Reviewed, UniProtKB/Swiss-Prot Q5RCH2 (PDIA2_PONAB)

Names and origin

Protein names

Recommended name:
    Protein disulfide-isomerase A2
    EC=5.3.4.1

Gene names

Name:

PDIA2

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	525 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	Part a large chaperone multiprotein complex comprising CABP1, DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor 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 Glycoprotein
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 – 21	21	Potential
	Chain	22 – 525	504	Protein disulfide-isomerase A2		PRO_0000034223
Regions
	Domain	27 – 152	126	Thioredoxin 1
	Domain	367 – 496	130	Thioredoxin 2
	Motif	522 – 525	4	Prevents secretion from ER Potential
Sites
	Active site	71	1	Nucleophile By similarity
	Active site	74	1	Nucleophile By similarity
	Active site	418	1	Nucleophile By similarity
	Active site	421	1	Nucleophile By similarity
	Site	72	1	Contributes to redox potential value By similarity
	Site	73	1	Contributes to redox potential value By similarity
	Site	138	1	Lowers pKa of C-terminal Cys of first active site By similarity
	Site	419	1	Contributes to redox potential value By similarity
	Site	420	1	Contributes to redox potential value By similarity
	Site	482	1	Lowers pKa of C-terminal Cys of second active site By similarity
Amino acid modifications
	Glycosylation	127	1	N-linked (GlcNAc...) Potential
	Glycosylation	284	1	N-linked (GlcNAc...) Potential
	Glycosylation	516	1	N-linked (GlcNAc...) Potential
	Disulfide bond	71 ↔ 74		Redox-active By similarity
	Disulfide bond	418 ↔ 421		Redox-active By similarity
Experimental info
	Sequence conflict	342	1	E → G in CAH92649. Ref.1
	Sequence conflict	485	1	G → E in CAH92649. Ref.1
	Sequence conflict	505	1	E → G in CAH92649. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q5RCH2-1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 0C402549E70D3F32	FASTA	525	58,124
	10 20 30 40 50 60 MSCQLLPVLL LLLLRASCPW GHEQGPRSPS EEPPEEEIPK EDGILVLSRH TLGLALREHP 70 80 90 100 110 120 ALLVEFYAPW CGHCQALAPE YSKAAAVLAA ESSVVMLAKV DGPAQPELAE EFGVTEYPTL 130 140 150 160 170 180 KFFRDGNRTH PEEYTGPREA EGIAEWLRRR VGPSAMRLED EAAAQALIDG RDLVVIGFFQ 190 200 210 220 230 240 DLHDEDVATF LALAQDALDM TFGLTDRPQL FQQFGLTKDT VVLFKKFDEG RADFPVDEEL 250 260 270 280 290 300 GLDLGDLSRF LVTHSMRLVT EFNSQTSAKI FAARILNHLL LFVNQTLAAH RELLVGFGEA 310 320 330 340 350 360 APHFRGQVLF VVVDVAADNE HVLQYFGLKA EAAPTLRLVN LETTKKYAPV DGGPVTTASI 370 380 390 400 410 420 TAFCHAVLNG QVKPYLLSQE VPPDWDQRPV KTLVGKNFEQ VAFDETKNVF VKFYAPWCTH 430 440 450 460 470 480 CKEMAPAWEA LAEKYQDHED VIIAELDATA NELDAFAVHG FPTLKYFPAG PGRKVIEYKS 490 500 510 520 TRDLGTFSKF LDNGGVLPTE EPLEEPAAPF PEPPANSTMG SKEEL

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	CR858298 mRNA. Translation: CAH90535.1. CR860523 mRNA. Translation: CAH92649.1.
RefSeq	NP_001125285.1.
UniGene	Pab.11836 Pab.19268
3D structure databases
SMR	Q5RCH2. Positions 36-499.
ModBase	Search...
Genome annotation databases
GeneID	100172183.
Organism-specific databases
CTD	100172183.
Phylogenomic databases
HOVERGEN	Q5RCH2.
InParanoid	Q5RCH2.
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	PS00014. ER_TARGET. 1 hit. PS00194. THIOREDOXIN_1. 2 hits. PS51352. THIOREDOXIN_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDIA2_PONAB

Accession

Primary (citable) accession number: Q5RCH2
Secondary accession number(s): Q5R6G7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	December 21, 2004
Last modified:	February 9, 2010
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)