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Q9Y646

- CBPQ_HUMAN

UniProt

Q9Y646 - CBPQ_HUMAN

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Protein

Carboxypeptidase Q

Gene

CPQ

Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi290 – 2901Zinc 1By similarity
Metal bindingi302 – 3021Zinc 1By similarity
Metal bindingi302 – 3021Zinc 2; catalyticBy similarity
Active sitei336 – 3361NucleophileBy similarity
Metal bindingi337 – 3371Zinc 2; catalyticBy similarity
Metal bindingi364 – 3641Zinc 1By similarity
Metal bindingi434 – 4341Zinc 2; catalyticBy similarity

GO - Molecular functioni

  1. carboxypeptidase activity Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. metallodipeptidase activity Source: UniProtKB
  4. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. peptide catabolic process Source: UniProtKB
  2. proteolysis Source: UniProtKB
  3. thyroid hormone generation Source: UniProtKB
  4. tissue regeneration Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

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
ProteomesiUP000005640: 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

  1. cytoplasm Source: UniProtKB
  2. endoplasmic reticulum Source: UniProtKB
  3. extracellular space Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
  5. Golgi apparatus Source: UniProtKB
  6. lysosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Lysosome, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Propeptidei21 – 44242 PublicationsPRO_5000055941Add
BLAST
Chaini45 – 472428Carboxypeptidase QPRO_5000055942Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi61 – 611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi179 – 1791N-linked (GlcNAc...)2 Publications
Glycosylationi353 – 3531N-linked (GlcNAc...)1 Publication
Glycosylationi356 – 3561N-linked (GlcNAc...)1 Publication
Glycosylationi396 – 3961N-linked (GlcNAc...)Sequence Analysis

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

MaxQBiQ9Y646.
PaxDbiQ9Y646.
PRIDEiQ9Y646.

PTM databases

PhosphoSiteiQ9Y646.

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

BgeeiQ9Y646.
ExpressionAtlasiQ9Y646. baseline and differential.
GenevestigatoriQ9Y646.

Organism-specific databases

HPAiHPA023235.
HPA024490.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi115676. 1 interaction.
STRINGi9606.ENSP00000220763.

Structurei

3D structure databases

ProteinModelPortaliQ9Y646.
SMRiQ9Y646. Positions 213-445.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M28 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2234.
GeneTreeiENSGT00390000018110.
HOGENOMiHOG000295607.
HOVERGENiHBG105014.
InParanoidiQ9Y646.
OMAiKVNISNY.
OrthoDBiEOG7SN8CJ.
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 AAD31418.1 differs from that shown. Reason: Frameshift at position 446.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371K → E in BAC11423. (PubMed:16303743)Curated
Sequence conflicti117 – 1171E → G in BAC11423. (PubMed:16303743)Curated
Sequence conflicti385 – 3851M → V in BAC11423. (PubMed:16303743)Curated
Sequence conflicti446 – 4461K → Q in AAD31418. (PubMed:10206990)Curated
Sequence conflicti449 – 4491N → D in AAD31418. (PubMed:10206990)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti138 – 1381S → N.
Corresponds to variant rs34088584 [ dbSNP | Ensembl ].
VAR_037466

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
XP_005250812.1. XM_005250755.1.
UniGeneiHs.156178.

Genome annotation databases

EnsembliENST00000220763; ENSP00000220763; ENSG00000104324.
GeneIDi10404.
KEGGihsa:10404.
UCSCiuc003yhw.3. human.

Polymorphism databases

DMDMi74735298.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS6273.1.
RefSeqi NP_057218.1. NM_016134.3.
XP_005250812.1. XM_005250755.1.
UniGenei Hs.156178.

3D structure databases

ProteinModelPortali Q9Y646.
SMRi Q9Y646. Positions 213-445.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115676. 1 interaction.
STRINGi 9606.ENSP00000220763.

Protein family/group databases

MEROPSi M28.014.

PTM databases

PhosphoSitei Q9Y646.

Polymorphism databases

DMDMi 74735298.

Proteomic databases

MaxQBi Q9Y646.
PaxDbi Q9Y646.
PRIDEi Q9Y646.

Protocols and materials databases

DNASUi 10404.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000220763 ; ENSP00000220763 ; ENSG00000104324 .
GeneIDi 10404.
KEGGi hsa:10404.
UCSCi uc003yhw.3. human.

Organism-specific databases

CTDi 10404.
GeneCardsi GC08P097657.
HGNCi HGNC:16910. CPQ.
HPAi HPA023235.
HPA024490.
neXtProti NX_Q9Y646.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2234.
GeneTreei ENSGT00390000018110.
HOGENOMi HOG000295607.
HOVERGENi HBG105014.
InParanoidi Q9Y646.
OMAi KVNISNY.
OrthoDBi EOG7SN8CJ.
PhylomeDBi Q9Y646.
TreeFami TF323248.

Miscellaneous databases

GenomeRNAii 10404.
NextBioi 39428.
PROi Q9Y646.

Gene expression databases

Bgeei Q9Y646.
ExpressionAtlasi Q9Y646. baseline and differential.
Genevestigatori Q9Y646.

Family and domain databases

InterProi IPR007484. Peptidase_M28.
[Graphical view ]
Pfami PF04389. Peptidase_M28. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.

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: October 29, 2014
This is version 90 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

External Data

Dasty 3