ID   PRLR_MELGA              Reviewed;         831 AA.
AC   Q91094; Q91091; Q91092;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Prolactin receptor;
DE            Short=PRL-R;
DE            Short=tPRLR;
DE   Flags: Precursor;
GN   Name=PRLR;
OS   Meleagris gallopavo (Wild turkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Meleagridinae; Meleagris.
OX   NCBI_TaxID=9103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   PubMed=8902221; DOI=10.1095/biolreprod55.5.1081;
RA   Zhou J.F., Zadworny D., Guemene D., Kuhnlein U.;
RT   "Molecular cloning, tissue distribution, and expression of the prolactin
RT   receptor during various reproductive states in Meleagris gallopavo.";
RL   Biol. Reprod. 55:1081-1090(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 82-121 AND 473-522.
RC   TISSUE=Ovary;
RA   Pitts G.R., You S.K., Foster D.N., el Halawani M.E.;
RL   Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This is a receptor for the anterior pituitary hormone
CC       prolactin.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
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.
CC   -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC       activation.
CC   -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; L76587; AAB01544.1; -; mRNA.
DR   EMBL; U22947; AAA75038.1; -; mRNA.
DR   EMBL; U22924; AAA75039.1; -; mRNA.
DR   RefSeq; NP_001290088.1; NM_001303159.1.
DR   AlphaFoldDB; Q91094; -.
DR   SMR; Q91094; -.
DR   PRIDE; Q91094; -.
DR   GeneID; 100126248; -.
DR   KEGG; mgp:100126248; -.
DR   CTD; 5618; -.
DR   InParanoid; Q91094; -.
DR   OrthoDB; 346239at2759; -.
DR   Proteomes; UP000001645; Unplaced.
DR   GO; GO:0044214; C:spanning component of plasma membrane; ISS:AgBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004925; F:prolactin receptor activity; IEA:InterPro.
DR   CDD; cd00063; FN3; 4.
DR   Gene3D; 2.60.40.10; -; 4.
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; IPR033230; PRLR.
DR   PANTHER; PTHR23036:SF86; PTHR23036:SF86; 3.
DR   Pfam; PF09067; EpoR_lig-bind; 2.
DR   Pfam; PF00041; fn3; 2.
DR   SMART; SM00060; FN3; 4.
DR   SUPFAM; SSF49265; SSF49265; 4.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS01352; HEMATOPO_REC_L_F1; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Membrane; Metal-binding; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW   Zinc.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..831
FT                   /note="Prolactin receptor"
FT                   /id="PRO_0000010986"
FT   TOPO_DOM        24..438
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        439..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        460..831
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          30..128
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          129..232
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          233..331
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          332..433
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          527..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          776..831
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           419..423
FT                   /note="WSXWS motif"
FT   MOTIF           471..479
FT                   /note="Box 1 motif"
FT   COMPBIAS        540..555
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        776..806
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         414
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         416
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        91
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        112
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        132
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        262
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        335
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        36..46
FT                   /evidence="ECO:0000250"
FT   DISULFID        75..86
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   831 AA;  94395 MW;  220916320F77FAC1 CRC64;
     MKQNLISSVQ IILLLPLTTV GLTSQSFPGK PKIIRCRSLE KETFSCWWKP GSDGGLPTNY
     TLFYSKDSEE KIYECPDYRT SGPNSCYFNR NYTNSWTTYN ITVTATNEIG SNSSDPQYVD
     VTSIVQPGSP VNLTLETQRY ANIMYLWAKW SPPLLADASS NHLYHYELRL KPEEKEEWET
     VPVGVQTQCK INRLNAGMRY VVQVRCMLDP GEWSEWSSER RILISGGLSP PEKPTITKCR
     SPEKETFTCW WKPGLDGGHP TNYTLLYSKE GEEQVYECPD YRTAGPNSCY FDKKHTSFWT
     VYNITVKATN EMGSNSSDPH YVDVTYIVQP DPPANVTLEL KKPINRKPYL MLTWSPPPLA
     DVRSGWLTLD YELRLKPEEG EEWETVFVGQ QTQYKMFSLN PGKKYIVQIH CKPDHHGSWS
     EWSSENYIEI PNDFRVKDMI VWIVLGVLSS LICLIMSWTM VLKGYRMITF ILPPVPGPKI
     KGIDTHLLET GKSEELLSAL GCHGFPPTSD CEELLIEYLE VEDSEDHQLM PSHDSGRPSK
     NAKITLKETD RDSGRGSCDS PSLLSEKCRE TCALPSALQI QDVRDVQAKK AGKRSWESYC
     VASERKALLF NNESAKSSTW PAVQLPNNQP PTFAYHSIVE ANKITSTTTN MNVAAVLVEN
     EERHQSLYSI SETISGGMEK QEEMENLHSK TTQTTVQVRQ NRSNEKLPFL NAALMDYVEV
     HKVRQDEEPT VLLKHKEKSG KIEKYTISGA SKEYTKVSTV MNHNILVLMP DSRVLHTPTS
     QEEPAKETSQ NPQQGQVETN MSYCMTAPRD CQREPSGSEY MDPSSFMPSF K