ID   Q9IBF6_XENLA            Unreviewed;       611 AA.
AC   Q9IBF6;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   02-SEP-2026, entry version 114.
DE   RecName: Full=Prolactin receptor {ECO:0000256|ARBA:ARBA00019818, ECO:0000256|RuleBase:RU365035};
DE            Short=PRL-R {ECO:0000256|RuleBase:RU365035};
GN   Name=prlr.L {ECO:0000313|Xenbase:XB-GENE-6252888};
GN   Synonyms=PRLR {ECO:0000256|RuleBase:RU365035}, prlr
GN   {ECO:0000313|Xenbase:XB-GENE-6252888};
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 {ECO:0000313|EMBL:BAA90400.1};
RN   [1] {ECO:0000313|EMBL:BAA90400.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=10830440; DOI=10.1046/j.1440-169x.2000.00496.x;
RA   Yamamoto T., Nakayama Y., Tajima T., Abe S., Kawahara A.;
RT   "Cloning of a cDNA for Xenopus prolactin receptor and its metamorphic
RT   expression profile.";
RL   Dev. Growth Differ. 42:167-174(2000).
CC   -!- FUNCTION: This is a receptor for the anterior pituitary hormone
CC       prolactin. {ECO:0000256|RuleBase:RU365035}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC       ECO:0000256|RuleBase:RU365035}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479, 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; AB030443; BAA90400.1; -; mRNA.
DR   RefSeq; NP_001079085.1; NM_001085616.1.
DR   AlphaFoldDB; Q9IBF6; -.
DR   GeneID; 373618; -.
DR   KEGG; xla:373618; -.
DR   AGR; Xenbase:XB-GENE-6252888; -.
DR   CTD; 373618; -.
DR   Xenbase; XB-GENE-6252888; prlr.L.
DR   OrthoDB; 8858139at2759; -.
DR   Bgee; 373618; Expressed in zone of skin and 12 other cell types or tissues.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043235; C:signaling receptor complex; IBA:GO_Central.
DR   GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
DR   GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR   CDD; cd00063; FN3; 1.
DR   FunFam; 2.60.40.10:FF:000287; Prolactin receptor; 1.
DR   FunFam; 2.60.40.10:FF:000358; Prolactin receptor; 1.
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   InterPro; IPR050379; Type-I_Cytokine_Rcpt.
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; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   PROSITE; PS50853; FN3; 1.
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};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365035};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU365035};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU365035};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU365035};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU365035};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU365035};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365035}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|RuleBase:RU365035"
FT   CHAIN           28..611
FT                   /note="Prolactin receptor"
FT                   /evidence="ECO:0000256|RuleBase:RU365035"
FT                   /id="PRO_5047589410"
FT   TRANSMEM        235..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365035"
FT   DOMAIN          132..229
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          335..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   611 AA;  68315 MW;  7E0DF76F21D8CE97 CRC64;
     MPQNLAPTTP SVAVTFLLFL YTVSLNAQSL PGKPVIDKCR SYEKVTFSCW WKPGSDGGLP
     TNYSLLYRKE NDPKIYECPD YVTSGLNSCF FDKAHTSFWI FYHIYVNATN ALGSNVSDEE
     SVDTTYIVQP YPPTNVSLAV ESGHHDLLLK WLPPAMVDVQ SGWLTLKYEV RYKEEKEQEW
     EAHLVGNQLK LKLFGLTPGG NYVVQVRCKP DSGHWSEWST ESYIQIPGGG KKTDLTLWIS
     IGALSAVICL TMIWTMALKR CSLMSCILPP VPGPKIMGFD TQLLKSGKSD ELLSALGCQS
     FPPTSDYDDL LVEFLEVDDS KQHLIASRDQ SQQKQNIKVC PADTDNDSGR GSCDSPFSHS
     EGCKELRNLQ PGVDSTDRGI HDHWPPQNTV MDGSFTNFSD NKSNMWPDVP STGNQISKSS
     YQDIKDITNL AISAMTASQH ELLIPCNDKN QLRCFKTIEI IDEEKTTKPS DFEDLRSKGV
     EADTVHLVPN DKPPFLPARM MDYVEVHKVS QNNALALIPK HNENSVRTDQ YSVLVPNREY
     TKVERVEGNN VLVLMQEMVN QVNPVTIEST KLKFQQSQSA NPMNMFSLAQ NGESRTQAGG
     MGYMDPSAFL S
//