ID LSHR_RAT Reviewed; 700 AA. AC P16235; P70646; Q63807; Q63808; Q63809; Q6LDI7; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 12-OCT-2022, entry version 184. DE RecName: Full=Lutropin-choriogonadotropic hormone receptor; DE Short=LH/CG-R; DE AltName: Full=Luteinizing hormone receptor; DE Short=LSH-R; DE Flags: Precursor; GN Name=Lhcgr; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2502842; DOI=10.1126/science.2502842; RA McFarland K.C., Sprengel R., Phillips H.S., Koehler M., Rosemblit N., RA Nikolics K., Segaloff D.L., Seeburg P.H.; RT "Lutropin-choriogonadotropin receptor: an unusual member of the G protein- RT coupled receptor family."; RL Science 245:494-499(1989). RN [2] RP NUCLEOTIDE SEQUENCE, AND ALTERNATIVE SPLICING. RC STRAIN=Sprague-Dawley; TISSUE=Ovary; RX PubMed=1353463; DOI=10.1016/0303-7207(92)90079-l; 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 regulated RT by an extensive alternative splicing of the primary transcript."; RL Mol. Cell. Endocrinol. 84:127-135(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2019252; DOI=10.1210/endo-128-5-2297; RA Koo Y.B., Slaughter R.G., Ji T.H.; RT "Structure of the luteinizing hormone receptor gene and multiple exons of RT the coding sequence."; RL Endocrinology 128:2297-2308(1991). RN [4] RP NUCLEOTIDE SEQUENCE, AND ALTERNATIVE SPLICING. RX PubMed=1976554; DOI=10.1016/0303-7207(90)90034-6; RA Bernard M.P., Myers R.V., Moyle W.R.; RT "Cloning of rat lutropin (LH) receptor analogs lacking the soybean lectin RT domain."; RL Mol. Cell. Endocrinol. 71:R19-R23(1990). RN [5] RP NUCLEOTIDE SEQUENCE, AND ALTERNATIVE SPLICING. RX PubMed=2281186; DOI=10.1016/b978-0-12-571146-3.50014-6; RA Segaloff D.L., Sprengel R., Nikolics K., Ascoli M.; RT "Structure of the lutropin/choriogonadotropin receptor."; RL Recent Prog. Horm. Res. 46:261-301(1990). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-320. RC TISSUE=Liver; RX PubMed=2040640; DOI=10.1016/s0021-9258(18)99170-2; RA Tsai-Morris C.H., Buczko E., Wang W., Xie X.-Z., Dufau M.L.; RT "Structural organization of the rat luteinizing hormone (LH) receptor RT gene."; RL J. Biol. Chem. 266:11355-11359(1991). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 295-700. RX PubMed=2174034; DOI=10.1016/s0021-9258(17)45380-4; RA Tsai-Morris C.H., Buczko E., Wang W., Dufau M.L.; RT "Intronic nature of the rat luteinizing hormone receptor gene defines a RT soluble receptor subspecies with hormone binding activity."; RL J. Biol. Chem. 265:19385-19388(1990). RN [8] RP PROTEIN SEQUENCE OF 27-44. RX PubMed=2601325; DOI=10.1016/0022-4731(89)90482-2; RA Dufau M.L., Minegishi T., Buczko E.S., Delgado C.J., Zhang R.; RT "Characterization and structure of ovarian and testicular LH/hCG RT receptors."; RL J. Steroid Biochem. 33:715-720(1989). RN [9] RP PROTEIN SEQUENCE OF 27-37. RX PubMed=2925659; DOI=10.1016/s0021-9258(18)83790-5; RA Roche P.C., Ryan R.J.; RT "Purification, characterization, and amino-terminal sequence of rat ovarian RT receptor for luteinizing hormone/human choriogonadotropin."; RL J. Biol. Chem. 264:4636-4641(1989). RN [10] RP MUTAGENESIS OF ASP-409; ASP-436; GLU-455 AND ASP-582. RX PubMed=1714448; DOI=10.1016/s0021-9258(18)98570-4; RA Ji I., Ji T.H.; RT "Asp383 in the second transmembrane domain of the lutropin receptor is RT important for high affinity hormone binding and cAMP production."; RL J. Biol. Chem. 266:14953-14957(1991). RN [11] RP PALMITOYLATION AT CYS-647 AND CYS-648, AND MUTAGENESIS OF CYS-647 AND RP CYS-648. RX PubMed=7776964; DOI=10.1210/mend.9.2.7776964; RA Zhu H., Wang H., Ascoli M.; RT "The lutropin/choriogonadotropin receptor is palmitoylated at intracellular RT cysteine residues."; RL Mol. Endocrinol. 