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P07237

- PDIA1_HUMAN

UniProt

P07237 - PDIA1_HUMAN

Protein

Protein disulfide-isomerase

Gene

P4HB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 195 (01 Oct 2014)
      Sequence version 3 (01 Nov 1997)
      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.2 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei53 – 531Nucleophile
    Sitei54 – 541Contributes to redox potential value
    Sitei55 – 551Contributes to redox potential value
    Active sitei56 – 561Nucleophile
    Sitei120 – 1201Lowers pKa of C-terminal Cys of first active site
    Active sitei397 – 3971NucleophileBy similarity
    Sitei398 – 3981Contributes to redox potential valueBy similarity
    Sitei399 – 3991Contributes to redox potential valueBy similarity
    Active sitei400 – 4001NucleophileBy similarity
    Sitei461 – 4611Lowers pKa of C-terminal Cys of second active siteBy similarity

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. procollagen-proline 4-dioxygenase activity Source: ProtInc
    3. protein binding Source: IntAct
    4. protein disulfide isomerase activity Source: RefGenome

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. cellular response to hypoxia Source: BHF-UCL
    3. extracellular matrix organization Source: Reactome
    4. lipoprotein metabolic process Source: Reactome
    5. peptidyl-proline hydroxylation to 4-hydroxy-L-proline Source: MGI
    6. protein folding Source: RefGenome
    7. regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: BHF-UCL
    8. response to endoplasmic reticulum stress Source: BHF-UCL
    9. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Chaperone, Isomerase

    Enzyme and pathway databases

    BRENDAi5.3.4.1. 2681.
    ReactomeiREACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_172715. Detoxification of Reactive Oxygen Species.
    REACT_6841. 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
    Prolyl 4-hydroxylase subunit beta
    p55
    Gene namesi
    Name:P4HB
    Synonyms:ERBA2L, PDI, PDIA1, PO4DB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:8548. P4HB.

    Subcellular locationi

    Endoplasmic reticulum lumen. Melanosome. 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 Probable. Localizes near CD4-enriched regions on lymphoid cell surfaces. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.Curated

    GO - Cellular componenti

    1. endoplasmic reticulum Source: BHF-UCL
    2. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
    3. endoplasmic reticulum lumen Source: Reactome
    4. extracellular region Source: UniProtKB
    5. extracellular vesicular exosome Source: UniProt
    6. melanosome Source: UniProtKB-SubCell
    7. plasma membrane Source: UniProtKB-SubCell
    8. procollagen-proline 4-dioxygenase complex Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA32876.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 17174 PublicationsAdd
    BLAST
    Chaini18 – 508491Protein disulfide-isomerasePRO_0000034195Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi53 ↔ 56Redox-active1 PublicationPROSITE-ProRule annotation
    Modified residuei200 – 2001N6-acetyllysineBy similarity
    Modified residuei222 – 2221N6-succinyllysineBy similarity
    Modified residuei271 – 2711N6-succinyllysineBy similarity
    Disulfide bondi397 ↔ 400Redox-activePROSITE-ProRule annotation

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    MaxQBiP07237.
    PaxDbiP07237.
    PeptideAtlasiP07237.
    PRIDEiP07237.

    2D gel databases

    DOSAC-COBS-2DPAGEP07237.
    OGPiP07237.
    REPRODUCTION-2DPAGEIPI00010796.
    P07237.
    SWISS-2DPAGEP07237.

    PTM databases

    PhosphoSiteiP07237.

    Miscellaneous databases

    PMAP-CutDBP07237.

    Expressioni

    Gene expression databases

    ArrayExpressiP07237.
    BgeeiP07237.
    CleanExiHS_P4HB.
    GenevestigatoriP07237.

    Organism-specific databases

    HPAiCAB012463.
    HPA018884.

    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 By similarity. Binds UBQLN1. Binds to CD4, and upon HIV-1 binding to the cell membrane, is part of a P4HB/PDI-CD4-CXCR4-gp120 complex.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ERO1LQ96HE72EBI-395883,EBI-2564539
    HM13Q8TCT93EBI-395883,EBI-347472
    PRDX4Q131622EBI-395883,EBI-2211957
    TAP1Q035184EBI-395883,EBI-747259

    Protein-protein interaction databases

    BioGridi111073. 75 interactions.
    IntActiP07237. 34 interactions.
    MINTiMINT-4999403.
    STRINGi9606.ENSP00000327801.

