Q5R6T1 (PDIA6_PONAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein disulfide-isomerase A6
EC=5.3.4.1

Gene names

Name:

PDIA6

Organism

Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Ponginae › Pongo

Protein attributes

Sequence length	440 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)

Function	May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin By similarity.
Catalytic activity	Catalyzes the rearrangement of -S-S- bonds in proteins.
Subunit structure	Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. Interacts with ITGB3 following platelet stimulation By similarity.
Subcellular location	Endoplasmic reticulum lumen By similarity. Cell membrane By similarity. Melanosome By similarity.
Sequence similarities	Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains.

Ontologies

Keywords
Cellular component	Cell membrane Endoplasmic reticulum Membrane
Domain	Redox-active center Repeat Signal
Molecular function	Chaperone Isomerase
PTM	Disulfide bond Phosphoprotein
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 platelet aggregation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell melanosome Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide isomerase activity Inferred from sequence or structural similarity. Source: UniProtKB 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 – 19	19	By similarity
	Chain	20 – 440	421	Protein disulfide-isomerase A6		PRO_0000034239
Regions
	Domain	20 – 132	113	Thioredoxin 1
	Domain	124 – 287	164	Thioredoxin 2
	Motif	437 – 440	4	Prevents secretion from ER Potential
	Compositional bias	422 – 434	13	Asp/Glu-rich (acidic)
Amino acid modifications
	Modified residue	428	1	Phosphoserine By similarity
	Disulfide bond	55 ↔ 58		Redox-active By similarity
	Disulfide bond	190 ↔ 193		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5R6T1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 34CC8CEEED17B34C	FASTA	440	48,110
	10 20 30 40 50 60 MALLVLGLVS CAFFLEVNGL YSSSDDVIEL TPSNFNREVI QSDSLWLVEF YAPWCGHCQR 70 80 90 100 110 120 LTPEWKKAAT ALKDVVKVGA VDADKHHSLG GQYGVQGFPT IKIFGSNKNR PEDYQGGRTG 130 140 150 160 170 180 EAIVDAALSA LRQLVKDRLG GQSGGYSSGK QGRSDSSSKK DVIELTDDSF DKNVLDSEDV 190 200 210 220 230 240 WMVEFYAPWC GHCKNLEPEW AAAASEVKEQ TKGKVKLAAV DATVNQVLAS RYGIRGFPTI 250 260 270 280 290 300 KIFQKGESPV DYDGGRTRSD IVSRALDLFS DNAPPPELLE IISEDIAKRT CEEHQLCVVS 310 320 330 340 350 360 VLPHILDTGA AGRNSYLEVL LKLADKYKKK MWGWLWTEAG AQSELETALG IGGFGYPAMA 370 380 390 400 410 420 AINARKMKFA LLKGSFSEQG INEFLRELSF GRGSTAPVGG GAFPTIVERE PWDGRDGELP 430 440 VEDDIDLSDV ELDDLGKDEL

References

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

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR860403 mRNA. Translation: CAH92529.1.
RefSeq	NP_001126483.1. NM_001133011.1.
3D structure databases
ProteinModelPortal	Q5R6T1.
SMR	Q5R6T1. Positions 20-132, 156-280.
ModBase	Search...
Proteomic databases
PRIDE	Q5R6T1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100173470.
KEGG	pon:100173470.
Organism-specific databases
CTD	10130.
Phylogenomic databases
HOVERGEN	HBG053548.
InParanoid	Q5R6T1.
KO	K09584.
Family and domain databases
Gene3D	3.40.30.10. 2 hits.
InterPro	IPR005788. Disulphide_isomerase. IPR005746. Thioredoxin. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. [Graphical view]
Pfam	PF00085. Thioredoxin. 2 hits. [Graphical view]
PRINTS	PR00421. THIOREDOXIN.
SUPFAM	SSF52833. Thiordxn-like_fd. 3 hits.
TIGRFAMs	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

PDIA6_PONAB

Accession

Primary (citable) accession number: Q5R6T1

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	December 21, 2004
Last modified:	May 29, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program