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P09103

- PDIA1_MOUSE

UniProt

P09103 - PDIA1_MOUSE

Protein

Protein disulfide-isomerase

Gene

P4hb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP By similarity.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei55 – 551NucleophileBy similarity
    Sitei56 – 561Contributes to redox potential valueBy similarity
    Sitei57 – 571Contributes to redox potential valueBy similarity
    Active sitei58 – 581NucleophileBy similarity
    Sitei122 – 1221Lowers pKa of C-terminal Cys of first active siteBy similarity
    Active sitei399 – 3991NucleophileBy similarity
    Sitei400 – 4001Contributes to redox potential valueBy similarity
    Sitei401 – 4011Contributes to redox potential valueBy similarity
    Active sitei402 – 4021NucleophileBy similarity
    Sitei463 – 4631Lowers pKa of C-terminal Cys of second active siteBy similarity

    GO - Molecular functioni

    1. procollagen-proline 4-dioxygenase activity Source: Ensembl
    2. protein disulfide isomerase activity Source: RefGenome

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. cellular response to hypoxia Source: Ensembl
    3. peptidyl-proline hydroxylation to 4-hydroxy-L-proline Source: MGI
    4. protein folding Source: RefGenome
    5. regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: RefGenome
    6. response to endoplasmic reticulum stress Source: RefGenome

    Keywords - Molecular functioni

    Chaperone, Isomerase

    Enzyme and pathway databases

    ReactomeiREACT_189141. Detoxification of Reactive Oxygen Species.
    REACT_198984. Collagen biosynthesis and modifying enzymes.
    REACT_216017. Chylomicron-mediated lipid transport.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein disulfide-isomerase (EC:5.3.4.1)
    Short name:
    PDI
    Alternative name(s):
    Cellular thyroid hormone-binding protein
    Endoplasmic reticulum resident protein 59
    Short name:
    ER protein 59
    Short name:
    ERp59
    Prolyl 4-hydroxylase subunit beta
    p55
    Gene namesi
    Name:P4hb
    Synonyms:Pdia1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:97464. P4hb.

    Subcellular locationi

    Endoplasmic reticulum lumen PROSITE-ProRule annotation. Melanosome By similarity. Cell membrane Curated; Peripheral membrane protein Curated
    Note: Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources. Localizes near CD4-enriched regions on lymphoid cell surfaces By similarity.By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum Source: MGI
    2. endoplasmic reticulum-Golgi intermediate compartment Source: Ensembl
    3. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    4. melanosome Source: UniProtKB-SubCell
    5. plasma membrane Source: UniProtKB-SubCell
    6. procollagen-proline 4-dioxygenase complex Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919By similarityAdd
    BLAST
    Chaini20 – 509490Protein disulfide-isomerasePRO_0000034196Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi55 ↔ 58Redox-activePROSITE-ProRule annotation
    Modified residuei202 – 2021N6-acetyllysine1 Publication
    Modified residuei224 – 2241N6-succinyllysine1 Publication
    Modified residuei273 – 2731N6-succinyllysine1 Publication
    Disulfide bondi399 ↔ 402Redox-activePROSITE-ProRule annotation

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    MaxQBiP09103.
    PaxDbiP09103.
    PRIDEiP09103.

    2D gel databases

    COMPLUYEAST-2DPAGEP09103.
    REPRODUCTION-2DPAGEP09103.
    SWISS-2DPAGEP09103.

    PTM databases

    PhosphoSiteiP09103.

    Expressioni

    Gene expression databases

    ArrayExpressiP09103.
    BgeeiP09103.
    CleanExiMM_P4HB.
    GenevestigatoriP09103.

    Interactioni

    Subunit structurei

    Homodimer. Monomers and homotetramers may also occur. Also constitutes the structural subunit of prolyl 4-hydroxylase and of the microsomal triacylglycerol transfer protein MTTP in mammalian cells. Stabilizes both enzymes and retain them in the ER without contributing to the catalytic activity. Binds UBQLN1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi202008. 1 interaction.
    IntActiP09103. 12 interactions.
    MINTiMINT-4122712.
    STRINGi10090.ENSMUSP00000026122.