    Structurei

    Secondary structure

    1
    508
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi21 – 233
    Beta strandi26 – 283
    Turni31 – 333
    Helixi34 – 407
    Beta strandi42 – 498
    Helixi54 – 7219
    Beta strandi78 – 836
    Turni84 – 863
    Helixi88 – 936
    Beta strandi101 – 1066
    Beta strandi110 – 1123
    Beta strandi114 – 1163
    Helixi122 – 13211
    Beta strandi137 – 1393
    Helixi143 – 1519
    Beta strandi153 – 1608
    Turni162 – 1654
    Helixi167 – 17812
    Beta strandi180 – 1823
    Beta strandi184 – 1874
    Helixi190 – 1956
    Beta strandi199 – 20911
    Beta strandi212 – 2154
    Helixi222 – 23211
    Beta strandi237 – 2393
    Turni242 – 2443
    Helixi245 – 2495
    Beta strandi250 – 2523
    Beta strandi255 – 2606
    Beta strandi265 – 2673
    Helixi268 – 28013
    Turni281 – 2855
    Beta strandi287 – 2915
    Helixi296 – 2983
    Helixi299 – 3046
    Helixi309 – 3113
    Beta strandi313 – 3197
    Beta strandi321 – 3233
    Beta strandi325 – 3273
    Beta strandi330 – 3323
    Helixi336 – 34712
    Beta strandi353 – 3553
    Helixi362 – 3643
    Beta strandi367 – 3726
    Turni374 – 3763
    Helixi377 – 3815
    Beta strandi387 – 3937
    Helixi398 – 41316
    Turni414 – 4163
    Beta strandi418 – 4269
    Turni427 – 4293
    Beta strandi439 – 4468
    Beta strandi448 – 4514
    Helixi463 – 4708
    Turni471 – 4733

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BJXNMR-A136-245[»]
    1MEKNMR-A18-137[»]
    1X5CNMR-A368-475[»]
    2BJXNMR-A136-245[»]
    2K18NMR-A135-357[»]
    3BJ5X-ray2.20A230-368[»]
    3UEMX-ray2.29A137-479[»]
    4EKZX-ray2.51A18-479[»]
    4EL1X-ray2.88A/B18-479[»]
    4JU5X-ray2.28A/B135-367[»]
    ProteinModelPortaliP07237.
    SMRiP07237. Positions 17-478.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07237.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini18 – 134117Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini349 – 475127Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi505 – 5084Prevents 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.
    HOGENOMiHOG000162459.
    HOVERGENiHBG005920.
    InParanoidiP07237.
    KOiK09580.
    OMAiYRDHENI.
    OrthoDBiEOG7VHSX1.
    PhylomeDBiP07237.
    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.

