|Institutional Source||Beutler Lab|
|Gene Name||protease, serine 2|
|Synonyms||TRYP, Tesp4, Ta, TRY8, Try2|
|Is this an essential gene?||Non essential (E-score: 0.000)|
|Stock #||R2009 (G1)|
|Chromosomal Location||41521787-41525079 bp(+) (GRCm38)|
|Type of Mutation||missense|
|DNA Base Change (assembly)||A to T at 41523976 bp|
|Amino Acid Change||Isoleucine to Phenylalanine at position 108 (I108F)|
|Ref Sequence||ENSEMBL: ENSMUSP00000065393 (fasta)|
|Gene Model||predicted gene model for transcript(s): [ENSMUST00000070380]|
|Predicted Effect||probably damaging
AA Change: I108F
PolyPhen 2 Score 0.973 (Sensitivity: 0.76; Specificity: 0.96)
AA Change: I108F
|Meta Mutation Damage Score||0.4192|
|Coding Region Coverage||
|Validation Efficiency||100% (47/47)|
|MGI Phenotype||FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] This gene belongs to the trypsin family of serine proteases and encodes anionic trypsinogen. It is part of a cluster of trypsinogen genes that are located within the T cell receptor beta locus. Enzymes of this family cleave peptide bonds that follow lysine or arginine residues. This protein is found at high levels in pancreatic juice and its upregulation is a characteristic feature of pancreatitis. This protein has also been found to activate pro-urokinase in ovarian tumors, suggesting a function in tumor invasion. In addition, this enzyme is able to cleave across the type II collagen triple helix in rheumatoid arthritis synovitis tissue, potentially participating in the degradation of type II collagen-rich cartilage matrix. Alternative splicing results in multiple transcript variants.[provided by RefSeq, Jan 2015]|
|Allele List at MGI|
|Other mutations in this stock||
|Other mutations in Prss2||
(F):5'- AGAGCCACTCCTGAGCAAGAAG -3'
(R):5'- AGATAGATGCCTGGTTTTGGAAAAC -3'
(F):5'- GCAAGAAGCTTGGGAACCCTG -3'
(R):5'- TTTTGGAAAACATGGGAAGGAAG -3'