    Structurei

    3D structure databases

    ProteinModelPortaliP09103.
    SMRiP09103. Positions 18-480.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 136117Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini348 – 477130Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi506 – 5094Prevents secretion from ER

    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.
    GeneTreeiENSGT00740000115202.
    HOGENOMiHOG000162459.
    HOVERGENiHBG005920.
    InParanoidiQ922C8.
    KOiK09580.
    OMAiYRDHENI.
    OrthoDBiEOG7VHSX1.
    TreeFamiTF106381.

    Family and domain databases

    Gene3Di3.40.30.10. 4 hits.
    InterProiIPR005788. Disulphide_isomerase.
    IPR005792. Prot_disulphide_isomerase.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view]
    PfamiPF00085. Thioredoxin. 2 hits.
    [Graphical view]
    SUPFAMiSSF52833. SSF52833. 4 hits.
    TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
    TIGR01126. 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.

    P09103-1 [UniParc]FASTAAdd to Basket

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    MLSRALLCLA LAWAARVGAD ALEEEDNVLV LKKSNFEEAL AAHKYLLVEF    50
    YAPWCGHCKA LAPEYAKAAA KLKAEGSEIR LAKVDATEES DLAQQYGVRG 100
    YPTIKFFKNG DTASPKEYTA GREADDIVNW LKKRTGPAAT TLSDTAAAES 150
    LVDSSEVTVI GFFKDVESDS AKQFLLAAEA IDDIPFGITS NSGVFSKYQL 200
    DKDGVVLFKK FDEGRNNFEG EITKEKLLDF IKHNQLPLVI EFTEQTAPKI 250
    FGGEIKTHIL LFLPKSVSDY DGKLSSFKRA AEGFKGKILF IFIDSDHTDN 300
    QRILEFFGLK KEECPAVRLI TLEEEMTKYK PESDELTAEK ITEFCHRFLE 350
    GKIKPHLMSQ EVPEDWDKQP VKVLVGANFE EVAFDEKKNV FVEFYAPWCG 400
    HCKQLAPIWD KLGETYKDHE NIIIAKMDST ANEVEAVKVH SFPTLKFFPA 450
    SADRTVIDYN GERTLDGFKK FLESGGQDGA GDDEDLDLEE ALEPDMEEDD 500
    DQKAVKDEL 509
    Length:509
    Mass (Da):57,058
    Last modified:July 27, 2011 - v2
    Checksum:i1FB0AA8ACCDB13EA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti68 – 681A → R in CAA29759. (PubMed:2830592)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06453 mRNA. Translation: CAA29759.1.
    J05185 mRNA. Translation: AAA39906.1.
    AK150002 mRNA. Translation: BAE29230.1.
    AK150422 mRNA. Translation: BAE29545.1.
    AK150805 mRNA. Translation: BAE29868.1.
    AK152141 mRNA. Translation: BAE30979.1.
    AK152217 mRNA. Translation: BAE31045.1.
    AK159606 mRNA. Translation: BAE35225.1.
    AK159965 mRNA. Translation: BAE35520.1.
    AK168330 mRNA. Translation: BAE40268.1.
    AK168893 mRNA. Translation: BAE40710.1.
    AK170603 mRNA. Translation: BAE41907.1.
    AL663030 Genomic DNA. Translation: CAM27084.1.
    BC008549 mRNA. Translation: AAH08549.1.
    BC093512 mRNA. Translation: AAH93512.1.
    CCDSiCCDS25742.1.
    PIRiA34930. ISMSSS.
    RefSeqiNP_035162.1. NM_011032.2.
    UniGeneiMm.16660.

