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CPD carboxypeptidase D [ Homo sapiens (human) ]

Gene ID: 1362, updated on 5-Mar-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_2023_10 current GRCh38.p14 (GCF_000001405.40) 17 NC_000017.11 (30378927..30469989)
RS_2023_10 current T2T-CHM13v2.0 (GCF_009914755.1) 17 NC_060941.1 (31323558..31414615)
105.20220307 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

Expression

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  • Project title: HPA RNA-seq normal tissues
  • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
  • BioProject: PRJEB4337
  • Publication: PMID 24309898
  • Analysis date: Wed Apr 4 07:08:55 2018

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. 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
  4. SiRNA-targeted carboxypeptidase D inhibits hepatocellular carcinoma growth. Jin T, et al. Cell Biol Int, 2013 Sep. PMID 23589395
  5. Prolactin and estrogen up-regulate carboxypeptidase-d to promote nitric oxide production and survival of mcf-7 breast cancer cells. Abdelmagid SA, et al. Endocrinology, 2008 Oct. PMID 18535109

See all (84) 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)

Genotypes

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_2023_10

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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