EPO_CANLF
ID EPO_CANLF Reviewed; 206 AA.
AC P33707; Q6PWU5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Erythropoietin;
DE Flags: Precursor;
GN Name=EPO;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RA Souza D.S., Vicentim D.L., Costa F.F., Saad S.T.O.;
RT "Description of the full length of canine erythropoietin.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-193.
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; AY572971; AAS77874.1; -; mRNA.
DR EMBL; L13027; AAA30842.1; -; mRNA.
DR PIR; I46199; I46199.
DR RefSeq; NP_001006647.1; NM_001006646.1.
DR AlphaFoldDB; P33707; -.
DR SMR; P33707; -.
DR STRING; 9615.ENSCAFP00000020937; -.
DR PaxDb; P33707; -.
DR GeneID; 404002; -.
DR CTD; 2056; -.
DR eggNOG; ENOG502RXRC; Eukaryota.
DR InParanoid; P33707; -.
DR OrthoDB; 1175751at2759; -.
DR Proteomes; UP000002254; Unplaced.
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..40
FT /evidence="ECO:0000250"
FT CHAIN 41..206
FT /note="Erythropoietin"
FT /id="PRO_0000008398"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..201
FT /evidence="ECO:0000250"
FT DISULFID 69..73
FT /evidence="ECO:0000250"
SQ SEQUENCE 206 AA; 22666 MW; 1EEC64A02CE4F5B0 CRC64;
MCEPAPPKPT QSAWHSFPEC PALLLLLSLL LLPLGLPVLG APPRLICDSR VLERYILEAR
EAENVTMGCA QGCSFSENIT VPDTKVNFYT WKRMDVGQQA LEVWQGLALL SEAILRGQAL
LANASQPSET PQLHVDKAVS SLRSLTSLLR ALGAQKEAMS LPEEASPAPL RTFTVDTLCK
LFRIYSNFLR GKLTLYTGEA CRRGDR