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P38659

- PDIA4_RAT

UniProt

P38659 - PDIA4_RAT

Protein

Protein disulfide-isomerase A4

Gene

Pdia4

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (25 Oct 2005)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein disulfide isomerase activity Source: UniProt

    GO - Biological processi

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

    Keywords - Molecular functioni

    Isomerase

    Keywords - Ligandi

    Calcium

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein disulfide-isomerase A4 (EC:5.3.4.1)
    Alternative name(s):
    Calcium-binding protein 2
    Short name:
    CaBP2
    Endoplasmic reticulum resident protein 70
    Short name:
    ER protein 70
    Short name:
    ERp70
    Endoplasmic reticulum resident protein 72
    Short name:
    ER protein 72
    Short name:
    ERp-72
    Short name:
    ERp72
    Gene namesi
    Name:Pdia4
    Synonyms:Cabp2, Erp70
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi619835. Pdia4.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    2. melanosome Source: UniProtKB-SubCell
    3. smooth endoplasmic reticulum Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 643623Protein disulfide-isomerase A4PRO_0000034231Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi89 ↔ 92Redox-activePROSITE-ProRule annotation
    Disulfide bondi204 ↔ 207Redox-activePROSITE-ProRule annotation
    Modified residuei364 – 3641N6-acetyllysineBy similarity
    Disulfide bondi553 ↔ 556Redox-activePROSITE-ProRule annotation

    Post-translational modificationi

    O-glycosylated.

    Keywords - PTMi

    Acetylation, Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP38659.
    PRIDEiP38659.

    Expressioni

    Inductioni

    Upon glucose starvation, as well as treatment with tunicamycin.

    Gene expression databases

    GenevestigatoriP38659.

    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.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Dmel_CG7484Q9VVJ72EBI-917435,EBI-128899From a different organism.
    PpibP243682EBI-917435,EBI-916926
    TgP068823EBI-917435,EBI-1549657

    Protein-protein interaction databases

    BioGridi250512. 5 interactions.
    IntActiP38659. 10 interactions.
    MINTiMINT-4565672.
    STRINGi10116.ENSRNOP00000008728.

    Structurei

    Secondary structure

    1
    643
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi284 – 2874
    Helixi291 – 30010
    Beta strandi305 – 3095
    Helixi316 – 32813
    Turni329 – 3313
    Beta strandi334 – 3374
    Helixi340 – 3467
    Beta strandi350 – 3567
    Helixi359 – 3613
    Beta strandi370 – 3734
    Helixi380 – 39011
    Beta strandi395 – 3984
    Turni400 – 4023
    Helixi403 – 4064
    Beta strandi409 – 4179
    Turni423 – 4253
    Helixi426 – 44015
    Beta strandi446 – 4527
    Turni453 – 4564
    Helixi457 – 4626
    Beta strandi473 – 4775
    Beta strandi483 – 4853
    Helixi493 – 50412

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EC3X-ray1.92A/B283-523[»]
    ProteinModelPortaliP38659.
    SMRiP38659. Positions 54-282, 521-643.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP38659.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 167147Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini167 – 299133Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini503 – 634132Thioredoxin 3PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi640 – 6434Prevents secretion from ER

    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.
    HOGENOMiHOG000162459.
    HOVERGENiHBG005920.
    InParanoidiP38659.
    KOiK09582.
    PhylomeDBiP38659.

    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.

    P38659-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLRKAWLLV LLLALTQLLA AASAEDAHED ASDSENPIED DDDEEEDEED    50
    EDDLEVKEEN GVWVLNDENF DNFVADKDTV LLEFYAPWCG HCKQFAPEYE 100
    KIASTLKDND PPIAVAKIDA TSASMLASKF DVSGYPTIKI LKKGQAVDYD 150
    GSRTQEEIVA KVREVSQPDW TPPPEVTLTL TKENFDDVVN NADIILVEFY 200
    APWCGHCKKL APEYEKAAKE LSKRSPPIPL AKVDATEQTD LAKRFDVSGY 250
    PTLKIFRKGR PFDYNGPREK YGIVDYMVEQ SGPPSKEILT LKQVQEFLKD 300
    GDDVVILGVF QGVGDPGYLQ YQDAANTLRE DYKFHHTFST EIAKFLKVSL 350
    GKLVLMQPEK FQSKYEPRMH VMDVQGSTEA SAIKDYVVKH ALPLVGHRKT 400
    SNDAKRYSKR PLVVVYYSVD FSFDYRTATQ FWRNKVLEVA KDFPEYTFAI 450
    ADEEDYATEV KDLGLSESGE DVNAAILDES GKKFAMEPEE FDSDALQEFV 500
    MAFKKGKLKP VIKSQPVPKN NKGPVRVVVG KTFDAIVMDP KKDVLIEFYA 550
    PWCGHCKQLE PVYTSLGKKY KGQKDLVIAK MDATANDITN DRYKVEGFPT 600
    IYFAPSGDKK NPIKFEGGNR DLEHLSKFID EHATKRSRTK EEL 643
    Length:643
    Mass (Da):72,720
    Last modified:October 25, 2005 - v2
    Checksum:iC5BC8536834543ED
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti43 – 431D → E in AAA19217. (PubMed:8477750)Curated
    Sequence conflicti391 – 3911A → D in AAA19217. (PubMed:8477750)Curated
    Sequence conflicti497 – 4971Q → R in AAA19217. (PubMed:8477750)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86870 mRNA. Translation: AAA19217.1.
    BC061535 mRNA. Translation: AAH61535.1.
    PIRiS32476.
    RefSeqiNP_446301.1. NM_053849.1.
    UniGeneiRn.39305.

    Genome annotation databases

    GeneIDi116598.
    KEGGirno:116598.
    UCSCiRGD:619835. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86870 mRNA. Translation: AAA19217.1 .
    BC061535 mRNA. Translation: AAH61535.1 .
    PIRi S32476.
    RefSeqi NP_446301.1. NM_053849.1.
    UniGenei Rn.39305.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3EC3 X-ray 1.92 A/B 283-523 [» ]
    ProteinModelPortali P38659.
    SMRi P38659. Positions 54-282, 521-643.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 250512. 5 interactions.
    IntActi P38659. 10 interactions.
    MINTi MINT-4565672.
    STRINGi 10116.ENSRNOP00000008728.

    Proteomic databases

    PaxDbi P38659.
    PRIDEi P38659.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 116598.
    KEGGi rno:116598.
    UCSCi RGD:619835. rat.

    Organism-specific databases

    CTDi 9601.
    RGDi 619835. Pdia4.

    Phylogenomic databases

    eggNOGi COG0526.
    HOGENOMi HOG000162459.
    HOVERGENi HBG005920.
    InParanoidi P38659.
    KOi K09582.
    PhylomeDBi P38659.

    Miscellaneous databases

    EvolutionaryTracei P38659.
    NextBioi 619299.

    Gene expression databases

    Genevestigatori P38659.

    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. "CaBP2 is a rat homolog of ERp72 with proteindisulfide isomerase activity."
      Van P.N., Rupp K., Lampen A., Soeling H.-D.
      Eur. J. Biochem. 213:789-795(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Wistar.
      Tissue: Liver.
    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].
      Tissue: Pituitary.
    3. "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.

    Entry informationi

    Entry nameiPDIA4_RAT
    AccessioniPrimary (citable) accession number: P38659
    Secondary accession number(s): Q6P7S5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: October 25, 2005
    Last modified: October 1, 2014
    This is version 129 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3