ID   EPO_SPAJD               Reviewed;         192 AA.
AC   Q6H8T0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Erythropoietin;
DE   Flags: Precursor;
GN   Name=EPO;
OS   Spalax judaei (Judean Mountains blind mole rat) (Nannospalax judaei).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Spalacidae; Spalacinae; Nannospalax.
OX   NCBI_TaxID=134510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=15210955; DOI=10.1073/pnas.0403540101;
RA   Shams I., Avivi A., Eviatar N.;
RT   "Hypoxic stress tolerance of the blind subterranean mole rat: expression of
RT   erythropoietin and hypoxia-inducible factor 1 alpha.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9698-9703(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 {ECO:0000250}.
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; AJ715794; CAG29399.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6H8T0; -.
DR   SMR; Q6H8T0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005128; F:erythropoietin receptor binding; IEA:InterPro.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0043249; P:erythrocyte maturation; IEA:UniProtKB-KW.
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; Secreted;
KW   Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..192
FT                   /note="Erythropoietin"
FT                   /id="PRO_0000313664"
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"
SQ   SEQUENCE   192 AA;  21372 MW;  72FCA94DE8C5AAB5 CRC64;
     MGVPDCLALP LLVTFLLLSL GLPVLGAPPR LICDSRVLER YILEAKEAEN ITMGCAEGPR
     FNENFTVPDT KVNFYAWKTM GVEEQAVEVW QGLSLLFEAI LRAQAVLANS SQPSEMLQLH
     VDKAISGLRS LTSLLRALGA QKEAISPPDT TQVIPLRRFT VDTFCKLFRI YSNFLRGKLK
     LYTGEACRRG DR