    P07237-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRRALLCLA VAALVRADAP EEEDHVLVLR KSNFAEALAA HKYLLVEFYA    50
    PWCGHCKALA PEYAKAAGKL KAEGSEIRLA KVDATEESDL AQQYGVRGYP 100
    TIKFFRNGDT ASPKEYTAGR EADDIVNWLK KRTGPAATTL PDGAAAESLV 150
    ESSEVAVIGF FKDVESDSAK QFLQAAEAID DIPFGITSNS DVFSKYQLDK 200
    DGVVLFKKFD EGRNNFEGEV TKENLLDFIK HNQLPLVIEF TEQTAPKIFG 250
    GEIKTHILLF LPKSVSDYDG KLSNFKTAAE SFKGKILFIF IDSDHTDNQR 300
    ILEFFGLKKE ECPAVRLITL EEEMTKYKPE SEELTAERIT EFCHRFLEGK 350
    IKPHLMSQEL PEDWDKQPVK VLVGKNFEDV AFDEKKNVFV EFYAPWCGHC 400
    KQLAPIWDKL GETYKDHENI VIAKMDSTAN EVEAVKVHSF PTLKFFPASA 450
    DRTVIDYNGE RTLDGFKKFL ESGGQDGAGD DDDLEDLEEA EEPDMEEDDD 500
    QKAVKDEL 508
    Length:508
    Mass (Da):57,116
    Last modified:November 1, 1997 - v3
    Checksum:i906CE6D9900B8FCE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 112AV → PW in CAA28775. (PubMed:3034602)Curated
    Sequence conflicti21 – 211E → D AA sequence (PubMed:9399589)Curated
    Sequence conflicti24 – 241D → V AA sequence (PubMed:9399589)Curated
    Sequence conflicti44 – 452LL → PP in CAA28775. (PubMed:3034602)Curated
    Sequence conflicti49 – 491Y → H in CAA28775. (PubMed:3034602)Curated
    Sequence conflicti141 – 1411P → R in AAA61169. (PubMed:3611107)Curated
    Sequence conflicti360 – 3623LPE → RAG in AAA61169. (PubMed:3611107)Curated
    Sequence conflicti372 – 3721L → P in AAA61169. (PubMed:3611107)Curated
    Sequence conflicti439 – 4391S → G in CAA28775. (PubMed:3034602)Curated
    Sequence conflicti444 – 4441K → G in CAA28775. (PubMed:3034602)Curated
    Sequence conflicti460 – 4601E → Q in CAA30112. (PubMed:3342239)Curated
    Sequence conflicti481 – 4811D → V in CAA28775. (PubMed:3034602)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05130 mRNA. Translation: CAA28775.1.
    J02783 mRNA. Translation: AAA61169.1.
    M22806
    , M22803, M22804, M22805 Genomic DNA. Translation: AAC13652.1.
    AK315631 mRNA. Translation: BAG37999.1.
    CH471099 Genomic DNA. Translation: EAW89690.1.
    BC010859 mRNA. Translation: AAH10859.1.
    BC029617 mRNA. Translation: AAH29617.1.
    BC071892 mRNA. Translation: AAH71892.1.
    S37207 Genomic DNA. Translation: AAB22262.2.
    X07077 mRNA. Translation: CAA30112.1.
    CCDSiCCDS11787.1.
    PIRiA31913. ISHUSS.
    RefSeqiNP_000909.2. NM_000918.3.
    UniGeneiHs.464336.

    Genome annotation databases

    EnsembliENST00000331483; ENSP00000327801; ENSG00000185624.
    GeneIDi5034.
    KEGGihsa:5034.
    UCSCiuc002kbn.1. human.

    Polymorphism databases

    DMDMi2507460.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05130 mRNA. Translation: CAA28775.1 .
    J02783 mRNA. Translation: AAA61169.1 .
    M22806
    , M22803 , M22804 , M22805 Genomic DNA. Translation: AAC13652.1 .
    AK315631 mRNA. Translation: BAG37999.1 .
    CH471099 Genomic DNA. Translation: EAW89690.1 .
    BC010859 mRNA. Translation: AAH10859.1 .
    BC029617 mRNA. Translation: AAH29617.1 .
    BC071892 mRNA. Translation: AAH71892.1 .
    S37207 Genomic DNA. Translation: AAB22262.2 .
    X07077 mRNA. Translation: CAA30112.1 .
    CCDSi CCDS11787.1.
    PIRi A31913. ISHUSS.
    RefSeqi NP_000909.2. NM_000918.3.
    UniGenei Hs.464336.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BJX NMR - A 136-245 [» ]
    1MEK NMR - A 18-137 [» ]
    1X5C NMR - A 368-475 [» ]
    2BJX NMR - A 136-245 [» ]
    2K18 NMR - A 135-357 [» ]
    3BJ5 X-ray 2.20 A 230-368 [» ]
    3UEM X-ray 2.29 A 137-479 [» ]
    4EKZ X-ray 2.51 A 18-479 [» ]
    4EL1 X-ray 2.88 A/B 18-479 [» ]
    4JU5 X-ray 2.28 A/B 135-367 [» ]
    ProteinModelPortali P07237.
    SMRi P07237. Positions 17-478.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111073. 75 interactions.
    IntActi P07237. 34 interactions.
    MINTi MINT-4999403.
    STRINGi 9606.ENSP00000327801.

