CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001802
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Carboxypeptidase Y 
Protein Synonyms/Alias
 cpY; Carboxypeptidase YSCY 
Gene Name
 PRC1 
Gene Synonyms/Alias
 YMR297W 
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
476DEEFASQKVRNWTASubiquitination[1]
496AGEVKSYKHFTYLRVacetylation[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
 Involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate. 
Sequence Annotation
 MOTIF 24 27 Vacuolar targeting signal.
 ACT_SITE 257 257
 ACT_SITE 449 449 By similarity.
 ACT_SITE 508 508
 BINDING 452 452 Substrate.
 BINDING 509 509 Substrate.
 CARBOHYD 124 124 N-linked (GlcNAc...).
 CARBOHYD 198 198 N-linked (GlcNAc...).
 CARBOHYD 279 279 N-linked (GlcNAc...).
 CARBOHYD 479 479 N-linked (GlcNAc...).
 DISULFID 167 409
 DISULFID 304 318
 DISULFID 328 351
 DISULFID 335 344
 DISULFID 373 379  
Keyword
 3D-structure; Carboxypeptidase; Complete proteome; Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome; Signal; Vacuole; Zymogen. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 532 AA 
Protein Sequence
MKAFTSLLCG LGLSTTLAKA ISLQRPLGLD KDVLLQAAEK FGLDLDLDHL LKELDSNVLD 60
AWAQIEHLYP NQVMSLETST KPKFPEAIKT KKDWDFVVKN DAIENYQLRV NKIKDPKILG 120
IDPNVTQYTG YLDVEDEDKH FFFWTFESRN DPAKDPVILW LNGGPGCSSL TGLFFELGPS 180
SIGPDLKPIG NPYSWNSNAT VIFLDQPVNV GFSYSGSSGV SNTVAAGKDV YNFLELFFDQ 240
FPEYVNKGQD FHIAGESYAG HYIPVFASEI LSHKDRNFNL TSVLIGNGLT DPLTQYNYYE 300
PMACGEGGEP SVLPSEECSA MEDSLERCLG LIESCYDSQS VWSCVPATIY CNNAQLAPYQ 360
RTGRNVYDIR KDCEGGNLCY PTLQDIDDYL NQDYVKEAVG AEVDHYESCN FDINRNFLFA 420
GDWMKPYHTA VTDLLNQDLP ILVYAGDKDF ICNWLGNKAW TDVLPWKYDE EFASQKVRNW 480
TASITDEVAG EVKSYKHFTY LRVFNGGHMV PFDVPENALS MVNEWIHGGF SL 532 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; IDA:SGD.
 GO:0000328; C:fungal-type vacuole lumen; TAS:SGD.
 GO:0004185; F:serine-type carboxypeptidase activity; IDA:SGD.
 GO:0046938; P:phytochelatin biosynthetic process; IDA:SGD.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0007039; P:vacuolar protein catabolic process; TAS:SGD. 
Interpro
 IPR001563; Peptidase_S10.
 IPR018202; Peptidase_S10_AS.
 IPR008442; Propeptide_carboxypepY. 
Pfam
 PF05388; Carbpep_Y_N
 PF00450; Peptidase_S10 
SMART
  
PROSITE
 PS00560; CARBOXYPEPT_SER_HIS
 PS00131; CARBOXYPEPT_SER_SER 
PRINTS
 PR00724; CRBOXYPTASEC.