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Protein

Carboxypeptidase Q

Gene

CPQ

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi290Zinc 1By similarity1
Metal bindingi302Zinc 1By similarity1
Metal bindingi302Zinc 2; catalyticBy similarity1
Active sitei336NucleophileBy similarity1
Metal bindingi337Zinc 2; catalyticBy similarity1
Metal bindingi364Zinc 1By similarity1
Metal bindingi434Zinc 2; catalyticBy similarity1

GO - Molecular functioni

  • carboxypeptidase activity Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • metallodipeptidase activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • peptide catabolic process Source: UniProtKB
  • proteolysis Source: UniProtKB
  • thyroid hormone generation Source: UniProtKB
  • tissue regeneration Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000104324-MONOMER.

Protein family/group databases

MEROPSiM28.014.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase Q (EC:3.4.17.-)
Alternative name(s):
Lysosomal dipeptidase
Plasma glutamate carboxypeptidase
Gene namesi
Name:CPQ
Synonyms:LCH1, PGCP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:16910. CPQ.

Subcellular locationi

  • Endoplasmic reticulum 1 Publication
  • Golgi apparatus 1 Publication
  • Lysosome By similarity
  • Secreted 1 Publication

  • Note: Secretion is stimulated by TSH/thyroid-stimulating hormone, INS/insulin and SST/somatostatin.By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • lysosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Lysosome, Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi10404.
OpenTargetsiENSG00000104324.

Polymorphism and mutation databases

BioMutaiCPQ.
DMDMi74735298.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
PropeptideiPRO_500005594121 – 442 PublicationsAdd BLAST24
ChainiPRO_500005594245 – 472Carboxypeptidase QAdd BLAST428

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi61N-linked (GlcNAc...)Sequence analysis1
Glycosylationi179N-linked (GlcNAc...)2 Publications1
Glycosylationi353N-linked (GlcNAc...)1 Publication1
Glycosylationi356N-linked (GlcNAc...)1 Publication1
Glycosylationi396N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

N-glycosylated. The secreted form is modified by hybrid or complex type oligosaccharide chains (By similarity).By similarity

Keywords - PTMi

Glycoprotein, Zymogen

Proteomic databases

EPDiQ9Y646.
MaxQBiQ9Y646.
PaxDbiQ9Y646.
PeptideAtlasiQ9Y646.
PRIDEiQ9Y646.

PTM databases

iPTMnetiQ9Y646.
PhosphoSitePlusiQ9Y646.

Expressioni

Tissue specificityi

Mainly detected in blood plasma. Abundant in placenta and kidney. Present at low level in muscles, liver and skin fibroblasts. Not detected in brain or white blood cells (at protein level).1 Publication

Inductioni

Up-regulated in the majority of hepatitis C virus-associated hepatocellular carcinoma.1 Publication

Gene expression databases

BgeeiENSG00000104324.
ExpressionAtlasiQ9Y646. baseline and differential.
GenevisibleiQ9Y646. HS.

Organism-specific databases

HPAiHPA023235.
HPA024490.

Interactioni

Subunit structurei

Homodimer. The monomeric form is inactive while the homodimer is active.

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

STRINGi9606.ENSP00000220763.

Structurei

3D structure databases

ProteinModelPortaliQ9Y646.
SMRiQ9Y646.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M28 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2195. Eukaryota.
COG2234. LUCA.
GeneTreeiENSGT00390000018110.
HOGENOMiHOG000295607.
HOVERGENiHBG105014.
InParanoidiQ9Y646.
KOiK01302.
OMAiRVVLFMN.
OrthoDBiEOG091G08CB.
PhylomeDBiQ9Y646.
TreeFamiTF323248.

Family and domain databases

InterProiIPR007484. Peptidase_M28.
[Graphical view]
PfamiPF04389. Peptidase_M28. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Y646-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFLIFAFFG GVHLLSLCSG KAICKNGISK RTFEEIKEEI ASCGDVAKAI
60 70 80 90 100
INLAVYGKAQ NRSYERLALL VDTVGPRLSG SKNLEKAIQI MYQNLQQDGL
110 120 130 140 150
EKVHLEPVRI PHWERGEESA VMLEPRIHKI AILGLGSSIG TPPEGITAEV
160 170 180 190 200
LVVTSFDELQ RRASEARGKI VVYNQPYINY SRTVQYRTQG AVEAAKVGAL
210 220 230 240 250
ASLIRSVASF SIYSPHTGIQ EYQDGVPKIP TACITVEDAE MMSRMASHGI
260 270 280 290 300
KIVIQLKMGA KTYPDTDSFN TVAEITGSKY PEQVVLVSGH LDSWDVGQGA
310 320 330 340 350
MDDGGGAFIS WEALSLIKDL GLRPKRTLRL VLWTAEEQGG VGAFQYYQLH
360 370 380 390 400
KVNISNYSLV MESDAGTFLP TGLQFTGSEK ARAIMEEVMS LLQPLNITQV
410 420 430 440 450
LSHGEGTDIN FWIQAGVPGA SLLDDLYKYF FFHHSHGDTM TVMDPKQMNV
460 470
AAAVWAVVSY VVADMEEMLP RS
Length:472
Mass (Da):51,888
Last modified:November 1, 1999 - v1
Checksum:iEB6CBD2149E042BF
GO

