PRLR_RAT
ID PRLR_RAT Reviewed; 610 AA.
AC P05710; Q62832; Q63451; Q63479; Q63723; Q64274;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Prolactin receptor;
DE Short=PRL-R;
DE AltName: Full=Lactogen receptor;
DE Flags: Precursor;
GN Name=Prlr;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2293022; DOI=10.1210/mend-4-8-1136;
RA Shirota M., Banville D., Ali S., Jolicoeur C., Boutin J.-M., Edery M.,
RA Djiane J., Kelly P.A.;
RT "Expression of two forms of prolactin receptor in rat ovary and liver.";
RL Mol. Endocrinol. 4:1136-1143(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Sprague-Dawley; TISSUE=Ovary;
RX PubMed=2159291; DOI=10.1016/0006-291x(90)92337-y;
RA Zhang R., Buczko E., Tsai-Morris C.-H., Hu Z.Z., Dufau M.L.;
RT "Isolation and characterization of two novel rat ovarian lactogen receptor
RT cDNA species.";
RL Biochem. Biophys. Res. Commun. 168:415-422(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 281-610.
RA Banville D., Stocco R., Murthy K.K., Boie Y., Kelly P.A.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=2832068; DOI=10.1016/0092-8674(88)90488-6;
RA Boutin J.-M., Jolicoeur C., Okamura H., Gagnon J., Edery M., Shirota M.,
RA Banville D., Dusanter-Fourt I., Djiane J., Kelly P.A.;
RT "Cloning and expression of the rat prolactin receptor, a member of the
RT growth hormone/prolactin receptor gene family.";
RL Cell 53:69-77(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC TISSUE=Lymphoma;
RX PubMed=1718958; DOI=10.1016/s0021-9258(18)54897-3;
RA Ali S., Pelligrini I., Kelly P.A.;
RT "A prolactin-dependent immune cell line (Nb2) expresses a mutant form of
RT prolactin receptor.";
RL J. Biol. Chem. 266:20110-20117(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RX PubMed=7929319; DOI=10.1016/s0021-9258(18)47161-x;
RA O'Neal K.D., Yu-Lee L.Y.;
RT "Differential signal transduction of the short, Nb2, and long prolactin
RT receptors. Activation of interferon regulatory factor-1 and cell
RT proliferation.";
RL J. Biol. Chem. 269:26076-26082(1994).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 20-229 IN COMPLEX WITH PLACENTAL
RP LACTOGEN, AND DISULFIDE BONDS.
RX PubMed=10966654; DOI=10.1038/79047;
RA Elkins P.A., Christinger H.W., Sandowski Y., Sakal E., Gertler A.,
RA de Vos A.M., Kossiakoff A.A.;
RT "Ternary complex between placental lactogen and the extracellular domain of
RT the prolactin receptor.";
RL Nat. Struct. Biol. 7:808-815(2000).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Long;
CC IsoId=P05710-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=P05710-2; Sequence=VSP_001725, VSP_001726;
CC Name=3; Synonyms=Medium;
CC IsoId=P05710-3; Sequence=VSP_001727, VSP_001728;
CC Name=4; Synonyms=NB2;
CC IsoId=P05710-4; Sequence=VSP_001729;
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; M57668; AAA41938.1; -; mRNA.
DR EMBL; M34083; AAA79273.1; -; mRNA.
DR EMBL; L48060; AAA79274.1; -; mRNA.
DR EMBL; U34730; AAA92053.1; -; Genomic_DNA.
DR EMBL; M19304; AAA41937.1; -; mRNA.
DR EMBL; M74152; AAA41946.1; -; mRNA.
DR EMBL; U07567; AAA61784.1; -; mRNA.
DR PIR; A29884; A29884.
DR PIR; A34631; A34631.
DR PIR; A36116; A36116.
DR PIR; A41070; A41070.
DR PIR; B34631; B34631.
DR RefSeq; NP_001029283.1; NM_001034111.1.
DR RefSeq; NP_036762.1; NM_012630.2. [P05710-3]
DR PDB; 1F6F; X-ray; 2.30 A; B/C=20-229.
DR PDB; 3EW3; X-ray; 3.80 A; B/C=20-229.
DR PDB; 3NPZ; X-ray; 3.35 A; B/C=20-229.
DR PDBsum; 1F6F; -.
DR PDBsum; 3EW3; -.
DR PDBsum; 3NPZ; -.
DR AlphaFoldDB; P05710; -.
DR SMR; P05710; -.
DR BioGRID; 246816; 1.
DR MINT; P05710; -.
DR STRING; 10116.ENSRNOP00000056718; -.
DR GlyGen; P05710; 3 sites.
DR iPTMnet; P05710; -.
DR PhosphoSitePlus; P05710; -.
DR PaxDb; P05710; -.
DR Ensembl; ENSRNOT00000080786; ENSRNOP00000072948; ENSRNOG00000057557. [P05710-1]
DR Ensembl; ENSRNOT00000080974; ENSRNOP00000074428; ENSRNOG00000057557. [P05710-3]
DR GeneID; 24684; -.
DR KEGG; rno:24684; -.
DR CTD; 5618; -.
DR RGD; 3407; Prlr.
DR eggNOG; ENOG502R22A; Eukaryota.
DR GeneTree; ENSGT00940000154851; -.
DR InParanoid; P05710; -.
DR OrthoDB; 346239at2759; -.
