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Protein

Protein disulfide-isomerase A6

Gene

Pdia6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase

Names & Taxonomyi

Protein namesi
Recommended name:
Protein disulfide-isomerase A6 (EC:5.3.4.1)
Alternative name(s):
Thioredoxin domain-containing protein 7
Gene namesi
Name:Pdia6
Synonyms:Txndc7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1919103. Pdia6.

Subcellular locationi

  • Endoplasmic reticulum lumen By similarity
  • Cell membrane By similarity
  • Melanosome By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19By similarityAdd BLAST19
ChainiPRO_000003423820 – 440Protein disulfide-isomerase A6Add BLAST421

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi55 ↔ 58Redox-activePROSITE-ProRule annotation
Modified residuei129PhosphoserineCombined sources1
Modified residuei156PhosphoserineBy similarity1
Modified residuei158PhosphoserineBy similarity1
Disulfide bondi190 ↔ 193Redox-activePROSITE-ProRule annotation
Modified residuei428PhosphoserineCombined sources1

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

EPDiQ922R8.
MaxQBiQ922R8.
PaxDbiQ922R8.
PeptideAtlasiQ922R8.
PRIDEiQ922R8.

2D gel databases

REPRODUCTION-2DPAGEQ922R8.

PTM databases

iPTMnetiQ922R8.
PhosphoSitePlusiQ922R8.
SwissPalmiQ922R8.

Expressioni

Gene expression databases

CleanExiMM_PDIA6.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi214980. 4 interactors.
IntActiQ922R8. 4 interactors.
MINTiMINT-1867499.
STRINGi10090.ENSMUSP00000052912.

Structurei

Secondary structure

1440
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi25 – 29Combined sources5
Turni32 – 34Combined sources3
Helixi35 – 38Combined sources4
Turni39 – 41Combined sources3
Beta strandi46 – 51Combined sources6
Helixi59 – 61Combined sources3
Helixi62 – 71Combined sources10
Turni72 – 75Combined sources4
Beta strandi76 – 82Combined sources7
Turni83 – 85Combined sources3
Helixi87 – 93Combined sources7
Beta strandi97 – 106Combined sources10
Helixi120 – 132Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DMLNMR-A16-132[»]
ProteinModelPortaliQ922R8.
SMRiQ922R8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ922R8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 133Thioredoxin 1PROSITE-ProRule annotationAdd BLAST114
Domaini151 – 287Thioredoxin 2PROSITE-ProRule annotationAdd BLAST137

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi437 – 440Prevents secretion from ERPROSITE-ProRule annotation4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi422 – 434Asp/Glu-rich (acidic)Add BLAST13

Sequence similaritiesi

Belongs to the protein disulfide isomerase family.Curated
Contains 2 thioredoxin domains.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

eggNOGiKOG0191. Eukaryota.
COG0526. LUCA.
HOVERGENiHBG053548.
InParanoidiQ922R8.
KOiK09584.

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 3 hits.
TIGRFAMsiTIGR01126. pdi_dom. 2 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q922R8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARLVLGLVS CTFFLAVSGL YSSSDDVIEL TPSNFNREVI QSDGLWLVEF
60 70 80 90 100
YAPWCGHCQR LTPEWKKAAT ALKDVVKVGA VNADKHQSLG GQYGVQGFPT
110 120 130 140 150
IKIFGANKNK PEDYQGGRTG EAIVDAALSA LRQLVKDRLG GRSGGYSSGK
160 170 180 190 200
QGRGDSSSKK DVVELTDDTF DKNVLDSEDV WMVEFYAPWC GHCKNLEPEW
210 220 230 240 250
AAAATEVKEQ TKGKVKLAAV DATVNQVLAS RYGIKGFPTI KIFQKGESPV
260 270 280 290 300
DYDGGRTRSD IVSRALDLFS DNAPPPELLE IINEDIAKKT CEEHQLCVVA
310 320 330 340 350
VLPHILDTGA AGRNSYLEVL LKLADKYKKK MWGWLWTEAG AQYELENALG
360 370 380 390 400
IGGFGYPAMA AINARKMKFA LLKGSFSEQG INEFLRELSF GRGSTAPVGG
410 420 430 440
GSFPTITPRE PWDGKDGELP VEDDIDLSDV ELDDLEKDEL
Length:440
Mass (Da):48,100
Last modified:April 12, 2005 - v3
Checksum:iE9FFA1F91AE06A20
GO

Sequence cautioni

The sequence AAH06865 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAC36392 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti224V → M in BAC36392 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK076558 mRNA. Translation: BAC36392.1. Different initiation.
BC006865 mRNA. Translation: AAH06865.2. Different initiation.
RefSeqiNP_082235.1. NM_027959.3.
UniGeneiMm.222825.

Genome annotation databases

GeneIDi71853.
KEGGimmu:71853.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK076558 mRNA. Translation: BAC36392.1. Different initiation.
BC006865 mRNA. Translation: AAH06865.2. Different initiation.
RefSeqiNP_082235.1. NM_027959.3.
UniGeneiMm.222825.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DMLNMR-A16-132[»]
ProteinModelPortaliQ922R8.
SMRiQ922R8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi214980. 4 interactors.
IntActiQ922R8. 4 interactors.
MINTiMINT-1867499.
STRINGi10090.ENSMUSP00000052912.

PTM databases

iPTMnetiQ922R8.
PhosphoSitePlusiQ922R8.
SwissPalmiQ922R8.

2D gel databases

REPRODUCTION-2DPAGEQ922R8.

Proteomic databases

EPDiQ922R8.
MaxQBiQ922R8.
PaxDbiQ922R8.
PeptideAtlasiQ922R8.
PRIDEiQ922R8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi71853.
KEGGimmu:71853.

Organism-specific databases

CTDi10130.
MGIiMGI:1919103. Pdia6.

Phylogenomic databases

eggNOGiKOG0191. Eukaryota.
COG0526. LUCA.
HOVERGENiHBG053548.
InParanoidiQ922R8.
KOiK09584.

Miscellaneous databases

ChiTaRSiPdia6. mouse.
EvolutionaryTraceiQ922R8.
PROiQ922R8.
SOURCEiSearch...

Gene expression databases

CleanExiMM_PDIA6.

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
InterProiIPR005788. Disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 3 hits.
TIGRFAMsiTIGR01126. pdi_dom. 2 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPDIA6_MOUSE
AccessioniPrimary (citable) accession number: Q922R8
Secondary accession number(s): Q8BK54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: April 12, 2005
Last modified: November 30, 2016
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.