PDIA2
Protein disulfide-isomerase A2
Also known as: PDA2, PDI, PDIA2_HUMAN, PDIP, PDIR
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q13087
- Gene
- PDIA2
- Ensembl
- ENSG00000185615
- Chromosome
- 16
- Canonical length
- 525 aa
- Protein class
- Enzymes, Predicted intracellular proteins
- Secretome location
- Intracellular and membrane
- Quaternary structure
- Homodimer
OverviewNCBI Gene
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, two catalytically active thioredoxin (TRX) domains, two TRX-like domains and a C-terminal ER-retention sequence. The protein plays a role in the folding of nascent proteins in the endoplasmic reticulum by forming disulfide bonds through its thiol isomerase, oxidase, and reductase activity. The encoded protein also possesses estradiol-binding activity and can modulate intracellular estradiol levels. [provided by RefSeq, Sep 2017]
Canonical amino-acid sequenceUniProt
525 residues, UniProt reviewed canonical sequence.
>Q13087|PDIA2
1 MSRQLLPVLL LLLLRASCPW GQEQGARSPS EEPPEEEIPK EDGILVLSRH TLGLALREHP
61 ALLVEFYAPW CGHCQALAPE YSKAAAVLAA ESMVVTLAKV DGPAQRELAE EFGVTEYPTL
121 KFFRNGNRTH PEEYTGPRDA EGIAEWLRRR VGPSAMRLED EAAAQALIGG RDLVVIGFFQ
181 DLQDEDVATF LALAQDALDM TFGLTDRPRL FQQFGLTKDT VVLFKKFDEG RADFPVDEEL
241 GLDLGDLSRF LVTHSMRLVT EFNSQTSAKI FAARILNHLL LFVNQTLAAH RELLAGFGEA
301 APRFRGQVLF VVVDVAADNE HVLQYFGLKA EAAPTLRLVN LETTKKYAPV DGGPVTAASI
361 TAFCHAVLNG QVKPYLLSQE IPPDWDQRPV KTLVGKNFEQ VAFDETKNVF VKFYAPWCTH
421 CKEMAPAWEA LAEKYQDHED IIIAELDATA NELDAFAVHG FPTLKYFPAG PGRKVIEYKS
481 TRDLETFSKF LDNGGVLPTE EPPEEPAAPF PEPPANSTMG SKEELLocalizationUniProt · AlphaFold · HPA
Whether an antibody against PDIA2 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Intracellular
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.33
- Highest tissue expression
- 2,364 nTPM
Expression across tissuesHPA
Tissue
- pancreas: 2,364 nTPM
- cerebellum: 190 nTPM
- stomach: 180 nTPM
- spinal cord: 83 nTPM
- cerebral cortex: 47 nTPM
- hypothalamus: 44 nTPM
Single-cell type
- pancreatic acinar cells: 1,558 nCPM
- gastric chief cells: 580 nCPM
- mucous neck cells: 184 nCPM
- parietal cells: 83 nCPM
- oligodendrocytes: 27 nCPM
- brain excitatory neurons: 25 nCPM
Immune cell
- basophil: 0 nTPM
- classical monocyte: 0 nTPM
- eosinophil: 0 nTPM
- gdT-cell: 0 nTPM
- intermediate monocyte: 0 nTPM
- MAIT T-cell: 0 nTPM
Brain region
- white matter: 60 nTPM
- cerebellum: 43 nTPM
- medulla oblongata: 36 nTPM
- pons: 26 nTPM
- spinal cord: 23 nTPM
- basal ganglia: 21 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 1.96
- gnomAD pLI
- 0
- gnomAD missense Z
- -1.73
- DepMap mean gene effect
- -0.03
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 2% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- platelet aggregation
- protein folding
- protein folding in endoplasmic reticulum
- protein retention in ER lumen
- response to endoplasmic reticulum stress
Molecular functions
- disulfide oxidoreductase activity
- protein disulfide isomerase activity
- protein-disulfide reductase activity
- steroid binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads PDIA2 as an antibody target. Whether an autoantibody or antibody against PDIA2 could matter depends on whether native PDIA2 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
PDIA2 is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label PDIA2 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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