ID   EPO_HORSE               Reviewed;         192 AA.
AC   Q867B1;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Erythropoietin;
DE   Flags: Precursor;
GN   Name=EPO;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   PubMed=14719696; DOI=10.2460/ajvr.2004.65.15;
RA   Sato F., Yamashita S., Kugo T., Hasegawa T., Mitsui I., Kijima-Suda I.;
RT   "Nucleotide sequence of equine erythropoietin and characterization of
RT   region-specific antibodies.";
RL   Am. J. Vet. Res. 65:15-19(2004).
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   -!- SIMILARITY: Belongs to the EPO/TPO family. {ECO:0000305}.
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DR   EMBL; AB100030; BAC55239.1; -; mRNA.
DR   RefSeq; NP_001075294.1; NM_001081825.1.
DR   AlphaFoldDB; Q867B1; -.
DR   SMR; Q867B1; -.
DR   STRING; 9796.ENSECAP00000037030; -.
DR   PaxDb; Q867B1; -.
DR   Ensembl; ENSECAT00000011172; ENSECAP00000008707; ENSECAG00000010733.
DR   GeneID; 100033849; -.
DR   KEGG; ecb:100033849; -.
DR   CTD; 2056; -.
DR   VGNC; VGNC:51127; EPO.
DR   GeneTree; ENSGT00390000017226; -.
DR   InParanoid; Q867B1; -.
DR   OrthoDB; 1175751at2759; -.
DR   Proteomes; UP000002281; Chromosome 13.
DR   Bgee; ENSECAG00000010733; Expressed in bone marrow and 8 other tissues.
DR   ExpressionAtlas; Q867B1; baseline.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
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; IBA:GO_Central.
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:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IBA:GO_Central.
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; PTHR10370; 1.
DR   Pfam; PF00758; EPO_TPO; 1.
DR   PIRSF; PIRSF001951; EPO; 1.
DR   PRINTS; PR00272; ERYTHROPTN.
DR   SUPFAM; SSF47266; SSF47266; 1.
DR   PROSITE; PS00817; EPO_TPO; 1.
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_0000008400"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        33..187
FT                   /evidence="ECO:0000250"
FT   DISULFID        55..59
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   192 AA;  20984 MW;  E02D098490B09C4F CRC64;
     MGVRECPALL LLLSLLLPPL GLPALGAPPR LICDSRVLER YILEAREAEN VTMGCAEGCS
     FGENVTVPDT KVNFYSWKRM EVEQQAVEVW QGLALLSEAI LQGQALLANS SQPSETLRLH
     VDKAVSSLRS LTSLLRALGA QKEAISPPDA ASAAPLRTFA VDTLCKLFRI YSNFLRGKLK
     LYTGEACRRG DR