PRLR_MOUSE
ID PRLR_MOUSE Reviewed; 608 AA.
AC Q08501; P15212; P15213; Q62099;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Prolactin receptor;
DE Short=PRL-R;
DE Flags: Precursor;
GN Name=Prlr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PRL-R3).
RC STRAIN=C3H/HeJ; TISSUE=Mammary gland;
RX PubMed=8262385; DOI=10.1016/0378-1119(93)90104-b;
RA Moore R.C., Oka T.;
RT "Cloning and sequencing of the cDNA encoding the murine mammary gland long-
RT form prolactin receptor.";
RL Gene 134:263-265(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PRL-R3).
RC STRAIN=Swiss Webster; TISSUE=Liver;
RX PubMed=8319571; DOI=10.1210/endo.133.1.8319571;
RA Clarke D.L., Linzer D.I.H.;
RT "Changes in prolactin receptor expression during pregnancy in the mouse
RT ovary.";
RL Endocrinology 133:224-232(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PRL-R3).
RA Sasaki M.;
RL Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PRL-R3).
RC STRAIN=BALB/cJ; TISSUE=Mammary gland;
RA Edery M., Pezet A., Nandi S., Kelly P.A.;
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PRL-R2 AND PRL-R1).
RC STRAIN=Swiss Webster; TISSUE=Liver;
RX PubMed=2725531; DOI=10.1210/mend-3-4-674;
RA Davis J.A., Linzer D.I.H.;
RT "Expression of multiple forms of the prolactin receptor in mouse liver.";
RL Mol. Endocrinol. 3:674-680(1989).
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 -!- INTERACTION:
CC Q08501; Q99490-2: AGAP2; Xeno; NbExp=2; IntAct=EBI-7737664, EBI-7737644;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=PRL-R3;
CC IsoId=Q08501-1; Sequence=Displayed;
CC Name=PRL-R1;
CC IsoId=Q08501-2; Sequence=VSP_001723, VSP_001724;
CC Name=PRL-R2;
CC IsoId=Q08501-3; Sequence=VSP_001721, VSP_001722;
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; L13593; AAC37641.1; -; mRNA.
DR EMBL; L14811; AAA02686.1; -; mRNA.
DR EMBL; D10214; BAA01066.1; -; mRNA.
DR EMBL; X73372; CAA51789.1; -; mRNA.
DR EMBL; M22959; AAA39977.1; -; mRNA.
DR EMBL; M22958; AAA39976.1; -; mRNA.
DR CCDS; CCDS27377.1; -. [Q08501-1]
DR CCDS; CCDS56975.1; -. [Q08501-2]
DR PIR; I53269; I53269.
DR PIR; I77524; I77524.
DR PIR; I77525; I77525.
DR RefSeq; NP_001240711.1; NM_001253782.2. [Q08501-2]
DR RefSeq; NP_035299.4; NM_011169.5. [Q08501-1]
DR RefSeq; XP_006520097.1; XM_006520034.3. [Q08501-1]
DR RefSeq; XP_006520098.1; XM_006520035.1. [Q08501-1]
DR RefSeq; XP_006520099.1; XM_006520036.1. [Q08501-1]
DR RefSeq; XP_006520100.1; XM_006520037.2. [Q08501-1]
DR RefSeq; XP_006520101.1; XM_006520038.1. [Q08501-2]
DR AlphaFoldDB; Q08501; -.
DR SMR; Q08501; -.
DR BioGRID; 202385; 6.
DR IntAct; Q08501; 3.
DR MINT; Q08501; -.
DR STRING; 10090.ENSMUSP00000122219; -.
DR GuidetoPHARMACOLOGY; 1721; -.
DR GlyGen; Q08501; 3 sites.
DR iPTMnet; Q08501; -.
DR PhosphoSitePlus; Q08501; -.
DR MaxQB; Q08501; -.
DR PaxDb; Q08501; -.
DR PRIDE; Q08501; -.
DR ProteomicsDB; 291814; -. [Q08501-1]
DR ProteomicsDB; 291815; -. [Q08501-2]
DR ProteomicsDB; 291816; -. [Q08501-3]
DR DNASU; 19116; -.
DR Ensembl; ENSMUST00000124470; ENSMUSP00000122219; ENSMUSG00000005268. [Q08501-1]
DR Ensembl; ENSMUST00000128450; ENSMUSP00000122209; ENSMUSG00000005268. [Q08501-3]
DR Ensembl; ENSMUST00000137867; ENSMUSP00000121935; ENSMUSG00000005268. [Q08501-3]
DR Ensembl; ENSMUST00000148257; ENSMUSP00000118355; ENSMUSG00000005268. [Q08501-2]
DR GeneID; 19116; -.
DR KEGG; mmu:19116; -.
DR UCSC; uc007vfw.2; mouse. [Q08501-3]
DR UCSC; uc007vfy.2; mouse. [Q08501-1]
DR UCSC; uc029snt.1; mouse. [Q08501-2]
DR CTD; 5618; -.
