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FLASH GENE
Symbol PDIA2 contributors: mct - updated : 12-05-2016
HGNC name protein disulfide isomerase family A, member 2
HGNC id 14180
Location 16p13.3      Physical location : 333.117 - 337.209
Synonym name
  • Rho GDP dissociation inhibitor gamma
  • protein disulfide isomerase-associated 2
  • protein disulfide isomerase, pancreatic
    • Synonym symbol(s) PDIR, PDIP, LA16c-314G4.2, PDA2, PDI, PDIp
    EC.number 5.3.4.1
    DNA
    TYPE functioning gene
    SPECIAL FEATURE head to head
    STRUCTURE 4.09 kb     11 Exon(s)
    MAPPING cloned Y linked N status confirmed
    RNA
    TRANSCRIPTS type messenger
    identificationnb exonstypebpproduct
    ProteinkDaAAspecific expressionYearPubmed
    11 - 1726 58.07 525 - 2014 25419565
    EXPRESSION
    Type restricted
       expressed in (based on citations)
    organ(s)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Endocrinepancreas   highly
    Nervousbrain    
    Reproductivefemale systemovary   
    Urinarybladder    
    cell lineage
    cell lines
    fluid/secretion
    at STAGE
    PROTEIN
    PHYSICAL PROPERTIES
    STRUCTURE
    motifs/domains
  • two thioredoxin domains
  • three predicted N-linked glycosylation sites
    • HOMOLOGY
    Homologene
    FAMILY
  • thioredoxin family
  • protein disulfide isomerase family
    • CATEGORY enzyme
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,cytoplasm,organelle,membrane
    intracellular,cytoplasm,organelle,endoplasmic reticulum
    intracellular,cytoplasm,cytosolic
    text
  • PDIA2 and F3 co-localise in the front edge of motile coronary smooth muscle cells (HVSMC
    • basic FUNCTION
  • catalyzing protein folding and thiol-disulfide interchange reactions
  • catalyzing disulfide bond formation in the endoplasmic reticulum of eukaryotes
  • involved in DNA-nuclear matrix anchoring
  • may be playing a role with HSPA5 in insulin biosynthesis, although an excess of PDIA2 disrupts normal proinsulin processing (Zhang 2009)
  • involved in insulin disulfide bond formation and an excess of this protein impedes normal insulin folding and probably exit from the ER (Zhang 2009)
  • likely a dynamic equilibrium between ERO1- and glutathione disulphide-mediated oxidation of PDIA2 constitutes an important element of ER redox homeostasis
  • involvement for PDIA2 in antigen presentation in addition to its previously described roles in autoimmunity and Parkinson disease
  • cell surface PDIA2 expression and function regulate the capacity of natriuretic peptides to generate cGMP through interaction with their receptors
  • ER-stress protein that controls tissue factor (TF) -procoagulant activity
    • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
    INTERACTION
    DNA
    RNA
    small molecule
    protein
  • interactions with LMAN1 and TXNDC4 provide a novel, dynamic control of SUMF1 trafficking and enzymatic activity
  • pH-dependent oxidation of PDIA2 by ERO1A
  • PDIA2 exhibits unfoldase activity for proinsulin, increasing retention of proinsulin within the ER of pancreatic beta-cells
  • RTN1 induces PDIA2 redistribution in ER vesicles, and concomitantly modulates its activity by decreasing the levels of its S-nitrosylated form
  • PDIA2 binds preferentially ERO1A, whereas ERP44 equally retains ERO1A and PRDX4
  • ERO1A oxidizes PDIA2 to introduce disulfides into substrates, and PDIA2 can feedback-regulate ERO1A activity
  • ER-stress protein-disulphide isomerase family A member 2 (PDIA2) regulates tissue factor (F3), and F3 is chaperoned by PDIA2 to the coronary smooth muscle cells (HVSMC) membrane and to the cell migratory front
    • cell & other
    REGULATION
    Other cytosolic form was clearly digested by caspase-3 and -7 (substrate of caspase-3 and -7, that has an anti-apoptotic action (Na 2007)
    ASSOCIATED DISORDERS
    ANIMAL & CELL MODELS