ID A0A2K6BK97_MACNE Unreviewed; 288 AA.
AC A0A2K6BK97;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:ENSMNEP00000011816.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000011816.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000011816.1}
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; A0A2K6BK97; -.
DR Ensembl; ENSMNET00000036009.1; ENSMNEP00000011816.1; ENSMNEG00000030216.1.
DR GeneTree; ENSGT00940000154851; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000030216; Expressed in adult mammalian kidney and 6 other cell types or tissues.
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:UP000233120};
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..288
FT /note="Prolactin receptor"
FT /evidence="ECO:0000256|RuleBase:RU365035"
FT /id="PRO_5015371592"
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 288 AA; 32836 MW; DFBE1830750AC5EF CRC64;
MKENVISATV FTLLLFLNTC LLNGQLPPGK PEIFKCRSPN KETFTCWWRP GTDGGLPTNY
SLTYHREGET LMHECPDYIT GGPNSCHFGK QYTSMWRTYV MMVNATNQMG SSFSDELYVD
VTYIVQPDPP LELTVEVKQP EDRKPYLWMK WSPPTLIDLK TGWFTLLYEI RLKPEKAAEW
ETHFAGQQTE FKILSLHPGQ KYLVQVRCKP DHGYWSAWSP ATFIQIPSDF IMNDTTVWIS
VAVLSAVICL IIVWAVALKG YSMVTCIFPP VPGPKIKGFD AHLLEVTP
//
