|Institutional Source||Beutler Lab|
|Gene Name||chymotrypsin-like elastase family, member 3A|
|Essential gene?||Probably non essential (E-score: 0.067)|
|Stock #||R7347 (G1)|
|Chromosomal Location||137401554-137409791 bp(-) (GRCm38)|
|Type of Mutation||missense|
|DNA Base Change (assembly)||T to C at 137402606 bp (GRCm38)|
|Amino Acid Change||Asparagine to Aspartic acid at position 235 (N235D)|
|Ref Sequence||ENSEMBL: ENSMUSP00000024200 (fasta)|
|Gene Model||predicted gene model for transcript(s): [ENSMUST00000024200]|
AA Change: N235D
PolyPhen 2 Score 0.953 (Sensitivity: 0.79; Specificity: 0.95)
AA Change: N235D
|Meta Mutation Damage Score||0.1462|
|Coding Region Coverage||
|Validation Efficiency||100% (80/80)|
|MGI Phenotype||FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] 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. Unlike other elastases, elastase 3A has little elastolytic activity. Like most of the human elastases, elastase 3A is secreted from the pancreas as a zymogen and, like other serine proteases such as trypsin, chymotrypsin and kallikrein, it has a digestive function in the intestine. Elastase 3A preferentially cleaves proteins after alanine residues. Elastase 3A may also function in the intestinal transport and metabolism of cholesterol. Both elastase 3A and elastase 3B have been referred to as protease E and as elastase 1. [provided by RefSeq, Jul 2008]|
|Allele List at MGI|
|Other mutations in this stock||
|Other mutations in Cela3a||
(F):5'- AAGGGTCTTCAGATTATCCCTCC -3'
(R):5'- CTGGGTGCTGTCTTACACTG -3'
(F):5'- TCCTAAACTCCCTGGCAGG -3'
(R):5'- TAATGCTGTGACCAAGTGCC -3'