ID   LSHR_RAT       STANDARD;      PRT;   700 AA.
AC   P16235; P70646; Q63807; Q63808; Q63809;
DT   01-APR-1990 (Rel. 14, Created)
DT   01-APR-1990 (Rel. 14, Last sequence update)
DT   01-OCT-2000 (Rel. 40, Last annotation update)
DE   LUTROPIN-CHORIOGONADOTROPIC HORMONE RECEPTOR PRECURSOR (LH/CG-R)
DE   (LSH-R) (LUTEINIZING HORMONE RECEPTOR).
GN   LHCGR.
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE=89332512; PubMed=2502842;
RA   McFarland K.C., Sprengel R., Phillips H.S., Koehler M.,
RA   Rosemblit N., Nikolics K., Segaloff D.L., Seeburg P.H.;
RT   "Lutropin-choriogonadotropin receptor: an unusual member of the G
RT   protein-coupled receptor family.";
RL   Science 245:494-499(1989).
RN   [2]
RP   SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING.
RC   STRAIN=SPRAGUE-DAWLEY; TISSUE=Ovary;
RX   MEDLINE=92347604; PubMed=1353463;
RA   Aatsinki J.T., Pietila E.M., Lakkakorpi J.T., Rajaniemi H.J.;
RT   "Expression of the LH/CG receptor gene in rat ovarian tissue is
RT   regulated by an extensive alternative splicing of the primary
RT   transcript.";
RL   Mol. Cell. Endocrinol. 84:127-135(1992).
RN   [3]
RP   SEQUENCE FROM N.A.
RX   MEDLINE=91209270; PubMed=2019252;
RA   Koo Y.B., Slaughter R.G., Ji T.H.;
RT   "Structure of the luteinizing hormone receptor gene and multiple
RT   exons of the coding sequence.";
RL   Endocrinology 128:2297-2308(1991).
RN   [4]
RP   SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING.
RX   MEDLINE=91006819; PubMed=1976554;
RA   Bernard M.P., Myers R.V., Moyle W.R.;
RT   "Cloning of rat lutropin (LH) receptor analogs lacking the soybean
RT   lectin domain.";
RL   Mol. Cell. Endocrinol. 71:R19-R23(1990).
RN   [5]
RP   SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING.
RX   MEDLINE=91126285; PubMed=2281186;
RA   Segaloff D.L., Sprengel R., Nikolics K., Ascoli M.;
RT   "Structure of the lutropin/choriogonadotropin receptor.";
RL   Recent Prog. Horm. Res. 46:261-303(1990).
RN   [6]
RP   SEQUENCE OF 295-700 FROM N.A.
RX   MEDLINE=91060531; PubMed=2174034;
RA   Tsai-Morris C.H., Buczko E., Wang W., Dufau M.L.;
RT   "Intronic nature of the rat luteinizing hormone receptor gene defines
RT   a soluble receptor subspecies with hormone binding activity.";
RL   J. Biol. Chem. 265:19385-19388(1990).
RN   [7]
RP   SEQUENCE OF 27-37.
RX   MEDLINE=89174723; PubMed=2925659;
RA   Roche P.C., Ryan R.J.;
RT   "Purification, characterization, and amino-terminal sequence of rat
RT   ovarian receptor for luteinizing hormone/human choriogonadotropin.";
RL   J. Biol. Chem. 264:4636-4641(1989).
RN   [8]
RP   MUTAGENESIS.
RX   MEDLINE=91332007; PubMed=1714448;
RA   Ji I., Ji T.H.;
RT   "Asp383 in the second transmembrane domain of the lutropin receptor
RT   is important for high affinity hormone binding and cAMP production.";
RL   J. Biol. Chem. 266:14953-14957(1991).
CC   -!- FUNCTION: RECEPTOR FOR LUTROPIN-CHORIOGONADOTROPIC HORMONE.
CC       THE ACTIVITY OF THIS RECEPTOR IS MEDIATED BY G PROTEINS WHICH
CC       ACTIVATE ADENYLATE CYCLASE.
