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Q9Y646 (CBPQ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carboxypeptidase Q

EC=3.4.17.-
Alternative name(s):
Lysosomal dipeptidase
Plasma glutamate carboxypeptidase
Gene names
Name:CPQ
Synonyms:LCH1, PGCP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length472 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Homodimer. The monomeric form is inactive while the homodimer is active. Ref.7 Ref.10

Subcellular location

Endoplasmic reticulum. Golgi apparatus. Lysosome By similarity. Secreted. Note: Secretion is stimulated by TSH/thyroid-stimulating hormone, INS/insulin and SST/somatostatin By similarity. Ref.1

Tissue specificity

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). Ref.1

Induction

Up-regulated in the majority of hepatitis C virus-associated hepatocellular carcinoma. Ref.8

Post-translational modification

N-glycosylated. The secreted form is modified by hybrid or complex type oligosaccharide chains By similarity. Ref.1

Sequence similarities

Belongs to the peptidase M28 family.

Sequence caution

The sequence AAD31418.1 differs from that shown. Reason: Frameshift at position 446.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 4424
PRO_5000055941
Chain45 – 472428Carboxypeptidase Q
PRO_5000055942

Sites

Active site3361Nucleophile By similarity
Metal binding2901Zinc 1 By similarity
Metal binding3021Zinc 1 By similarity
Metal binding3021Zinc 2; catalytic By similarity
Metal binding3371Zinc 2; catalytic By similarity
Metal binding3641Zinc 1 By similarity
Metal binding4341Zinc 2; catalytic By similarity

Amino acid modifications

Glycosylation611N-linked (GlcNAc...) Potential
Glycosylation1791N-linked (GlcNAc...) Ref.9 Ref.11
Glycosylation3531N-linked (GlcNAc...) Ref.9
Glycosylation3561N-linked (GlcNAc...) Ref.9
Glycosylation3961N-linked (GlcNAc...) Potential

Natural variations

Natural variant1381S → N.
Corresponds to variant rs34088584 [ dbSNP | Ensembl ].
VAR_037466

Experimental info

Sequence conflict371K → E in BAC11423. Ref.4
Sequence conflict1171E → G in BAC11423. Ref.4
Sequence conflict3851M → V in BAC11423. Ref.4
Sequence conflict4461K → Q in AAD31418. Ref.1
Sequence conflict4491N → D in AAD31418. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9Y646 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: EB6CBD2149E042BF

FASTA47251,888
        10         20         30         40         50         60 
MKFLIFAFFG GVHLLSLCSG KAICKNGISK RTFEEIKEEI ASCGDVAKAI INLAVYGKAQ 

        70         80         90        100        110        120 
NRSYERLALL VDTVGPRLSG SKNLEKAIQI MYQNLQQDGL EKVHLEPVRI PHWERGEESA 

       130        140        150        160        170        180 
VMLEPRIHKI AILGLGSSIG TPPEGITAEV LVVTSFDELQ RRASEARGKI VVYNQPYINY 

       190        200        210        220        230        240 
SRTVQYRTQG AVEAAKVGAL ASLIRSVASF SIYSPHTGIQ EYQDGVPKIP TACITVEDAE 

       250        260        270        280        290        300 
MMSRMASHGI KIVIQLKMGA KTYPDTDSFN TVAEITGSKY PEQVVLVSGH LDSWDVGQGA 

       310        320        330        340        350        360 
MDDGGGAFIS WEALSLIKDL GLRPKRTLRL VLWTAEEQGG VGAFQYYQLH KVNISNYSLV 

       370        380        390        400        410        420 
MESDAGTFLP TGLQFTGSEK ARAIMEEVMS LLQPLNITQV LSHGEGTDIN FWIQAGVPGA 

       430        440        450        460        470 
SLLDDLYKYF FFHHSHGDTM TVMDPKQMNV AAAVWAVVSY VVADMEEMLP RS 

« Hide

References

« Hide 'large scale' references
[1]"Purification, cDNA cloning, and expression of a new human blood plasma glutamate carboxypeptidase homologous to N-acetyl-aspartyl-alpha-glutamate carboxypeptidase/prostate-specific membrane antigen."
Gingras R., Richard C., El-Alfy M., Morales C.R., Potier M., Pshezhetsky A.V.
J. Biol. Chem. 274:11742-11750(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 45-75, ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION.
[2]"Cloning of the human aminopeptidase gene."
Liu C.H., Lin B.Y., Chang L.Y.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Heart.
[4]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skin.
[7]"Purification and primary structure determination of human lysosomal dipeptidase."
Dolenc I., Mihelic M.
Biol. Chem. 384:317-320(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 45-74, HOMODIMERIZATION.
[8]"Identification of novel tumor markers in hepatitis C virus-associated hepatocellular carcinoma."
Smith M.W., Yue Z.N., Geiss G.K., Sadovnikova N.Y., Carter V.S., Boix L., Lazaro C.A., Rosenberg G.B., Bumgarner R.E., Fausto N., Bruix J., Katze M.G.
Cancer Res. 63:859-864(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[9]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-179; ASN-353 AND ASN-356.
Tissue: Plasma.
[10]"Presence of the propeptide on recombinant lysosomal dipeptidase controls both activation and dimerization."
Dolenc I., Pain R., Turk V.
Biol. Chem. 388:47-51(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: HOMODIMERIZATION.
[11]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-179.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS6273.1.
RefSeqNP_057218.1. NM_016134.3.
XP_005250812.1. XM_005250755.1.
UniGeneHs.156178.

3D structure databases

ProteinModelPortalQ9Y646.
SMRQ9Y646. Positions 75-445.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115676. 1 interaction.
STRING9606.ENSP00000220763.

Protein family/group databases

MEROPSM28.014.

PTM databases

PhosphoSiteQ9Y646.

Polymorphism databases

DMDM74735298.

Proteomic databases

MaxQBQ9Y646.
PaxDbQ9Y646.
PRIDEQ9Y646.

Protocols and materials databases

DNASU10404.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000220763; ENSP00000220763; ENSG00000104324.
GeneID10404.
KEGGhsa:10404.
UCSCuc003yhw.3. human.

Organism-specific databases

CTD10404.
GeneCardsGC08P097657.
HGNCHGNC:16910. CPQ.
HPAHPA023235.
HPA024490.
neXtProtNX_Q9Y646.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2234.
HOGENOMHOG000295607.
HOVERGENHBG105014.
OMAKVNISNY.
OrthoDBEOG7SN8CJ.
PhylomeDBQ9Y646.
TreeFamTF323248.

Gene expression databases

ArrayExpressQ9Y646.
BgeeQ9Y646.
GenevestigatorQ9Y646.

Family and domain databases

InterProIPR007484. Peptidase_M28.
[Graphical view]
PfamPF04389. Peptidase_M28. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi10404.
NextBio39428.
PROQ9Y646.

Entry information

Entry nameCBPQ_HUMAN
AccessionPrimary (citable) accession number: Q9Y646
Secondary accession number(s): B2RD88 expand/collapse secondary AC list , Q8NBZ1, Q9UNM8, Q9Y5X6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM