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P08003

- PDIA4_MOUSE

UniProt

P08003 - PDIA4_MOUSE

Protein

Protein disulfide-isomerase A4

Gene

Pdia4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 3 (30 Nov 2010)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    GO - Molecular functioni

    1. protein disulfide isomerase activity Source: UniProt

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. chaperone-mediated protein folding Source: UniProt
    3. protein folding Source: RefGenome
    4. response to endoplasmic reticulum stress Source: RefGenome

    Keywords - Molecular functioni

    Isomerase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein disulfide-isomerase A4 (EC:5.3.4.1)
    Alternative name(s):
    Endoplasmic reticulum resident protein 72
    Short name:
    ER protein 72
    Short name:
    ERp-72
    Short name:
    ERp72
    Gene namesi
    Name:Pdia4
    Synonyms:Cai, Erp72
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:104864. Pdia4.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: MGI
    2. endoplasmic reticulum Source: MGI
    3. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    4. melanosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 638618Protein disulfide-isomerase A4PRO_0000034230Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi36 – 361N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi84 ↔ 87Redox-activePROSITE-ProRule annotation
    Disulfide bondi199 ↔ 202Redox-activePROSITE-ProRule annotation
    Modified residuei359 – 3591N6-acetyllysineBy similarity
    Disulfide bondi548 ↔ 551Redox-activePROSITE-ProRule annotation

    Keywords - PTMi

    Acetylation, Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP08003.
    PaxDbiP08003.
    PRIDEiP08003.

    PTM databases

    PhosphoSiteiP08003.

    Expressioni

    Gene expression databases

    BgeeiP08003.
    CleanExiMM_PDIA4.
    GenevestigatoriP08003.

    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.

    Protein-protein interaction databases

    BioGridi198446. 1 interaction.
    IntActiP08003. 5 interactions.
    MINTiMINT-4106888.

    Structurei

    Secondary structure

    1
    638
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi52 – 543
    Beta strandi57 – 593
    Turni62 – 643
    Helixi65 – 695
    Beta strandi73 – 797
    Helixi85 – 884
    Helixi91 – 10212
    Beta strandi103 – 1064
    Beta strandi109 – 1135
    Turni115 – 1173
    Helixi119 – 1246
    Beta strandi129 – 1379
    Beta strandi140 – 1434
    Helixi150 – 16112
    Beta strandi162 – 1643
    Beta strandi171 – 1733
    Turni177 – 1793
    Turni181 – 1833
    Helixi184 – 1863
    Beta strandi188 – 1958
    Helixi200 – 21819
    Beta strandi219 – 2213
    Beta strandi225 – 2295
    Turni230 – 2323
    Helixi234 – 2396
    Beta strandi244 – 25411
    Beta strandi256 – 2583
    Helixi265 – 27713
    Beta strandi519 – 5224
    Turni525 – 5273
    Helixi528 – 5325
    Beta strandi537 – 5437
    Helixi550 – 56516
    Beta strandi568 – 5769
    Turni578 – 5803
    Beta strandi591 – 5999
    Helixi619 – 6279
    Beta strandi628 – 6303

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DJ1NMR-A46-172[»]
    2DJ2NMR-A171-277[»]
    2DJ3NMR-A519-638[»]
    ProteinModelPortaliP08003.
    SMRiP08003. Positions 47-507, 516-638.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08003.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 162142Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini162 – 294133Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini498 – 629132Thioredoxin 3PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi635 – 6384Prevents secretion from ER

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi39 – 5012Asp/Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the protein disulfide isomerase family.Curated
    Contains 3 thioredoxin domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Redox-active center, Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG0526.
    GeneTreeiENSGT00740000115037.
    HOGENOMiHOG000162459.
    HOVERGENiHBG005920.
    InParanoidiQ6NXW4.
    KOiK09582.
    OrthoDBiEOG7VHSX1.
    PhylomeDBiP08003.
    TreeFamiTF106382.

