EPOR_XENLA
ID EPOR_XENLA Reviewed; 525 AA.
AC Q4W815;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Erythropoietin receptor;
DE Short=EPO-R;
DE Short=EpoR;
DE Short=xlEPOR;
DE Flags: Precursor;
GN Name=epor {ECO:0000312|EMBL:BAD98623.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAD98623.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Erythrocyte {ECO:0000269|PubMed:16091591};
RX PubMed=16091591; DOI=10.1093/jb/mvi113;
RA Aizawa Y., Nogawa N., Kosaka N., Maeda Y., Watanabe T., Miyazaki H.,
RA Kato T.;
RT "Expression of erythropoietin receptor-like molecule in Xenopus laevis and
RT erythrocytopenia upon administration of its recombinant soluble form.";
RL J. Biochem. 138:167-175(2005).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Spleen {ECO:0000269|PubMed:16378761};
RX PubMed=16378761; DOI=10.1016/j.modgep.2005.09.004;
RA Yergeau D.A., Schmerer M., Kuliyev E., Evans T., Mead P.E.;
RT "Cloning and expression pattern of the Xenopus erythropoietin receptor.";
RL Gene Expr. Patterns 6:420-425(2006).
CC -!- FUNCTION: Receptor for erythropoietin. Mediates erythropoietin-induced
CC erythroblast proliferation and differentiation.
CC {ECO:0000269|PubMed:16091591}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16091591};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:16091591}.
CC -!- TISSUE SPECIFICITY: Expressed in the ventral blood island from stage 28
CC through to stage 36. Expressed in the circulating blood by stage 40. In
CC the adult, highly expressed in peripheral blood cells including
CC immature erythrocytes and basophils, and moderately expressed in the
CC hematopoietic organs: liver, kidney and spleen. Expressed at a low
CC level in adult brain. {ECO:0000269|PubMed:16091591,
CC ECO:0000269|PubMed:16378761}.
CC -!- DEVELOPMENTAL STAGE: First expressed at a low level at stage 18 (late
CC neurula), with high levels of expression seen from stage 32 through to
CC stage 48 (tadpole). {ECO:0000269|PubMed:16378761}.
CC -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC folding and thereby efficient intracellular transport and cell-surface
CC receptor binding. {ECO:0000250|UniProtKB:P19235}.
CC -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC activation. {ECO:0000250|UniProtKB:P19235}.
CC -!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is
CC involved in modulation of cellular responses. The phosphorylated ITIM
CC motif can bind the SH2 domain of several SH2-containing phosphatases
CC (By similarity). {ECO:0000250|UniProtKB:P19235}.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 1
CC subfamily. {ECO:0000255}.
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DR EMBL; AB189477; BAD98623.1; -; mRNA.
DR RefSeq; NP_001089173.1; NM_001095704.1.
DR AlphaFoldDB; Q4W815; -.
DR SMR; Q4W815; -.
DR GeneID; 734211; -.
DR KEGG; xla:734211; -.
DR CTD; 734211; -.
DR Xenbase; XB-GENE-6251686; epor.L.
DR OrthoDB; 1442632at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 734211; Expressed in lung and 17 other tissues.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004900; F:erythropoietin receptor activity; ISS:UniProtKB.
DR GO; GO:0030218; P:erythrocyte differentiation; IEP:UniProtKB.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR009167; Erythropoietin_rcpt.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR015152; Growth/epo_recpt_lig-bind.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR23037:SF28; PTHR23037:SF28; 1.
DR Pfam; PF09067; EpoR_lig-bind; 1.
DR PIRSF; PIRSF001959; EPO_receptor; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..525
FT /note="Erythropoietin receptor"
FT /evidence="ECO:0000255"
FT /id="PRO_0000284702"
FT TOPO_DOM 33..249
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..525
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 146..246
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 434..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 232..236
FT /note="WSXWS motif"
FT /evidence="ECO:0000250|UniProtKB:P19235"
FT MOTIF 281..289
FT /note="Box 1 motif"
FT /evidence="ECO:0000250|UniProtKB:P19235"
FT MOTIF 487..492
FT /note="ITIM motif"
FT /evidence="ECO:0000250|UniProtKB:P19235"
FT COMPBIAS 434..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 117
FT /note="Required for ligand binding"
FT /evidence="ECO:0000250|UniProtKB:P19235"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..68
FT /evidence="ECO:0000250|UniProtKB:P19235"
FT DISULFID 91..107
FT /evidence="ECO:0000250|UniProtKB:P19235"
FT CONFLICT 80
FT /note="F -> Y (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="M -> V (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 525 AA; 59673 MW; F0D68E8ABBD77035 CRC64;
MGAPSSLLFS TAHWRTVPFL LAFWVLLSTG TAEDPTMTPE FLRHISEKIP EEYQNPHCFT
RDLNDFICFW EGERRKNASF SYSEDDQIKW CQLRTEVASN NTWWYICEFP VTDVVLFAGI
TISAYPCHKC QTAREIYINE LVLLNPPLNV TVKEKQDPRG LLISWKPPHF QKNHDINNEI
KYQVNYSTPG ADMQTVEVEA GNTEIFLTDI VPAAYTVTVR CKADGVSYNG YWSDWTAPIT
IATIIDLRLL LLLSIAIFVA LIAGVGVYIF MRHGMYLKHK VWPQVPTPEN NFQGLFTTHK
GNFKLWLGQA DAYLLWISRH VFQEDPSSTL EVLSELPPAA LPQSFNPNPL KDSYVVLDEN
RMPCSLEWLE AQRHKTVIVG AESMDSRLQT VNKDVVLEDT SKGQIAVKAN NRVHSLEGDG
SQGEAFREDE YVEAPRMEHE RHRVSRENSV SSDGKQSIPS SFEYTELQTC EGLLSPKPRP
VPPRMPLKYA YLDMSSSGEH SPPPSPNFYQ NSPITNFLAP IYSQS
