ID A0A2Y9N9J0_DELLE Unreviewed; 675 AA.
AC A0A2Y9N9J0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Lutropin-choriogonadotropic hormone receptor {ECO:0000256|ARBA:ARBA00022266, ECO:0000256|RuleBase:RU361222};
GN Name=LHCGR {ECO:0000256|RuleBase:RU361222,
GN ECO:0000313|RefSeq:XP_022429596.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022429596.1};
RN [1] {ECO:0000313|RefSeq:XP_022429596.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022429596.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Receptor for lutropin-choriogonadotropic hormone. The
CC activity of this receptor is mediated by G proteins which activate
CC adenylate cyclase. {ECO:0000256|RuleBase:RU361222}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|RuleBase:RU361222}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361222}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC FSH/LSH/TSH subfamily. {ECO:0000256|RuleBase:RU361222}.
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 RefSeq; XP_022429596.1; XM_022573888.2.
DR AlphaFoldDB; A0A2Y9N9J0; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004964; F:luteinizing hormone receptor activity; IEA:InterPro.
DR CDD; cd15359; 7tmA_LHCGR; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR002131; Gphrmn_rcpt_fam.
DR InterPro; IPR026906; LRR_5.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002273; LSH_rcpt.
DR PANTHER; PTHR24372; GLYCOPROTEIN HORMONE RECEPTOR; 1.
DR PANTHER; PTHR24372:SF1; LUTROPIN-CHORIOGONADOTROPIC HORMONE RECEPTOR; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF13306; LRR_5; 2.
DR PRINTS; PR00373; GLYCHORMONER.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01144; LSHRECEPTOR.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU361222};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040,
KW ECO:0000256|RuleBase:RU361222};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361222};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU361222};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|RuleBase:RU361222};
KW Sulfation {ECO:0000256|ARBA:ARBA00022641};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU361222};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361222};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361222}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT CHAIN 26..675
FT /note="Lutropin-choriogonadotropic hormone receptor"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT /id="PRO_5015797404"
FT TRANSMEM 340..361
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 373..394
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 417..438
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 459..482
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 502..527
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 548..570
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT TRANSMEM 582..602
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361222"
FT DOMAIN 352..599
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
SQ SEQUENCE 675 AA; 75611 MW; 826B852B22685FAD CRC64;
MGRWPPALRP LLLLLLLPPP PLTRAMRGEP CPEPCSCPPD GALRCPGPRA GLSRLSLTYL
PIKVIPSQAF RGLNEVIKIE ISQSDSLEKI EANAFDSLLN LSEILIQNTK NLVYIEPGAF
TNLPRLKYLS ICNTGIRKLP DVTKIFSSEF NFILEICDNL HITTVPGNAF QGMNNESITL
KLYGNGFEEI QSHAFNGTTL ISLDISSTKL QALPSYGLES IQTLIATSSY SLKRLPSRET
LTNLLDATLT YPSHCCAFRN MPTKEQNFSF SIFKNFSKQC ESTARRPNNE TLYSAIFAES
ELSGWDYDYG FCLPKTLQCA PEPDAFNPCE DIMGYDFLRV LIWLINILAI TGNVTVLFVL
LTSRYKLTVP RFLMCNLSFA DFCMGLYLLL IASVDAQTKG QYYNHAIDWQ TGSGCSAAGF
FTVFASELSV YTLTVITLER WHTITYAIQL DQKLRLKHAI PIMLGGWLFS TLIAMLPLVG
VSNYMKVSIC LPMDVENTLS QVYILTILMF NVVAFIVICA CYIKIYFAVQ NPELMATNKD
TKIAKKMAVL IFTDFTCMAP ISFFAISAAF KVPLITVTNS KVLLVLFYPV NSCANPFLYA
IFTKAFRRDF FLLLSKFGCC KYRAELYRRK DFSAYTSNCK NGFTGSNKPS QSTLKVTTLQ
CQYSAVLDKT CCKEC
//