ID K9N4F1_ANAPL Unreviewed; 627 AA.
AC K9N4F1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Prolactin receptor {ECO:0000256|ARBA:ARBA00019818, ECO:0000256|RuleBase:RU365035};
DE Short=PRL-R {ECO:0000256|RuleBase:RU365035};
GN Name=PRLR {ECO:0000256|RuleBase:RU365035};
OS Anas platyrhynchos (Mallard) (Anas boschas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839 {ECO:0000313|EMBL:AFY12624.1};
RN [1] {ECO:0000313|EMBL:AFY12624.1}
RP NUCLEOTIDE SEQUENCE.
RA Ji W., Duan X., Sun G., Dong B., Chen Z., Bian Y.;
RT "A novel prolactin receptor gene with only one ligand binding region and
RT tissue expression of the gene in the duck.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This is a receptor for the anterior pituitary hormone
CC prolactin. {ECO:0000256|RuleBase:RU365035}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU365035}; Single-
CC pass type I membrane protein {ECO:0000256|RuleBase:RU365035}.
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:0000256|RuleBase:RU365035}.
CC -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC activation. {ECO:0000256|RuleBase:RU365035}.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 1
CC subfamily. {ECO:0000256|ARBA:ARBA00007885,
CC ECO:0000256|RuleBase:RU365035}.
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DR EMBL; KC183720; AFY12624.1; -; mRNA.
DR AlphaFoldDB; K9N4F1; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004896; F:cytokine receptor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
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; PTHR23036; CYTOKINE RECEPTOR; 1.
DR PANTHER; PTHR23036:SF86; PROLACTIN RECEPTOR; 1.
DR Pfam; PF09067; EpoR_lig-bind; 1.
DR Pfam; PF00041; fn3; 1.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS01352; HEMATOPO_REC_L_F1; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|RuleBase:RU365035}; Membrane {ECO:0000256|RuleBase:RU365035};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU365035};
KW Receptor {ECO:0000256|RuleBase:RU365035, ECO:0000313|EMBL:AFY12624.1};
KW Signal {ECO:0000256|RuleBase:RU365035};
KW Transmembrane {ECO:0000256|RuleBase:RU365035};
KW Transmembrane helix {ECO:0000256|RuleBase:RU365035};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365035}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU365035"
FT CHAIN 25..627
FT /note="Prolactin receptor"
FT /evidence="ECO:0000256|RuleBase:RU365035"
FT /id="PRO_5015375378"
FT TRANSMEM 236..259
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365035"
FT DOMAIN 30..128
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 129..230
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 323..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 627 AA; 70782 MW; BC22A0957869E887 CRC64;
MKQELMSSIQ IILLLPLTAM GLTGQSYPGK PKIIRCRSLE KETFSCWWKP GSDGGLPTNY
TLFYSKDSEE KIYECPDYRT SGPNSCYFNK NHTNPWTTYN ITVTATNEIG SNSSDPHYVD
VTYIVQPDPP VNVTLELKKP MNRKPYLVLT WSPPPLADVR SGWLTLEYEL RLKPEEGEEW
ETIFVGQQTQ YKMFSLNPGK KYIVQIHCKP DHHGSWSEWS SEKYIQIPND FRVKDMIVWI
IVGVLSSLIC LIMSWTMVLK GYRMIAFILP PVPGPKIKGI DTHLLETGKS EELLSALGCH
GFPPTSDCEE LLIEYLEVED SEDQQLMPSH SNGNPSKKGK TTPKETDSDS GRGSCDSPSL
LSEKCRESHA LPSMLQTQDV RDVQENKAVK RSWGTQCVAS ERKTLLSNTE STKSSTWPAA
QLPDNQPPMF AYHSTVDARK ITLITTNVNV APVLVKNEEK HQSRYSVTET VPGDMEEQGE
MENLHSKTEQ TAVQVKQNRP NEKSPFLNGT LMDYVEVHKV KQDEEPAVLL KHKENSGKTE
DYTIPGTSKE YTKVSTVVDH NILVLMPDSR VQHTPMSQEP AKETSQNLQQ GQAEKNMSYC
LTAPSDCKRE TSGSEYMDPS SFMPSFK
//