Sequence cautioni

The sequence AAD31418 differs from that shown. Reason: Frameshift at position 446.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti37K → E in BAC11423 (PubMed:16303743).Curated1
Sequence conflicti117E → G in BAC11423 (PubMed:16303743).Curated1
Sequence conflicti385M → V in BAC11423 (PubMed:16303743).Curated1
Sequence conflicti446K → Q in AAD31418 (PubMed:10206990).Curated1
Sequence conflicti449N → D in AAD31418 (PubMed:10206990).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_037466138S → N.Corresponds to variant rs34088584dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF119386 mRNA. Translation: AAD31418.1. Frameshift.
AF107833 mRNA. Translation: AAD43213.1.
AF107834 mRNA. Translation: AAD43214.1.
AK075132 mRNA. Translation: BAC11423.1.
AK315447 mRNA. Translation: BAG37835.1.
CH471060 Genomic DNA. Translation: EAW91757.1.
BC020689 mRNA. Translation: AAH20689.1.
CCDSiCCDS6273.1.
RefSeqiNP_057218.1. NM_016134.3.
UniGeneiHs.156178.

Genome annotation databases

EnsembliENST00000220763; ENSP00000220763; ENSG00000104324.
GeneIDi10404.
KEGGihsa:10404.
UCSCiuc003yhw.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF119386 mRNA. Translation: AAD31418.1. Frameshift.
AF107833 mRNA. Translation: AAD43213.1.
AF107834 mRNA. Translation: AAD43214.1.
AK075132 mRNA. Translation: BAC11423.1.
AK315447 mRNA. Translation: BAG37835.1.
CH471060 Genomic DNA. Translation: EAW91757.1.
BC020689 mRNA. Translation: AAH20689.1.
CCDSiCCDS6273.1.
RefSeqiNP_057218.1. NM_016134.3.
UniGeneiHs.156178.

3D structure databases

ProteinModelPortaliQ9Y646.
SMRiQ9Y646.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000220763.

Protein family/group databases

MEROPSiM28.014.

PTM databases

iPTMnetiQ9Y646.
PhosphoSitePlusiQ9Y646.

Polymorphism and mutation databases

BioMutaiCPQ.
DMDMi74735298.

Proteomic databases

EPDiQ9Y646.
MaxQBiQ9Y646.
PaxDbiQ9Y646.
PeptideAtlasiQ9Y646.
PRIDEiQ9Y646.

Protocols and materials databases

DNASUi10404.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000220763; ENSP00000220763; ENSG00000104324.
GeneIDi10404.
KEGGihsa:10404.
UCSCiuc003yhw.5. human.

Organism-specific databases

CTDi10404.
DisGeNETi10404.
GeneCardsiCPQ.
HGNCiHGNC:16910. CPQ.
HPAiHPA023235.
HPA024490.
neXtProtiNX_Q9Y646.
OpenTargetsiENSG00000104324.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2195. Eukaryota.
COG2234. LUCA.
GeneTreeiENSGT00390000018110.
HOGENOMiHOG000295607.
HOVERGENiHBG105014.
InParanoidiQ9Y646.
KOiK01302.
OMAiRVVLFMN.
OrthoDBiEOG091G08CB.
PhylomeDBiQ9Y646.
TreeFamiTF323248.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000104324-MONOMER.

Miscellaneous databases

GenomeRNAii10404.
PROiQ9Y646.

Gene expression databases

BgeeiENSG00000104324.
ExpressionAtlasiQ9Y646. baseline and differential.
GenevisibleiQ9Y646. HS.

Family and domain databases

InterProiIPR007484. Peptidase_M28.
[Graphical view]
PfamiPF04389. Peptidase_M28. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCBPQ_HUMAN
AccessioniPrimary (citable) accession number: Q9Y646
Secondary accession number(s): B2RD88
, Q8NBZ1, Q9UNM8, Q9Y5X6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: November 1, 1999
Last modified: November 2, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.