9:141-150(1995). CC -!- FUNCTION: Receptor for lutropin-choriogonadotropic hormone. The CC activity of this receptor is mediated by G proteins which activate CC adenylate cyclase. {ECO:0000250|UniProtKB:P22888}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P22888}; CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P22888}. Secreted. CC Note=Some isoforms may be secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=11; CC Comment=Additional isoforms seem to exist.; CC Name=1; CC IsoId=P16235-1; Sequence=Displayed; CC Name=1759; CC IsoId=P16235-2; Sequence=VSP_001969, VSP_001977, VSP_001978; CC Name=1834; CC IsoId=P16235-3; Sequence=VSP_001977, VSP_001978; CC Name=1950; CC IsoId=P16235-4; Sequence=VSP_001968; CC Name=2075; CC IsoId=P16235-5; Sequence=VSP_001971, VSP_001973; CC Name=C1; CC IsoId=P16235-6; Sequence=VSP_001975, VSP_001976; CC Name=C2; CC IsoId=P16235-7; Sequence=VSP_001970; CC Name=EA2; CC IsoId=P16235-8; Sequence=VSP_001972; CC Name=EB; CC IsoId=P16235-9; Sequence=VSP_001972, VSP_001977, VSP_001978; CC Name=B1; CC IsoId=P16235-10; Sequence=VSP_001972, VSP_001974, VSP_001979; CC Name=B3; CC IsoId=P16235-11; Sequence=VSP_001974, VSP_001979; CC -!- PTM: Sulfated. {ECO:0000250|UniProtKB:P22888}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC FSH/LSH/TSH subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}. CC -!- WEB RESOURCE: Name=Sequence-structure-function-analysis of glycoprotein CC hormone receptors; CC URL="http://www.ssfa-gphr.de/"; 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 EMBL; M26199; AAA41528.1; -; mRNA. DR EMBL; M61212; AAA41527.1; -; Genomic_DNA. DR EMBL; M61211; AAA41527.1; JOINED; Genomic_DNA. DR EMBL; S40803; AAB22680.1; -; Genomic_DNA. DR EMBL; S40787; AAB22680.1; JOINED; Genomic_DNA. DR EMBL; S40903; AAB22680.1; JOINED; Genomic_DNA. DR EMBL; S40904; AAB22680.1; JOINED; Genomic_DNA. DR EMBL; S40905; AAB22680.1; JOINED; Genomic_DNA. DR EMBL; S40907; AAB22680.1; JOINED; Genomic_DNA. DR EMBL; S40909; AAB22680.1; JOINED; Genomic_DNA. DR EMBL; S40918; AAB22680.1; JOINED; Genomic_DNA. DR EMBL; S40920; AAB22680.1; JOINED; Genomic_DNA. DR EMBL; S40795; AAB22680.1; JOINED; Genomic_DNA. DR EMBL; S40798; AAB22680.1; JOINED; Genomic_DNA. DR EMBL; S40795; AAB22681.1; -; Genomic_DNA. DR EMBL; S40787; AAB22681.1; JOINED; Genomic_DNA. DR EMBL; S40903; AAB22681.1; JOINED; Genomic_DNA. DR EMBL; S40904; AAB22681.1; JOINED; Genomic_DNA. DR EMBL; S40905; AAB22681.1; JOINED; Genomic_DNA. DR EMBL; S40907; AAB22681.1; JOINED; Genomic_DNA. DR EMBL; S40909; AAB22681.1; JOINED; Genomic_DNA. DR EMBL; S40918; AAB22681.1; JOINED; Genomic_DNA. DR EMBL; S40920; AAB22681.1; JOINED; Genomic_DNA. DR EMBL; S40803; AAB22682.2; -; Genomic_DNA. DR EMBL; S40787; AAB22682.2; JOINED; Genomic_DNA. DR EMBL; S40903; AAB22682.2; JOINED; Genomic_DNA. DR EMBL; S40907; AAB22682.2; JOINED; Genomic_DNA. DR EMBL; S40909; AAB22682.2; JOINED; Genomic_DNA. DR EMBL; S40918; AAB22682.2; JOINED; Genomic_DNA. DR EMBL; S40920; AAB22682.2; JOINED; Genomic_DNA. DR EMBL; S40795; AAB22682.2; JOINED; Genomic_DNA. DR EMBL; S40798; AAB22682.2; JOINED; Genomic_DNA. DR EMBL; S40803; AAB22683.1; -; Genomic_DNA. DR EMBL; S40787; AAB22683.1; JOINED; Genomic_DNA. DR EMBL; S40903; AAB22683.1; JOINED; Genomic_DNA. DR EMBL; S40904; AAB22683.1; JOINED; Genomic_DNA. DR EMBL; S40905; AAB22683.1; JOINED; Genomic_DNA. DR EMBL; S40907; AAB22683.1; JOINED; Genomic_DNA. DR EMBL; S40909; AAB22683.1; JOINED; Genomic_DNA. DR EMBL; S40918; AAB22683.1; JOINED; Genomic_DNA. DR EMBL; S40920; AAB22683.1; JOINED; Genomic_DNA. DR EMBL; S40795; AAB22683.1; JOINED; Genomic_DNA. DR EMBL; S40798; AAB22683.1; JOINED; Genomic_DNA. DR EMBL; S40803; AAB22684.2; -; Genomic_DNA. DR EMBL; S40787; AAB22684.2; JOINED; Genomic_DNA. DR EMBL; S40903; AAB22684.2; JOINED; Genomic_DNA. DR EMBL; S40904; AAB22684.2; JOINED; Genomic_DNA. DR EMBL; S40905; AAB22684.2; JOINED; Genomic_DNA. DR EMBL; S40909; AAB22684.2; JOINED; Genomic_DNA. DR EMBL; S40918; AAB22684.2; JOINED; Genomic_DNA. DR EMBL; S40920; AAB22684.2; JOINED; Genomic_DNA. DR EMBL; S40795; AAB22684.2; JOINED; Genomic_DNA. DR EMBL; S40798; AAB22684.2; JOINED; Genomic_DNA. DR EMBL; M68928; AAA41529.1; -; Genomic_DNA. DR EMBL; M68917; AAA41529.1; JOINED; Genomic_DNA. DR EMBL; M68918; AAA41529.1; JOINED; Genomic_DNA. DR EMBL; M68919; AAA41529.1; JOINED; Genomic_DNA. DR EMBL; M68920; AAA41529.1; JOINED; Genomic_DNA. DR EMBL; M68921; AAA41529.1; JOINED; Genomic_DNA. DR EMBL; M68922; AAA41529.1; JOINED; Genomic_DNA. DR EMBL; M68923; AAA41529.1; JOINED; Genomic_DNA. DR EMBL; M68925; AAA41529.1; JOINED; Genomic_DNA. DR EMBL; M68926; AAA41529.1; JOINED; Genomic_DNA. DR EMBL; M68927; AAA41529.1; JOINED; Genomic_DNA. DR EMBL; AH004953; AAB42193.1; -; Genomic_DNA. DR PIR; A49744; A49744. DR PIR; I57668; I57668. DR PIR; I77461; I77461. DR RefSeq; NP_037110.1; NM_012978.1. [P16235-1] DR AlphaFoldDB; P16235; -. DR SMR; P16235; -. DR STRING; 10116.ENSRNOP00000022481; -. DR BindingDB; P16235; -. DR ChEMBL; CHEMBL2456; -. DR DrugCentral; P16235; -. DR GlyGen; P16235; 6 sites. DR iPTMnet; P16235; -. DR PhosphoSitePlus; P16235; -. DR SwissPalm; P16235; -. DR PaxDb; P16235; -. DR Ensembl; ENSRNOT00000022481; ENSRNOP00000022481; ENSRNOG00000016712. [P16235-1] DR Ensembl; ENSRNOT00000096915; ENSRNOP00000089069; ENSRNOG00000016712. [P16235-2] DR Ensembl; ENSRNOT00000098297; ENSRNOP00000079785; ENSRNOG00000016712. [P16235-8] DR GeneID; 25477; -. DR KEGG; rno:25477; -. DR UCSC; RGD:3007; rat. [P16235-1] DR CTD; 3973; -. DR RGD; 3007; Lhcgr. DR eggNOG; KOG2087; Eukaryota. DR GeneTree; ENSGT00940000157364; -. DR InParanoid; P16235; -. DR OrthoDB; 257031at2759; -. DR PhylomeDB; P16235; -. DR Reactome; R-RNO-375281; Hormone ligand-binding receptors. DR PRO; PR:P16235; -. DR Proteomes; UP000002494; Chromosome 6. DR GO; GO:0005737; C:cytoplasm; IDA:RGD. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD. DR GO; GO:0005768; C:endosome; IDA:RGD. DR GO; GO:0005615; C:extracellular space; IDA:RGD. DR GO; GO:0005887; C:integral component of plasma membrane; IDA:RGD. DR GO; GO:0031233; C:intrinsic component of external side of plasma membrane; IDA:RGD. DR GO; GO:0005764; C:lysosome; IDA:RGD. DR GO; GO:0005634; C:nucleus; IDA:RGD. DR GO; GO:0005886; C:plasma membrane; IDA:RGD. DR GO; GO:0043235; C:receptor complex; IDA:RGD. DR GO; GO:0051117; F:ATPase binding; IPI:RGD. DR GO; GO:0038106; F:choriogonadotropin hormone binding; ISO:RGD. DR GO; GO:0035472; F:choriogonadotropin hormone receptor activity; ISO:RGD. DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IDA:RGD. DR GO; GO:0042802; F:identical protein binding; IDA:RGD. DR GO; GO:0004964; F:luteinizing hormone receptor activity; ISS:UniProtKB. DR GO; GO:0017046; F:peptide hormone binding; IDA:RGD. DR GO; GO:0007190; P:activation of adenylate cyclase activity; IDA:RGD. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:RGD. DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IDA:RGD. DR GO; GO:0050482; P:arachidonic acid secretion; IDA:RGD. DR GO; GO:0071371; P:cellular response to gonadotropin stimulus; ISO:RGD. DR GO; GO:0071373; P:cellular response to luteinizing hormone stimulus; ISS:UniProtKB. DR GO; GO:0007417; P:central nervous system development; IEP:RGD. DR GO; GO:0050890; P:cognition; ISO:RGD. DR GO; GO:0046544; P:development of secondary male sexual characteristics; ISO:RGD. DR GO; GO:0008585; P:female gonad development; ISO:RGD. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD. DR GO; GO:0009755; P:hormone-mediated signaling pathway; IDA:RGD. DR GO; GO:0042700; P:luteinizing hormone signaling pathway; IDA:RGD. DR GO; GO:0008584; P:male gonad development; ISO:RGD. DR GO; GO:0001541; P:ovarian follicle development; ISO:RGD. DR GO; GO:0022602; P:ovulation cycle process; ISO:RGD. DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:RGD. DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IDA:RGD. DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IDA:RGD. DR GO; GO:0046886; P:positive regulation of hormone biosynthetic process; IDA:RGD. DR GO; GO:0032962; P:positive regulation of inositol trisphosphate biosynthetic process; ISO:RGD. DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IDA:RGD. DR GO; GO:0006622; P:protein targeting to lysosome; IMP:RGD. DR GO; GO:0050810; P:regulation of steroid biosynthetic process; IEP:RGD. DR GO; GO:0090030; P:regulation of steroid hormone biosynthetic process; ISO:RGD. DR GO; GO:0034699; P:response to luteinizing hormone; IDA:CAFA. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD. DR GO; GO:0072520; P:seminiferous tubule development; ISO:RGD. DR GO; GO:0007283; P:spermatogenesis; ISO:RGD. DR GO; GO:0060065; P:uterus development; ISO:RGD. DR Gene3D; 3.80.10.10; -; 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 Pfam; PF00001; 7tm_1; 1. DR Pfam; PF13306; LRR_5; 2. DR PRINTS; PR00373; GLYCHORMONER. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR01144; LSHRECEPTOR. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Direct protein sequencing; KW Disulfide bond; G-protein coupled receptor; Glycoprotein; KW Leucine-rich repeat; Lipoprotein; Membrane; Palmitate; Receptor; KW Reference proteome; Repeat; Secreted; Signal; Sulfation; Transducer; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..26 FT /evidence="ECO:0000269|PubMed:2601325, FT ECO:0000269|PubMed:2925659" FT CHAIN 27..700 FT /note="Lutropin-choriogonadotropic hormone receptor" FT /id="PRO_0000012783" FT TOPO_DOM 27..362 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 