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P07823

- GRP78_MESAU

UniProt

P07823 - GRP78_MESAU

Protein

78 kDa glucose-regulated protein

Gene

HSPA5

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      Previous versions | rss
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    Functioni

    Probably plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei96 – 961ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi36 – 394ATPBy similarity
    Nucleotide bindingi227 – 2293ATPBy similarity
    Nucleotide bindingi293 – 3008ATPBy similarity
    Nucleotide bindingi364 – 3674ATPBy similarity

    GO - Molecular functioni

    1. ATPase activity Source: UniProtKB
    2. ATP binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. protein domain specific binding Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. maintenance of protein localization in endoplasmic reticulum Source: UniProtKB
    3. positive regulation of cell migration Source: UniProtKB

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    78 kDa glucose-regulated protein
    Short name:
    GRP-78
    Alternative name(s):
    Heat shock 70 kDa protein 5
    Immunoglobulin heavy chain-binding protein
    Short name:
    BiP
    Gene namesi
    Name:HSPA5
    Synonyms:GRP78
    OrganismiMesocricetus auratus (Golden hamster)
    Taxonomic identifieri10036 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

    Subcellular locationi

    Endoplasmic reticulum lumen PROSITE-ProRule annotation. Melanosome By similarity. Cytoplasm By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    2. intracellular membrane-bounded organelle Source: UniProtKB
    3. melanosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Add
    BLAST
    Chaini19 – 65463678 kDa glucose-regulated proteinPRO_0000013567Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei125 – 1251N6-acetyllysineBy similarity
    Modified residuei160 – 1601Nitrated tyrosineBy similarity
    Modified residuei213 – 2131N6-acetyllysineBy similarity
    Modified residuei326 – 3261N6-acetyllysineBy similarity
    Modified residuei353 – 3531N6-acetyllysineBy similarity
    Modified residuei447 – 4471N6-succinyllysineBy similarity
    Modified residuei518 – 5181PhosphothreonineBy similarity
    Modified residuei585 – 5851N6,N6,N6-trimethyllysine; by METTL21A; in vitroBy similarity
    Modified residuei649 – 6491PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Methylation, Nitration, Phosphoprotein

    Proteomic databases

    PRIDEiP07823.

    Expressioni

    Tissue specificityi

    Detected in the acrosome and principal piece of the caput epididymal spermatazoa, not detected in the cauda epididymal spermatazoa (at protein level).1 Publication

    Interactioni

    Subunit structurei

    Interacts with DNAJC1 (via J domain) By similarity. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. 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. Interacts with TMEM132A and TRIM21. May form a complex with ERLEC1, OS9, SEL1L and SYVN1 By similarity. Interacts with MX1. Interacts with METTL23 and DNAJC10. Interacts with CEMIP; the interaction induces calcium leakage from the endoplamic reticulum and cell migration By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P279583EBI-371776,EBI-6904269From a different organism.

    Protein-protein interaction databases

    DIPiDIP-29677N.
    IntActiP07823. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP07823.
    SMRiP07823. Positions 28-570.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi651 – 6544Prevents secretion from ER

    Sequence similaritiesi

    Belongs to the heat shock protein 70 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG051845.

    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.

    P07823-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKFPMVAAAL LLLCAVRAEE EDKKEDVGTV VGIDLGTTYS CVGVFKNGRV    50
    EIIANDQGNR ITPSYVAFTP EGERLIGDAA KNQLTSNPEN TVFDAKRLIG 100
    RTWNDPSVQQ DIKFLPFKVV EKKTKPYIQV DIGGGQTKTF APEEISAMVL 150
    TKMKETAEAY LGKKVTHAVV TVPAYFNDAQ RQATKDAGTI AGLNVMRIIN 200
    EPTAAAIAYG LDKREGEKNI LVFDLGGGTF DVSLLTIDNG VFEVVATNGD 250
    THLGGEDFDQ RVMEHFIKLY KKKTGKDVRK DNRAVQKLRR EVEKAKRALS 300
    SQHQARIEIE SFFEGEDFSE TLTRAKFEEL NMDLFRSTMK PVQKVLEDSD 350
    LKKSDIDEIV LVGGSTRIPK IQQLVKEFFN GKEPSRGINP DEAVAYGAAV 400
    QAGVLSGDQD TGDLVLLDVC PLTLGIETVG GVMTKLIPRN TVVPTKKSQI 450
    FSTASDNQPT VTIKVYEGER PLTKDNHLLG TFDLTGIPPA PRGVPQIEVT 500
    FEIDVNGILR VTAEDKGTGN KNKITITNDQ NRLTPEEIER MVNDAEKFAE 550
    EDKKLKERID TRNELESYAY SLKNQIGDKE KLGGKLSSED KETMEKAVEE 600
    KIEWLESHQD ADIEDFKAKK KELEEIVQPI ISKLYGSAGP PPTGEEDTSE 650
    KDEL 654
    Length:654
    Mass (Da):72,379
    Last modified:August 1, 1988 - v1
    Checksum:i25CF665F59113A49
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17169 mRNA. Translation: AAA51448.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17169 mRNA. Translation: AAA51448.1 .

    3D structure databases

    ProteinModelPortali P07823.
    SMRi P07823. Positions 28-570.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-29677N.
    IntActi P07823. 2 interactions.

    Proteomic databases

    PRIDEi P07823.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG051845.

    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 nucleotide sequence encoding the hamster 78-kDa glucose-regulated protein (GRP78) and its conservation between hamster and rat."
      Ting J., Wooden S.K., Kriz R., Kelleher K., Kaufman R.J., Lee A.S.
      Gene 55:147-152(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa."
      Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.
      Asian J. Androl. 12:344-355(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiGRP78_MESAU
    AccessioniPrimary (citable) accession number: P07823
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 105 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3