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P08110 (ENPL_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 123. 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:
Endoplasmin
Alternative name(s):
Heat shock 108 kDa protein
Short name=HSP 108
Short name=HSP108
Heat shock protein 90 kDa beta member 1
Transferrin-binding protein
Gene names
Name:HSP90B1
Synonyms:TRA1
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length795 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Molecular chaperone that functions in the processing and transport of secreted proteins. Has ATPase activity By similarity. HAMAP-Rule MF_00505

Subunit structure

Homodimer; disulfide-linked.

Subcellular location

Endoplasmic reticulum lumen HAMAP-Rule MF_00505.

Sequence similarities

Belongs to the heat shock protein 90 family.

Ontologies

Keywords
   Biological processStress response
   Cellular componentEndoplasmic reticulum
   DomainSignal
   LigandATP-binding
Calcium
Nucleotide-binding
   Molecular functionChaperone
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: InterPro

response to stress

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentendoplasmic reticulum

Inferred from sequence or structural similarity. Source: AgBase

endoplasmic 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 – 2121 Potential
Chain22 – 795774Endoplasmin HAMAP-Rule MF_00505
PRO_0000013601

Regions

Motif792 – 7954Prevents secretion from ER HAMAP-Rule MF_00505

Sites

Binding site1061ATP By similarity
Binding site1481ATP By similarity
Binding site1611ATP By similarity
Binding site1671ATP By similarity
Binding site1981ATP; via amide nitrogen By similarity
Binding site4471ATP By similarity

Amino acid modifications

Glycosylation611N-linked (GlcNAc...) Potential
Glycosylation1061N-linked (GlcNAc...) Potential
Glycosylation2161N-linked (GlcNAc...) Ref.4
Glycosylation4441N-linked (GlcNAc...) Potential
Glycosylation4801N-linked (GlcNAc...) Potential
Glycosylation5011N-linked (GlcNAc...) Potential
Disulfide bond137Interchain By similarity

Experimental info

Sequence conflict2061D → E in AAA48827. Ref.2
Sequence conflict2061D → E in CAA28629. Ref.3
Sequence conflict2671V → L in AAA48827. Ref.2
Sequence conflict3031E → Q in AAA48827. Ref.2
Sequence conflict3071N → D in AAA48827. Ref.2
Sequence conflict3071N → D in CAA28629. Ref.3
Sequence conflict3171E → H in AAA48827. Ref.2
Sequence conflict3781G → A in AAA48827. Ref.2
Sequence conflict593 – 5942EG → DR in AAA48827. Ref.2
Sequence conflict6531W → C in AAA48827. Ref.2
Sequence conflict669 – 6757GKDISTN → VFSS in CAA28629. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P08110 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: BE1B29E1DBEC5A9A

FASTA79591,555
        10         20         30         40         50         60 
MKSAWALALA CTLLLAASVT AEEVDVDATV EEDLGKSREG SRTDDEVVQR EEEAIQLDGL 

        70         80         90        100        110        120 
NASQIKEIRE KSEKFAFQAE VNRMMKLIIN SLYKNKEIFL RELISNASDA LDKIRLISLT 

       130        140        150        160        170        180 
DENALAGNEE LTVKIKCDKE KNMLHVTDTG IGMTKEELIK NLGTIAKSGT SEFLNKMTEM 

       190        200        210        220        230        240 
QDDSQSTSEL IGQFGVGFYS AFLVADRVIV TSKHNNDTQH IWESDSNEFS VIDDPRGNTL 

       250        260        270        280        290        300 
GRGTTITLVL KEEASDYLEL DTVKNLVKKY SQFINFPIYV WSSKTETVEE PVEEEEAKEE 

       310        320        330        340        350        360 
KEETDDNEAA VEEEEEEKKP KTKKVEKTVW DWELMNDIKP IWQRPSKEVE EDEYKAFYKT 

       370        380        390        400        410        420 
FSKEHDDPMA YIHFTAEGEV TFKSILFVPN SAPRGLFDEY GSKKSDFIKL YVRRVFITDD 

       430        440        450        460        470        480 
FHDMMPKYLN FVKGVVDSDD LPLNVSRETL QQHKLLKVIR KKLVRKTLDM IKKIAEEKYN 

       490        500        510        520        530        540 
DTFWKEFGTN VKLGVIEDHS NRTRLAKLLR FQSSHHESNL TSLDQYVERM KEKQDKIYFM 

       550        560        570        580        590        600 
AGASRKEAES SPFVERLLKK GYEVIYLTEP VDEYCIQALP EFDGKRFQNV AKEGVKFEES 

       610        620        630        640        650        660 
EKSKESREAL EKEFEPLLNW MKDKALKDKI EKAVLSQRLT QSPCALVASQ YGWSGNMERI 

       670        680        690        700        710        720 
MKAQAYQTGK DISTNYYASQ KKTFEINPRH PLIKDMLRRV KENEDDKTVS DLAVVLFETA 

       730        740        750        760        770        780 
TLRSGYMLPD TKEYGDRIER MLRLSLNIDL DAKVEEEPEE PEDAAEEAEQ DEEEVDADAE 

       790 
DSETQKESTD VKDEL 

« Hide

References

[1]"Amino acid sequence of a chicken heat shock protein derived from the complementary DNA nucleotide sequence."
Kulomaa M.S., Weigel N.L., Kleinsek D.A., Beattie W.G., Conneely O.M., March C., Zarucki-Schulz T., Schrader W.T., O'Malley B.W.
Biochemistry 25:6244-6251(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning of a steroid-regulated 108K heat shock protein gene from hen oviduct."
Kleinsek D.A., Beattie W.G., Tsai M.J., O'Malley B.W.
Nucleic Acids Res. 14:10053-10069(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Oviduct.
[3]Forsgren M.
Submitted (SEP-1987) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Oviduct.
[4]"A chicken transferrin binding protein is heat shock protein 108."
Hayes G.R., Himpler B.S., Weiner K.X.B., Lucas J.J.
Biochem. Biophys. Res. Commun. 200:65-70(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-216.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14772 mRNA. Translation: AAA48826.1.
M31321 Genomic DNA. Translation: AAA48827.1.
X04961 Genomic DNA. Translation: CAA28629.1.
PIRHHCH08. A24461.
I50255.
RefSeqNP_989620.1. NM_204289.1.
UniGeneGga.4724.

3D structure databases

ProteinModelPortalP08110.
SMRP08110. Positions 68-754.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid675192. 1 interaction.
IntActP08110. 1 interaction.

Proteomic databases

PaxDbP08110.
PRIDEP08110.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID374163.
KEGGgga:374163.

Organism-specific databases

CTD7184.

Phylogenomic databases

eggNOGCOG0326.
HOGENOMHOG000031988.
HOVERGENHBG007374.
InParanoidP08110.
KOK09487.
PhylomeDBP08110.

Family and domain databases

Gene3D3.30.565.10. 2 hits.
HAMAPMF_00505. HSP90.
InterProIPR003594. HATPase_ATP-bd.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERPTHR11528. PTHR11528. 1 hit.
PfamPF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view]
PIRSFPIRSF002583. Hsp90. 1 hit.
PRINTSPR00775. HEATSHOCK90.
SMARTSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 2 hits.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00298. HSP90. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20813673.
PROP08110.

Entry information

Entry nameENPL_CHICK
AccessionPrimary (citable) accession number: P08110
Secondary accession number(s): Q90869, Q90870
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: June 11, 2014
This is version 123 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