DR PhylomeDB; P05710; -.
DR Reactome; R-RNO-1170546; Prolactin receptor signaling.
DR Reactome; R-RNO-982772; Growth hormone receptor signaling.
DR EvolutionaryTrace; P05710; -.
DR PRO; PR:P05710; -.
DR Proteomes; UP000002494; Chromosome 2.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005127; F:ciliary neurotrophic factor receptor binding; 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:0004923; F:leukemia inhibitory factor receptor activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017046; F:peptide hormone binding; ISO:RGD.
DR GO; GO:0004925; F:prolactin receptor activity; IMP:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0042976; P:activation of Janus kinase activity; ISO:RGD.
DR GO; GO:0007171; P:activation of transmembrane receptor protein tyrosine kinase activity; ISO:RGD.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0007595; P:lactation; ISO:RGD.
DR GO; GO:0060749; P:mammary gland alveolus development; ISO:RGD.
DR GO; GO:0060644; P:mammary gland epithelial cell differentiation; ISO:RGD.
DR GO; GO:0061180; P:mammary gland epithelium development; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0038165; P:oncostatin-M-mediated signaling pathway; IEA:GOC.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0060736; P:prostate gland growth; ISO:RGD.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; ISO:RGD.
DR GO; GO:0030155; P:regulation of cell adhesion; ISO:RGD.
DR GO; GO:0030856; P:regulation of epithelial cell differentiation; ISO:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR CDD; cd00063; FN3; 1.
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 Pfam; PF00041; fn3; 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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Membrane; Metal-binding; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..610
FT /note="Prolactin receptor"
FT /id="PRO_0000010981"
FT TOPO_DOM 20..229
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 230..253
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 254..610
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 22..122
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 124..224
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 317..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 210..214
FT /note="WSXWS motif"
FT MOTIF 262..270
FT /note="Box 1 motif"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..41
FT /evidence="ECO:0000269|PubMed:10966654"
FT DISULFID 70..81
FT /evidence="ECO:0000269|PubMed:10966654"
FT VAR_SEQ 131..150
FT /note="EVKQLKDKKTYLWVKWSPPT -> DYRWEVSCHQEALPKSAKLN (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:2159291"
FT /id="VSP_001725"
FT VAR_SEQ 151..610
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2159291"
FT /id="VSP_001726"
FT VAR_SEQ 281..310
FT /note="KGKSEELLSALGCQDFPPTSDCEDLLVEFL -> TGSPSKYKVDLYLALPGG
FT FQKLDNAGELDY (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:2832068"
FT /id="VSP_001727"
FT VAR_SEQ 311..610
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:2832068"
FT /id="VSP_001728"
FT VAR_SEQ 342..539
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:1718958,
FT ECO:0000303|PubMed:7929319"
FT /id="VSP_001729"
FT CONFLICT 236
FT /note="V -> A (in Ref. 2; AAA79273)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="G -> V (in Ref. 2; AAA79273)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="E -> K (in Ref. 1; AAA41938)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="Q -> E (in Ref. 2; AAA79273)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="A -> G (in Ref. 2; AAA79273)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="T -> M (in Ref. 1; AAA41938)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="Q -> K (in Ref. 2; AAA79273)"
FT /evidence="ECO:0000305"
FT STRAND 27..37
FT /evidence="ECO:0007829|PDB:1F6F"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:1F6F"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:1F6F"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:1F6F"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:1F6F"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:1F6F"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:1F6F"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:1F6F"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:1F6F"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1F6F"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:1F6F"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:1F6F"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:3NPZ"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:1F6F"
FT STRAND 161..171
FT /evidence="ECO:0007829|PDB:1F6F"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:1F6F"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:1F6F"
FT STRAND 196..208
FT /evidence="ECO:0007829|PDB:1F6F"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:1F6F"
SQ SEQUENCE 610 AA; 68599 MW; 83D04D832861295D CRC64;
MPSALAFVLL VLNISLLKGQ SPPGKPEIHK CRSPDKETFT CWWNPGTDGG LPTNYSLTYS
KEGEKTTYEC PDYKTSGPNS CFFSKQYTSI WKIYIITVNA TNQMGSSSSD PLYVDVTYIV
EPEPPRNLTL EVKQLKDKKT YLWVKWSPPT ITDVKTGWFT MEYEIRLKPE EAEEWEIHFT
GHQTQFKVFD LYPGQKYLVQ TRCKPDHGYW SRWSQESSVE MPNDFTLKDT TVWIIVAILS
AVICLIMVWA VALKGYSMMT CIFPPVPGPK IKGFDTHLLE KGKSEELLSA LGCQDFPPTS
DCEDLLVEFL EVDDNEDERL MPSHSKEYPG QGVKPTHLDP DSDSGHGSYD SHSLLSEKCE
EPQAYPPTLH IPEITEKPEN PEANIPPTVD PQSTNPNFHV DAPKSSTWPL LPGQHMPRSP
YHSVADVCKL AGSPVNTLDS FLDKAEENVL KLSKALETGE EEVAEQKGAK SFPSDKQNTP
WPLLQEKSPT VYVKPPDYVE IHKVNKDGVL SLFPKQRENN QTEKPGVPET SKEYAKVSGI
TDNNILVLVP DSRAQNTALL EESAKKAPPS FEADQSEKDL ASFTATSSNR RLQLGRLDYL
DPTCFMHSFH
