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Database: UniProt
Entry: A0A3B3ZSU9_9GOBI
LinkDB: A0A3B3ZSU9_9GOBI
Original site: A0A3B3ZSU9_9GOBI 
ID   A0A3B3ZSU9_9GOBI        Unreviewed;       499 AA.
AC   A0A3B3ZSU9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Erythropoietin receptor {ECO:0000256|ARBA:ARBA00018355};
OS   Periophthalmus magnuspinnatus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX   NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000007610.1, ECO:0000313|Proteomes:UP000261520};
RN   [1] {ECO:0000313|Ensembl:ENSPMGP00000007610.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   AlphaFoldDB; A0A3B3ZSU9; -.
DR   Ensembl; ENSPMGT00000008096.1; ENSPMGP00000007610.1; ENSPMGG00000005658.1.
DR   Proteomes; UP000261520; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
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   PANTHER; PTHR23037; CYTOKINE RECEPTOR; 1.
DR   PANTHER; PTHR23037:SF28; ERYTHROPOIETIN RECEPTOR; 1.
DR   Pfam; PF09067; EpoR_lig-bind; 1.
DR   Pfam; PF00041; fn3; 1.
DR   PIRSF; PIRSF001959; EPO_receptor; 1.
DR   SMART; SM00060; FN3; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   PROSITE; PS50853; FN3; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR001959-2};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        221..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          118..216
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          409..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        30..40
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001959-2"
FT   DISULFID        65..81
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001959-2"
SQ   SEQUENCE   499 AA;  56686 MW;  847BD38D94AF8D67 CRC64;
     MSATRSNKAG TGQQSIMSML LHEESKNPKC FAESRKDLTC FWEENEKAGS VDQYSFVYKY
     HESKCPLKAF HLTSGRKLYV CHLNQTQLFV QMDIEVNRDG HLIHNRSLLI ESTFLLDPPA
     NVTVSNGAKP GQVNISWIPP PVKYMDDSMM YEVFYSPMDS HIGKVEVARA SSELVLRGLQ
     PATRYKVQVR VNLDGVSYSG YWSAWSDPVF ILTPPADLDP LIISLSVIIS FIFLVLSLTM
     LVSHRRYLLK KVWPTIPTPE NKFQGLFTIY GGDFQKWLGH TDGDLWQSPN VFYPEEGPSP
     LEVLSELPVS PLLQCPPLPP KGCRVPQEVK TEMDMGPSLQ REDSTQSEDW TTKSHDHWLM
     ERLQALQQHP IPYSQESQDT YVTLSHNNNE DVQDSIPVEN VPLEVLFTSR KESESPSDLG
     SGSGQLSSQS SFEYSNQEWA HKPPGYTYMA VADSGVSMDY SSMNRLEDIG RVPVFTHEYK
     NDIALRRAFV TRQHHVHNY
//
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