PDIA3

Functionⁱ

Caution

Was originally thought to be a phosphatidylinositol 4,5-bisphosphate phosphodiesterase type I (phospholipase C-alpha).Curated

Catalytic activityⁱ

Catalyzes the rearrangement of -S-S- bonds in proteins.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	57	NucleophileBy similarity	1
Siteⁱ	58	Contributes to redox potential valueBy similarity	1
Siteⁱ	59	Contributes to redox potential valueBy similarity	1
Active siteⁱ	60	NucleophileBy similarity	1
Siteⁱ	119	Lowers pKa of C-terminal Cys of first active siteBy similarity	1
Active siteⁱ	406	NucleophileBy similarity	1
Siteⁱ	407	Contributes to redox potential valueBy similarity	1
Siteⁱ	408	Contributes to redox potential valueBy similarity	1
Active siteⁱ	409	NucleophileBy similarity	1
Siteⁱ	471	Lowers pKa of C-terminal Cys of second active siteBy similarity	1

GO - Molecular functionⁱ

cysteine-type endopeptidase activity
Source: ProtInc
Traceable author statementⁱ
- 9399589
disulfide oxidoreductase activity
Source: ParkinsonsUK-UCL
Traceable author statementⁱ
- 22013210
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 16905107
peptide disulfide oxidoreductase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 16677074
phospholipase C activity
Source: ProtInc
Traceable author statementⁱ
- 3398923
protein disulfide isomerase activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
RNA binding
Source: UniProtKB
Inferred from high throughput direct assayⁱ
- 22658674

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
cell redox homeostasis Source: InterPro
positive regulation of extrinsic apoptotic signaling pathway Source: Ensembl
protein folding
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
protein folding in endoplasmic reticulum
Source: ParkinsonsUK-UCL
Traceable author statementⁱ
- 22013210
response to endoplasmic reticulum stress
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Isomerase

Molecular function

Isomerase

Enzyme and pathway databases

BRENDAⁱ	5.3.4.1 2681
Reactomeⁱ	R-HSA-1236974 ER-Phagosome pathway R-HSA-901042 Calnexin/calreticulin cycle R-HSA-983170 Antigen Presentation: Folding, assembly and peptide loading of class I MHC

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Protein disulfide-isomerase A3 (EC:5.3.4.1) Alternative name(s): 58 kDa glucose-regulated protein 58 kDa microsomal protein Short name: p58 Disulfide isomerase ER-60 Endoplasmic reticulum resident protein 57 Short name: ER protein 57 Short name: ERp57 Endoplasmic reticulum resident protein 60 Short name: ER protein 60 Short name: ERp60
Gene namesⁱ	Name:PDIA3 Synonyms:ERP57, ERP60, GRP58
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 15

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000167004.12
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:4606 PDIA3
MIMⁱ	602046 gene
neXtProtⁱ	NX_P30101

Keywords - Cellular componentⁱ

Endoplasmic reticulum

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	57	C → A: No loss of activity. No loss of activity; when associated with A-406. 1 Publication	1
Mutagenesisⁱ	57	C → S: Activity changed to serine protease. 1 Publication	1
Mutagenesisⁱ	60	C → S: Activity changed to serine protease; when associated with S-409. 1 Publication	1
Mutagenesisⁱ	406	C → A: No loss of activity. No loss of activity; when associated with A-57. 1 Publication	1
Mutagenesisⁱ	406	C → S: Activity changed to serine protease. 1 Publication	1
Mutagenesisⁱ	409	C → S: Activity changed to serine protease; when associated with S-60. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	2923
Open Targets More...OpenTargetsⁱ	ENSG00000167004
PharmGKBⁱ	PA29000

Polymorphism and mutation databases

BioMutaⁱ	PDIA3
DMDMⁱ	2507461

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 24	Combined sources5 PublicationsAdd BLAST		24
ChainⁱPRO_0000034225	25 – 505	Protein disulfide-isomerase A3Add BLAST		481

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Disulfide bondⁱ	57 ↔ 60	Redox-activePROSITE-ProRule annotation
Disulfide bondⁱ	57	Interchain (with C-115 in TAPBP); in linked form1 Publication
Modified residueⁱ	61	N6-methyllysineCombined sources	1
Disulfide bondⁱ	85 ↔ 92	1 Publication
Modified residueⁱ	129	N6-succinyllysineBy similarity	1
Modified residueⁱ	152	N6-acetyllysineBy similarity	1
Modified residueⁱ	218	N6-succinyllysineBy similarity	1
Modified residueⁱ	252	N6-acetyllysineBy similarity	1
Modified residueⁱ	319	PhosphothreonineCombined sources	1
Modified residueⁱ	362	N6-acetyllysineBy similarity	1
Disulfide bondⁱ	406 ↔ 409	Redox-activePROSITE-ProRule annotation
Modified residueⁱ	494	N6-acetyllysineBy similarity	1

