PRLR_CHICK
ID PRLR_CHICK Reviewed; 831 AA.
AC Q04594;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Prolactin receptor;
DE Short=PRL-R;
DE Short=cPRLR;
DE Flags: Precursor;
GN Name=PRLR;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn; TISSUE=Kidney;
RX PubMed=1445292; DOI=10.1016/0006-291x(92)91082-2;
RA Tanaka M., Maeda K., Okubo T., Nakashima K.;
RT "Double antenna structure of chicken prolactin receptor deduced from the
RT cDNA sequence.";
RL Biochem. Biophys. Res. Commun. 188:490-496(1992).
CC -!- FUNCTION: This is a receptor for the anterior pituitary hormone
CC prolactin.
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; D13154; BAA02439.1; -; mRNA.
DR PIR; JQ1655; JQ1655.
DR RefSeq; NP_990185.1; NM_204854.1.
DR AlphaFoldDB; Q04594; -.
DR SMR; Q04594; -.
DR STRING; 9031.ENSGALP00000038374; -.
DR GeneID; 395660; -.
DR KEGG; gga:395660; -.
DR CTD; 5618; -.
DR VEuPathDB; HostDB:geneid_395660; -.
DR eggNOG; ENOG502R22A; Eukaryota.
DR InParanoid; Q04594; -.
DR OrthoDB; 346239at2759; -.
DR PhylomeDB; Q04594; -.
DR PRO; PR:Q04594; -.
DR Proteomes; UP000000539; 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; TAS: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; 4.
DR Gene3D; 2.60.40.10; -; 4.
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; 3.
DR Pfam; PF09067; EpoR_lig-bind; 2.
DR Pfam; PF00041; fn3; 2.
DR SMART; SM00060; FN3; 4.
DR SUPFAM; SSF49265; SSF49265; 4.
DR PROSITE; PS50853; FN3; 4.
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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..831
FT /note="Prolactin receptor"
FT /id="PRO_0000010984"
FT TOPO_DOM 24..438
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..831
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..128
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 129..227
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 230..331
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 332..433
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 527..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 419..423
FT /note="WSXWS motif"
FT MOTIF 471..479
FT /note="Box 1 motif"
FT COMPBIAS 539..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 414
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 416
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 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
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 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
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 831 AA; 94102 MW; 1C4E75791DCADBE9 CRC64;
MKQDLISSVQ IILFLPLTTV GLAGQSFPGK PKIIRCRSLE KETFSCWWKP GSDGGLPTNY
TLFYSKDSEE EIYECPDYRT SGPNSCYFNK NHTSPWTTFN ITVTATNEIG SNSSDPQYVD
VTSIVQPGSP VNLTLETKRS ANIMYLWAKW SPPLLADASS NHLYHYELRI KPEEKEEWET
ISVGVQTQCK INRLNAGMRY VVQVRCTLDP GEWSEWSSER HILIPSGQSP PEKPTIIKCR
SPEKETFTCW WKPGLDGGHP TNYTLLYSKE GEEQVYECPD YRTAGPNSCY FDKKHTSFWT
IYNITVRATN EMGSNSSDPH YVDVTYIVQP DPPVNVTLEL KKPINRKPYL VLTWSPPPLA
DVRSGWLTLE YELRLKPEEG EEWETIFVGQ QTQYKMFSLN PGKKYIIQIH CKPDHHGSWS
EWSSENYIQI PNDFRVKDMI VWIVLGVLSS LICLIMSWTM VLKGYRMITF MLPPVPGPKI
KGIDTHLLET GKSEELLSAL GCHGLPPTSD CEELLIEYLE VEDSEDQQLM PSHDNGHPSK
NAKITRKETD SDSGRGSCDS PSLLSEKCRE TCALPPVLQT QEVRDVQEKK AAKRSWETQY
VASERKALLS NSESAKSSTW PAVQLPNSQP PMFAYHSIVD AHKITLNTTN TNVAAVLVED
EEEHQSQCSL TETIPGEMEK QGEMENLHSK TEQTTAQVKQ NRSNERLPFL DAALMDYVEV
HKVIRQDEEP AVLLKHKENS GKIEKYTISG ASKEYTKVST VMDHNILVLM PDSRVPHTPA
SQEPAKETSQ SLQQGQVEKN MSYCLTAPSD CKRETGGSEY MDPSSFMPSF K
