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    CPD carboxypeptidase D [ Homo sapiens (human) ]

    Gene ID: 1362, updated on 10-Dec-2024

    Summary

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    Official Symbol
    CPDprovided by HGNC
    Official Full Name
    carboxypeptidase Dprovided by HGNC
    Primary source
    HGNC:HGNC:2301
    See related
    Ensembl:ENSG00000108582 MIM:603102; AllianceGenome:HGNC:2301
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Homo sapiens
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
    Also known as
    GP180
    Summary
    The metallocarboxypeptidase family of enzymes is divided into 2 subfamilies based on sequence similarities. The pancreatic carboxypeptidase-like and the regulatory B-type carboxypeptidase subfamilies. Carboxypeptidase D has been identified as a regulatory B-type carboxypeptidase. CPD is a homolog of duck gp180, a hepatitis B virus-binding protein. Transcript variants utilizing alternative polyadenylation signals exist for this gene. [provided by RefSeq, Jul 2008]
    Expression
    Ubiquitous expression in thyroid (RPKM 44.8), gall bladder (RPKM 23.6) and 24 other tissues See more
    Orthologs
    mouse all
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    Genomic context

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    See CPD in Genome Data Viewer
    Location:
    17q11.2
    Exon count:
    22
    Annotation release Status Assembly Chr Location
    RS_2024_08 current GRCh38.p14 (GCF_000001405.40) 17 NC_000017.11 (30378927..30469989)
    RS_2024_08 current T2T-CHM13v2.0 (GCF_009914755.1) 17 NC_060941.1 (31323558..31414615)
    RS_2024_09 previous assembly GRCh37.p13 (GCF_000001405.25) 17 NC_000017.10 (28705945..28797007)

    Chromosome 17 - NC_000017.11Genomic Context describing neighboring genes Neighboring gene transmembrane and immunoglobulin domain containing 1 Neighboring gene OCT4-NANOG-H3K27ac hESC enhancer GRCh37_chr17:28667189-28667899 Neighboring gene NANOG-H3K27ac hESC enhancer GRCh37_chr17:28667900-28668609 Neighboring gene Sharpr-MPRA regulatory region 7119 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr17:28672567-28673066 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 11994 Neighboring gene RNA, U6 small nuclear 990, pseudogene Neighboring gene ATAC-STARR-seq lymphoblastoid active region 11995 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 11996 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr17:28705846-28706773 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 11997 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr17:28715045-28715730 Neighboring gene Sharpr-MPRA regulatory region 2970 Neighboring gene OCT4-NANOG hESC enhancer GRCh37_chr17:28732022-28732693 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 11998 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 11999 Neighboring gene golgi SNAP receptor complex member 1 Neighboring gene NANOG-H3K27ac hESC enhancer GRCh37_chr17:28863435-28863984 Neighboring gene H3K4me1 hESC enhancer GRCh37_chr17:28868427-28868928 Neighboring gene arachidonate 12-lipoxygenase pseudogene 1

    Genomic regions, transcripts, and products

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    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Amyloid formation by human carboxypeptidase D transthyretin-like domain under physiological conditions. Garcia-Pardo J, et al. J Biol Chem, 2014 Dec 5. PMID 25294878, Free PMC Article
    2. Carboxypeptidase-D is elevated in prostate cancer and its anti-apoptotic activity is abolished by combined androgen and prolactin receptor targeting. Thomas LN, et al. Prostate, 2014 May. PMID 24615730
    3. Identification of a membrane-bound carboxypeptidase as the mammalian homolog of duck gp180, a hepatitis B virus-binding protein. McGwire GB, et al. Life Sci, 1997. PMID 9064476
    4. Prolactin/Stat5 and androgen R1881 coactivate carboxypeptidase-D gene in breast cancer cells. Koirala S, et al. Mol Endocrinol, 2014 Mar. PMID 24433040, Free PMC Article
    5. SiRNA-targeted carboxypeptidase D inhibits hepatocellular carcinoma growth. Jin T, et al. Cell Biol Int, 2013 Sep. PMID 23589395