Keywords - PTMⁱ

Acetylation, Disulfide bond, Methylation, Phosphoprotein

Proteomic databases

EPDⁱ	P30101
PaxDbⁱ	P30101
PeptideAtlas More...PeptideAtlasⁱ	P30101
PRIDEⁱ	P30101
ProteomicsDBⁱ	54635
TopDownProteomicsⁱ	P30101

2D gel databases

DOSAC-COBS 2D-PAGE database More...DOSAC-COBS-2DPAGEⁱ	P30101
REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEⁱ	P30101
SWISS-2DPAGEⁱ	P30101
UCD-2DPAGEⁱ	P30101

PTM databases

iPTMnetⁱ	P30101
PhosphoSitePlusⁱ	P30101
SwissPalmⁱ	P30101

Expressionⁱ

Tissue specificityⁱ

Detected in the flagellum and head region of spermatozoa (at protein level).1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000167004 Expressed in 226 organ(s), highest expression level in corpus epididymis
CleanExⁱ	HS_PDIA3
ExpressionAtlasⁱ	P30101 baseline and differential
Genevisibleⁱ	P30101 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB011199 CAB075744 HPA002645 HPA003230

HPAⁱ

CAB011199
CAB075744
HPA002645
HPA003230

Interactionⁱ

Subunit structureⁱ

Subunit of the TAP complex, also known as the peptide loading complex (PLC). Can form disulfide-linked heterodimers with TAPBP. Interacts with ERP27 and CANX. Interacts with SERPINA2 and with the S and Z variants of SERPINA1. Interacts with ATP2A2 (By similarity).By similarity4 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-979862,EBI-979862
APP	P05067	3	EBI-979862,EBI-77613
Calr	P18418	2	EBI-979862,EBI-916742	From Rattus norvegicus.
CANX	P24643	3	EBI-979862,EBI-15596385	From Canis lupus familiaris.
CLU	P10909	2	EBI-979862,EBI-1104674
ERO1A	Q96HE7	3	EBI-979862,EBI-2564539
ERO1B	Q86YB8	2	EBI-979862,EBI-2806988
PRDX4	Q13162	2	EBI-979862,EBI-2211957
STIM1	Q13586	3	EBI-979862,EBI-448878
TAP1	Q03518	4	EBI-979862,EBI-747259

GO - Molecular functionⁱ

identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 16905107

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	109180, 152 interactors
ComplexPortalⁱ	CPX-2375 Tapasin-ERp57 complex
CORUMⁱ	P30101
Database of interacting proteins More...DIPⁱ	DIP-29132N
IntActⁱ	P30101, 92 interactors
Molecular INTeraction database More...MINTⁱ	P30101
STRINGⁱ	9606.ENSP00000300289

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	27 – 29	Combined sources	3
Turnⁱ	32 – 34	Combined sources	3
Helixⁱ	35 – 38	Combined sources	4
Helixⁱ	39 – 41	Combined sources	3
Beta strandⁱ	43 – 53	Combined sources	11
Helixⁱ	58 – 73	Combined sources	16
Turnⁱ	74 – 77	Combined sources	4
Beta strandⁱ	80 – 84	Combined sources	5
Turnⁱ	85 – 87	Combined sources	3
Helixⁱ	89 – 94	Combined sources	6
Beta strandⁱ	99 – 107	Combined sources	9
Beta strandⁱ	110 – 114	Combined sources	5
Helixⁱ	121 – 131	Combined sources	11
Beta strandⁱ	136 – 138	Combined sources	3
Helixⁱ	142 – 149	Combined sources	8
Beta strandⁱ	151 – 153	Combined sources	3
Beta strandⁱ	155 – 161	Combined sources	7
Helixⁱ	166 – 177	Combined sources	12
Turnⁱ	178 – 181	Combined sources	4
Beta strandⁱ	182 – 187	Combined sources	6
Helixⁱ	190 – 196	Combined sources	7
Beta strandⁱ	198 – 206	Combined sources	9
Helixⁱ	209 – 211	Combined sources	3
Beta strandⁱ	218 – 221	Combined sources	4
Helixⁱ	229 – 239	Combined sources	11
Turnⁱ	240 – 243	Combined sources	4
Turnⁱ	249 – 251	Combined sources	3
Helixⁱ	252 – 255	Combined sources	4
Beta strandⁱ	256 – 265	Combined sources	10
Turnⁱ	269 – 271	Combined sources	3
Helixⁱ	273 – 292	Combined sources	20
Beta strandⁱ	298 – 303	Combined sources	6
Turnⁱ	304 – 307	Combined sources	4
Helixⁱ	308 – 311	Combined sources	4
Helixⁱ	312 – 314	Combined sources	3
Beta strandⁱ	325 – 329	Combined sources	5
Beta strandⁱ	331 – 333	Combined sources	3
Beta strandⁱ	335 – 337	Combined sources	3
Helixⁱ	347 – 358	Combined sources	12
Beta strandⁱ	376 – 381	Combined sources	6
Turnⁱ	383 – 385	Combined sources	3
Helixⁱ	386 – 390	Combined sources	5
Beta strandⁱ	396 – 402	Combined sources	7
Helixⁱ	407 – 422	Combined sources	16
Turnⁱ	423 – 425	Combined sources	3
Beta strandⁱ	427 – 435	Combined sources	9
Turnⁱ	436 – 438	Combined sources	3
Beta strandⁱ	449 – 456	Combined sources	8
Helixⁱ	473 – 483	Combined sources	11