CC   -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN.
CC   -!- ALTERNATIVE PRODUCTS: AT LEAST 11 ISOFORMS WHICH DIFFER IN
CC       SUBCELLULAR LOCATION ARE PRODUCED BY ALTERNATIVE SPLICING
CC       OF THE SAME GENE.
CC   -!- SIMILARITY: BELONGS TO FAMILY 1 OF G-PROTEIN COUPLED RECEPTORS.
CC       FSH/LSH/TSH SUBFAMILY.
CC   -!- SIMILARITY: CONTAINS 7 LEUCINE-RICH REPEATS (LRR).
CC   --------------------------------------------------------------------------
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CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
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CC   or send an email to license@isb-sib.ch).
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DR   EMBL; M26199; AAA41528.1; -.
DR   EMBL; M61212; AAA41527.1; -.
DR   EMBL; M61211; AAA41527.1; JOINED.
DR   EMBL; S40803; AAB22680.1; -.
DR   EMBL; S40787; AAB22680.1; JOINED.
DR   EMBL; S40903; AAB22680.1; JOINED.
DR   EMBL; S40904; AAB22680.1; JOINED.
DR   EMBL; S40905; AAB22680.1; JOINED.
DR   EMBL; S40907; AAB22680.1; JOINED.
DR   EMBL; S40909; AAB22680.1; JOINED.
DR   EMBL; S40918; AAB22680.1; JOINED.
DR   EMBL; S40920; AAB22680.1; JOINED.
DR   EMBL; S40795; AAB22680.1; JOINED.
DR   EMBL; S40798; AAB22680.1; JOINED.
DR   EMBL; S40795; AAB22681.1; -.
DR   EMBL; S40787; AAB22681.1; JOINED.
DR   EMBL; S40903; AAB22681.1; JOINED.
DR   EMBL; S40904; AAB22681.1; JOINED.
DR   EMBL; S40905; AAB22681.1; JOINED.
DR   EMBL; S40907; AAB22681.1; JOINED.
DR   EMBL; S40909; AAB22681.1; JOINED.
DR   EMBL; S40918; AAB22681.1; JOINED.
DR   EMBL; S40920; AAB22681.1; JOINED.
DR   EMBL; S40803; AAB22682.2; -.
DR   EMBL; S40787; AAB22682.2; JOINED.
DR   EMBL; S40903; AAB22682.2; JOINED.
DR   EMBL; S40907; AAB22682.2; JOINED.
DR   EMBL; S40909; AAB22682.2; JOINED.
DR   EMBL; S40918; AAB22682.2; JOINED.
DR   EMBL; S40920; AAB22682.2; JOINED.
DR   EMBL; S40795; AAB22682.2; JOINED.
DR   EMBL; S40798; AAB22682.2; JOINED.
DR   EMBL; S40803; AAB22683.1; -.
DR   EMBL; S40787; AAB22683.1; JOINED.
DR   EMBL; S40903; AAB22683.1; JOINED.
DR   EMBL; S40904; AAB22683.1; JOINED.
DR   EMBL; S40905; AAB22683.1; JOINED.
DR   EMBL; S40907; AAB22683.1; JOINED.
DR   EMBL; S40909; AAB22683.1; JOINED.
DR   EMBL; S40918; AAB22683.1; JOINED.
DR   EMBL; S40920; AAB22683.1; JOINED.
DR   EMBL; S40795; AAB22683.1; JOINED.
DR   EMBL; S40798; AAB22683.1; JOINED.
DR   EMBL; S40803; AAB22684.2; -.
DR   EMBL; S40787; AAB22684.2; JOINED.
DR   EMBL; S40903; AAB22684.2; JOINED.
DR   EMBL; S40904; AAB22684.2; JOINED.
DR   EMBL; S40905; AAB22684.2; JOINED.
DR   EMBL; S40909; AAB22684.2; JOINED.
DR   EMBL; S40918; AAB22684.2; JOINED.
DR   EMBL; S40920; AAB22684.2; JOINED.
