CPM carboxypeptidase M [Homo sapiens (human)] - Gene

Summary

Official Symbol: CPMprovided by HGNC
Official Full Name: carboxypeptidase Mprovided by HGNC
Primary source: HGNC:HGNC:2311
See related: Ensembl:ENSG00000135678 MIM:114860
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
Summary: The protein encoded by this gene is a membrane-bound arginine/lysine carboxypeptidase. Its expression is associated with monocyte to macrophage differentiation. This encoded protein contains hydrophobic regions at the amino and carboxy termini and has 6 potential asparagine-linked glycosylation sites. The active site residues of carboxypeptidases A and B are conserved in this protein. Three alternatively spliced transcript variants encoding the same protein have been described for this gene. [provided by RefSeq, Jul 2008]
Expression: Broad expression in fat (RPKM 56.0), lung (RPKM 21.3) and 19 other tissues See more
Orthologs: mouse all

Genomic context

Location:: 12q15

Exon count:: 11

Annotation release	Status	Assembly	Chr	Location
109	current	GRCh38.p12 (GCF_000001405.38)	12	NC_000012.12 (68842193..68963240, complement)
105	previous assembly	GRCh37.p13 (GCF_000001405.25)	12	NC_000012.11 (69244955..69357020, complement)

Chromosome 12 - NC_000012.12 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

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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GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

Low CPM expression is associated with colorectal cancer.
Title: MicroRNA-146a promote cell migration and invasion in human colorectal cancer via carboxypeptidase M/src-FAK pathway.
CPM binding to extracellular loop 2 of the B1R results in positive allosteric modulation of B1R signaling, and disruption of this interaction could provide a novel therapeutic approach to reduce pathological B1R signaling.
Title: Carboxypeptidase M is a positive allosteric modulator of the kinin B1 receptor.
Carboxypeptidase M expression is lost in human renal cell carcinoma tumor cells, whereas it is abundant in tumor-associated foam cells and neovasculature.
Title: Mapping of carboxypeptidase m in normal human kidney and renal cell carcinoma: expression in tumor-associated neovasculature and macrophages.
novel marker and cellular player in lipid uptake and/or metabolism of activated macrophages by promoting foam cell formation
Title: Carboxypeptidase-M is regulated by lipids and CSFs in macrophages and dendritic cells and expressed selectively in tissue granulomas and foam cells.
CPM and B1Rs on cell membranes form a critical complex that potentiates B1R signaling.
Title: Cross-talk between carboxypeptidase M and the kinin B1 receptor mediates a new mode of G protein-coupled receptor signaling.
Observational study and genome-wide association study of gene-disease association. (HuGE Navigator)
Title: Genome-wide association-, replication-, and neuroimaging study implicates HOMER1 in the etiology of major depression.
CPM amplification could be used as an alternative diagnostic tool for the diagnosis of well-differentiated liposarcoma/atypical lipomatous tumors.
Title: Carboxypeptidase M: a biomarker for the discrimination of well-differentiated liposarcoma from lipoma.
Cleavage of the C-terminal lysine residue of SDF-1alpha by CPM leads to attenuated chemotactic responses.
Title: Carboxypeptidase M expressed by human bone marrow cells cleaves the C-terminal lysine of stromal cell-derived factor-1alpha: another player in hematopoietic stem/progenitor cell mobilization?
Carboxypeptidase M and kinin B1 receptors interact to facilitate efficient b1 signaling from B2 agonists
Title: Carboxypeptidase M and kinin B1 receptors interact to facilitate efficient b1 signaling from B2 agonists.
Results report the crystallization of human carboxypeptidase M and its 3.0 angstrom crystal structure.
Title: Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity.

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

NHGRI GWAS Catalog

Description
A genome-wide association study identifies susceptibility loci of silica related pneumoconiosis in Han Chinese. NHGRI GWA Catalog NHGRI GWA CatalogPubMed
Genome-wide association-, replication-, and neuroimaging study implicates HOMER1 in the etiology of major depression. NHGRI GWA Catalog NHGRI GWA CatalogPubMed

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
Tat	tat	Microarray analysis indicates HIV-1 Tat-induced upregulation of carboxypeptidase M (CPM) in primary human brain microvascular endothelial cells	PubMed

Go to the HIV-1, Human Interaction Database

Pathways from BioSystems

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Metabolism of proteins, organism-specific biosystem (from REACTOME)
Metabolism of proteins, organism-specific biosystemProtein metabolism comprises the pathways of translation, post-translational modification and protein folding.
Post-translational modification: synthesis of GPI-anchored proteins, organism-specific biosystem (from REACTOME)
Post-translational modification: synthesis of GPI-anchored proteins, organism-specific biosystemGlycosylphosphatidyl inositol (GPI) acts as a membrane anchor for many cell surface proteins. GPI is synthesized in the endoplasmic reticulum. In humans, a single pathway consisting of eleven reactio...
Post-translational protein modification, organism-specific biosystem (from REACTOME)
Post-translational protein modification, organism-specific biosystemAfter translation, many newly formed proteins undergo further covalent modifications that alter their functional properties and that are essentially irreversible under physiological conditions in the...