Show more details

3D structure databases

ProteinModelPortalⁱ	P30101
SMRⁱ	P30101
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P30101

EvolutionaryTraceⁱ

P30101

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	25 – 133	Thioredoxin 1PROSITE-ProRule annotationAdd BLAST		109
Domainⁱ	343 – 485	Thioredoxin 2PROSITE-ProRule annotationAdd BLAST		143

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	502 – 505	Prevents secretion from ERBy similarity		4

Sequence similaritiesⁱ

Belongs to the protein disulfide isomerase family.Curated

Keywords - Domainⁱ

Redox-active center, Repeat, Signal

Phylogenomic databases

eggNOGⁱ	KOG0190 Eukaryota COG0526 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00930000150840
HOGENOMⁱ	HOG000162459
HOVERGENⁱ	HBG005920
InParanoidⁱ	P30101
KEGG Orthology (KO) More...KOⁱ	K08056
OMAⁱ	VAIVKMD
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G05J9
PhylomeDBⁱ	P30101
TreeFamⁱ	TF106382

Family and domain databases

InterProⁱ	View protein in InterPro IPR005788 Disulphide_isomerase IPR005792 Prot_disulphide_isomerase IPR036249 Thioredoxin-like_sf IPR017937 Thioredoxin_CS IPR013766 Thioredoxin_domain
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00085 Thioredoxin, 2 hits
SUPFAMⁱ	SSF52833 SSF52833, 4 hits
TIGRFAMsⁱ	TIGR01130 ER_PDI_fam, 1 hit TIGR01126 pdi_dom, 2 hits
PROSITEⁱ	View protein in PROSITE PS00194 THIOREDOXIN_1, 2 hits PS51352 THIOREDOXIN_2, 2 hits

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show all Align All

P30101-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MRLRRLALFP GVALLLAAAR LAAASDVLEL TDDNFESRIS DTGSAGLMLV 
        60         70         80         90        100
EFFAPWCGHC KRLAPEYEAA ATRLKGIVPL AKVDCTANTN TCNKYGVSGY 
       110        120        130        140        150
PTLKIFRDGE EAGAYDGPRT ADGIVSHLKK QAGPASVPLR TEEEFKKFIS 
       160        170        180        190        200
DKDASIVGFF DDSFSEAHSE FLKAASNLRD NYRFAHTNVE SLVNEYDDNG 
       210        220        230        240        250
EGIILFRPSH LTNKFEDKTV AYTEQKMTSG KIKKFIQENI FGICPHMTED 
       260        270        280        290        300
NKDLIQGKDL LIAYYDVDYE KNAKGSNYWR NRVMMVAKKF LDAGHKLNFA 
       310        320        330        340        350
VASRKTFSHE LSDFGLESTA GEIPVVAIRT AKGEKFVMQE EFSRDGKALE 
       360        370        380        390        400
RFLQDYFDGN LKRYLKSEPI PESNDGPVKV VVAENFDEIV NNENKDVLIE 
       410        420        430        440        450
FYAPWCGHCK NLEPKYKELG EKLSKDPNIV IAKMDATAND VPSPYEVRGF 
       460        470        480        490        500
PTIYFSPANK KLNPKKYEGG RELSDFISYL QREATNPPVI QEEKPKKKKK 

