CELA2A

Chymotrypsin-like elastase family member 2A is an enzyme that in humans is encoded by the CELA2A gene.^[5][6][7]

CELA2A
Identifiers
Aliases	CELA2A, ELA2A, PE-1, chymotrypsin like elastase family member 2A, chymotrypsin like elastase 2A, AOMS4
External IDs	OMIM: 609443; MGI: 95316; HomoloGene: 40598; GeneCards: CELA2A; OMA:CELA2A - orthologs
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1p36.21 Start 15,456,728 bp[1] End 15,472,091 bp[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4 D3|4 74.75 cM Start 141,542,273 bp[2] End 141,553,471 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in body of pancreas islet of Langerhans duodenum testicle right adrenal gland left adrenal gland left adrenal cortex right adrenal cortex ectocervix fundus Top expressed in pyloric antrum islet of Langerhans pancreatic acinus duodenum sexually immature organism blastocyst embryo embryo morula esophagus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function serine hydrolase activity peptidase activity serine-type peptidase activity hydrolase activity endopeptidase activity serine-type endopeptidase activity Cellular component keratohyalin granule extracellular region extracellular space cytosol Biological process proteolysis cornification Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 63036 13706 Ensembl ENSG00000142615 ENSMUSG00000058579 UniProt P08217 P05208 RefSeq (mRNA) NM_033440 NM_007919 RefSeq (protein) NP_254275 NP_031945 Location (UCSC) Chr 1: 15.46 – 15.47 Mb Chr 4: 141.54 – 141.55 Mb PubMed search [3] [4]
Wikidata
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Function

Elastases form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin. Humans have six elastase genes which encode the structurally similar proteins elastase 1, 2, 2A, 2B, 3A, and 3B. Like most of the human elastases, elastase 2A is secreted from the pancreas as a zymogen. In other species, elastase 2A has been shown to preferentially cleave proteins after leucine, methionine, and phenylalanine residues. Clinical literature that describes human elastase 1 activity in the pancreas is actually referring to elastase 2A.^[7]