CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010858
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cysteine proteinase 1, mitochondrial 
Protein Synonyms/Alias
 Bleomycin hydrolase; BLM hydrolase; Homocysteine-thiolactonase; HTLase; Hcy-thiolactonase; Leucine aminopeptidase 3; Y3 
Gene Name
 LAP3 
Gene Synonyms/Alias
 BLH1; GAL6; YCP1; YNL239W; N1118 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
71ADDALLNKTRLQKQDubiquitination[1]
288TPLEFASKYAKLDPSacetylation[2]
358FFGSHTPKFMDKKTGacetylation[2]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919] 
Functional Description
 The normal physiological role of the enzyme is unknown, but it is not essential for the viability of yeast cells. Has aminopeptidase activity, shortening substrate peptides sequentially by 1 amino acid. Has bleomycin hydrolase activity, which can protect the cell from the toxic effects of bleomycin. Has homocysteine-thiolactonase activity, protecting the cell against homocysteine toxicity. Acts as a repressor in the GAL4 regulatory system, but this does not require either the peptidase or nucleic acid-binding activities. 
Sequence Annotation
 ACT_SITE 102 102
 ACT_SITE 398 398
 ACT_SITE 421 421  
Keyword
 3D-structure; Alternative initiation; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Hydrolase; Mitochondrion; Protease; Reference proteome; Thiol protease; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 483 AA 
Protein Sequence
MLPTSVSRSL YLKTFRSHLL RAPQIVLKRM SSSIDISKIN SWNKEFQSDL THQLATTVLK 60
NYNADDALLN KTRLQKQDNR VFNTVVSTDS TPVTNQKSSG RCWLFAATNQ LRLNVLSELN 120
LKEFELSQAY LFFYDKLEKA NYFLDQIVSS ADQDIDSRLV QYLLAAPTED GGQYSMFLNL 180
VKKYGLIPKD LYGDLPYSTT ASRKWNSLLT TKLREFAETL RTALKERSAD DSIIVTLREQ 240
MQREIFRLMS LFMDIPPVQP NEQFTWEYVD KDKKIHTIKS TPLEFASKYA KLDPSTPVSL 300
INDPRHPYGK LIKIDRLGNV LGGDAVIYLN VDNETLSKLV VKRLQNNKAV FFGSHTPKFM 360
DKKTGVMDIE LWNYPAIGYN LPQQKASRIR YHESLMTHAM LITGCHVDET SKLPLRYRVE 420
NSWGKDSGKD GLYVMTQKYF EEYCFQIVVD INELPKELAS KFTSGKEEPI VLPIWDPMGA 480
LAK 483 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
 GO:0008234; F:cysteine-type peptidase activity; IDA:SGD.
 GO:0003690; F:double-stranded DNA binding; IDA:SGD.
 GO:0003729; F:mRNA binding; IDA:SGD.
 GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:SGD.
 GO:0003697; F:single-stranded DNA binding; IDA:SGD.
 GO:0043418; P:homocysteine catabolic process; IMP:SGD.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:SGD.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0046677; P:response to antibiotic; IDA:SGD. 
Interpro
 IPR000169; Pept_cys_AS.
 IPR025660; Pept_his_AS.
 IPR004134; Peptidase_C1B. 
Pfam
 PF03051; Peptidase_C1_2 
SMART
  
PROSITE
 PS00640; THIOL_PROTEASE_ASN
 PS00139; THIOL_PROTEASE_CYS
 PS00639; THIOL_PROTEASE_HIS 
PRINTS