Reviewed, UniProtKB/Swiss-Prot Q5RDG4 (PDIA3_PONAB)

Names and origin

Protein names

Recommended name:
    Protein disulfide-isomerase A3
    EC=5.3.4.1

Gene names

Name:

PDIA3

Organism

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

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.
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Redox-active center Repeat Signal
Molecular function	Isomerase
PTM	Disulfide bond
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro
Cellular component	endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein disulfide isomerase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Chain	25 – 505	481	Protein disulfide-isomerase A3		PRO_0000292595
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)
	Q5RDG4-1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 529E5B6692D0D7E9	FASTA	505	56,782
	10 20 30 40 50 60 MRLRRLALFP GVALLLAAAR LAAASDVLEL TDDNFESRIS DTGSAGLMLV EFFAPWCGHC 70 80 90 100 110 120 KRLAPEYEAA ATRLKGIVPL AKVDCTANTN TCNKYGVSGY PTLKIFRDGE EAGAYDGPRT 130 140 150 160 170 180 ADGIVSHLKK QAGPASVPLR TEEEFKKFIS DKDASIVGFF DDSFSEAHSE FLKAASNLRD 190 200 210 220 230 240 NYRFAHTNVE SLVNEYDDNG EGIILFRPSH LTNKFEDKTV AYTEQKMTSG KIKKFIQENI 250 260 270 280 290 300 FGICPHMTED NKDLIQGKDL LIAYYDVDYE KNAKGSNYWR NRVMMVAKKF LDAGHKLNFA 310 320 330 340 350 360 VASRKTFSHE LSDFGLESTA GEIPVVAIRT AKGEKFVMQE EFSRDGKALE RFLQDYFDGN 370 380 390 400 410 420 LKRYLKSEPI PESNDGPVKV VVAENFDEIV NNENKDVLIE FYAPWCGHCK NLEPKYKELG 430 440 450 460 470 480 EKLSKDPNIV IAKMDATAND VPSPYEVRGF PTIYFSPANK KLNPKKYEGG RELSDFISYL 490 500 QREATNPPVI QEEKPKKKKK AQEDL

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR857946 mRNA. Translation: CAH90193.1.
RefSeq	NP_001127250.1.
UniGene	Pab.7080
3D structure databases
HSSP	HSSP built from PDB template 2DJJ based on UniProtKB P55059.
SMR	Q5RDG4. Positions 25-137, 134-365, 357-488.
ModBase	Search...
Proteomic databases
PRIDE	Q5RDG4.
Genome annotation databases
GeneID	100174305.
Organism-specific databases
CTD	100174305.
Phylogenomic databases
HOVERGEN	Q5RDG4.
Enzyme and pathway databases
BRENDA	5.3.4.1. 269192.
Family and domain databases
InterPro	IPR005788. Disulphide_isomerase. IPR005792. Prot_disulphide_isomerase. IPR017936. Thioredoxin-like. IPR012336. Thioredoxin-like_fold. IPR006662. Thioredoxin-like_subdom. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 2 hits.
Pfam	PF00085. Thioredoxin. 2 hits. [Graphical view]
PRINTS	PR00421. THIOREDOXIN.
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_PONAB

Accession

Primary (citable) accession number: Q5RDG4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	December 21, 2004
Last modified:	February 9, 2010
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)