    Chemistry

    BindingDBi P07237.
    ChEMBLi CHEMBL2364681.

    PTM databases

    PhosphoSitei P07237.

    Polymorphism databases

    DMDMi 2507460.

    2D gel databases

    DOSAC-COBS-2DPAGE P07237.
    OGPi P07237.
    REPRODUCTION-2DPAGE IPI00010796.
    P07237.
    SWISS-2DPAGE P07237.

    Proteomic databases

    MaxQBi P07237.
    PaxDbi P07237.
    PeptideAtlasi P07237.
    PRIDEi P07237.

    Protocols and materials databases

    DNASUi 5034.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000331483 ; ENSP00000327801 ; ENSG00000185624 .
    GeneIDi 5034.
    KEGGi hsa:5034.
    UCSCi uc002kbn.1. human.

    Organism-specific databases

    CTDi 5034.
    GeneCardsi GC17M079801.
    HGNCi HGNC:8548. P4HB.
    HPAi CAB012463.
    HPA018884.
    MIMi 176790. gene.
    neXtProti NX_P07237.
    PharmGKBi PA32876.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0526.
    HOGENOMi HOG000162459.
    HOVERGENi HBG005920.
    InParanoidi P07237.
    KOi K09580.
    OMAi YRDHENI.
    OrthoDBi EOG7VHSX1.
    PhylomeDBi P07237.
    TreeFami TF106381.

    Enzyme and pathway databases

    BRENDAi 5.3.4.1. 2681.
    Reactomei REACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_172715. Detoxification of Reactive Oxygen Species.
    REACT_6841. Chylomicron-mediated lipid transport.

    Miscellaneous databases

    ChiTaRSi P4HB. human.
    EvolutionaryTracei P07237.
    GeneWikii P4HB.
    GenomeRNAii 5034.
    NextBioi 19398.
    PMAP-CutDB P07237.
    PROi P07237.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07237.
    Bgeei P07237.
    CleanExi HS_P4HB.
    Genevestigatori P07237.

