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P06761 (GRP78_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Steroidogenesis-activator polypeptide
Gene names
Name:Hspa5
Synonyms:Grp78
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length654 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

May form a complex with ERLEC1, OS9, SEL1L and SYVN1 By similarity. Interacts with DNAJC1 (via J domain). Interacts with TRIM21 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. 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. Ref.7

Subcellular location

Endoplasmic reticulum lumen. Melanosome By similarity. Cytoplasm By similarity.

Sequence similarities

Belongs to the heat shock protein 70 family.

Ontologies

Keywords
   Cellular componentCytoplasm
Endoplasmic reticulum
   DomainSignal
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
Methylation
Nitration
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processER overload response

Inferred from electronic annotation. Source: Ensembl

activation of signaling protein activity involved in unfolded protein response

Inferred from electronic annotation. Source: Ensembl

cellular response to antibiotic

Inferred from expression pattern PubMed 19332540. Source: RGD

cellular response to glucose starvation

Inferred from electronic annotation. Source: Ensembl

cellular response to interleukin-4

Inferred from electronic annotation. Source: Ensembl

cerebellar Purkinje cell layer development

Inferred from electronic annotation. Source: Ensembl

cerebellum structural organization

Inferred from electronic annotation. Source: Ensembl

maintenance of protein localization in endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein ubiquitination

Inferred from electronic annotation. Source: Ensembl

proteolysis involved in cellular protein catabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentCOP9 signalosome

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from direct assay PubMed 19474315. Source: MGI

endoplasmic reticulum chaperone complex

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum-Golgi intermediate compartment

Inferred from electronic annotation. Source: Ensembl

integral component of endoplasmic reticulum membrane

Inferred from electronic annotation. Source: Ensembl

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

midbody

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from direct assay PubMed 20533907. Source: RGD

smooth endoplasmic reticulum

Inferred from direct assay PubMed 22665516. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ribosome binding

Inferred from electronic annotation. Source: Ensembl

unfolded protein binding

Inferred from physical interaction PubMed 11884402. Source: RGD

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Chain19 – 65463678 kDa glucose-regulated protein
PRO_0000013569

Regions

Nucleotide binding36 – 394ATP By similarity
Nucleotide binding227 – 2293ATP By similarity
Nucleotide binding293 – 3008ATP By similarity
Nucleotide binding364 – 3674ATP By similarity
Motif651 – 6544Prevents secretion from ER

Sites

Binding site961ATP By similarity

Amino acid modifications

Modified residue1251N6-acetyllysine By similarity
Modified residue1601Nitrated tyrosine By similarity
Modified residue2131N6-acetyllysine By similarity
Modified residue3261N6-acetyllysine By similarity
Modified residue3531N6-acetyllysine By similarity
Modified residue4471N6-succinyllysine By similarity
Modified residue5181Phosphothreonine By similarity
Modified residue5851N6,N6,N6-trimethyllysine; by METTL21A; in vitro By similarity
Modified residue6491Phosphoserine By similarity

Experimental info

Sequence conflict291T → M in AAA41277. Ref.3
Sequence conflict6491S → D AA sequence Ref.5
Sequence conflict6511K → KK AA sequence Ref.5

Sequences

Sequence LengthMass (Da)Tools
P06761 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 9D686C6484150108

FASTA65472,347
        10         20         30         40         50         60 
MKFTVVAAAL LLLCAVRAEE EDKKEDVGTV VGIDLGTTYS CVGVFKNGRV EIIANDQGNR 

        70         80         90        100        110        120 
ITPSYVAFTP EGERLIGDAA KNQLTSNPEN TVFDAKRLIG RTWNDPSVQQ DIKFLPFKVV 

       130        140        150        160        170        180 
EKKTKPYIQV DIGGGQTKTF APEEISAMVL TKMKETAEAY LGKKVTHAVV TVPAYFNDAQ 

       190        200        210        220        230        240 
RQATKDAGTI AGLNVMRIIN EPTAAAIAYG LDKREGEKNI LVFDLGGGTF DVSLLTIDNG 

