PRLR_COLLI
ID PRLR_COLLI Reviewed; 830 AA.
AC Q90374;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Prolactin receptor;
DE Short=PRL-R;
DE Flags: Precursor;
GN Name=PRLR;
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cropsac;
RX PubMed=7516866; DOI=10.1210/endo.135.1.7516866;
RA Chen X., Horseman N.D.;
RT "Cloning, expression, and mutational analysis of the pigeon prolactin
RT receptor.";
RL Endocrinology 135:269-276(1994).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U07694; AAA20646.1; -; mRNA.
DR PIR; I50455; I50455.
DR RefSeq; NP_001269751.1; NM_001282822.1.
DR AlphaFoldDB; Q90374; -.
DR SMR; Q90374; -.
DR STRING; 8932.XP_005506057.1; -.
DR GeneID; 102086225; -.
DR KEGG; clv:102086225; -.
DR CTD; 5618; -.
DR eggNOG; ENOG502R22A; Eukaryota.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:AgBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004925; F:prolactin receptor activity; IEA:InterPro.
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; Repeat;
KW Signal; Transmembrane; Transmembrane helix; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..830
FT /note="Prolactin receptor"
FT /id="PRO_0000010985"
FT TOPO_DOM 24..439
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 461..830
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..228
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 231..331
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 333..434
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT MOTIF 420..424
FT /note="WSXWS motif"
FT MOTIF 472..480
FT /note="Box 1 motif"
FT BINDING 415
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 417
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 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
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 830 AA; 94507 MW; 3B074E83CDF69EFF CRC64;
MKQKLRSSVQ IILLFALTAV GLTGQSYPGK PKIIRCRSLE KETFSCWWKP GSDGGLPTNY
TLFYSKDSEE KIYECPDYGM SGPNSCYFDK NHTNPWTTYN ITVMAMNEIG SNSSDPQYVD
VTSIVQPDAP VNLSLETKTS ASTTYLLAKW SPPPLADVTS NSHVYRYELR LKPEEKEEWE
TVSVGVQTQY KVNRLQAGVK YVVQVRCVLD IGEWSEWSSE RHIHIPNGES PPEKPTIIKC
RSPEKETFTC WWKPGSDGGH PTNYTLLYSK EGEERVYECP DYKTAGPNSC YFDKKHTSFW
TIYNITVKAT NEIGSNVSDP LYVDVTYIVQ TDPPVNVTLE LKKTVNRKPY LVLTWSPPPL
ADVRSGWLTL DYELRLKPEE AEEWETIFVG QQTHYKMFSL NPGKKYIVQI HCKPDHHGSW
SEWSLEKYLQ IPTDFRIKDM VVWIIVGVLS SLICLVMSWT MVLKGYRMIA FILPPVPGPK
IKGIDTHLLE TGKSEELLSA LGCHGFPPTS DCEELLIEYL EVEDSEDQQL MPSHDNGHPS
KNAKMIAKET DSDSGRGSCD SPSLLSEKCR ESRAILSTLQ TQDIRDVQEN NGRRHWETQC
IASEQKILLF NNESTKSPIW PAAQLPDNQP PMFAYHSTVD VHKITLCTID VNIAPVLVEN
EEQHQPQYPI TETVHDNMEK HREVENLYSK TDQTTVQVKQ NRPNDKSPFS KPKLMDYVEV
HKVRQDEVAA VLLKHKENSG KIEKYTVPGT SKEYTKVSTV VDHNILVLMP DSRIQHIPVS
QEPAMEMSQN LQQGQTEKNM SYCLTVPSEC KRETSASEYM DPSSFIPAFK