    Genome annotation databases

    EnsembliENSMUST00000026122; ENSMUSP00000026122; ENSMUSG00000025130.
    GeneIDi18453.
    KEGGimmu:18453.
    UCSCiuc007mti.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06453 mRNA. Translation: CAA29759.1 .
    J05185 mRNA. Translation: AAA39906.1 .
    AK150002 mRNA. Translation: BAE29230.1 .
    AK150422 mRNA. Translation: BAE29545.1 .
    AK150805 mRNA. Translation: BAE29868.1 .
    AK152141 mRNA. Translation: BAE30979.1 .
    AK152217 mRNA. Translation: BAE31045.1 .
    AK159606 mRNA. Translation: BAE35225.1 .
    AK159965 mRNA. Translation: BAE35520.1 .
    AK168330 mRNA. Translation: BAE40268.1 .
    AK168893 mRNA. Translation: BAE40710.1 .
    AK170603 mRNA. Translation: BAE41907.1 .
    AL663030 Genomic DNA. Translation: CAM27084.1 .
    BC008549 mRNA. Translation: AAH08549.1 .
    BC093512 mRNA. Translation: AAH93512.1 .
    CCDSi CCDS25742.1.
    PIRi A34930. ISMSSS.
    RefSeqi NP_035162.1. NM_011032.2.
    UniGenei Mm.16660.

    3D structure databases

    ProteinModelPortali P09103.
    SMRi P09103. Positions 18-480.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202008. 1 interaction.
    IntActi P09103. 12 interactions.
    MINTi MINT-4122712.
    STRINGi 10090.ENSMUSP00000026122.

    PTM databases

    PhosphoSitei P09103.

    2D gel databases

    COMPLUYEAST-2DPAGE P09103.
    REPRODUCTION-2DPAGE P09103.
    SWISS-2DPAGE P09103.

    Proteomic databases

    MaxQBi P09103.
    PaxDbi P09103.
    PRIDEi P09103.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000026122 ; ENSMUSP00000026122 ; ENSMUSG00000025130 .
    GeneIDi 18453.
    KEGGi mmu:18453.
    UCSCi uc007mti.1. mouse.

    Organism-specific databases

    CTDi 5034.
    MGIi MGI:97464. P4hb.

    Phylogenomic databases

    eggNOGi COG0526.
    GeneTreei ENSGT00740000115202.
    HOGENOMi HOG000162459.
    HOVERGENi HBG005920.
    InParanoidi Q922C8.
    KOi K09580.
    OMAi YRDHENI.
    OrthoDBi EOG7VHSX1.
    TreeFami TF106381.

    Enzyme and pathway databases

    Reactomei REACT_189141. Detoxification of Reactive Oxygen Species.
    REACT_198984. Collagen biosynthesis and modifying enzymes.
    REACT_216017. Chylomicron-mediated lipid transport.

    Miscellaneous databases

    ChiTaRSi P4HB. mouse.
    NextBioi 294144.
    PROi P09103.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09103.
    Bgeei P09103.
    CleanExi MM_P4HB.
    Genevestigatori P09103.

    Family and domain databases

    Gene3Di 3.40.30.10. 4 hits.
    InterProi IPR005788. Disulphide_isomerase.
    IPR005792. Prot_disulphide_isomerase.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    Pfami PF00085. Thioredoxin. 2 hits.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 4 hits.
    TIGRFAMsi TIGR01130. ER_PDI_fam. 1 hit.
    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. "Nucleotide sequence of a full-length cDNA clone encoding a mouse cellular thyroid hormone binding protein (p55) that is homologous to protein disulfide isomerase and the beta-subunit of prolyl-4-hydroxylase."
      Gong Q.-H., Fukuda T., Parkison C., Cheng S.-Y.
      Nucleic Acids Res. 16:1203-1203(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "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].
    3. "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, DBA/2 and NOD.
      Tissue: Bone marrow and Stomach.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. "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 and FVB/N.
      Tissue: Liver and Mammary tumor.
    6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-224 AND LYS-273, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast and Liver.

    Entry informationi

    Entry nameiPDIA1_MOUSE
    AccessioniPrimary (citable) accession number: P09103
    Secondary accession number(s): Q922C8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 147 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3