DR MGI; MGI:97763; Prlr.
DR VEuPathDB; HostDB:ENSMUSG00000005268; -.
DR eggNOG; ENOG502R22A; Eukaryota.
DR GeneTree; ENSGT00940000154851; -.
DR HOGENOM; CLU_017892_2_0_1; -.
DR InParanoid; Q08501; -.
DR OMA; YHYELRL; -.
DR PhylomeDB; Q08501; -.
DR TreeFam; TF330851; -.
DR Reactome; R-MMU-1170546; Prolactin receptor signaling.
DR Reactome; R-MMU-982772; Growth hormone receptor signaling.
DR BioGRID-ORCS; 19116; 6 hits in 72 CRISPR screens.
DR ChiTaRS; Prlr; mouse.
DR PRO; PR:Q08501; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q08501; protein.
DR Bgee; ENSMUSG00000005268; Expressed in choroid plexus epithelium and 149 other tissues.
DR ExpressionAtlas; Q08501; baseline and differential.
DR Genevisible; Q08501; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
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: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:MGI.
DR GO; GO:0004925; F:prolactin receptor activity; IDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0042976; P:activation of Janus kinase activity; ISO:MGI.
DR GO; GO:0007171; P:activation of transmembrane receptor protein tyrosine kinase activity; ISO:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0007595; P:lactation; IMP:MGI.
DR GO; GO:0060749; P:mammary gland alveolus development; IMP:MGI.
DR GO; GO:0060644; P:mammary gland epithelial cell differentiation; IGI:MGI.
DR GO; GO:0061180; P:mammary gland epithelium development; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
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; IMP:YuBioLab.
DR GO; GO:0060736; P:prostate gland growth; IMP:MGI.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IMP:MGI.
DR GO; GO:0030155; P:regulation of cell adhesion; IMP:MGI.
DR GO; GO:0030856; P:regulation of epithelial cell differentiation; IMP:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
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 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 Alternative splicing; Disulfide bond; Glycoprotein; Membrane;
KW Metal-binding; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..608
FT /note="Prolactin receptor"
FT /id="PRO_0000010978"
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..608
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 377..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..487
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 COMPBIAS 394..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..41
FT /evidence="ECO:0000250"
FT DISULFID 70..81
FT /evidence="ECO:0000250"
FT VAR_SEQ 281..303
FT /note="KGKSEELLSALGCQDFPPTSDCE -> LWCSILQLTSLVKIPTTEFLCDL
FT (in isoform PRL-R1)"
FT /evidence="ECO:0000303|PubMed:2725531"
FT /id="VSP_001723"
FT VAR_SEQ 281..292
FT /note="KGKSEELLSALG -> VHNKEQLENYVY (in isoform PRL-R2)"
FT /evidence="ECO:0000303|PubMed:2725531"
FT /id="VSP_001721"
FT VAR_SEQ 293..608
FT /note="Missing (in isoform PRL-R2)"
FT /evidence="ECO:0000303|PubMed:2725531"
FT /id="VSP_001722"
FT VAR_SEQ 304..608
FT /note="Missing (in isoform PRL-R1)"
FT /evidence="ECO:0000303|PubMed:2725531"
FT /id="VSP_001724"
FT CONFLICT 558
FT /note="L -> F (in Ref. 2; CAA51789)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 608 AA; 68241 MW; B8CE202B2EFC9FC6 CRC64;
MSSALAYMLL VLSISLLNGQ SPPGKPEIHK CRSPDKETFT CWWNPGSDGG LPTNYSLTYS
KEGEKNTYEC PDYKTSGPNS CFFSKQYTSI WKIYIITVNA TNEMGSSTSD PLYVDVTYIV
EPEPPRNLTL EVKQLKDKKT YLWVKWLPPT ITDVKTGWFT MEYEIRLKSE EADEWEIHFT
GHQTQFKVFD LYPGQKYLVQ TRCKPDHGYW SRWGQEKSIE IPNDFTLKDT TVWIIVAVLS
AVICLIMVWA VALKGYSMMT CIFPPVPGPK IKGFDTHLLE KGKSEELLSA LGCQDFPPTS
DCEDLLVEFL EVDDNEDERL MPSHSKEYPG QGVKPTHLDP DSDSGHGSYD SHSLLSEKCE
EPQAYPPAFH IPEITEKPEN PEANIPPTPN PQNNTPNCHT DTSKSTTWPL PPGQHTRRSP
YHSIADVCKL AGSPGDTLDS FLDKAEENVL KLSEDAGEEE VAVQEGAKSF PSDKQNTSWP
PLQEKGPIVY AKPPDYVEIH KVNKDGVLSL LPKQRENHQT ENPGVPETSK EYAKVSGVTD
NNILVLVPDS RAQNTALLEE SAKKVPPSLE QNQSEKDLAS FTATSSNCRL QLGRLDYLDP
TCFMHSFH