AQEDL

Length:505

Mass (Da):56,782

Last modified:November 1, 1997 - v4

Checksum:ⁱ529E5B6692D0D7E9

GO

Computationally mapped potential isoform sequencesⁱ

There are 3 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

H7BZJ3	H7BZJ3_HUMAN	Protein disulfide-isomerase A3 Protein disulfide-isomerase A3	PDIA3	123	Annotation score:
F8WBW5	F8WBW5_HUMAN	Protein disulfide-isomerase A3 Protein disulfide-isomerase A3	PDIA3	75	Annotation score:
F8WBS6	F8WBS6_HUMAN	Protein disulfide-isomerase A3 Protein disulfide-isomerase A3	PDIA3	71	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	19	A → G in BAA11928 (PubMed:9399589).Curated	1
Sequence conflictⁱ	22	A → V in BAA11928 (PubMed:9399589).Curated	1
Sequence conflictⁱ	217	D → Y in BAA03759 (PubMed:7945384).Curated	1
Sequence conflictⁱ	225	Q → P in CAA89996 (PubMed:8624847).Curated	1
Sequence conflictⁱ	238	E → G in CAA89996 (PubMed:8624847).Curated	1
Sequence conflictⁱ	272	N → D in BAA03759 (PubMed:7945384).Curated	1
Sequence conflictⁱ	272	N → D in AAC51518 (PubMed:9205111).Curated	1
Sequence conflictⁱ	355	D → G in BAA03759 (PubMed:7945384).Curated	1
Sequence conflictⁱ	358	D → G in BAA03759 (PubMed:7945384).Curated	1
Sequence conflictⁱ	368	E → D in BAA03759 (PubMed:7945384).Curated	1

Mass spectrometryⁱ

Molecular mass is 54265.22 Da from positions 25 - 505. Determined by MALDI. 1 Publication

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_020027	415	K → R. Corresponds to variant dbSNP:rs6413485Ensembl.		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	D16234 mRNA Translation: BAA03759.1 U42068 mRNA Translation: AAC50331.1 Z49835 mRNA Translation: CAA89996.1 U75885 U75884 Genomic DNA Translation: AAC51518.1 D83485 mRNA Translation: BAA11928.1 BC014433 mRNA Translation: AAH14433.1 BC036000 mRNA Translation: AAH36000.4 BC071878 mRNA Translation: AAH71878.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS10101.1
PIRⁱ	JC5704 S55507 S63994 S68363
NCBI Reference Sequences More...RefSeqⁱ	NP_005304.3, NM_005313.4
UniGeneⁱ	Hs.591095

Genome annotation databases

Ensemblⁱ	ENST00000300289; ENSP00000300289; ENSG00000167004
GeneIDⁱ	2923
KEGGⁱ	hsa:2923

Keywords - Coding sequence diversityⁱ

Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P30101	Protein disulfide-isomerase A3		PONAB		505	UniRef100_P30101
Protein disulfide-isomerase		HUMAN		505
Protein disulfide-isomerase		PANTR		505
Protein disulfide-isomerase		PANPA		505
Protein disulfide-isomerase		GORGO		383
+2

Protein	Similar proteins		Species	Score	Length	Source
P30101	Protein disulfide-isomerase A3		PONAB		505	UniRef90_P30101
Protein disulfide-isomerase A3		RAT		505
Protein disulfide-isomerase A3		MOUSE		505
Protein disulfide-isomerase A3		CHLAE		505
Protein disulfide-isomerase A3		BOVIN		505
+142

Protein	Similar proteins		Species	Score	Length	Source
P30101	Protein disulfide-isomerase A3		PONAB		505	UniRef50_P30101
Protein disulfide-isomerase A3		CHLAE		505
Protein disulfide-isomerase A3		MOUSE		505
Protein disulfide-isomerase A3		RAT		505
Protein disulfide-isomerase A3		BOVIN		505
+458

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	D16234 mRNA Translation: BAA03759.1 U42068 mRNA Translation: AAC50331.1 Z49835 mRNA Translation: CAA89996.1 U75885 U75884 Genomic DNA Translation: AAC51518.1 D83485 mRNA Translation: BAA11928.1 BC014433 mRNA Translation: AAH14433.1 BC036000 mRNA Translation: AAH36000.4 BC071878 mRNA Translation: AAH71878.1
CCDSⁱ	CCDS10101.1
PIRⁱ	JC5704 S55507 S63994 S68363
RefSeqⁱ	NP_005304.3, NM_005313.4
UniGeneⁱ	Hs.591095

