CMA1
Chymase
Also known as: CMA1_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P23946
- Gene
- CMA1
- Ensembl
- ENSG00000092009
- Chromosome
- 14
- Canonical length
- 247 aa
- Protein class
- Enzymes, Metabolic proteins, Plasma proteins, Predicted intracellular proteins, Predicted secreted proteins
- Subcellular location
- Cytosol,Cytoplasmic bodies
- Secretome location
- Secreted to blood
OverviewNCBI Gene
This gene encodes a chymotryptic serine proteinase that belongs to the peptidase family S1. It is expressed in mast cells and is thought to function in the degradation of the extracellular matrix, the regulation of submucosal gland secretion, and the generation of vasoactive peptides. In the heart and blood vessels, this protein, rather than angiotensin converting enzyme, is largely responsible for converting angiotensin I to the vasoactive peptide angiotensin II. Alternative splicing results in multiple variants. [provided by RefSeq, Apr 2015]
Canonical amino-acid sequenceUniProt
247 residues, UniProt reviewed canonical sequence.
>P23946|CMA1
1 MLLLPLPLLL FLLCSRAEAG EIIGGTECKP HSRPYMAYLE IVTSNGPSKF CGGFLIRRNF
61 VLTAAHCAGR SITVTLGAHN ITEEEDTWQK LEVIKQFRHP KYNTSTLHHD IMLLKLKEKA
121 SLTLAVGTLP FPSQFNFVPP GRMCRVAGWG RTGVLKPGSD TLQEVKLRLM DPQACSHFRD
181 FDHNLQLCVG NPRKTKSAFK GDSGGPLLCA GVAQGIVSYG RSDAKPPAVF TRISHYRPWI
241 NQILQANLocalizationUniProt · AlphaFold · HPA
Whether an antibody against CMA1 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
- Secreted
- Secreted
- Yes
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.28
- Highest tissue expression
- 17 nTPM
Expression across tissuesHPA
Tissue
- breast: 17 nTPM
- urinary bladder: 10 nTPM
- esophagus: 9.6 nTPM
- adipose tissue: 8.5 nTPM
- colon: 8.2 nTPM
- skin: 8.1 nTPM
Single-cell type
- mast cells: 161 nCPM
- smooth muscle cells: 5.2 nCPM
- pdcs: 1.8 nCPM
- enteric transient amplifying cells: 0.4 nCPM
- esophageal apical cells: 0.4 nCPM
- basal keratinocytes: 0.2 nCPM
Immune cell
- T-reg: 0.2 nTPM
- basophil: 0 nTPM
- classical monocyte: 0 nTPM
- eosinophil: 0 nTPM
- gdT-cell: 0 nTPM
- intermediate monocyte: 0 nTPM
Brain region
- medulla oblongata: 1.8 nTPM
- midbrain: 1.4 nTPM
- spinal cord: 1.4 nTPM
- choroid plexus: 1.3 nTPM
- cerebral cortex: 1.2 nTPM
- hypothalamus: 1.2 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)
- 1.88
- gnomAD pLI
- 0
- gnomAD missense Z
- -1.75
- DepMap mean gene effect
- 0.14
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 2% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- angiotensin maturation
- basement membrane disassembly
- cellular response to glucose stimulus
- cytokine precursor processing
- extracellular matrix disassembly
- midbrain development
- peptide metabolic process
- positive regulation of angiogenesis
- protein catabolic process
- protein maturation
- regulation of inflammatory response
Molecular functions
- endopeptidase activity
- peptide binding
- serine-type endopeptidase activity
- serine-type peptidase activity
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads CMA1 as an antibody target. Whether an autoantibody or antibody against CMA1 could matter depends on whether native CMA1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
CMA1 is annotated as secreted, so native CMA1 circulates and is directly accessible to antibodies. Secreted and cell-surface proteins are the autoantibody targets most likely to act like drugs, blocking or depleting the native protein.
Annotation status
The present source text does not explicitly label CMA1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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