ID   PRLR_ORENI              Reviewed;         630 AA.
AC   Q91513;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Prolactin receptor;
DE            Short=PRL-R;
DE   Flags: Precursor;
GN   Name=prlr;
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   PubMed=7597076; DOI=10.1073/pnas.92.13.6037;
RA   Sandra O., Sohm F., de Luze A., Prunet P., Edery M., Kelly P.A.;
RT   "Expression cloning of a cDNA encoding a fish prolactin receptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:6037-6041(1995).
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; L34783; AAA98997.1; -; mRNA.
DR   PIR; I51086; I51086.
DR   RefSeq; NP_001266477.1; NM_001279548.1.
DR   AlphaFoldDB; Q91513; -.
DR   SMR; Q91513; -.
DR   STRING; 8128.ENSONIP00000009724; -.
DR   GeneID; 100534586; -.
DR   KEGG; onl:100534586; -.
DR   CTD; 407651; -.
DR   eggNOG; ENOG502R22A; Eukaryota.
DR   InParanoid; Q91513; -.
DR   OrthoDB; 346239at2759; -.
DR   Proteomes; UP000005207; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 2.
DR   Gene3D; 2.60.40.10; -; 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; IPR033230; PRLR.
DR   PANTHER; PTHR23036:SF86; PTHR23036:SF86; 2.
DR   Pfam; PF09067; EpoR_lig-bind; 1.
DR   SMART; SM00060; FN3; 2.
DR   SUPFAM; SSF49265; SSF49265; 2.
DR   PROSITE; PS50853; FN3; 2.
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:0000250"
FT   CHAIN           24..630
FT                   /note="Prolactin receptor"
FT                   /id="PRO_0000010983"
FT   TOPO_DOM        24..234
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        259..630
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          31..128
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          130..230
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          339..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           216..220
FT                   /note="WSXWS motif"
FT   MOTIF           267..275
FT                   /note="Box 1 motif"
FT   COMPBIAS        367..382
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         212
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         213
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        37..47
FT                   /evidence="ECO:0000250"
FT   DISULFID        76..87
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   630 AA;  70811 MW;  A451563F3D12979D CRC64;
     MMTKVGEVLL LLLLPAFVPH TDGTHYSLPG KPTEIKCRSP EKETFTCWWK PGSDGGLPTT
     YALYYRKEGS DVVHECPDYH TAGKNSCFFN KNNTLIWVSY NITVVATNAL GKTYSDPQDI
     DVVYIVQPHP PEKLEVTVMK DQGWPFLRVS WEPPRKADTR SGWITLIYEL RVKLEDEESE
     WENHAAGQQK MFNIFSLRSG GTYLIQVRCK PDHGFWSEWS STSYVKVPEY LHREKSVWIL
     VLVFSAFILL LLTWLIHMNS HSLKHCMLPP VPGPKIKGFD KQLLKSGKSD EVFSALVVSD
     FPPTTSNYED LLVEYLEVYM PEQQELMVDK GKDHDGCLKS IGSASDSDSG RGSCDSDNLL
     MDKSGAPKEE QQQQNQEGDQ IGKETQGPKE AWEKEAMPCA NEDVVSPDAS SEKVKTWPSV
     FSPVTPYSPL DPHNSLEMHK QHCLSNTQFP PGSPSSDHYI KEALQSSYWE VCFNNNQPYP
     QTEVHPQLQA HSDRNISAVN DRNAPTGLLL PTRMTEYVEV QRVNEENKVL LHPIPSGHSR
     EKACPWVGQR DDYSKVKGVD SDNGLLLQRE VVEEESMEMA GAAESCYTSS IAFTTPKQTA
     CSPVALPVQD ERVLAVSGYV DTATVFSVHT