DR   EMBL; S40795; AAB22684.2; JOINED.
DR   EMBL; S40798; AAB22684.2; JOINED.
DR   EMBL; M68928; AAA41529.1; -.
DR   EMBL; M68917; AAA41529.1; JOINED.
DR   EMBL; M68918; AAA41529.1; JOINED.
DR   EMBL; M68919; AAA41529.1; JOINED.
DR   EMBL; M68920; AAA41529.1; JOINED.
DR   EMBL; M68921; AAA41529.1; JOINED.
DR   EMBL; M68922; AAA41529.1; JOINED.
DR   EMBL; M68923; AAA41529.1; JOINED.
DR   EMBL; M68925; AAA41529.1; JOINED.
DR   EMBL; M68926; AAA41529.1; JOINED.
DR   EMBL; M68927; AAA41529.1; JOINED.
DR   PIR; A32460; A32460.
DR   PIR; A41343; A41343.
DR   HSSP; P22888; 1LUT.
DR   GCRDb; GCR_0138; -.
DR   GCRDb; GCR_0139; -.
DR   GCRDb; GCR_0262; -.
DR   GCRDb; GCR_0612; -.
DR   GCRDb; GCR_0613; -.
DR   GCRDb; GCR_0614; -.
DR   InterPro; IPR000276; -.
DR   InterPro; IPR001611; -.
DR   InterPro; IPR002131; -.
DR   InterPro; IPR002273; -.
DR   Pfam; PF00001; 7tm_1; 1.
DR   Pfam; PF00560; LRR; 2.
DR   PRINTS; PR00373; GLYCHORMONER.
DR   PRINTS; PR01144; LSHRECEPTOR.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
KW   G-protein coupled receptor; Transmembrane; Glycoprotein; Signal;
KW   Phosphorylation; Repeat; Leucine-rich repeat; Alternative splicing.
FT   SIGNAL        1     26
FT   CHAIN        27    700       LUTROPIN-CHORIOGONADOTROPIC HORMONE
FT                                RECEPTOR.
FT   DOMAIN       27    362       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    363    390       1 (POTENTIAL).
FT   DOMAIN      391    399       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM    400    422       2 (POTENTIAL).
FT   DOMAIN      423    443       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    444    466       3 (POTENTIAL).
FT   DOMAIN      467    486       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM    487    509       4 (POTENTIAL).
FT   DOMAIN      510    529       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    530    551       5 (POTENTIAL).
FT   DOMAIN      552    574       CYTOPLASMIC (POTENTIAL).
FT   TRANSMEM    575    598       6 (POTENTIAL).
FT   DOMAIN      599    609       EXTRACELLULAR (POTENTIAL).
FT   TRANSMEM    610    631       7 (POTENTIAL).
FT   DOMAIN      632    700       CYTOPLASMIC (POTENTIAL).
FT   REPEAT       52     75       LRR 1.
FT   REPEAT      126    150       LRR 2.
FT   REPEAT      152    175       LRR 3.
FT   REPEAT      176    200       LRR 4.
FT   REPEAT      202    224       LRR 5.
FT   REPEAT      225    248       LRR 6.
FT   REPEAT      250    271       LRR 7.
FT   DISULFID    443    518       BY SIMILARITY.
FT   CARBOHYD    103    103       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    178    178       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    199    199       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    295    295       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    303    303       N-LINKED (GLCNAC...) (POTENTIAL).
FT   CARBOHYD    317    317       N-LINKED (GLCNAC...) (POTENTIAL).
FT   VARSPLIC     83    132       MISSING (IN ISOFORM 1950).
FT   VARSPLIC    133    157       MISSING (IN ISOFORM 1759).
FT   VARSPLIC    184    700       MISSING (IN ISOFORM C2).
FT   VARSPLIC    232    251       DISSTKLQALPSHGLESIQT -> PCRATGWSPFRRSSPC
FT                                LPTH (IN ISOFORM 2075).
