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Database: UniProt
Entry: A0A091G631_9AVES
LinkDB: A0A091G631_9AVES
Original site: A0A091G631_9AVES 
ID   A0A091G631_9AVES        Unreviewed;       644 AA.
AC   A0A091G631;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Lutropin-choriogonadotropic hormone receptor {ECO:0000256|ARBA:ARBA00022266, ECO:0000256|RuleBase:RU361222};
DE   Flags: Fragment;
GN   Name=LHCGR {ECO:0000256|RuleBase:RU361222};
GN   ORFNames=N303_12271 {ECO:0000313|EMBL:KFO77403.1};
OS   Cuculus canorus (common cuckoo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX   NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO77403.1, ECO:0000313|Proteomes:UP000053760};
RN   [1] {ECO:0000313|EMBL:KFO77403.1, ECO:0000313|Proteomes:UP000053760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO77403.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KL447819; KFO77403.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091G631; -.
DR   STRING; 55661.A0A091G631; -.
DR   Proteomes; UP000053760; Unassembled WGS sequence.
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; 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   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:UP000053760};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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   TRANSMEM        338..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   TRANSMEM        371..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   TRANSMEM        416..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   TRANSMEM        457..480
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   TRANSMEM        500..525
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   TRANSMEM        546..568
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   TRANSMEM        580..600
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361222"
FT   DOMAIN          350..597
FT                   /note="G-protein coupled receptors family 1 profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50262"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO77403.1"
FT   NON_TER         644
FT                   /evidence="ECO:0000313|EMBL:KFO77403.1"
SQ   SEQUENCE   644 AA;  72177 MW;  96357226DFDAB6FA CRC64;
     SFTHLPVKVI PSHAFEGLRD AFIIEISQSD SLERIEASAF DSLPTLSEIL ILNTKNLLHI
     EDGAFRNLPR LKYLSICNTG IRQFPDLTQI FSLEAHFILE LCDNLRMTTI PQNAFQGMNN
     ESLTLKLYKN GFEGIHSHAF NGTKLNQLIL KDNKNLRWIH NDALRGATGP DVLDISSTAL
     ESLPSYGLEA IQVLNATSSY SLKSLPPLDK FSSLLEAVLT YPSHCCAFRN LRTEKQNSLL
     SIFDNFSKEC ESTMRKPTNE ILDDSYNTSL WSAEKNSYQF ATDEETSPYS YSAIFDDSEM
     TNFDFEYDFC QPKILTCTPE PDAFNPCEDI LGYSFLRVLI WFINILAIAG NFTVLLVLIT
     SHYKLTVPRF LMCNLSFADF CMGLYLLLIA SVDAQTSGQY YNHAIDWQTG SGCSTAGFFT
     VFASELSVYT LTVITVERWH TITYAMQLDR KLRLRHAVPI MLGGWIFSIL IAALPLLGIS
     SYMKVSICLP MDIETGLSQA YILLILVLNV VAFIVICACY IKIYIAVQNP ELVAANKDTK
     IAKRMAILIF TDFTCMAPIS FFAISAAFKV PLITVTNSKI LLVLFYPVNS CANPFLYAIF
     TKAFQKLYRM NCFSTYTSNC KNGSSAAAPN KASQALLLLS VLEK
//
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