    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. "Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene."
      Pihlajaniemi T., Helaakoski T., Tasanen K., Myllylae R., Huhtala M.-L., Koivu J., Kivirikko K.I.
      EMBO J. 6:643-649(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum."
      Cheng S.-Y., Gong Q.-H., Parkison C., Robinson E.A., Appella E., Merlino G.T., Pastan I.
      J. Biol. Chem. 262:11221-11227(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Characterization of the human gene for a polypeptide that acts both as the beta subunit of prolyl 4-hydroxylase and as protein disulfide isomerase."
      Tasanen K., Parkkonen T., Chow L.T., Kivirikko K.I., Pihlajaniemi T.
      J. Biol. Chem. 263:16218-16224(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Blood.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Synovium.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Tissue: Colon, Lung and Skin.
    7. "Promoter of the gene for the multifunctional protein disulfide isomerase polypeptide. Functional significance of the six CCAAT boxes and other promoter elements."
      Tasanen K., Oikarinen J., Kivirikko K.I., Pihlajaniemi T.
      J. Biol. Chem. 267:11513-11519(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
    8. "A two-dimensional gel database of human colon carcinoma proteins."
      Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.
      Electrophoresis 18:605-613(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 18-41.
      Tissue: Colon carcinoma.
    9. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 18-30.
      Tissue: Platelet.
    10. Frutiger S., Hughes G.J.
      Submitted (FEB-1996) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 18-29.
      Tissue: Liver.
    11. "Development of a database of amino acid sequences for human colon carcinoma proteins separated by two-dimensional polyacrylamide gel electrophoresis."
      Ward L.D., Hong J., Whitehead R.H., Simpson R.J.
      Electrophoresis 11:883-891(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 18-26.
    12. "Human liver protein map: a reference database established by microsequencing and gel comparison."
      Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
      Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY PROTEIN SEQUENCE OF 19-28.
      Tissue: Liver.
    13. "Functions of characteristic Cys-Gly-His-Cys (CGHC) and Gln-Glu-Asp-Leu (QEDL) motifs of microsomal ER-60 protease."
      Urade R., Oda T., Ito H., Moriyama T., Utsumi S., Kito M.
      J. Biochem. 122:834-842(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-28.
    14. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 201-207; 223-230; 286-308 AND 402-409, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    15. "Characterization of a cDNA for human glutathione-insulin transhydrogenase (protein-disulfide isomerase/oxidoreductase)."
      Morris J.I., Varandani P.T.
      Biochim. Biophys. Acta 949:169-180(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 293-508.
    16. "Two-dimensional gel electrophoresis, protein electroblotting and microsequencing: a direct link between proteins and genes."
      Bauw G., Rasmussen H.H., van den Bulcke M., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
      Electrophoresis 11:528-536(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 317-325; 350-369 AND 401-419.
    17. "Protein-disulfide isomerase (PDI) in FRTL5 cells. pH-dependent thyroglobulin/PDI interactions determine a novel PDI function in the post-endoplasmic reticulum of thyrocytes."
      Mezghrani A., Courageot J., Mani J.-C., Pugniere M., Bastiani P., Miquelis R.
      J. Biol. Chem. 275:1920-1929(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    18. "The catalytic activity of protein disulfide isomerase is involved in human immunodeficiency virus envelope-mediated membrane fusion after CD4 cell binding."
      Fenouillet E., Barbouche R., Courageot J., Miquelis R.
      J. Infect. Dis. 183:744-752(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS, SUBCELLULAR LOCATION.
    19. "Is protein disulfide isomerase a redox-dependent molecular chaperone?"
      Lumb R.A., Bulleid N.J.
      EMBO J. 21:6763-6770(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death."
      Ko H.S., Uehara T., Nomura Y.
      J. Biol. Chem. 277:35386-35392(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBQLN1.
    21. "Inhibitors of protein-disulfide isomerase prevent cleavage of disulfide bonds in receptor-bound glycoprotein 120 and prevent HIV-1 entry."
      Gallina A., Hanley T.M., Mandel R., Trahey M., Broder C.C., Viglianti G.A., Ryser H.J.
      J. Biol. Chem. 277:50579-50588(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS.
    22. "Protein-disulfide isomerase-mediated reduction of two disulfide bonds of HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is required for fusion."
      Barbouche R., Miquelis R., Jones I.M., Fenouillet E.
      J. Biol. Chem. 278:3131-3136(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS.
    23. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    24. Cited for: REVIEW.
    25. "Thiol/disulfide exchange is a prerequisite for CXCR4-tropic HIV-1 envelope-mediated T-cell fusion during viral entry."
      Markovic I., Stantchev T.S., Fields K.H., Tiffany L.J., Tomic M., Weiss C.D., Broder C.C., Strebel K., Clouse K.A.
      Blood 103:1586-1594(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS.
    26. "Glycosaminoglycans and protein disulfide isomerase-mediated reduction of HIV Env."
      Barbouche R., Lortat-Jacob H., Jones I.M., Fenouillet E.
      Mol. Pharmacol. 67:1111-1118(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS.
    27. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase."
      Kemmink J., Darby N.J., Dijkstra K., Scheek R.M., Creighton T.E.
      Protein Sci. 4:2587-2593(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 18-137.
    30. "Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy."
      Kemmink J., Darby N.J., Dijkstra K., Nilges M., Creighton T.E.
      Biochemistry 35:7684-7691(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 18-137, DISULFIDE BOND.
    31. "The structure in solution of the B domain of protein disulfide isomerase."
      Kemmink J., Dijkstra K., Mariani M., Scheek R.M., Penka E., Nilges M., Darby N.J.
      J. Biomol. NMR 13:357-368(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 136-245.
    32. "The solution structure of the second thioredoxin-like domain of human protein disulfide-isomerase."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 368-477.

    Entry informationi

    Entry nameiPDIA1_HUMAN
    AccessioniPrimary (citable) accession number: P07237
    Secondary accession number(s): B2RDQ2
    , P30037, P32079, Q15205, Q6LDE5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 195 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Reduces and may activate fusogenic properties of HIV-1 gp120 surface protein, thereby enabling HIV-1 entry into the cell.

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3