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Q9Y646

- CBPQ_HUMAN

UniProt

Q9Y646 - CBPQ_HUMAN

Protein

Carboxypeptidase Q

Gene

CPQ

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    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

    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: UniProt
    5. Golgi apparatus Source: UniProtKB
    6. lysosome Source: UniProtKB

    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...)3 Publications
    Glycosylationi353 – 3531N-linked (GlcNAc...)2 Publications
    Glycosylationi356 – 3561N-linked (GlcNAc...)2 Publications
    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

    ArrayExpressiQ9Y646.
    BgeeiQ9Y646.
    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 75-445.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M28 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2234.
    HOGENOMiHOG000295607.
    HOVERGENiHBG105014.
    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

    MKFLIFAFFG GVHLLSLCSG KAICKNGISK RTFEEIKEEI ASCGDVAKAI    50
    INLAVYGKAQ NRSYERLALL VDTVGPRLSG SKNLEKAIQI MYQNLQQDGL 100
    EKVHLEPVRI PHWERGEESA VMLEPRIHKI AILGLGSSIG TPPEGITAEV 150
    LVVTSFDELQ RRASEARGKI VVYNQPYINY SRTVQYRTQG AVEAAKVGAL 200
    ASLIRSVASF SIYSPHTGIQ EYQDGVPKIP TACITVEDAE MMSRMASHGI 250
    KIVIQLKMGA KTYPDTDSFN TVAEITGSKY PEQVVLVSGH LDSWDVGQGA 300
    MDDGGGAFIS WEALSLIKDL GLRPKRTLRL VLWTAEEQGG VGAFQYYQLH 350
    KVNISNYSLV MESDAGTFLP TGLQFTGSEK ARAIMEEVMS LLQPLNITQV 400
    LSHGEGTDIN FWIQAGVPGA SLLDDLYKYF FFHHSHGDTM TVMDPKQMNV 450
    AAAVWAVVSY VVADMEEMLP RS 472
    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 75-445.
    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.
    HOGENOMi HOG000295607.
    HOVERGENi HBG105014.
    OMAi KVNISNY.
    OrthoDBi EOG7SN8CJ.
    PhylomeDBi Q9Y646.
    TreeFami TF323248.

    Miscellaneous databases

    GenomeRNAii 10404.
    NextBioi 39428.
    PROi Q9Y646.

    Gene expression databases

    ArrayExpressi Q9Y646.
    Bgeei Q9Y646.
    Genevestigatori Q9Y646.

    Family and domain databases

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

    Publicationsi

    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 1, 2014
    This is version 89 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