC 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 amino
CC acid residues long (By similarity). Involved in cytoplasmic peptide
CC degradation. Able to degrade the amyloid-beta precursor protein and
CC generate amyloidogenic fragments (By similarity). Also acts as a
CC regulator of cannabinoid signaling pathway by mediating degradation of
CC hemopressin, an antagonist peptide of the cannabinoid receptor CNR1 (By
CC similarity). {ECO:0000250|UniProtKB:P24155,
CC ECO:0000250|UniProtKB:P52888}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage of bonds with hydrophobic residues at
CC P1, P2 and P3' and a small residue at P1' in substrates of 5 to 15
CC residues.; EC=3.4.24.15; Evidence={ECO:0000250|UniProtKB:P52888};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P52888};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P52888};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P47788}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P47788}.
CC -!- SIMILARITY: Belongs to the peptidase M3 family. {ECO:0000305}.
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DR EMBL; BT025355; ABF57311.1; -; mRNA.
DR EMBL; BC149983; AAI49984.1; -; mRNA.
DR RefSeq; NP_001029163.2; NM_001033991.3.
DR AlphaFoldDB; Q1JPJ8; -.
DR SMR; Q1JPJ8; -.
DR STRING; 9913.ENSBTAP00000027246; -.
DR MEROPS; M03.001; -.
DR PaxDb; Q1JPJ8; -.
DR PeptideAtlas; Q1JPJ8; -.
DR PRIDE; Q1JPJ8; -.
DR GeneID; 510889; -.
DR KEGG; bta:510889; -.
DR CTD; 7064; -.
DR eggNOG; KOG2089; Eukaryota.
DR HOGENOM; CLU_001805_2_0_1; -.
DR InParanoid; Q1JPJ8; -.
DR OrthoDB; 642479at2759; -.
DR TreeFam; TF300459; -.
DR BRENDA; 3.4.24.15; 908.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR Gene3D; 1.10.1370.10; -; 1.
DR Gene3D; 1.20.1050.40; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR024080; Neurolysin/TOP_N.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804; PTHR11804; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease;
KW Phosphoprotein; Protease; Reference proteome; Zinc.
FT CHAIN 1..687
FT /note="Thimet oligopeptidase"
FT /id="PRO_0000263069"
FT ACT_SITE 474
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 473
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 477
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 480
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C1A5"
FT MOD_RES 278
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8C1A5"
FT MOD_RES 538
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52888"
FT CONFLICT 50
FT /note="C -> R (in Ref. 2; AAI49984)"
FT /evidence="ECO:0000305"
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
