Selected-GenAtlas references	SOURCE	GeneCards	NCBI Gene	Swiss-Prot	Ensembl
	HGNC	UniGene	Nucleotide	OMIM	UCSC

Home Page

FLASH GENE

Symbol

PDIA2

contributors: mct - updated : 12-05-2016

HGNC name	protein disulfide isomerase family A, member 2
HGNC id	14180

FLASH GENE DNA RNA EXPRESSION PROTEIN DISORDER ANIMAL & CELL MODELS

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

identification nb exons type bp product Protein kDa AA specific expression Year Pubmed NM_006849 11 - 1726 NP_006840 58.07 525 - 2014 25419565

EXPRESSION

Type	restricted

expressed in	(based on citations)
organ(s)	System Organ level 1 Organ level 2 Organ level 3 Organ level 4 Level Pubmed Species Stage Rna symbol Endocrine pancreas       highly Nervous brain         Reproductive female system ovary       Urinary bladder

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