       250        260        270        280        290        300 
VFEVVATNGD THLGGEDFDQ RVMEHFIKLY KKKTGKDVRK DNRAVQKLRR EVEKAKRALS 

       310        320        330        340        350        360 
SQHQARIEIE SFFEGEDFSE TLTRAKFEEL NMDLFRSTMK PVQKVLEDSD LKKSDIDEIV 

       370        380        390        400        410        420 
LVGGSTRIPK IQQLVKEFFN GKEPSRGINP DEAVAYGAAV QAGVLSGDQD TGDLVLLDVC 

       430        440        450        460        470        480 
PLTLGIETVG GVMTKLIPRN TVVPTKKSQI FSTASDNQPT VTIKVYEGER PLTKDNHLLG 

       490        500        510        520        530        540 
TFDLTGIPPA PRGVPQIEVT FEIDVNGILR VTAEDKGTGN KNKITITNDQ NRLTPEEIER 

       550        560        570        580        590        600 
MVNDAEKFAE EDKKLKERID TRNELESYAY SLKNQIGDKE KLGGKLSPED KETMEKAVEE 

       610        620        630        640        650 
KIEWLESHQD ADIEDFKAKK KELEEIVQPI ISKLYGSGGP PPTGEEDTSE KDEL 

« Hide

References

« Hide 'large scale' references
[1]"An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein."
Munro S., Pelham H.R.B.
Cell 46:291-300(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: Prostate.
[3]"Rat gene encoding the 78-kDa glucose-regulated protein GRP78: its regulatory sequences and the effect of protein glycosylation on its expression."
Chang S.C., Wooden S.K., Nakaki T., Kim Y.K., Lin A.Y., Kung L., Attenello J.W., Lee A.S.
Proc. Natl. Acad. Sci. U.S.A. 84:680-684(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
[4]Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 50-60; 165-181; 307-324; 475-492 AND 533-540, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain, Hippocampus and Spinal cord.
[5]"Steroidogenesis-activator polypeptide isolated from a rat Leydig cell tumor."
Pedersen R.C., Brownie A.C.
Science 236:188-190(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 626-654.
[6]"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.
[7]"Cloning and characterization of a novel GRP78-binding protein in the rat brain."
Oh-hashi K., Naruse Y., Amaya F., Shimosato G., Tanaka M.
J. Biol. Chem. 278:10531-10537(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TMEM132A.
Strain: Sprague-Dawley.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14050 mRNA. Translation: AAA40817.1.
BC062017 mRNA. Translation: AAH62017.1.
M14866 Genomic DNA. Translation: AAA41277.1.
PIRHHRTGB. A23948.
RefSeqNP_037215.1. NM_013083.2.
UniGeneRn.11088.

3D structure databases

ProteinModelPortalP06761.
SMRP06761. Positions 28-570.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247646. 8 interactions.
IntActP06761. 16 interactions.
MINTMINT-4575479.
STRING10116.ENSRNOP00000025064.

PTM databases

PhosphoSiteP06761.

Proteomic databases

PaxDbP06761.
PRIDEP06761.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000025067; ENSRNOP00000025064; ENSRNOG00000018294.
GeneID25617.
KEGGrno:25617.
UCSCRGD:2843. rat.

Organism-specific databases

CTD3309.
RGD2843. Hspa5.

Phylogenomic databases

eggNOGCOG0443.
GeneTreeENSGT00750000117237.
HOGENOMHOG000228135.
HOVERGENHBG051845.
InParanoidP06761.
KOK09490.
OMADKRAVQK.
OrthoDBEOG780RKX.
PhylomeDBP06761.
TreeFamTF105044.

Gene expression databases

GenevestigatorP06761.

Family and domain databases

InterProIPR018181. Heat_shock_70_CS.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio607375.
PROP06761.

Entry information

Entry nameGRP78_RAT
AccessionPrimary (citable) accession number: P06761
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: April 1, 1988
Last modified: April 16, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families