    See all (97) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. prolactin induction of VEGF-C and Runx2 was inhibited partly by Carboxypeptidase-D inhibitors, implicating nitric oxide , produced by PRL-regulated Carboxypeptidase-D, in breast cancer progression
      Title: Prolactin/androgen-inducible carboxypeptidase-D increases with nitrotyrosine and Ki67 for breast cancer progression in vivo, and upregulates progression markers VEGF-C and Runx2 in vitro.
    2. Carboxypeptidase-D (CPD) overexpression coincides with high-grade lung cancer and the CPD overexpression could reverse the inhibitory effects of miR-214
      Title: microRNA-214 Governs Lung Cancer Growth and Metastasis by Targeting Carboxypeptidase-D.
    3. The human carboxypeptidase D transthyretin-like domain forms amyloid under physiological conditions.
      Title: Amyloid formation by human carboxypeptidase D transthyretin-like domain under physiological conditions.
    4. Prolactin and R1881, acting through Stat5 and androgen receptor, act cooperatively to stimulate CPD gene transcription in breast cancer cells.
      Title: Prolactin/Stat5 and androgen R1881 coactivate carboxypeptidase-D gene in breast cancer cells.
    5. CPD immunostaining and testosterone/prolactin-stimulated CPD expression were higher in prostate cancer than benign tissues/cells. Elevated CPD increased NO production, which was abolished when both androgen and prolactin receptors were inhibited.
      Title: Carboxypeptidase-D is elevated in prostate cancer and its anti-apoptotic activity is abolished by combined androgen and prolactin receptor targeting.
    6. Carboxypeptidase D (CPD) is frequently upregulated in hepatocellular carcinoma; targeting CPD inhibits hepatocellular carcinoma cell proliferation through induction of G1 cell-cycle arrest and apoptosis.
      Title: SiRNA-targeted carboxypeptidase D inhibits hepatocellular carcinoma growth.
    7. Either high glucose or insulin (with low glucose) up-regulates beta-cell CPD (but not CPE).
      Title: Differential regulation and localization of carboxypeptidase D and carboxypeptidase E in human and mouse β-cells.
    8. prolactin or E2 up-regulated CPD mRNA and protein expression in MCF-7 breast cancer cells promoting their survival
      Title: Prolactin and estrogen up-regulate carboxypeptidase-d to promote nitric oxide production and survival of mcf-7 breast cancer cells.
    9. First report to demonstrate carboxypeptidase D as part of the transforming growth factor (TGF)-beta pathway as a TGF-beta target gene implicated in the pathogenesis of lupus erythematosus.
      Title: Carboxypeptidase D: a novel TGF-beta target gene dysregulated in patients with lupus erythematosus.
    10. Palmitoylation of carboxypeptidase D has a role in intracellular trafficking
      Title: Palmitoylation of carboxypeptidase D. Implications for intracellular trafficking.
    Submit: New GeneRIF Correction See all GeneRIFs (12)

    Phenotypes

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    Find tests for this gene in the NIH Genetic Testing Registry (GTR)

    Review eQTL and phenotype association data in this region using PheGenI

    Variation

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    See variants in ClinVar

    See studies and variants in dbVar

    See Variation Viewer (GRCh37.p13)

    See Variation Viewer (GRCh38)

    HIV-1 interactions

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    Protein interactions

    Protein Gene Interaction Pubs
    Envelope surface glycoprotein gp160, precursor env HIV-1 gp160 interacts with CPD; predicted interaction to be within the Golgi PubMed

    Go to the HIV-1, Human Interaction Database

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Markers

    Homology

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    enables metallocarboxypeptidase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables serine-type carboxypeptidase activity TAS
    Traceable Author Statement
    more info
    		 PubMed 
    enables zinc ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in peptide metabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in protein processing IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    Component Evidence Code Pubs
    located_in extracellular exosome HDA PubMed 
    is_active_in extracellular space IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in membrane HDA PubMed 
    located_in plasma membrane IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    carboxypeptidase D
    Names
    metallocarboxypeptidase D
    NP_001186704.1
    NP_001295.2

    NCBI Reference Sequences (RefSeq)

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    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_001199775.1 → NP_001186704.1  carboxypeptidase D isoform 2

      Status: REVIEWED

      Description
      Transcript Variant: This variant (2) differs in the 5' UTR and coding region and uses an alternate start codon compared to variant 1. The resulting protein (isoform 2) is shorter and has a distinct N-terminus compared to isoform 1.
      Source sequence(s)
      AC006050, AK316409, CA436219
      Consensus CDS
      CCDS56025.1
      UniProtKB/Swiss-Prot
      O75976
      Related
      ENSP00000444443.2, ENST00000543464.6
      Conserved Domains (4) summary
      cd03863
      Location:249 → 544
      M14_CPD_II; Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain II subgroup
      cd06245
      Location:685 → 963
      M14_CPD_III; Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain III subgroup
      cd11308
      Location:548 → 623
      Peptidase_M14NE-CP-C_like; Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain
      cl11393
      Location:3 → 132
      Peptidase_M14_like; M14 family of metallocarboxypeptidases and related proteins

    2. NM_001304.5 → NP_001295.2  carboxypeptidase D isoform 1 precursor

      See identical proteins and their annotated locations for NP_001295.2

      Status: REVIEWED

      Description
      Transcript Variant: This variant (1) represents the longer transcript and encodes the longer protein (isoform 1).
      Source sequence(s)
      AC006050, AC090685, BC045624, CA436219
      Consensus CDS
      CCDS11257.1
      UniProtKB/Swiss-Prot
      B7Z7T9, B7ZAU4, F5GZH6, O15377, O75976, Q86SH9, Q86XE6
      Related
      ENSP00000225719.4, ENST00000225719.9
      Conserved Domains (4) summary
      cd03863
      Location:496 → 791
      M14_CPD_II; Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain II subgroup
      cd03868
      Location:58 → 379
      M14_CPD_I; Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain I subgroup
      cd06245
      Location:932 → 1210
      M14_CPD_III; Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase D, domain III subgroup
      cd11308
      Location:795 → 870
      Peptidase_M14NE-CP-C_like; Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain

    RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference GRCh38.p14 Primary Assembly

    Genomic

    1. NC_000017.11 Reference GRCh38.p14 Primary Assembly

      Range
      30378927..30469989
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    Alternate T2T-CHM13v2.0

    Genomic

    1. NC_060941.1 Alternate T2T-CHM13v2.0

      Range
      31323558..31414615
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    O75976.2 GenPept UniProtKB/Swiss-Prot:O75976

    Gene LinkOut

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