ID A0A2K6LP48_RHIBE Unreviewed; 378 AA.
AC A0A2K6LP48;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Prolactin receptor {ECO:0000256|RuleBase:RU365035};
DE Short=PRL-R {ECO:0000256|RuleBase:RU365035};
GN Name=PRLR {ECO:0000256|RuleBase:RU365035,
GN ECO:0000313|Ensembl:ENSRBIP00000025276.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000025276.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000025276.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000025276.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: This is a receptor for the anterior pituitary hormone
CC prolactin. {ECO:0000256|RuleBase:RU365035}.
CC -!- SUBUNIT: Interacts with SMARCA1. Interacts with NEK3 and VAV2 and this
CC interaction is prolactin-dependent. {ECO:0000256|RuleBase:RU365035}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU365035}; Single-
CC pass type I membrane protein {ECO:0000256|RuleBase:RU365035}.
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:0000256|RuleBase:RU365035}.
CC -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC activation. {ECO:0000256|RuleBase:RU365035}.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 1
CC subfamily. {ECO:0000256|RuleBase:RU365035}.
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DR AlphaFoldDB; A0A2K6LP48; -.
DR Ensembl; ENSRBIT00000049185.1; ENSRBIP00000025276.1; ENSRBIG00000036512.1.
DR GeneTree; ENSGT00940000154851; -.
DR Proteomes; UP000233180; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR23036; CYTOKINE RECEPTOR; 1.
DR PANTHER; PTHR23036:SF86; PROLACTIN RECEPTOR; 1.
DR Pfam; PF09067; EpoR_lig-bind; 1.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR PROSITE; PS50853; FN3; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|RuleBase:RU365035}; Membrane {ECO:0000256|RuleBase:RU365035};
KW Metal-binding {ECO:0000256|RuleBase:RU365035};
KW Receptor {ECO:0000256|RuleBase:RU365035};
KW Reference proteome {ECO:0000313|Proteomes:UP000233180};
KW Signal {ECO:0000256|RuleBase:RU365035};
KW Transmembrane {ECO:0000256|RuleBase:RU365035};
KW Transmembrane helix {ECO:0000256|RuleBase:RU365035};
KW Zinc {ECO:0000256|RuleBase:RU365035}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU365035"
FT CHAIN 25..378
FT /note="Prolactin receptor"
FT /evidence="ECO:0000256|RuleBase:RU365035"
FT /id="PRO_5015375729"
FT TRANSMEM 237..258
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365035"
FT DOMAIN 129..229
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
SQ SEQUENCE 378 AA; 42926 MW; FCB6643A9ECA79EF CRC64;
MKENVVSATV FTLLLFLNTC LLNGQLPPGK PEIFKCRSPN KETFTCWWRP GTDGGLPTNY
SLTYHREGET LMHECPDYIT GGPNSCHFGK QYTSMWRTYI MMVNATNQMG SSFSDELYVD
VTYIVQPDPP LELTVEVKQP EDRKPYLWMK WSPPTLIDLK TGWFTLLYEI RLKPEKAAEW
ETHFAGQQTE FKILSLHPGQ KYLVQVRCKP DHGYWSAWSP ATFIQIPSDF IMNDTTVWIS
VAVLSAVICL IIVWAVALKG YSMVTCIFPP VPGPKIKGFD AHLLEKGKSE ELLSALGCQD
FPPTSDYEDL LVEYLEVDDS EDQHLMSVHS KEHPSQGDPL MLGVSHYKNL KSYSPRKISS
QGRLQPAVFT KAKLTTVQ
//