    Family and domain databases

    Gene3Di3.40.30.10. 4 hits.
    InterProiIPR005788. Disulphide_isomerase.
    IPR005792. Prot_disulphide_isomerase.
    IPR017068. Protein_diS-isomerase_A4.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view]
    PfamiPF00085. Thioredoxin. 3 hits.
    [Graphical view]
    PIRSFiPIRSF036862. Disulphide_isom_A4. 1 hit.
    SUPFAMiSSF52833. SSF52833. 5 hits.
    TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
    TIGR01126. pdi_dom. 3 hits.
    PROSITEiPS00014. ER_TARGET. 1 hit.
    PS00194. THIOREDOXIN_1. 3 hits.
    PS51352. THIOREDOXIN_2. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P08003-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLRKAWLLV LLLALTQLLA AASAGDAHED TSDTENATEE EEEEDDDDLE    50
    VKEENGVWVL NDGNFDNFVA DKDTVLLEFY APWCGHCKQF APEYEKIAST 100
    LKDNDPPIAV AKIDATSASM LASKFDVSGY PTIKILKKGQ AVDYDGSRTQ 150
    EEIVAKVREV SQPDWTPPPE VTLSLTKDNF DDVVNNADII LVEFYAPWCG 200
    HCKKLAPEYE KAAKELSKRS PPIPLAKVDA TEQTDLAKRF DVSGYPTLKI 250
    FRKGRPFDYN GPREKYGIVD YMIEQSGPPS KEILTLKQVQ EFLKDGDDVV 300
    IIGLFQGDGD PAYLQYQDAA NNLREDYKFH HTFSPEIAKF LKVSLGKLVL 350
    THPEKFQSKY EPRFHVMDVQ GSTEASAIKD YVVKHALPLV GHRKTSNDAK 400
    RYSKRPLVVV YYSVDFSFDY RAATQFWRNK VLEVAKDFPE YTFAIADEED 450
    YATEVKDLGL SESGEDVNAA ILDESGKKFA MEPEEFDSDT LREFVTAFKK 500
    GKLKPVIKSQ PVPKNNKGPV KVVVGKTFDA IVMDPKKDVL IEFYAPWCGH 550
    CKQLEPIYTS LGKKYKGQKD LVIAKMDATA NDITNDQYKV EGFPTIYFAP 600
    SGDKKNPIKF EGGNRDLEHL SKFIDEHATK RSRTKEEL 638
    Length:638
    Mass (Da):71,982
    Last modified:November 30, 2010 - v3
    Checksum:i2DDE2CE80BD77F6E
    GO

    Sequence cautioni

    The sequence CAA68777.1 differs from that shown. Reason: Frameshift at position 544.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti28 – 281H → Q in AAA39907. (PubMed:2295602)Curated
    Sequence conflicti28 – 281H → Q in BAE27045. (PubMed:16141072)Curated
    Sequence conflicti28 – 281H → Q in AAI41079. (PubMed:15489334)Curated
    Sequence conflicti39 – 391E → EEEE in BAC25863. (PubMed:16141072)Curated
    Sequence conflicti39 – 391E → EEEE in BAE41134. (PubMed:16141072)Curated
    Sequence conflicti39 – 391E → EEEE in BAE36446. (PubMed:16141072)Curated
    Sequence conflicti39 – 391E → EEEE in BAE29664. (PubMed:16141072)Curated
    Sequence conflicti468 – 4681N → S in BAC25863. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05186 mRNA. Translation: AAA39907.1.
    AK028292 mRNA. Translation: BAC25863.1.
    AK146288 mRNA. Translation: BAE27045.1.
    AK150566 mRNA. Translation: BAE29664.1.
    AK161534 mRNA. Translation: BAE36446.1.
    AK169387 mRNA. Translation: BAE41134.1.
    BC066857 mRNA. Translation: AAH66857.1.
    BC141078 mRNA. Translation: AAI41079.1.
    Y00884 mRNA. Translation: CAA68777.1. Frameshift.
    PIRiB34930. ISMSER.
    S06318.
    RefSeqiNP_033917.2. NM_009787.2.
    UniGeneiMm.2442.

