ID A0A3B4BJV9_9GOBI Unreviewed; 622 AA.
AC A0A3B4BJV9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Prolactin receptor {ECO:0000256|RuleBase:RU365035};
DE Short=PRL-R {ECO:0000256|RuleBase:RU365035};
GN Name=PRLR {ECO:0000256|RuleBase:RU365035};
OS Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000028802.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000028802.1}
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 -!- 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}.
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 AlphaFoldDB; A0A3B4BJV9; -.
DR Ensembl; ENSPMGT00000030664.1; ENSPMGP00000028802.1; ENSPMGG00000023032.1.
DR Proteomes; UP000261520; Unplaced.
DR GO; GO:0016020; C:membrane; 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; 2.
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 Transmembrane {ECO:0000256|RuleBase:RU365035};
KW Transmembrane helix {ECO:0000256|RuleBase:RU365035};
KW Zinc {ECO:0000256|RuleBase:RU365035}.
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365035"
FT DOMAIN 15..115
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 117..216
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
SQ SEQUENCE 622 AA; 70320 MW; CB69D717B1D2EFCC CRC64;
ILWKWSMRLI YSLGPPGKPT LTNCRSPEKE TFTCWWKPGP DGGLPTTYAL YYLKDNSETV
YECPDYHTAG RNSCFFNKNE TSVWVNYNIT VVATNKMGRT FSDPVDVDVA YIVQPHTPEN
VTVNVMEDEG WPFLRVSWES PHKADIRSGW ITLVYELRSK MEGEEEWEEH FPGQQKTFNI
FSVRSGSSYL VQVRCRPDHG FWSEWSPTTK TKVPKFFLGR SLWILILVFS ILVVLILAWI
IYMNCHSLKH SILPPVPGPK IKGFDHQRLK NGSYKDGLGA LMIPEYPPSS SSNDDDLLVE
YLEVFVTGEQ DISMEEGKEI QDHYCKSESS TCDSDSGHGS CDSHTLLIDK CKETSKDELN
SNCEDASEII ELEISQNNQD EKTLSYDGRP DTCNGRVKTW PSVFTPLPQY TLSAIPQKSS
LEIVKQHCLS DTLFPPGSMS SNLVNQNESF GPSYWEFSLN SKQLPQIHSQ SSKHLQAYSD
INISKKDNEI TTLFKSTQYV EVKNVNNKDM VLLQPVESGS QSHAEGCPHV HQGKDYSKVK
GVNSDKMLLL ESGVNVMGQE TATCFCDKSE TNAMKESGYM SSANVWKHKH PPMQTVLPVQ
EEQKPFAANG YVDTATMFSV PM
//