FT   VARSPLIC    232    293       MISSING (IN ISOFORM E/A2, ISOFORM EB AND
FT                                ISOFORM B1).
FT   VARSPLIC    252    700       MISSING (IN ISOFORM 2075).
FT   VARSPLIC    294    367       QNFSFSIFENFSKQCESTVRKADNETLYSAIFEENELSGW
FT                                DYDYGFCSPKTLQCAPEPDAFNPCEDIMGYAFLR ->
FT                                IFHFPFLKTSPNNAKAQLEKQITRRFIPPSLRRMNSVAGI
FT                                MIMASVHPRHSNVLQNQMLSTPVKILWAMPSLGS (IN
FT                                ISOFORM B1 AND ISOFORM B3).
FT   VARSPLIC    294    294       Q -> P (IN ISOFORM C1).
FT   VARSPLIC    295    700       MISSING (IN ISOFORM C1).
FT   VARSPLIC    321    342       YSAIFEENELSGWDYDYGFCSP -> LHGALPAAHCLRGLP
FT                                NKRPVL (IN ISOFORM 1834, ISOFORM 1759 AND
FT                                ISOFORM EB).
FT   VARSPLIC    343    700       MISSING (IN ISOFORMS 1834, ISOFORM 1759
FT                                AND ISOFORM EB).
FT   VARSPLIC    368    700       MISSING (IN ISOFORM B1 AND ISOFORM B3).
FT   VARIANT      82     82       I -> M (IN ISOFORM 1950).
FT   VARIANT     179    179       E -> G (IN ISOFORM 1759).
FT   VARIANT     233    233       I -> T (IN ISOFORM 1950).
FT   VARIANT     646    646       G -> S (IN ISOFORM 1950).
FT   MUTAGEN     409    409       D->N: SIGNIFICANT REDUCTION OF BINDING.
FT   MUTAGEN     436    436       D->N: NO CHANGE IN BINDING OR CAMP PROD.
FT   MUTAGEN     455    455       E->Q: NO CHANGE IN BINDING OR CAMP PROD.
FT   MUTAGEN     582    582       D->N: NO CHANGE IN BINDING OR CAMP PROD.
FT   CONFLICT     33     33       R -> L (IN REF. 7).
SQ   SEQUENCE   700 AA;  78035 MW;  31807E73BAC94F1F CRC64;
     MGRRVPALRQ LLVLAVLLLK PSQLQSRELS GSRCPEPCDC APDGALRCPG PRAGLARLSL
     TYLPVKVIPS QAFRGLNEVV KIEISQSDSL ERIEANAFDN LLNLSELLIQ NTKNLLYIEP
     GAFTNLPRLK YLSICNTGIR TLPDVTKISS SEFNFILEIC DNLHITTIPG NAFQGMNNES
     VTLKLYGNGF EEVQSHAFNG TTLISLELKE NIYLEKMHSG AFQGATGPSI LDISSTKLQA
     LPSHGLESIQ TLIALSSYSL KTLPSKEKFT SLLVATLTYP SHCCAFRNLP KKEQNFSFSI
     FENFSKQCES TVRKADNETL YSAIFEENEL SGWDYDYGFC SPKTLQCAPE PDAFNPCEDI
     MGYAFLRVLI WLINILAIFG NLTVLFVLLT SRYKLTVPRF LMCNLSFADF CMGLYLLLIA
     SVDSQTKGQY YNHAIDWQTG SGCGAAGFFT VFASELSVYT LTVITLERWH TITYAVQLDQ
     KLRLRHAIPI MLGGWLFSTL IATMPLVGIS NYMKVSICLP MDVESTLSQV YILSILILNV
     VAFVVICACY IRIYFAVQNP ELTAPNKDTK IAKKMAILIF TDFTCMAPIS FFAISAAFKV
     PLITVTNSKI LLVLFYPVNS CANPFLYAIF TKAFQRDFLL LLSRFGCCKR RAELYRRKEF
     SAYTSNCKNG FPGASKPSQA TLKLSTVHCQ QPIPPRALTH
//
