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EPO_MACMU
ID   EPO_MACMU               Reviewed;         192 AA.
AC   Q28513;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Erythropoietin;
DE   Flags: Precursor;
GN   Name=EPO;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
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; L10609; AAA36842.1; -; mRNA.
DR   PIR; I84613; I84613.
DR   RefSeq; NP_001036201.1; NM_001042736.1.
DR   AlphaFoldDB; Q28513; -.
DR   SMR; Q28513; -.
DR   STRING; 9544.ENSMMUP00000030108; -.
DR   GeneID; 719294; -.
DR   KEGG; mcc:719294; -.
DR   CTD; 2056; -.
DR   eggNOG; ENOG502RXRC; Eukaryota.
DR   InParanoid; Q28513; -.
DR   Proteomes; UP000006718; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005128; F:erythropoietin receptor binding; ISS:UniProtKB.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
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   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..27
FT                   /evidence="ECO:0000250"
FT   CHAIN           28..192
FT                   /note="Erythropoietin"
FT                   /id="PRO_0000008404"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        152
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        34..187
FT                   /evidence="ECO:0000250"
FT   DISULFID        56..60
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   192 AA;  21081 MW;  275560A264628CD1 CRC64;
     MGVHECPAWL WLLLSLVSLP LGLPVPGAPP RLVCDSRVLE RYLLEAKEAE NVTMGCSESC
     SLNENITVPD TKVNFYAWKR IEVGQQAVEV WQGLALLSEA VLRGQAVLAN SSQPFEPLQL
     HMDKAISGLR SITTLLRALG AQEAISLPDA ASAAPLRTIT ADTFCKLFRV YSNFLRGKLK
     LYTGEACRRG DR
 
 
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