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P59769

- GRP78_ASPAW

UniProt

P59769 - GRP78_ASPAW

Protein

78 kDa glucose-regulated protein homolog

Gene

bipA

Organism
Aspergillus awamori (Black koji mold)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (11 Jul 2003)
      Previous versions | rss
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    Functioni

    Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.By similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB

    GO - Biological processi

    1. response to unfolded protein Source: UniProtKB

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    78 kDa glucose-regulated protein homolog
    Short name:
    GRP-78
    Alternative name(s):
    Immunoglobulin heavy chain-binding protein homolog
    Short name:
    BiP
    Gene namesi
    Name:bipA
    Synonyms:bip
    OrganismiAspergillus awamori (Black koji mold)
    Taxonomic identifieri105351 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    Subcellular locationi

    Endoplasmic reticulum lumen PROSITE-ProRule annotation

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3838Sequence AnalysisAdd
    BLAST
    Chaini39 – 67263478 kDa glucose-regulated protein homologPRO_0000013577Add
    BLAST

    Proteomic databases

    PRIDEiP59769.

    Expressioni

    Inductioni

    By heat shock and tunicamycin. Not induced by carbon source starvation.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliP59769.
    SMRiP59769. Positions 49-589.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi669 – 6724Prevents secretion from ERPROSITE-ProRule annotation

    Sequence similaritiesi

    Belongs to the heat shock protein 70 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di1.20.1270.10. 1 hit.
    2.60.34.10. 1 hit.
    InterProiIPR018181. Heat_shock_70_CS.
    IPR029048. HSP70_C.
    IPR029047. HSP70_peptide-bd.
    IPR013126. Hsp_70_fam.
    [Graphical view]
    PfamiPF00012. HSP70. 1 hit.
    [Graphical view]
    PRINTSiPR00301. HEATSHOCK70.
    SUPFAMiSSF100920. SSF100920. 1 hit.
    SSF100934. SSF100934. 1 hit.
    PROSITEiPS00014. ER_TARGET. 1 hit.
    PS00297. HSP70_1. 1 hit.
    PS00329. HSP70_2. 1 hit.
    PS01036. HSP70_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P59769-1 [UniParc]FASTAAdd to Basket

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    MARISHQGAA KPFTAWTTIF YLLLVFIAPL AFFGTAHAQD ETSPQESYGT    50
    VIGIDLGTTY SCVGVMQNGK VEILVNDQGN RITPSYVAFT DEERLVGDAA 100
    KNQYAANPRR TIFDIKRLIG RKFDDKDVQK DAKHFPYKVV NKDGKPHVKV 150
    DVNQTPKTLT PEEVSAMVLG KMKEIAEGYL GKKVTHAVVT VPAYFNDAQR 200
    QATKDAGTIA GLNVLRVVNE PTAAAIAYGL DKTGDERQVI VYDLGGGTFD 250
    VSLLSIDNGV FEVLATAGDT HLGGEDFDQR VMDHFVKLYN KKNNVDVTKD 300
    LKAMGKLKRE VEKAKRTLSS QMSTRIEIEA FHNGEDFSET LTRAKFEELN 350
    MDLFKKTLKP VEQVLKDAKV KKSEVDDIVL VGGSTRIPKV QALLEEFFGG 400
    KKASKGINPD EAVAFGAAVQ GGVLSGEEGT GDVVLMDVNP LTLGIETTGG 450
    VMTKLIPRNT VIPTRKSQIF STAADNQPTV LIQVYEGERS LTKDNNLLGK 500
    FELTGIPPAP RGVPQIEVSF DLDANGILKV HASDKGTGKA ESITITNDKG 550
    RLSQEEIDRM VAEAEEFAEE DKAIKAKIEA RNTLENYAFS LKNQVNDENG 600
    LGGQIDEDDK QTILDAVKEV TEWLEDNAAT ATTEDFEEQK EQLSNVAYPI 650
    TSKLYGSAPA DEDDEPSGHD EL 672
    Length:672
    Mass (Da):73,459
    Last modified:July 11, 2003 - v1
    Checksum:iC701807FCE08C175
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti316 – 3161R → G in CAA73106. (PubMed:9294262)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08867 Genomic DNA. Translation: CAA70090.1.
    Y12504 Genomic DNA. Translation: CAA73106.1.
    PIRiT43723.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08867 Genomic DNA. Translation: CAA70090.1 .
    Y12504 Genomic DNA. Translation: CAA73106.1 .
    PIRi T43723.

    3D structure databases

    ProteinModelPortali P59769.
    SMRi P59769. Positions 49-589.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P59769.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 1.20.1270.10. 1 hit.
    2.60.34.10. 1 hit.
    InterProi IPR018181. Heat_shock_70_CS.
    IPR029048. HSP70_C.
    IPR029047. HSP70_peptide-bd.
    IPR013126. Hsp_70_fam.
    [Graphical view ]
    Pfami PF00012. HSP70. 1 hit.
    [Graphical view ]
    PRINTSi PR00301. HEATSHOCK70.
    SUPFAMi SSF100920. SSF100920. 1 hit.
    SSF100934. SSF100934. 1 hit.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    PS00297. HSP70_1. 1 hit.
    PS00329. HSP70_2. 1 hit.
    PS01036. HSP70_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The ER chaperone encoding bipA gene of black Aspergilli is induced by heat shock and unfolded proteins."
      van Gemeren I.A., Punt P.J., Drint-Kuyvenhoven A., Broekhuijsen M.P., van't Hoog A., Beijersbergen A., Verrips C.T., van den Hondel C.A.M.J.J.
      Gene 198:43-52(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
      Strain: ATCC 11358 / K-6615 / CBS 115.52.
    2. "Characterization of the bip gene of Aspergillus awamori encoding a protein with an HDEL retention signal homologous to the mammalian BiP involved in polypeptide secretion."
      Hijarrubia M.J., Casqueiro J., Gutierrez S., Fernandez F.J., Martin J.F.
      Curr. Genet. 32:139-146(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 22342 / NRRL 3112.

    Entry informationi

    Entry nameiGRP78_ASPAW
    AccessioniPrimary (citable) accession number: P59769
    Secondary accession number(s): O13280, O14453
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2003
    Last sequence update: July 11, 2003
    Last modified: October 1, 2014
    This is version 51 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3