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

D11S2560 (e-PCR)
- UniSTS:37928

G64384 (e-PCR)
- UniSTS:163887

RH98659 (e-PCR)
- UniSTS:87090

D8S2279 (e-PCR)
- UniSTS:473907

D8S2282 (e-PCR)
- UniSTS:473910

D10S2448 (e-PCR)
- UniSTS:474444

L18426 (e-PCR)
- UniSTS:34648

RH44527 (e-PCR)
- UniSTS:75113

D15S1477 (e-PCR)
- UniSTS:474482

D1S1425 (e-PCR)
- UniSTS:149621

DXS8011 (e-PCR)
- UniSTS:37245

D12S1501 (e-PCR)
- UniSTS:154000

RH44674 (e-PCR)
- UniSTS:14774

GDB:631802 (e-PCR)
- UniSTS:158429

STS-J04970 (e-PCR)
- UniSTS:69353

Homology

Homologs of the CPM gene: The CPM gene is conserved in chimpanzee, Rhesus monkey, cow, mouse, rat, chicken, zebrafish, fruit fly, mosquito, and frog.
Orthologs from Annotation Pipeline: 247 organisms have orthologs with human gene CPM
Orthologs

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
carboxypeptidase activity	TAS Traceable Author Statement more info	PubMed
metallocarboxypeptidase activity	IBA Inferred from Biological aspect of Ancestor more info	PubMed
zinc ion binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
anatomical structure morphogenesis	TAS Traceable Author Statement more info	PubMed
peptide metabolic process	IBA Inferred from Biological aspect of Ancestor more info	PubMed
protein processing	IBA Inferred from Biological aspect of Ancestor more info	PubMed

Component	Evidence Code	Pubs
anchored component of membrane	IEA Inferred from Electronic Annotation more info
cell surface	HDA more info	PubMed
extracellular exosome	HDA more info	PubMed
extracellular region	TAS Traceable Author Statement more info
extracellular space	IBA Inferred from Biological aspect of Ancestor more info	PubMed
plasma membrane	TAS Traceable Author Statement more info

General protein information

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Preferred Names: carboxypeptidase M

Names: renal carboxypeptidase; urinary carboxypeptidase B

NP_001005502.1

EC 3.4.17.12

NP_001865.1

EC 3.4.17.12

NP_938079.1

EC 3.4.17.12

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)

NM_001005502.2 → NP_001005502.1 carboxypeptidase M precursor

See identical proteins and their annotated locations for NP_001005502.1

Status: REVIEWED

Description

Transcript Variant: This variant (3) differs in the 5' UTR compared to variants 1 and 2. All three variants encode the same protein.

Source sequence(s)

AC025423, AF368463, BC016943, BC022276, BQ431065, DA831499, DA833423, DB006895

Consensus CDS

CCDS8987.1

UniProtKB/Swiss-Prot

P14384

Related

ENSP00000339157.3, ENST00000338356.7

Conserved Domains (2) summary

cd03866
Location:18 → 310

M14_CPM; Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase M subgroup

cd11308
Location:314 → 394

Peptidase_M14NE-CP-C_like; Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain
NM_001874.4 → NP_001865.1 carboxypeptidase M precursor

See identical proteins and their annotated locations for NP_001865.1

Status: REVIEWED

Description

Transcript Variant: This variant (1) differs in the 5' UTR compared to variants 2 and 3. All three variants encode the same protein.

Source sequence(s)

AC025423, AF368463, BC016943, BC022276, BQ431065, DA831499, DA833423, J04970

Consensus CDS

CCDS8987.1

UniProtKB/Swiss-Prot

P14384

Related

ENSP00000447255.1, ENST00000546373.5

Conserved Domains (2) summary

cd03866
Location:18 → 310

M14_CPM; Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase M subgroup

cd11308
Location:314 → 394

Peptidase_M14NE-CP-C_like; Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain
NM_198320.4 → NP_938079.1 carboxypeptidase M precursor

See identical proteins and their annotated locations for NP_938079.1

Status: REVIEWED

Description

Transcript Variant: This variant (2) differs in the 5' UTR compared to variants 1 and 3. All three variants encode the same protein.

Source sequence(s)

AC025423, AF368463, BC016943, BC022276, BQ431065, DA205368, DA831499, DA833423, J04970

Consensus CDS

CCDS8987.1

UniProtKB/Swiss-Prot

P14384

Related

ENSP00000448517.1, ENST00000551568.5

Conserved Domains (2) summary

cd03866
Location:18 → 310

M14_CPM; Peptidase M14 carboxypeptidase subfamily N/E-like; Carboxypeptidase M subgroup

cd11308
Location:314 → 394

Peptidase_M14NE-CP-C_like; Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain