PRLR_BOVIN
ID PRLR_BOVIN Reviewed; 581 AA.
AC Q28172; O18880; O46591;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Prolactin receptor;
DE Short=PRL-R;
DE Flags: Precursor;
GN Name=PRLR;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORM LONG).
RC TISSUE=Endometrium;
RX PubMed=1338725; DOI=10.1016/0303-7207(92)90210-w;
RA Scott P., Kessler M.A., Schuler L.A.;
RT "Molecular cloning of the bovine prolactin receptor and distribution of
RT prolactin and growth hormone receptor transcripts in fetal and utero-
RT placental tissues.";
RL Mol. Cell. Endocrinol. 89:47-58(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), AND TISSUE SPECIFICITY.
RC TISSUE=Endometrium;
RX PubMed=9231767; DOI=10.1210/endo.138.8.5292;
RA Schuler L.A., Nagel R.J., Gao J., Horseman N.D., Kessler M.A.;
RT "Prolactin receptor heterogeneity in bovine fetal and maternal tissues.";
RL Endocrinology 138:3187-3194(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 25-234, AND PROTEIN SEQUENCE OF 25-33.
RC TISSUE=Mammary gland;
RX PubMed=7738463; DOI=10.1677/joe.0.1440393;
RA Tchelet A., Staten N.R., Creely D.P., Krivi G.G., Gertler A.;
RT "Extracellular domain of prolactin receptor from bovine mammary gland:
RT expression in Escherichia coli, purification and characterization of its
RT interaction with lactogenic hormones.";
RL J. Endocrinol. 144:393-403(1995).
RN [4]
RP ALTERNATIVE SPLICING.
RX PubMed=9343303; DOI=10.1677/jme.0.0190109;
RA Bignon C., Binart N., Ormandy C., Schuler L.A., Kelly P.A., Djiane J.;
RT "Long and short forms of the ovine prolactin receptor: cDNA cloning and
RT genomic analysis reveal that the two forms arise by different alternative
RT splicing mechanisms in ruminants and in rodents.";
RL J. Mol. Endocrinol. 19:109-120(1997).
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=2;
CC Name=Long;
CC IsoId=Q28172-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q28172-2; Sequence=VSP_001718, VSP_001719;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined; liver,
CC peripheral blood lymphocytes, endometrium, corpus luteum, intestine,
CC fetal thymus, fetal spleen, fetal liver and fetal brain.
CC {ECO:0000269|PubMed:9231767}.
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; L02549; AAA51417.1; -; mRNA.
DR EMBL; AF027403; AAB83999.1; -; mRNA.
DR EMBL; AF042780; AAB97748.1; -; Genomic_DNA.
DR EMBL; AF042780; AAB97747.1; ALT_SEQ; Genomic_DNA.
DR PIR; I45971; I45971.
DR RefSeq; NP_001034815.1; NM_001039726.2. [Q28172-1]
DR RefSeq; NP_776580.1; NM_174155.3. [Q28172-2]
DR AlphaFoldDB; Q28172; -.
DR SMR; Q28172; -.
DR STRING; 9913.ENSBTAP00000014437; -.
DR PaxDb; Q28172; -.
DR PRIDE; Q28172; -.
DR GeneID; 281422; -.
DR KEGG; bta:281422; -.
DR CTD; 5618; -.
DR eggNOG; ENOG502R22A; Eukaryota.
DR InParanoid; Q28172; -.
DR Proteomes; UP000009136; Unplaced.
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; IDA:AgBase.
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; IBA:GO_Central.
DR GO; GO:0004925; F:prolactin receptor activity; IBA:GO_Central.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
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 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 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 Alternative splicing; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Membrane; Metal-binding; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix; Zinc.
FT SIGNAL 1..24
FT /evidence="ECO:0000305|PubMed:7738463"
FT CHAIN 25..581
FT /note="Prolactin receptor"
FT /id="PRO_0000010975"
FT TOPO_DOM 25..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..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 324..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..499
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 324..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..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 DISULFID 36..46
FT /evidence="ECO:0000250"
FT DISULFID 75..86
FT /evidence="ECO:0000250"
FT VAR_SEQ 286..296
FT /note="KGKSEELLRAL -> ISQPSRLVSMF (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:9231767"
FT /id="VSP_001718"
FT VAR_SEQ 297..581
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:9231767"
FT /id="VSP_001719"
FT CONFLICT 120
FT /note="H -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="E -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="L -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="E -> H (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 156..157
FT /note="MT -> IM (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="L -> P (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 581 AA; 65153 MW; 7385C0D6956EE139 CRC64;
MKENAASRVV FILLLFLSVS LLNGQSPPEK PKLVKCRSPG KETFTCWWEP GADGGLPTNY
TLTYHKEGET LIHECPDYKT GGPNSCYFSK KHTSIWKMYV ITVNAINQMG ISSSDPLYVH
VTYIVEPEPP ANLTLELKHP EDRKPYLWIK WSPPTMTDVK SGWFIIQYEI RLKPEKATDW
ETHFTLKQTQ LKIFNLYPGQ KYLVQIRCKP DHGYWSEWSP ESSIQIPNDF PVKDTSMWIF
VAILSAVICL IMVWAVALKG YSMVTCILPP VPGPKIKGFD VHLLEKGKSE ELLRALESQD
FPPTSDCEDL LMEFIEVDDC EDQQLMPRPS KEHTEQGVKP MHLDLDSDSG RGSCDSPSLL
SEKCDEPQAH PSKFHTPEGP EKLENPETNL TCLQAPQSTS VEGKIPYFLA NGPKSSTWPF
PQPPSLYSPR YSYHNIADVC ELALGMAGTT ATSLDQTDQH ALKASKTIET GREGKATKQR
ESEGCSSKPD QDTVWPRPQD KTPLISAKPL EYVEIHKVSQ DGVLALFPKQ NEKFGAPEAS
KEYSKVSRVT DSNILVLVPD PQAQNLTLLE EPAKKAPPAL P
