ID   EPO_MICOE               Reviewed;         192 AA.
AC   Q0Z956;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Erythropoietin;
DE   Flags: Precursor;
GN   Name=EPO;
OS   Microtus oeconomus (Tundra vole).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Arvicolinae; Microtus.
OX   NCBI_TaxID=64717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RA   Wang Y., Chen X.-Q., Du J.-Z.;
RT   "Cloning of erythropoietin cDNA from root vole (Microtus oeconomus).";
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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; DQ658370; ABG47336.1; -; mRNA.
DR   AlphaFoldDB; Q0Z956; -.
DR   SMR; Q0Z956; -.
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_0000313663"
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;  21232 MW;  E29C578F32AE0497 CRC64;
     MGVPERPTLL LLLSLLLLPL GLPVLCAPPR LICDGRVLER YILEAREAEN VTMGCAEGPR
     LSENITVPDT KVNFNAWKRM EVQEQAVEVW QGLSLLSEAI LRGQALLANS SQPSGMLQLH
     IDKAISGLRS LTSLLRVLGA QKESISPPDA TPPAPLRTLM VENFCKLFRV YSNFLRGKLK
     LYTGEACRRG DR