EPO_DANRE
ID EPO_DANRE Reviewed; 183 AA.
AC Q2XNF5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Erythropoietin;
DE AltName: Full=Erythropoietin-L2;
DE Flags: Precursor;
GN Name=epo;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Paffett-Lugassy N., Yang C., Paw B., Leschinsky I., Barut B., Bahary N.,
RA Caro J., Handin R., Zon L.;
RT "Functional conservation of epo-epor signaling in zebrafish.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND GLYCOSYLATION.
RX PubMed=17706649; DOI=10.1016/j.febslet.2007.07.073;
RA Chu C.-Y., Cheng C.-H., Chen G.-D., Chen Y.-C., Hung C.-C., Huang K.-Y.,
RA Huang C.-J.;
RT "The zebrafish erythropoietin: functional identification and biochemical
RT characterization.";
RL FEBS Lett. 581:4265-4271(2007).
CC -!- FUNCTION: Erythropoietin is the principal hormone involved in the
CC regulation of erythrocyte differentiation and the maintenance of a
CC physiological level of circulating erythrocyte mass.
CC {ECO:0000269|PubMed:17706649}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17706649}.
CC -!- TISSUE SPECIFICITY: Expressed in heart and liver.
CC {ECO:0000269|PubMed:17706649}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17706649}.
CC -!- SIMILARITY: Belongs to the EPO/TPO family. {ECO:0000305}.
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DR EMBL; DQ278896; ABB77436.1; -; mRNA.
DR EMBL; EF426727; ABQ41211.1; -; mRNA.
DR RefSeq; NP_001033098.1; NM_001038009.2.
DR AlphaFoldDB; Q2XNF5; -.
DR SMR; Q2XNF5; -.
DR STRING; 7955.ENSDARP00000100433; -.
DR PaxDb; Q2XNF5; -.
DR Ensembl; ENSDART00000111066; ENSDARP00000100433; ENSDARG00000055163.
DR GeneID; 100004455; -.
DR KEGG; dre:100004455; -.
DR CTD; 100004455; -.
DR ZFIN; ZDB-GENE-061218-3; epoa.
DR eggNOG; ENOG502RXRC; Eukaryota.
DR GeneTree; ENSGT00390000017226; -.
DR InParanoid; Q2XNF5; -.
DR TreeFam; TF333413; -.
DR Reactome; R-DRE-9027276; Erythropoietin activates Phosphoinositide-3-kinase (PI3K).
DR PRO; PR:Q2XNF5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000055163; Expressed in cardiac ventricle and 27 other tissues.
DR ExpressionAtlas; Q2XNF5; baseline.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:ZFIN.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
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 GO; GO:0030097; P:hemopoiesis; IDA:ZFIN.
DR GO; GO:0048823; P:nucleate erythrocyte development; IDA:ZFIN.
DR GO; GO:0048793; P:pronephros development; IMP:ZFIN.
DR GO; GO:0014823; P:response to activity; IDA:ZFIN.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
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.
PE 1: Evidence at protein level;
KW Disulfide bond; Erythrocyte maturation; Glycoprotein; Hormone;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..183
FT /note="Erythropoietin"
FT /id="PRO_0000313665"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..178
FT /evidence="ECO:0000250"
FT DISULFID 52..56
FT /evidence="ECO:0000250"
SQ SEQUENCE 183 AA; 20384 MW; AF8E73FF524DBD50 CRC64;
MFHGSGLFAL LLMVLEWTRP GLSSPLRPIC DLRVLDHFIK EAWDAEAAMR TCKDDCSIAT
NVTVPLTRVD FEVWEAMNIE EQAQEVQSGL HMLNEAIGSL QISNQTEVLQ SHIDASIRNI
ASIRQVLRSL SIPEYVPPTS SGEDKETQKI SSISELFQVH VNFLRGKARL LLANAPVCRQ
GVS