CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014975
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Carboxypeptidase Q 
Protein Synonyms/Alias
 Hematopoietic lineage switch 2 related protein; Hls2-rp; Liver annexin-like protein 1; LAL-1; Plasma glutamate carboxypeptidase 
Gene Name
 Cpq 
Gene Synonyms/Alias
 Pgcp 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
182QPYTDYGKTVQYRERacetylation[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
 Carboxypeptidase that may play an important role in the hydrolysis of circulating peptides. Catalyzes the hydrolysis of dipeptides with unsubstituted terminals into amino acids. May play a role in the liberation of thyroxine hormone from its thyroglobulin (Tg) precursor. 
Sequence Annotation
 ACT_SITE 336 336 Nucleophile (By similarity).
 METAL 290 290 Zinc 2 (By similarity).
 METAL 302 302 Zinc 1 (By similarity).
 METAL 302 302 Zinc 2 (By similarity).
 METAL 337 337 Zinc 1 (By similarity).
 METAL 364 364 Zinc 2 (By similarity).
 METAL 434 434 Zinc 1 (By similarity).
 CARBOHYD 61 61 N-linked (GlcNAc...) (Potential).
 CARBOHYD 353 353 N-linked (GlcNAc...) (Potential).
 CARBOHYD 396 396 N-linked (GlcNAc...) (Potential).  
Keyword
 Carboxypeptidase; Complete proteome; Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Hydrolase; Lysosome; Metal-binding; Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc; Zymogen. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 472 AA 
Protein Sequence
MRFLFFLFVA VVHLFSLGSG KAIYKSGVSQ RTFQEIKEEI ANYEDVAKAI INLAVYGKYQ 60
NRSYERLGLL VDTVGPRLSG SKNLEKAIQI MYQNLQQDGL ENVHLEQVRI PHWERGEESA 120
VMVVPRIHKL AILGLGGSIG TPPEGITAEV LVVASFVELQ RRASEARGKI VVYNQPYTDY 180
GKTVQYRERG AVEAAKVGAV ASLIRSVASF SIYSPHTGHQ GYQDGVPKIP TACITIEDAE 240
MMSRMASRGD KIVIHLKMGA KTYPDTDSFN TVAEITGSKY PEEVVLVSGH LDSWDVGQGA 300
LDDGGGAFIS WEALSLVKDL GLRPKRTLRL VLWTAEEQGG VGASQYYELH KANISKYSLV 360
MEADSGTFLP TGLQFTGSDK ARAIMKEVMS LLQPLNITKV FNDAEGTDIN FWIQAGVPGA 420
SLRDDLYKYF FFHHSHGDTM TAMDPKQMNV AAAVWAVVAY VVADMEEMLP RS 472 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
 GO:0005615; C:extracellular space; IDA:UniProtKB.
 GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
 GO:0005764; C:lysosome; IDA:UniProtKB.
 GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0070573; F:metallodipeptidase activity; ISS:UniProtKB.
 GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
 GO:0043171; P:peptide catabolic process; ISS:UniProtKB.
 GO:0006508; P:proteolysis; IDA:UniProtKB.
 GO:0006590; P:thyroid hormone generation; IDA:UniProtKB.
 GO:0042246; P:tissue regeneration; IEP:RGD. 
Interpro
 IPR007484; Peptidase_M28. 
Pfam
 PF04389; Peptidase_M28 
SMART
  
PROSITE
  
PRINTS