CPM
Carboxypeptidase M
Also known as: CBPM_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P14384
- Gene
- CPM
- Ensembl
- ENSG00000135678
- Chromosome
- 12
- Canonical length
- 443 aa
- Protein class
- Enzymes, Plasma proteins, Predicted intracellular proteins, Predicted membrane proteins
- Subcellular location
- Vesicles
OverviewNCBI Gene
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]
Canonical amino-acid sequenceUniProt
443 residues, UniProt reviewed canonical sequence.
>P14384|CPM
1 MDFPCLWLGL LLPLVAALDF NYHRQEGMEA FLKTVAQNYS SVTHLHSIGK SVKGRNLWVL
61 VVGRFPKEHR IGIPEFKYVA NMHGDETVGR ELLLHLIDYL VTSDGKDPEI TNLINSTRIH
121 IMPSMNPDGF EAVKKPDCYY SIGRENYNQY DLNRNFPDAF EYNNVSRQPE TVAVMKWLKT
181 ETFVLSANLH GGALVASYPF DNGVQATGAL YSRSLTPDDD VFQYLAHTYA SRNPNMKKGD
241 ECKNKMNFPN GVTNGYSWYP LQGGMQDYNY IWAQCFEITL ELSCCKYPRE EKLPSFWNNN
301 KASLIEYIKQ VHLGVKGQVF DQNGNPLPNV IVEVQDRKHI CPYRTNKYGE YYLLLLPGSY
361 IINVTVPGHD PHITKVIIPE KSQNFSALKK DILLPFQGQL DSIPVSNPSC PMIPLYRNLP
421 DHSAATKPSL FLFLVSLLHI FFKLocalizationUniProt · AlphaFold · HPA
Whether an antibody against CPM can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Cell surface
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.25
- Highest tissue expression
- 146 nTPM
Expression across tissuesHPA
Tissue
- adipose tissue: 146 nTPM
- placenta: 66 nTPM
- lung: 56 nTPM
- kidney: 39 nTPM
- breast: 38 nTPM
- colon: 31 nTPM
Single-cell type
- mast cells: 1,287 nCPM
- kupffer cells: 829 nCPM
- proximal tubule cells: 717 nCPM
- adipocytes: 702 nCPM
- alveolar cells type 2: 686 nCPM
- endometrial glandular cells: 613 nCPM
Immune cell
- classical monocyte: 21 nTPM
- myeloid DC: 17 nTPM
- intermediate monocyte: 15 nTPM
- non-classical monocyte: 7.5 nTPM
- total PBMC: 7.3 nTPM
- naive B-cell: 3.5 nTPM
Brain region
- thalamus: 60 nTPM
- white matter: 49 nTPM
- medulla oblongata: 43 nTPM
- basal ganglia: 29 nTPM
- cerebral cortex: 28 nTPM
- pons: 28 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.88
- gnomAD pLI
- 0
- gnomAD missense Z
- 1.97
- DepMap mean gene effect
- -0.2
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
Molecular functions
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Peptidase M14, carboxypeptidase A
- Carboxypeptidase-like, regulatory domain superfamily
- Peptidase M14 domain-containing protein
- Zinc carboxypeptidases, zinc-binding region 1
- Zinc carboxypeptidases, zinc-binding region 2
- Zinc carboxypeptidase
- Carboxypeptidase regulatory-like domain
- Carboxypeptidase M, N-terminal domain
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of CPM in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads CPM as an antibody target. Whether an autoantibody or antibody against CPM could matter depends on whether native CPM is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
CPM is annotated at the cell surface, where native CPM is exposed to circulating antibodies and is a prime autoantibody target that could block, deplete, or overstimulate it.
Annotation status
The present source text does not explicitly label CPM as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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