|Institutional Source||Beutler Lab|
|Gene Name||protein disulfide isomerase associated 5|
|Is this an essential gene?||Probably non essential (E-score: 0.114)|
|Stock #||R0468 (G1)|
|Chromosomal Location||35397312-35490873 bp(-) (GRCm38)|
|Type of Mutation||missense|
|DNA Base Change (assembly)||A to G at 35397507 bp|
|Amino Acid Change||Leucine to Proline at position 502 (L502P)|
|Ref Sequence||ENSEMBL: ENSMUSP00000023550 (fasta)|
|Gene Model||predicted gene model for transcript(s): [ENSMUST00000023550]|
|Predicted Effect||probably damaging
AA Change: L502P
PolyPhen 2 Score 1.000 (Sensitivity: 0.00; Specificity: 1.00)
AA Change: L502P
|Predicted Effect||noncoding transcript
|Meta Mutation Damage Score||0.5141|
|Coding Region Coverage||
|Validation Efficiency||100% (61/61)|
|MGI Phenotype||FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] This gene encodes a member of the disulfide isomerase (PDI) family of endoplasmic reticulum (ER) proteins that catalyze protein folding and thiol-disulfide interchange reactions. The encoded protein has an N-terminal ER-signal sequence, three catalytically active thioredoxin (TRX) domains, a TRX-like domain, and a C-terminal ER-retention sequence. The N-terminal TRX-like domain is the primary binding site for the major ER chaperone calreticulin and possibly other proteins and substrates as well. Alternative splicing results in multiple protein- and non-protein-coding transcript variants. [provided by RefSeq, Dec 2016]|
|Allele List at MGI|
|Other mutations in this stock||
|Other mutations in Pdia5||
(F):5'- GCTCGTGAAAACATACTCTACCACTGAA -3'
(R):5'- TGCCATAGCCAGTAGTGTCTCCC -3'
(F):5'- AACATACTCTACCACTGAATAAATGG -3'
(R):5'- cctcctctgacaccccc -3'