CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003814
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lysosomal protective protein 
Protein Synonyms/Alias
 Carboxypeptidase C; Carboxypeptidase L; Cathepsin A; Protective protein cathepsin A; PPCA; Protective protein for beta-galactosidase; Lysosomal protective protein 32 kDa chain; Lysosomal protective protein 20 kDa chain 
Gene Name
 CTSA 
Gene Synonyms/Alias
 PPGB 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
429QRRPWLVKYGDSGEQubiquitination[1, 2]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 Protective protein appears to be essential for both the activity of beta-galactosidase and neuraminidase, it associates with these enzymes and exerts a protective function necessary for their stability and activity. This protein is also a carboxypeptidase and can deamidate tachykinins. 
Sequence Annotation
 ACT_SITE 178 178
 ACT_SITE 400 400 By similarity.
 ACT_SITE 457 457
 CARBOHYD 145 145 N-linked (GlcNAc...).
 CARBOHYD 333 333 N-linked (GlcNAc...).
 DISULFID 88 362
 DISULFID 240 256
 DISULFID 241 246
 DISULFID 281 331  
Keyword
 3D-structure; Carboxypeptidase; Complete proteome; Direct protein sequencing; Disease mutation; Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease; Reference proteome; Signal; Zymogen. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 480 AA 
Protein Sequence
MIRAAPPPLF LLLLLLLLLV SWASRGEAAP DQDEIQRLPG LAKQPSFRQY SGYLKGSGSK 60
HLHYWFVESQ KDPENSPVVL WLNGGPGCSS LDGLLTEHGP FLVQPDGVTL EYNPYSWNLI 120
ANVLYLESPA GVGFSYSDDK FYATNDTEVA QSNFEALQDF FRLFPEYKNN KLFLTGESYA 180
GIYIPTLAVL VMQDPSMNLQ GLAVGNGLSS YEQNDNSLVY FAYYHGLLGN RLWSSLQTHC 240
CSQNKCNFYD NKDLECVTNL QEVARIVGNS GLNIYNLYAP CAGGVPSHFR YEKDTVVVQD 300
LGNIFTRLPL KRMWHQALLR SGDKVRMDPP CTNTTAASTY LNNPYVRKAL NIPEQLPQWD 360
MCNFLVNLQY RRLYRSMNSQ YLKLLSSQKY QILLYNGDVD MACNFMGDEW FVDSLNQKME 420
VQRRPWLVKY GDSGEQIAGF VKEFSHIAFL TIKGAGHMVP TDKPLAAFTM FSRFLNKQPY 480 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
 GO:0043202; C:lysosomal lumen; TAS:Reactome.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0004180; F:carboxypeptidase activity; TAS:ProtInc.
 GO:0008047; F:enzyme activator activity; TAS:ProtInc.
 GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
 GO:0006687; P:glycosphingolipid metabolic process; TAS:Reactome.
 GO:0006886; P:intracellular protein transport; TAS:ProtInc.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome. 
Interpro
 IPR001563; Peptidase_S10.
 IPR018202; Peptidase_S10_AS. 
Pfam
 PF00450; Peptidase_S10 
SMART
  
PROSITE
 PS00560; CARBOXYPEPT_SER_HIS
 PS00131; CARBOXYPEPT_SER_SER 
PRINTS
 PR00724; CRBOXYPTASEC.