CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005270
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Thimet oligopeptidase 
Protein Synonyms/Alias
 Endo-oligopeptidase A; Endopeptidase 24.15; PZ-peptidase; Soluble metallo-endopeptidase 
Gene Name
 Thop1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
92PQHVSPNKDIRAASTacetylation[1]
220GKLKVTLKYPHYFPLacetylation[1]
229PHYFPLLKKCHVPETacetylation[1]
257EENCAILKELVSLRAacetylation[1]
538APEDLLEKLIKSRQAacetylation[1]
667QFLGRDPKQDAFLLSacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
 Involved in the metabolism of neuropeptides under 20 amino acid residues long. Involved in cytoplasmic peptide degradation. 
Sequence Annotation
 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 257 257 N6-acetyllysine (By similarity).
 MOD_RES 278 278 Phosphotyrosine (By similarity).
 MOD_RES 538 538 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease; Phosphoprotein; Protease; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 687 AA 
Protein Sequence
MKPPAACAGD VVDTVSPCST VNHLRWDLSA QQIRALTTQL IEQTKCVYDR VGAQDFEDVS 60
YESTLKALAD VEVTYTVQRN ILDFPQHVSP NKDIRAASTE ADKKLSEFDV EMSMRQDVYQ 120
RVVWLQEKIP KDSLKPEAAR YLERLIKLGR RNGLHLPQDT QEKIKNIKKR LSLLCIDFNK 180
NLNEDTTFLP FTREELGGLP EDFLNSLEKT EDGKLKVTLK YPHYFPLLKK CHVPETRRLL 240
EEAFNCRCKE ENCAILKELV SLRAQKSNLL GFRTHADYVL EMNMAKTSQT VATFLDELAR 300
KLKPLGEQER AVILELKEAE CAKRGLPFDG RIHAWDMRYY MNQVEETRYR VDQNLLKEYF 360
PMQVVTRGLL AIYQELLGLT FTLEEGAAAW HEDVRLYSVR DAASGEEIGK FYLDLYPREG 420
KYGHAACFGL QPGCLRQDGS RQLAIAAMVA NFTKPTPDVP SLLQHDEVET YFHEFGHVMH 480
QLCSQAEFAM FSGTHVERDF VEAPSQMLEN WVWEKEPLMR MSQHYRTGGE APEDLLEKLI 540
KSRQANAGLF NLRQIVLAKV DQVLHTQTDV DPAEEYARLC QEILGVPATP GTNMPATFGH 600
LAGGYDAQYY GYLWSEVYSM DMFHTRFKQE GVLSPKVGMD YRTSILRPGG SEDASTMLKQ 660
FLGRDPKQDA FLLSKGLQVE GCEPPAC 687 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004222; F:metalloendopeptidase activity; TAS:RGD.
 GO:0042277; F:peptide binding; IDA:RGD.
 GO:0007243; P:intracellular protein kinase cascade; IEA:Compara.
 GO:0006518; P:peptide metabolic process; IEA:Compara.
 GO:0006508; P:proteolysis; TAS:RGD. 
Interpro
 IPR024079; MetalloPept_cat_dom.
 IPR024077; Neurolysin/TOP_dom2.
 IPR024080; Neurolysin/TOP_N.
 IPR001567; Pept_M3A_M3B. 
Pfam
 PF01432; Peptidase_M3 
SMART
  
PROSITE
 PS00142; ZINC_PROTEASE 
PRINTS