P38657 (PDIA3_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PDIA3
Synonyms:	GRP58

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	505 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	Catalyzes the rearrangement of -S-S- bonds in proteins.
Subunit structure	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 By similarity.
Subcellular location	Endoplasmic reticulum lumen By similarity. Melanosome By similarity.
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains.
Caution	Was originally thought to be a phosphatidylinositol-4,5-bisphosphate phosphodiesterase type I (phospholipase C-alpha).

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Redox-active center Repeat Signal
Molecular function	Isomerase
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro positive regulation of apoptotic process Inferred from sequence or structural similarity. Source: AgBase
Cellular component	endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide isomerase activity Inferred from electronic annotation. Source: EC protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	By similarity
	Chain	25 – 505	481	Protein disulfide-isomerase A3		PRO_0000034224
Regions
	Domain	25 – 133	109	Thioredoxin 1
	Domain	343 – 485	143	Thioredoxin 2
	Motif	502 – 505	4	Prevents secretion from ER By similarity
Sites
	Active site	57	1	Nucleophile By similarity
	Active site	60	1	Nucleophile By similarity
	Active site	406	1	Nucleophile By similarity
	Active site	409	1	Nucleophile By similarity
	Site	58	1	Contributes to redox potential value By similarity
	Site	59	1	Contributes to redox potential value By similarity
	Site	119	1	Lowers pKa of C-terminal Cys of first active site By similarity
	Site	407	1	Contributes to redox potential value By similarity
	Site	408	1	Contributes to redox potential value By similarity
	Site	471	1	Lowers pKa of C-terminal Cys of second active site By similarity
Amino acid modifications
	Disulfide bond	57 ↔ 60		Redox-active; alternate By similarity
	Disulfide bond	57		Interchain (with C-115 in TAPBP); alternate By similarity
	Disulfide bond	85 ↔ 92		By similarity
	Disulfide bond	406 ↔ 409		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P38657 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: A85911748DC70A23	FASTA	505	56,930
	10 20 30 40 50 60 MRLRRLALFP GLALLLAAAR LAAASDVLEL TDDNFESRIT DTGSSGLMLV EFFAPWCGHC 70 80 90 100 110 120 KKLAPEYEAA ATRLKGIVPL AKVDCTANTN TCNKYGVSGY PTLKIFRDGE ESGAYDGPRT 130 140 150 160 170 180 ADGIVSHLKK QAGPASVPLK SEEEFEKFIS DKDASVVGFF KDLFSEAHSE FLKAASNLRD 190 200 210 220 230 240 NYRFAHTNVE SLVNKYDDDG EGITLFRPSH LTNKFEDKTV AYTEQKMTSG KIKRFIQENI 250 260 270 280 290 300 FGICPHMTED NKDLLQGKDL LIAYYDVDYE KNAKGSNYWR NRVMMVAKKF LDAGQKLHFA 310 320 330 340 350 360 VASRKTFSHE LSDFGLESTT GEIPVVAVRT AKGEKFVMQE EFSRDGKALE RFLEDYFDGN 370 380 390 400 410 420 LKRYLKSEPI PESNDGPVKV VVAENFDEIV NNENKDVLIE FYAPWCGHCK NLEPKYKELG 430 440 450 460 470 480 EKLRKDPNIV IAKMDATAND VPSPYEVRGF PTIYFSPANK KQNPKKYEGG RELSDFISYL 490 500 KREATNPPVI QEEKPKKKKK AQEDL

References

[1]	"Molecular cloning of the human glucose-regulated protein ERp57/GRP58, a thiol-dependent reductase. Identification of its secretory form and inducible expression by the oncogenic transformation." Hirano N., Shibasaki F., Sakai R., Tanaka T., Nishida J., Yazaki Y., Takenawa T., Hirai H. Eur. J. Biochem. 234:336-342(1995) [PubMed: 8529662] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D16235 mRNA. Translation: BAA03760.1.
IPI	IPI00689325.
PIR	JC2385.
UniGene	Bt.2562.
3D structure databases
ProteinModelPortal	P38657.
SMR	P38657. Positions 25-488.
ModBase	Search...
Protein-protein interaction databases
STRING	P38657.
Proteomic databases
PRIDE	P38657.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	maNOG09167.
GeneTree	ENSGT00590000082864.
HOVERGEN	HBG005920.
InParanoid	P38657.
OrthoDB	EOG42Z4PX.
PhylomeDB	P38657.
Family and domain databases
InterPro	IPR005788. Disulphide_isomerase. IPR005792. Prot_disulphide_isomerase. IPR005746. Thioredoxin. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 3 hits.
Pfam	PF00085. Thioredoxin. 2 hits. [Graphical view]
PRINTS	PR00421. THIOREDOXIN.
SUPFAM	SSF52833. Thiordxn-like_fd. 4 hits.
TIGRFAMs	TIGR01130. ER_PDI_fam. 1 hit. TIGR01126. Pdi_dom. 2 hits.
PROSITE	PS00194. THIOREDOXIN_1. 2 hits. PS51352. THIOREDOXIN_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDIA3_BOVIN

Accession

Primary (citable) accession number: P38657

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	September 21, 2011
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program