ID   PRLR_CEREL              Reviewed;         581 AA.
AC   Q28235;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Prolactin receptor;
DE            Short=PRL-R;
DE   Flags: Precursor;
GN   Name=PRLR;
OS   Cervus elaphus (Red deer).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC   Cervinae; Cervus.
OX   NCBI_TaxID=9860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=7561644; DOI=10.1677/joe.0.1460313;
RA   Clarke L.A., Edery M., Loudon A.S., Randall V.A., Postel-Vinay M.-C.,
RA   Kelly P.A., Jabbour H.N.;
RT   "Expression of the prolactin receptor gene during the breeding and non-
RT   breeding seasons in red deer (Cervus elaphus): evidence for the expression
RT   of two forms in the testis.";
RL   J. Endocrinol. 146:313-321(1995).
CC   -!- FUNCTION: This is a receptor for the anterior pituitary hormone
CC       prolactin.
CC   -!- SUBUNIT: Interacts with SMARCA1. Interacts with NEK3 and VAV2 and this
CC       interaction is prolactin-dependent. {ECO:0000250}.
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; X94953; CAA64419.1; -; mRNA.
DR   AlphaFoldDB; Q28235; -.
DR   SMR; Q28235; -.
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; Repeat;
KW   Signal; Transmembrane; Transmembrane helix; Zinc.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..581
FT                   /note="Prolactin receptor"
FT                   /id="PRO_0000010976"
FT   TOPO_DOM        25..234
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        259..581
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          27..127
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          129..229
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          321..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          462..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           215..219
FT                   /note="WSXWS motif"
FT   MOTIF           267..275
FT                   /note="Box 1 motif"
FT   COMPBIAS        321..349
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..487
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         211
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         212
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        132
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        233
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   581 AA;  65159 MW;  975E47CB63CF28EC CRC64;
     MKENVASRAV FILLLFLNAS LLNGQSPPGK PKIIKCRSPG KETFTCWWEP GSDGGLPTNY
     TLTYHKEGET LIHECPDYKT GGPNTCYFSK KHTSIWKIYV ITVNAINQMG VSSSDPLYVD
     VTYIVEPEPP ANLTLELKHP EDRKPYLWIK WFPPTLTDVK SGWFMIQYEI RLKPETAADW
     EIHFAAKQTQ LKIFSLYPGQ KYLVQVRCKP DHGYWSEWSP ESSIQIPNDF PVNDTTVWIF
     VAVLSAVICL IMVWAVALKG YSMMTCILPP VPGPKIKGFD IHLLEKGKSE ELLRALESQD
     FPPTSDCEDL LMEFIEVDDS EDQQLMPRPS KEHMEQGVKP MHMDPDSDSG RGSCDSPSLF
     SEKCDEPQAH PFKFYTPEDP EKLENPETNL TCLQAPQSTS REDKIPYFHA NGPKSSTWPF
     PQPPSLHNPR YSYHNIADVC ELALGMAGTT ATLLDQTDQH ALKPSKTIET GGEGKAAKQR
     ESEGCSSKPD QDTGWPLPQD KTPLISAKPL EYVEIHKVSQ DGVLALFPKQ NEKVGAPETS
     KEYSKVSRVT DSNILVLVPD TQVQNLTLLE EPAKEAPPAL P