THOP1_PIG
ID THOP1_PIG Reviewed; 687 AA.
AC P47788;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Thimet oligopeptidase;
DE EC=3.4.24.15 {ECO:0000250|UniProtKB:P52888};
DE AltName: Full=Endopeptidase 24.15;
GN Name=THOP1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=8168506; DOI=10.1111/j.1432-1033.1994.tb18725.x;
RA Kato A., Sugiura N., Hagiwara H., Hirose S.;
RT "Cloning, amino acid sequence and tissue distribution of porcine thimet
RT oligopeptidase. A comparison with soluble angiotensin-binding protein.";
RL Eur. J. Biochem. 221:159-165(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=9182559; DOI=10.1074/jbc.272.24.15313;
RA Kato A., Sugiura N., Saruta Y., Hosoiri T., Yasue H., Hirose S.;
RT "Targeting of endopeptidase 24.16 to different subcellular compartments by
RT alternative promoter usage.";
RL J. Biol. Chem. 272:15313-15322(1997).
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:0000269|PubMed:8168506}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8168506}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8168506}.
CC -!- SIMILARITY: Belongs to the peptidase M3 family. {ECO:0000305}.
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DR EMBL; D21871; BAA04882.1; -; mRNA.
DR EMBL; AB000438; BAA19107.1; -; Genomic_DNA.
DR PIR; S43250; S43250.
DR RefSeq; NP_999388.1; NM_214223.2.
DR AlphaFoldDB; P47788; -.
DR SMR; P47788; -.
DR STRING; 9823.ENSSSCP00000014316; -.
DR MEROPS; M03.001; -.
DR PaxDb; P47788; -.
DR PeptideAtlas; P47788; -.
DR PRIDE; P47788; -.
DR GeneID; 397442; -.
DR KEGG; ssc:397442; -.
DR CTD; 7064; -.
DR eggNOG; KOG2089; Eukaryota.
DR InParanoid; P47788; -.
DR OrthoDB; 642479at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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_0000078154"
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"
SQ SEQUENCE 687 AA; 78144 MW; 70AEF85C6C466929 CRC64;
MKPPAACAGD ALDVAAPCSA VNYLRWDLSA QQIGELTTEL IEQTKRVYDR VGTQELQDVS
YENTLKALAD VEVSYTVQRN ILDFPQHVSP CKDIRTASTE ADKKLSEFDV EMSMRQDVYQ
RIVWLQEKVQ KDSLRPEAAR YLERLIKLGR RNGLHLPKET QEKIKSIKKK LSLLCIDFNK
NLNEDTTFLP VTREELGGLP EDFLNSLEKT EDEKLKVTLK YPHYFPLLKK CHVPETRRKV
EEAFNCRCKE ENCAILRELV RLRAQKSSLL GFSTHADYVL EMNMAKTSQV VATFLDELAQ
KLKPLGEQER AVILELKKAE CTKRGLDFDG RINAWDMRYY MNQVEETRYR VDQNLLKEYF
PMQVVTRGLL GIYQELLGLT FHLEEGAAVW HEDVMLYSVR DAASGKVIGK FYLDLYPREG
KYGHAACFGL QPGCLRQDGS RQIAIAAMVA NFTKPTPDAP SLLQHDEVET YFHEFGHVMH
QLCSQAEFAM FSGTHVERDF VEAPSQMLEN WVWEAEPLLR MSQHYRTGSA IPQELLEKLI
KSRQANTGLF NLRQIVLAKV DQALHTQTAA DPAEEYARLC QEILGVPATP GTNMPATFGH
LAGGYDAQYY GYLWSEVYSA DMFHTRFKQE GILSGKVGMD YRSCILRPGG SEDASVMLKL
FLGRDPKQDA FLLSKGLQVE GCEPPAS
