ID   EPO_RAT                 Reviewed;         192 AA.
AC   P29676; P70504;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   24-JAN-2024, entry version 144.
DE   RecName: Full=Erythropoietin;
DE   Flags: Precursor;
GN   Name=Epo;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Kidney;
RX   PubMed=1420369; DOI=10.1016/0167-4781(92)90146-q;
RA   Nagao M., Suga H., Okano M., Masuda S., Narita H., Ikura K., Sasaki R.;
RT   "Nucleotide sequence of rat erythropoietin.";
RL   Biochim. Biophys. Acta 1171:99-102(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4-192.
RC   STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX   PubMed=8364201;
RA   Wen D., Boissel J.-P.R., Tracy T.E., Gruninger R.H., Mulcahy L.S.,
RA   Czelusniak J., Goodman M., Bunn H.F.;
RT   "Erythropoietin structure-function relationships: high degree of sequence
RT   homology among mammals.";
RL   Blood 82:1507-1516(1993).
CC   -!- FUNCTION: Hormone involved in the regulation of erythrocyte
CC       proliferation and differentiation and the maintenance of a
CC       physiological level of circulating erythrocyte mass. Binds to EPOR
CC       leading to EPOR dimerization and JAK2 activation thereby activating
CC       specific downstream effectors, including STAT1 and STAT3.
CC       {ECO:0000250|UniProtKB:P01588}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Produced by kidney or liver of adult mammals and by
CC       liver of fetal or neonatal mammals.
CC   -!- SIMILARITY: Belongs to the EPO/TPO family. {ECO:0000305}.
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DR   EMBL; D10763; BAA01593.1; -; mRNA.
DR   EMBL; L10608; AAA41126.1; -; mRNA.
DR   PIR; S28148; S28148.
DR   RefSeq; NP_058697.1; NM_017001.1.
DR   AlphaFoldDB; P29676; -.
DR   SMR; P29676; -.
DR   STRING; 10116.ENSRNOP00000001914; -.
DR   GlyCosmos; P29676; 3 sites, No reported glycans.
DR   GlyGen; P29676; 3 sites.
DR   PhosphoSitePlus; P29676; -.
DR   PaxDb; 10116-ENSRNOP00000001914; -.
DR   Ensembl; ENSRNOT00000001914.5; ENSRNOP00000001914.3; ENSRNOG00000001412.5.
DR   Ensembl; ENSRNOT00055000490; ENSRNOP00055000353; ENSRNOG00055000288.
DR   Ensembl; ENSRNOT00060017722; ENSRNOP00060013773; ENSRNOG00060010482.
DR   Ensembl; ENSRNOT00065000112; ENSRNOP00065000111; ENSRNOG00065000066.
DR   GeneID; 24335; -.
DR   KEGG; rno:24335; -.
DR   UCSC; RGD:2559; rat.
DR   AGR; RGD:2559; -.
DR   CTD; 2056; -.
DR   RGD; 2559; Epo.
DR   eggNOG; ENOG502RXRC; Eukaryota.
DR   GeneTree; ENSGT00390000017226; -.
DR   HOGENOM; CLU_110946_0_0_1; -.
DR   InParanoid; P29676; -.
DR   OMA; AMEFPRL; -.
DR   OrthoDB; 4338688at2759; -.
DR   PhylomeDB; P29676; -.
DR   TreeFam; TF333413; -.
DR   Reactome; R-RNO-9027276; Erythropoietin activates Phosphoinositide-3-kinase (PI3K).
DR   Reactome; R-RNO-9027284; Erythropoietin activates RAS.
DR   PRO; PR:P29676; -.
DR   Proteomes; UP000002494; Chromosome 12.
DR   Bgee; ENSRNOG00000001412; Expressed in ovary and 3 other cell types or tissues.
DR   GO; GO:0044297; C:cell body; IDA:RGD.
DR   GO; GO:0009986; C:cell surface; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0005125; F:cytokine activity; ISO:RGD.
DR   GO; GO:0005128; F:erythropoietin receptor binding; ISS:UniProtKB.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0030295; F:protein kinase activator activity; ISO:RGD.
DR   GO; GO:0006953; P:acute-phase response; IEP:RGD.
DR   GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR   GO; GO:0071474; P:cellular hyperosmotic response; ISO:RGD.
DR   GO; GO:0007566; P:embryo implantation; ISO:RGD.
DR   GO; GO:0030218; P:erythrocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0043249; P:erythrocyte maturation; IEA:UniProtKB-KW.
DR   GO; GO:0038162; P:erythropoietin-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0042541; P:hemoglobin biosynthetic process; ISO:RGD.
DR   GO; GO:0033028; P:myeloid cell apoptotic process; ISO:RGD.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR   GO; GO:0010523; P:negative regulation of calcium ion transport into cytosol; ISO:RGD.
DR   GO; GO:1902251; P:negative regulation of erythrocyte apoptotic process; ISO:RGD.
DR   GO; GO:1902219; P:negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress; ISO:RGD.
DR   GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; ISO:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0042104; P:positive regulation of activated T cell proliferation; IDA:RGD.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:RGD.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:RGD.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:RGD.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IDA:RGD.
DR   GO; GO:0046579; P:positive regulation of Ras protein signal transduction; ISO:RGD.
DR   GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0048678; P:response to axon injury; IEP:RGD.
DR   GO; GO:0071548; P:response to dexamethasone; IEP:RGD.
DR   GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
DR   GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR   GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0070555; P:response to interleukin-1; IEP:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR   GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR   GO; GO:0009651; P:response to salt stress; IEP:RGD.
DR   GO; GO:0033574; P:response to testosterone; IEP:RGD.
DR   GO; GO:0033189; P:response to vitamin A; IEP:RGD.
DR   Gene3D; 1.20.1250.10; -; 1.
DR   InterPro; IPR009079; 4_helix_cytokine-like_core.
DR   InterPro; IPR019767; EPO/TPO_CS.
DR   InterPro; IPR001323; EPO_TPO.
DR   InterPro; IPR003013; Erythroptn.
DR   PANTHER; PTHR10370; ERYTHROPOIETIN; 1.
DR   PANTHER; PTHR10370:SF0; ERYTHROPOIETIN; 1.
DR   Pfam; PF00758; EPO_TPO; 1.
DR   PIRSF; PIRSF001951; EPO; 1.
DR   PRINTS; PR00272; ERYTHROPTN.
DR   SUPFAM; SSF47266; 4-helical cytokines; 1.
DR   PROSITE; PS00817; EPO_TPO; 1.
DR   Genevisible; P29676; RN.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Erythrocyte maturation; Glycoprotein; Hormone;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000250"
FT   CHAIN           27..192
FT                   /note="Erythropoietin"
FT                   /id="PRO_0000008408"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        33..187
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   192 AA;  21286 MW;  3EA632737E7D2443 CRC64;
     MGVPERPTLL LLLSLLLIPL GLPVLCAPPR LICDSRVLER YILEAKEAEN VTMGCAEGPR
     LSENITVPDT KVNFYAWKRM KVEEQAVEVW QGLSLLSEAI LQAQALQANS SQPPESLQLH
     IDKAISGLRS LTSLLRVLGA QKELMSPPDA TQAAPLRTLT ADTFCKLFRV YSNFLRGKLK
     LYTGEACRRG DR
//