Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P29676 (EPO_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. 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:
Erythropoietin
Gene names
Name:Epo
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length192 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Erythropoietin is the principal hormone involved in the regulation of erythrocyte differentiation and the maintenance of a physiological level of circulating erythrocyte mass.

Subcellular location

Secreted.

Tissue specificity

Produced by kidney or liver of adult mammals and by liver of fetal or neonatal mammals.

Sequence similarities

Belongs to the EPO/TPO family.

Ontologies

Keywords
   Biological processErythrocyte maturation
   Cellular componentSecreted
   DomainSignal
   Molecular functionHormone
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from expression pattern PubMed 19330822. Source: RGD

apoptotic process

Inferred from electronic annotation. Source: Ensembl

cellular hyperosmotic response

Inferred from electronic annotation. Source: Ensembl

embryo implantation

Inferred from electronic annotation. Source: Ensembl

erythrocyte maturation

Inferred from electronic annotation. Source: UniProtKB-KW

hemoglobin biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of calcium ion transport into cytosol

Inferred from electronic annotation. Source: Ensembl

negative regulation of cation channel activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of erythrocyte apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress

Inferred from electronic annotation. Source: Ensembl

peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA replication

Inferred from electronic annotation. Source: Ensembl

positive regulation of Ras protein signal transduction

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron differentiation

Inferred from direct assay PubMed 12876482. Source: RGD

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

positive regulation of tyrosine phosphorylation of Stat5 protein

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

response to axon injury

Inferred from expression pattern PubMed 15470751. Source: RGD

response to electrical stimulus

Inferred from expression pattern PubMed 19185286. Source: RGD

response to estrogen

Inferred from expression pattern PubMed 15784734. Source: RGD

response to hyperoxia

Inferred from expression pattern PubMed 19768476. Source: RGD

response to hypoxia

Inferred from expression pattern PubMed 19497871. Source: RGD

response to interleukin-1

Inferred from expression pattern PubMed 9321887. Source: RGD

response to lipopolysaccharide

Inferred from expression pattern PubMed 9321887. Source: RGD

response to nutrient

Inferred from expression pattern PubMed 19136608. Source: RGD

response to salt stress

Inferred from expression pattern PubMed 16815869. Source: RGD

response to testosterone

Inferred from expression pattern PubMed 15778925. Source: RGD

response to vitamin A

Inferred from expression pattern PubMed 9027729. Source: RGD

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

extracellular region

Inferred from direct assay PubMed 15470751. Source: RGD

extracellular space

Inferred from direct assay PubMed 19136608. Source: RGD

   Molecular_functionprotein kinase activator activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 By similarity
Chain27 – 192166Erythropoietin
PRO_0000008408

Amino acid modifications

Glycosylation501N-linked (GlcNAc...) By similarity
Glycosylation641N-linked (GlcNAc...) By similarity
Glycosylation1091N-linked (GlcNAc...) By similarity
Disulfide bond33 ↔ 187 By similarity

Sequences

Sequence LengthMass (Da)Tools
P29676 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 3EA632737E7D2443

FASTA19221,286
        10         20         30         40         50         60 
MGVPERPTLL LLLSLLLIPL GLPVLCAPPR LICDSRVLER YILEAKEAEN VTMGCAEGPR 

        70         80         90        100        110        120 
LSENITVPDT KVNFYAWKRM KVEEQAVEVW QGLSLLSEAI LQAQALQANS SQPPESLQLH 

       130        140        150        160        170        180 
IDKAISGLRS LTSLLRVLGA QKELMSPPDA TQAAPLRTLT ADTFCKLFRV YSNFLRGKLK 

       190 
LYTGEACRRG DR 

« Hide

References

[1]"Nucleotide sequence of rat erythropoietin."
Nagao M., Suga H., Okano M., Masuda S., Narita H., Ikura K., Sasaki R.
Biochim. Biophys. Acta 1171:99-102(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Kidney.
[2]"Erythropoietin structure-function relationships: high degree of sequence homology among mammals."
Wen D., Boissel J.-P.R., Tracy T.E., Gruninger R.H., Mulcahy L.S., Czelusniak J., Goodman M., Bunn H.F.
Blood 82:1507-1516(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-192.
Strain: Sprague-Dawley.
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D10763 mRNA. Translation: BAA01593.1.
L10608 mRNA. Translation: AAA41126.1.
PIRS28148.
RefSeqNP_058697.1. NM_017001.1.
UniGeneRn.11365.

3D structure databases

ProteinModelPortalP29676.
SMRP29676. Positions 27-192.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000001914.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000001914; ENSRNOP00000001914; ENSRNOG00000001412.
GeneID24335.
KEGGrno:24335.
UCSCRGD:2559. rat.

Organism-specific databases

CTD2056.
RGD2559. Epo.

Phylogenomic databases

eggNOGNOG43828.
GeneTreeENSGT00390000017226.
HOGENOMHOG000052505.
HOVERGENHBG003978.
InParanoidP29676.
KOK05437.
OMANVTMGCA.
OrthoDBEOG7DVDCR.
PhylomeDBP29676.
TreeFamTF333413.

Gene expression databases

GenevestigatorP29676.

Family and domain databases

Gene3D1.20.1250.10. 1 hit.
InterProIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR019767. EPO/TPO_CS.
IPR001323. EPO_TPO.
IPR003013. Erythroptn.
[Graphical view]
PANTHERPTHR10370. PTHR10370. 1 hit.
PfamPF00758. EPO_TPO. 1 hit.
[Graphical view]
PIRSFPIRSF001951. EPO. 1 hit.
PRINTSPR00272. ERYTHROPTN.
SUPFAMSSF47266. SSF47266. 1 hit.
PROSITEPS00817. EPO_TPO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio603023.
PROP29676.

Entry information

Entry nameEPO_RAT
AccessionPrimary (citable) accession number: P29676
Secondary accession number(s): P70504
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 16, 2014
This is version 95 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