ID A0A0D9R391_CHLSB Unreviewed; 511 AA.
AC A0A0D9R391;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Erythropoietin receptor {ECO:0000256|ARBA:ARBA00018355, ECO:0000256|PIRNR:PIRNR001959};
DE Short=EPO-R {ECO:0000256|PIRNR:PIRNR001959};
GN Name=EPOR {ECO:0000313|Ensembl:ENSCSAP00000003080.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000003080.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000003080.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000003080.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Receptor for erythropoietin. {ECO:0000256|PIRNR:PIRNR001959}.
CC -!- SUBUNIT: Forms homodimers on EPO stimulation.
CC {ECO:0000256|PIRNR:PIRNR001959}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 1
CC subfamily. {ECO:0000256|ARBA:ARBA00007885,
CC ECO:0000256|PIRNR:PIRNR001959}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AQIB01140941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A0D9R391; -.
DR STRING; 60711.ENSCSAP00000003080; -.
DR Ensembl; ENSCSAT00000004836.1; ENSCSAP00000003080.1; ENSCSAG00000006800.1.
DR eggNOG; ENOG502RYHW; Eukaryota.
DR GeneTree; ENSGT00940000160315; -.
DR OMA; ERCWGTM; -.
DR Proteomes; UP000029965; Chromosome 6.
DR Bgee; ENSCSAG00000006800; Expressed in adrenal cortex and 3 other cell types or tissues.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0004900; F:erythropoietin receptor activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0046697; P:decidualization; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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 InterPro; IPR003528; Long_hematopoietin_rcpt_CS.
DR PANTHER; PTHR23037; CYTOKINE RECEPTOR; 1.
DR PANTHER; PTHR23037:SF28; ERYTHROPOIETIN RECEPTOR; 1.
DR Pfam; PF09067; EpoR_lig-bind; 1.
DR PIRSF; PIRSF001959; EPO_receptor; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS01352; HEMATOPO_REC_L_F1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR001959-2};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Membrane {ECO:0000256|PIRNR:PIRNR001959, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|PIRNR:PIRNR001959};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..511
FT /note="Erythropoietin receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002344809"
FT TRANSMEM 251..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 147..247
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 383..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 117
FT /note="Required for ligand binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR001959-1"
FT SITE 371
FT /note="Interaction with APS and STAT5, and activation"
FT /evidence="ECO:0000256|PIRSR:PIRSR001959-1"
FT SITE 429
FT /note="Required for STAT5/PTPN11/SOCS3 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR001959-1"
FT SITE 457
FT /note="Interaction with PTPN6"
FT /evidence="ECO:0000256|PIRSR:PIRSR001959-1"
FT SITE 459
FT /note="Required for STAT1/STAT3 activation"
FT /evidence="ECO:0000256|PIRSR:PIRSR001959-1"
FT SITE 488
FT /note="Required for CrkL binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR001959-1"
FT DISULFID 52..62
FT /evidence="ECO:0000256|PIRSR:PIRSR001959-2"
FT DISULFID 91..107
FT /evidence="ECO:0000256|PIRSR:PIRSR001959-2"
SQ SEQUENCE 511 AA; 55558 MW; A45C651333DFCF44 CRC64;
MDHLGASLWP QVGSLCLLLA GAAWAPPPNL PDPKFESKAA LLVARGPEEL LCFTERLEDL
VCFWEEAASA GVGLDNYSFS YHLEDEPWKL CRLHQAPTAR GAVRFWCSLP TADTSSFVPL
ELRVTAASGA PRYHRIIHIN EVVLLDAPVG LVARLADEGG HIVLRWLPPP EAPMTSHIRY
EVDVLAGNGA GSVQRVEILE GRTECVLSNL RGRTRYTFAV RARMTEPSFG GFWSAWSEPV
SLLTPSDLDP LILTLSLILV LILVLLTVLA LLSHRRFNRA LKQKIWPGIP SPESEFEGLF
TTHKGNFQLW LYQNDGCLWW SPCTPFTEDP PASLEVLSER CWGTMQAVEP GTDDEGPLLE
PVGSGHAQDT YLVLDKWLLP QNPPIEDLPG PDGSVDTVAM DEGSEASSCS SALASKPSPE
GASAASFEYT ILDPSSQLLR PWALSPELPP TPPHLKYLYL VVSDSGISTD YSSGDSQGAQ
GGLSDGPYSN PYENSLIPAA EPLPPSYVAC S
//