    Genome annotation databases

    EnsembliENSMUST00000077290; ENSMUSP00000076521; ENSMUSG00000025823.
    GeneIDi12304.
    KEGGimmu:12304.
    UCSCiuc009btf.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05186 mRNA. Translation: AAA39907.1 .
    AK028292 mRNA. Translation: BAC25863.1 .
    AK146288 mRNA. Translation: BAE27045.1 .
    AK150566 mRNA. Translation: BAE29664.1 .
    AK161534 mRNA. Translation: BAE36446.1 .
    AK169387 mRNA. Translation: BAE41134.1 .
    BC066857 mRNA. Translation: AAH66857.1 .
    BC141078 mRNA. Translation: AAI41079.1 .
    Y00884 mRNA. Translation: CAA68777.1 . Frameshift.
    PIRi B34930. ISMSER.
    S06318.
    RefSeqi NP_033917.2. NM_009787.2.
    UniGenei Mm.2442.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DJ1 NMR - A 46-172 [» ]
    2DJ2 NMR - A 171-277 [» ]
    2DJ3 NMR - A 519-638 [» ]
    ProteinModelPortali P08003.
    SMRi P08003. Positions 47-507, 516-638.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198446. 1 interaction.
    IntActi P08003. 5 interactions.
    MINTi MINT-4106888.

    PTM databases

    PhosphoSitei P08003.

    Proteomic databases

    MaxQBi P08003.
    PaxDbi P08003.
    PRIDEi P08003.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000077290 ; ENSMUSP00000076521 ; ENSMUSG00000025823 .
    GeneIDi 12304.
    KEGGi mmu:12304.
    UCSCi uc009btf.1. mouse.

    Organism-specific databases

    CTDi 9601.
    MGIi MGI:104864. Pdia4.

    Phylogenomic databases

    eggNOGi COG0526.
    GeneTreei ENSGT00740000115037.
    HOGENOMi HOG000162459.
    HOVERGENi HBG005920.
    InParanoidi Q6NXW4.
    KOi K09582.
    OrthoDBi EOG7VHSX1.
    PhylomeDBi P08003.
    TreeFami TF106382.

    Miscellaneous databases

    ChiTaRSi PDIA4. mouse.
    EvolutionaryTracei P08003.
    NextBioi 280830.
    PROi P08003.
    SOURCEi Search...

    Gene expression databases

    Bgeei P08003.
    CleanExi MM_PDIA4.
    Genevestigatori P08003.

    Family and domain databases

    Gene3Di 3.40.30.10. 4 hits.
    InterProi IPR005788. Disulphide_isomerase.
    IPR005792. Prot_disulphide_isomerase.
    IPR017068. Protein_diS-isomerase_A4.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    Pfami PF00085. Thioredoxin. 3 hits.
    [Graphical view ]
    PIRSFi PIRSF036862. Disulphide_isom_A4. 1 hit.
    SUPFAMi SSF52833. SSF52833. 5 hits.
    TIGRFAMsi TIGR01130. ER_PDI_fam. 1 hit.
    TIGR01126. pdi_dom. 3 hits.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    PS00194. THIOREDOXIN_1. 3 hits.
    PS51352. THIOREDOXIN_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase."
      Mazzarella R.A., Srinivasan M., Haugejorden S.M., Green M.
      J. Biol. Chem. 265:1094-1101(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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 and DBA/2.
      Tissue: Amnion, Bone marrow, Head, Ovary and Uterus.
    3. "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: C57BL/6J.
      Tissue: Brain and Embryonic germ cell.
    4. "An mRNA sharing sequences with a variant granulocyte-macrophage colony stimulating factor cDNA clone."
      Gough N.M., King J.A., Dunn A.R.
      Nucleic Acids Res. 15:10584-10584(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-638.
      Strain: BALB/c.
      Tissue: T-cell.
    5. "A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins."
      Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.
      Mol. Biol. Cell 13:4456-4469(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: COMPONENT OF A CHAPERONE COMPLEX.
    6. "The solution structure of thioredoxin domains of mouse protein disulfide-isomerase A4."
      RIKEN structural genomics initiative (RSGI)
      Submitted (SEP-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 46-277 AND 516-638.

    Entry informationi

    Entry nameiPDIA4_MOUSE
    AccessioniPrimary (citable) accession number: P08003
    Secondary accession number(s): P15841
    , Q3TT79, Q3UJW0, Q6NXW4, Q8BMT8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 148 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, 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