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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

  1. protein disulfide isomerase activity Source: UniProtKB

GO - Biological processi

  1. apoptotic cell clearance Source: GO_Central
  2. cell redox homeostasis Source: InterPro
  3. platelet activation Source: UniProtKB
  4. platelet aggregation Source: UniProtKB
  5. protein folding Source: GO_Central
  6. response to endoplasmic reticulum stress Source: GO_Central
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
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:1919103. Pdia6.

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation. Cell membrane By similarity. Melanosome By similarity

GO - Cellular componenti

  1. endoplasmic reticulum Source: GO_Central
  2. endoplasmic reticulum chaperone complex Source: ParkinsonsUK-UCL
  3. endoplasmic reticulum-Golgi intermediate compartment Source: MGI
  4. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  5. extracellular vesicular exosome Source: MGI
  6. melanosome Source: UniProtKB
  7. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919By similarityAdd
BLAST
Chaini20 – 440421Protein disulfide-isomerase A6PRO_0000034238Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi55 ↔ 58Redox-activePROSITE-ProRule annotation
Modified residuei129 – 1291PhosphoserineBy similarity
Disulfide bondi190 ↔ 193Redox-activePROSITE-ProRule annotation
Modified residuei428 – 4281PhosphoserineBy similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiQ922R8.
PaxDbiQ922R8.
PRIDEiQ922R8.

2D gel databases

REPRODUCTION-2DPAGEQ922R8.

PTM databases

PhosphoSiteiQ922R8.

Expressioni

Gene expression databases

CleanExiMM_PDIA6.
GenevestigatoriQ922R8.

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. 3 interactions.
IntActiQ922R8. 4 interactions.
MINTiMINT-1867499.

Structurei

Secondary structure

1
440
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 295
Turni32 – 343
Helixi35 – 384
Turni39 – 413
Beta strandi46 – 516
Helixi59 – 613
Helixi62 – 7110
Turni72 – 754
Beta strandi76 – 827
Turni83 – 853
Helixi87 – 937
Beta strandi97 – 10610
Helixi120 – 13213

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DMLNMR-A16-132[»]
ProteinModelPortaliQ922R8.
SMRiQ922R8. Positions 20-272.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ922R8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 133114Thioredoxin 1PROSITE-ProRule annotationAdd
BLAST
Domaini151 – 287137Thioredoxin 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi437 – 4404Prevents secretion from ERPROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi422 – 43413Asp/Glu-rich (acidic)Add
BLAST

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

eggNOGiCOG0526.
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 AAH06865.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAC36392.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti224 – 2241V → M in BAC36392 (PubMed:16141072).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2DMLNMR-A16-132[»]
ProteinModelPortaliQ922R8.
SMRiQ922R8. Positions 20-272.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi214980. 3 interactions.
IntActiQ922R8. 4 interactions.
MINTiMINT-1867499.

PTM databases

PhosphoSiteiQ922R8.

2D gel databases

REPRODUCTION-2DPAGEQ922R8.

Proteomic databases

MaxQBiQ922R8.
PaxDbiQ922R8.
PRIDEiQ922R8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi71853.
KEGGimmu:71853.

Organism-specific databases

CTDi10130.
MGIiMGI:1919103. Pdia6.

Phylogenomic databases

eggNOGiCOG0526.
HOVERGENiHBG053548.
InParanoidiQ922R8.
KOiK09584.

Miscellaneous databases

ChiTaRSiPdia6. mouse.
EvolutionaryTraceiQ922R8.
NextBioi334734.
PROiQ922R8.
SOURCEiSearch...

Gene expression databases

CleanExiMM_PDIA6.
GenevestigatoriQ922R8.

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...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Testis.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary tumor.
  3. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 119-132 AND 393-409, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  4. "The solution structure of the first thioredoxin domain of mouse protein disulfide-isomerase A6."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 16-132.

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: March 4, 2015
This is version 118 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

External Data

Dasty 3

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 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.