PRLR_PIG
ID PRLR_PIG Reviewed; 625 AA.
AC Q6JTA8; O46679; Q6JTA9; Q6JTB0;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Prolactin receptor;
DE Short=PRL-R;
DE Flags: Precursor;
GN Name=PRLR {ECO:0000312|EMBL:AAQ76843.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1] {ECO:0000312|EMBL:AAQ76843.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Landrace, and Yucatan;
RA Trott J.F., Hovey R.C.;
RT "Cloning and characterization of multiple forms of the pig (Sus scrofa)
RT prolactin receptor.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 531-625.
RX PubMed=9321486; DOI=10.1007/s003359900576;
RA Vincent A.L., Wang L., Tuggle C.K., Robic A., Rothschild M.F.;
RT "Prolactin receptor maps to pig chromosome 16.";
RL Mamm. Genome 8:793-794(1997).
CC -!- FUNCTION: This is a receptor for the anterior pituitary hormone
CC prolactin. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SMARCA1. Interacts with NEK3 and VAV2 and this
CC interaction is prolactin-dependent. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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. {ECO:0000250}.
CC -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC activation. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 1
CC subfamily. {ECO:0000305}.
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DR EMBL; AY308824; AAQ76841.1; -; mRNA.
DR EMBL; AY308825; AAQ76842.1; -; mRNA.
DR EMBL; AY308826; AAQ76843.1; -; mRNA.
DR EMBL; U96306; AAC02897.1; -; Genomic_DNA.
DR RefSeq; NP_001001868.1; NM_001001868.1.
DR RefSeq; XP_013840184.1; XM_013984730.1.
DR AlphaFoldDB; Q6JTA8; -.
DR SMR; Q6JTA8; -.
DR STRING; 9823.ENSSSCP00000028480; -.
DR PaxDb; Q6JTA8; -.
DR PRIDE; Q6JTA8; -.
DR Ensembl; ENSSSCT00045046488; ENSSSCP00045032262; ENSSSCG00045026954.
DR GeneID; 414916; -.
DR KEGG; ssc:414916; -.
DR CTD; 5618; -.
DR eggNOG; ENOG502R22A; Eukaryota.
DR HOGENOM; CLU_017892_2_0_1; -.
DR InParanoid; Q6JTA8; -.
DR OrthoDB; 346239at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; Q6JTA8; SS.
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; 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 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..625
FT /note="Prolactin receptor"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010979"
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..625
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..128
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 325..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..601
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 325..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 104
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|UniProtKB:P16471"
FT DISULFID 75..86
FT /evidence="ECO:0000250|UniProtKB:P16471"
FT CONFLICT 372
FT /note="P -> R (in Ref. 1; AAQ76842)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="L -> P (in Ref. 1; AAQ76842)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="A -> G (in Ref. 1; AAQ76842)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="K -> R (in Ref. 1; AAQ76842)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="M -> L (in Ref. 1; AAQ76842)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="G -> S (in Ref. 1; AAQ76842)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="S -> G (in Ref. 1; AAQ76843)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 625 AA; 69573 MW; 751B2B593ABFC51B CRC64;
MKENVPSTVV FILLLFLNIS LLNGQSPPGK PEIFKCRSPE KETFTCWWKP GADGGLPTNY
TLTYHKEGET FTHECPDYKT GGPNSCYFNK KHTSIWTIYI ITVNATNQMG SSSSDPRYVD
VTYIVEPDPP VNLTLELKKP EDQKPYLWIK WLPPTLVDVR SGWLTLQYEI RLQPEKTAEW
ETHFAGQQTQ FKILSLYPGQ KYLVQVRCKP DHGFWSEWSP ESSIQIPNDF SMKDTTMWIF
VAILSAVVCL IMIWAVALKG YSMVACILPP VPGPKIKGFD THLLEKGKSE ELLSALGCQD
FPPTSDCEDL LVEFLEVDDS EDQQLMPAHS KEHPSQGRKP THLDPDSDSG RGSCDSPSLL
SEKCDEPRAN PPKFHTPEGI EKPGDPETNL PRPQDPQSTS VESKLLYFHA DGSKSSTWPL
PQPPILHDPG SSYHNLADVG QLVLGTAGAT AALLEKTDRH AFNPPKTTET GGEGRATEQK
ESESFHSKTD QGTVWLLPQD KGPFVSPKPM EYVEIHKVSK DGALALLPKQ QENGDRPEKA
GAPETSKEYA QVSRVMDNHI LVLVQDPRAR NVAPFEEPTK ETPPSRPQNP AAKDLASFTT
APGHCRHPLG GLDYLDPAGF MHSFQ
