Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q922R8

- PDIA6_MOUSE

UniProt

Q922R8 - PDIA6_MOUSE

Protein

Protein disulfide-isomerase A6

Gene

Pdia6

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 3 (12 Apr 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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: RefGenome
    2. cell redox homeostasis Source: InterPro
    3. platelet activation Source: UniProtKB
    4. platelet aggregation Source: UniProtKB
    5. protein folding Source: RefGenome
    6. response to endoplasmic reticulum stress Source: RefGenome

    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: RefGenome
    2. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    3. melanosome Source: UniProtKB
    4. plasma membrane Source: UniProtKB

    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
    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:
    PDBe
    RCSB PDB
    PDBj
    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

    MARLVLGLVS CTFFLAVSGL YSSSDDVIEL TPSNFNREVI QSDGLWLVEF    50
    YAPWCGHCQR LTPEWKKAAT ALKDVVKVGA VNADKHQSLG GQYGVQGFPT 100
    IKIFGANKNK PEDYQGGRTG EAIVDAALSA LRQLVKDRLG GRSGGYSSGK 150
    QGRGDSSSKK DVVELTDDTF DKNVLDSEDV WMVEFYAPWC GHCKNLEPEW 200
    AAAATEVKEQ TKGKVKLAAV DATVNQVLAS RYGIKGFPTI KIFQKGESPV 250
    DYDGGRTRSD IVSRALDLFS DNAPPPELLE IINEDIAKKT CEEHQLCVVA 300
    VLPHILDTGA AGRNSYLEVL LKLADKYKKK MWGWLWTEAG AQYELENALG 350
    IGGFGYPAMA AINARKMKFA LLKGSFSEQG INEFLRELSF GRGSTAPVGG 400
    GSFPTITPRE PWDGKDGELP VEDDIDLSDV ELDDLEKDEL 440
    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.
    The sequence BAC36392.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK076558 mRNA. Translation: BAC36392.1 . Different initiation.
    BC006865 mRNA. Translation: AAH06865.2 . Different initiation.
    RefSeqi NP_082235.1. NM_027959.3.
    UniGenei Mm.222825.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DML NMR - A 16-132 [» ]
    ProteinModelPortali Q922R8.
    SMRi Q922R8. Positions 20-272.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 214980. 3 interactions.
    IntActi Q922R8. 4 interactions.
    MINTi MINT-1867499.

    PTM databases

    PhosphoSitei Q922R8.

    2D gel databases

    REPRODUCTION-2DPAGE Q922R8.

    Proteomic databases

    MaxQBi Q922R8.
    PaxDbi Q922R8.
    PRIDEi Q922R8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 71853.
    KEGGi mmu:71853.

    Organism-specific databases

    CTDi 10130.
    MGIi MGI:1919103. Pdia6.

    Phylogenomic databases

    eggNOGi COG0526.
    HOVERGENi HBG053548.
    InParanoidi Q922R8.
    KOi K09584.

    Miscellaneous databases

    ChiTaRSi PDIA6. mouse.
    EvolutionaryTracei Q922R8.
    NextBioi 334734.
    PROi Q922R8.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_PDIA6.
    Genevestigatori Q922R8.

    Family and domain databases

    Gene3Di 3.40.30.10. 2 hits.
    InterProi IPR005788. Disulphide_isomerase.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    Pfami PF00085. Thioredoxin. 2 hits.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 3 hits.
    TIGRFAMsi TIGR01126. pdi_dom. 2 hits.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    PS00194. THIOREDOXIN_1. 2 hits.
    PS51352. THIOREDOXIN_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 113 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