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	2ALB	NMR	-	A	25-137	[»]
	2DMM	NMR	-	A	357-485	[»]
	2H8L	X-ray	2.00	A/B/C	134-376	[»]
	3F8U	X-ray	2.60	A/C	25-505	[»]
	6ENY	electron microscopy	5.80	D	25-505	[»]
ProteinModelPortalⁱ	P30101
SMRⁱ	P30101
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	109180, 152 interactors
ComplexPortalⁱ	CPX-2375 Tapasin-ERp57 complex
CORUMⁱ	P30101
DIPⁱ	DIP-29132N
IntActⁱ	P30101, 92 interactors
MINTⁱ	P30101
STRINGⁱ	9606.ENSP00000300289

PTM databases

iPTMnetⁱ	P30101
PhosphoSitePlusⁱ	P30101
SwissPalmⁱ	P30101

Polymorphism and mutation databases

BioMutaⁱ	PDIA3
DMDMⁱ	2507461

2D gel databases

DOSAC-COBS-2DPAGEⁱ	P30101
REPRODUCTION-2DPAGEⁱ	P30101
SWISS-2DPAGEⁱ	P30101
UCD-2DPAGEⁱ	P30101

Proteomic databases

EPDⁱ	P30101
PaxDbⁱ	P30101
PeptideAtlasⁱ	P30101
PRIDEⁱ	P30101
ProteomicsDBⁱ	54635
TopDownProteomicsⁱ	P30101

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	2923
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000300289; ENSP00000300289; ENSG00000167004
GeneIDⁱ	2923
KEGGⁱ	hsa:2923

Organism-specific databases

CTDⁱ	2923
DisGeNETⁱ	2923
EuPathDBⁱ	HostDB:ENSG00000167004.12
GeneCardsⁱ	PDIA3
HGNCⁱ	HGNC:4606 PDIA3
HPAⁱ	CAB011199 CAB075744 HPA002645 HPA003230
MIMⁱ	602046 gene
neXtProtⁱ	NX_P30101
OpenTargetsⁱ	ENSG00000167004
PharmGKBⁱ	PA29000
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0190 Eukaryota COG0526 LUCA
GeneTreeⁱ	ENSGT00930000150840
HOGENOMⁱ	HOG000162459
HOVERGENⁱ	HBG005920
InParanoidⁱ	P30101
KOⁱ	K08056
OMAⁱ	VAIVKMD
OrthoDBⁱ	EOG091G05J9
PhylomeDBⁱ	P30101
TreeFamⁱ	TF106382

Enzyme and pathway databases

BRENDAⁱ	5.3.4.1 2681
Reactomeⁱ	R-HSA-1236974 ER-Phagosome pathway R-HSA-901042 Calnexin/calreticulin cycle R-HSA-983170 Antigen Presentation: Folding, assembly and peptide loading of class I MHC

Miscellaneous databases

ChiTaRSⁱ	PDIA3 human
EvolutionaryTraceⁱ	P30101
GenomeRNAiⁱ	2923
Protein Ontology More...PROⁱ	PR:P30101
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000167004 Expressed in 226 organ(s), highest expression level in corpus epididymis
CleanExⁱ	HS_PDIA3
ExpressionAtlasⁱ	P30101 baseline and differential
Genevisibleⁱ	P30101 HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR005788 Disulphide_isomerase IPR005792 Prot_disulphide_isomerase IPR036249 Thioredoxin-like_sf IPR017937 Thioredoxin_CS IPR013766 Thioredoxin_domain
Pfamⁱ	View protein in Pfam PF00085 Thioredoxin, 2 hits
SUPFAMⁱ	SSF52833 SSF52833, 4 hits
TIGRFAMsⁱ	TIGR01130 ER_PDI_fam, 1 hit TIGR01126 pdi_dom, 2 hits
PROSITEⁱ	View protein in PROSITE PS00194 THIOREDOXIN_1, 2 hits PS51352 THIOREDOXIN_2, 2 hits
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	PDIA3_HUMAN
Accessionⁱ	P30101Primary (citable) accession number: P30101 Secondary accession number(s): Q13453 , Q14255, Q8IYF8, Q9UMU7
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
	Last sequence update:	November 1, 1997
	Last modified:	November 7, 2018
	This is version 219 of the entry and version 4 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 15
Human chromosome 15: entries, gene names and cross-references to MIM

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UniProtKB - P30101 (PDIA3_HUMAN)

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Protein disulfide-isomerase A3

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Caution

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Endoplasmic reticulum

Other locations

Endoplasmic reticulum

Endosome

Extracellular region or secreted

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Motif

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism and mutation databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Mass spectrometryⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