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Q91883 (GRP78_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 82. 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·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
Gene names
Name:hspa5
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length658 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Probably plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum.

Subcellular location

Endoplasmic reticulum lumen.

Sequence similarities

Belongs to the heat shock protein 70 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   DomainSignal
   LigandATP-binding
Nucleotide-binding
Gene Ontology (GO)
   Cellular_componentendoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 65863978 kDa glucose-regulated protein
PRO_0000013571

Regions

Nucleotide binding38 – 414ATP By similarity
Nucleotide binding228 – 2303ATP By similarity
Nucleotide binding294 – 3018ATP By similarity
Nucleotide binding365 – 3684ATP By similarity
Motif655 – 6584Prevents secretion from ER By similarity

Sites

Binding site981ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q91883 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 43E1468F532E80CF

FASTA65872,635
        10         20         30         40         50         60 
MVTMKLFALV LLVSASVFAS DDDDKKDDIG TVVGIDLGTT YSCVGVFKNG RVEIIANDQG 

        70         80         90        100        110        120 
NRITPSYVAF TPEGERLIGD AAKNQLTSNP ENTVFDAKRL IGRTWNDPSV QQDIKYLPFK 

       130        140        150        160        170        180 
VIEKKTKPYI EVDIGDQMKT FAPEEISAMV LVKMKETAEA YLGRKVTHAV VTVPAYFNDA 

       190        200        210        220        230        240 
QRQATKDAGT IAGLNVMRII NEPTAAAIAY GLDKKEGEKN ILVFDLGGGT FDVSLLTIDN 

       250        260        270        280        290        300 
GVFEVVATNG DTHLGGEDFD QRVMEHFIKL YKKKTGKDVR ADKRAVQKLR REVEKAKRAL 

       310        320        330        340        350        360 
SAQHQSRIEI ESFFEGEDFS ETLTRAKFEE LNMDLFRSTM KPVQKVLDDS DLKKSDIDEI 

       370        380        390        400        410        420 
VLVGGSTRIP KIQQLVKELF NGKEPSRGIN PDEAVAYGAA VQAGVLSGDQ DTGDLVLLDV 

       430        440        450        460        470        480 
CPLTLGIETV GGVMTKLIPR NTVVPTKKSQ IFSTASDNQP TVTIKVYEGE RPLTKDNHLL 

       490        500        510        520        530        540 
GTFDLTGIPP APRGVPQIEV TFEIDVNGIL RVTAEDKGTG NKNKITITND QNRLTPEEIE 

       550        560        570        580        590        600 
RMVTDAEKFA EEDKKLKERI DTRNELESYA YSLKNQIGDK EKLGGKLSSE DKETIEKAVE 

       610        620        630        640        650 
EKIEWLESHQ DADIEDFKAK KKELEEIVQP IVGKLYGGAG APPPEGAEGA EETEKDEL 

« Hide

References

[1]"Degradation and endoplasmic reticulum retention of unassembled alpha- and beta-subunits of Na,K-ATPase correlate with interaction of BiP."
Beggah A., Mathews P., Beguin P., Geering K.
J. Biol. Chem. 271:20895-20902(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U62807 mRNA. Translation: AAB08760.1.
RefSeqNP_001081462.1. NM_001087993.1.
UniGeneXl.3204.

3D structure databases

ProteinModelPortalQ91883.
SMRQ91883. Positions 30-571.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ91883.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397850.
KEGGxla:397850.

Phylogenomic databases

HOVERGENHBG051845.
KOK09490.

Family and domain databases

Gene3D1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
SUPFAMSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGRP78_XENLA
AccessionPrimary (citable) accession number: Q91883
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 82 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