363..390 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 391..399 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 400..422 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 423..443 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 444..466 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 467..486 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 487..509 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 510..529 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 530..551 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 552..574 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 575..598 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 599..609 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 610..631 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 632..700 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 126..150 FT /note="LRR 1" FT REPEAT 152..175 FT /note="LRR 2" FT REPEAT 176..200 FT /note="LRR 3" FT REPEAT 202..224 FT /note="LRR 4" FT REPEAT 225..248 FT /note="LRR 5" FT REPEAT 250..271 FT /note="LRR 6" FT MOD_RES 335 FT /note="Sulfotyrosine" FT /evidence="ECO:0000250|UniProtKB:P22888" FT LIPID 647 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000305|PubMed:7776964" FT LIPID 648 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000305|PubMed:7776964" FT CARBOHYD 103 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 178 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 199 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 295 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 303 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 317 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 443..518 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" FT VAR_SEQ 83..132 FT /note="Missing (in isoform 1950)" FT /evidence="ECO:0000305" FT /id="VSP_001968" FT VAR_SEQ 133..157 FT /note="Missing (in isoform 1759)" FT /evidence="ECO:0000305" FT /id="VSP_001969" FT VAR_SEQ 184..700 FT /note="Missing (in isoform C2)" FT /evidence="ECO:0000305" FT /id="VSP_001970" FT VAR_SEQ 232..293 FT /note="Missing (in isoform EA2, isoform EB and isoform B1)" FT /evidence="ECO:0000305" FT /id="VSP_001972" FT VAR_SEQ 232..251 FT /note="DISSTKLQALPSHGLESIQT -> PCRATGWSPFRRSSPCLPTH (in FT isoform 2075)" FT /evidence="ECO:0000305" FT /id="VSP_001971" FT VAR_SEQ 252..700 FT /note="Missing (in isoform 2075)" FT /evidence="ECO:0000305" FT /id="VSP_001973" FT VAR_SEQ 294..367 FT /note="QNFSFSIFENFSKQCESTVRKADNETLYSAIFEENELSGWDYDYGFCSPKTL FT QCAPEPDAFNPCEDIMGYAFLR -> IFHFPFLKTSPNNAKAQLEKQITRRFIPPSLRR FT MNSVAGIMIMASVHPRHSNVLQNQMLSTPVKILWAMPSLGS (in isoform B1 FT and isoform B3)" FT /evidence="ECO:0000305" FT /id="VSP_001974" FT VAR_SEQ 294 FT /note="Q -> P (in isoform C1)" FT /evidence="ECO:0000305" FT /id="VSP_001975" FT VAR_SEQ 295..700 FT /note="Missing (in isoform C1)" FT /evidence="ECO:0000305" FT /id="VSP_001976" FT VAR_SEQ 321..342 FT /note="YSAIFEENELSGWDYDYGFCSP -> LHGALPAAHCLRGLPNKRPVL (in FT isoform 1834, isoform 1759 and isoform EB)" FT /evidence="ECO:0000305" FT /id="VSP_001977" FT VAR_SEQ 343..700 FT /note="Missing (in isoform 1834, isoform 1759 and isoform FT EB)" FT /evidence="ECO:0000305" FT /id="VSP_001978" FT VAR_SEQ 368..700 FT /note="Missing (in isoform B1 and isoform B3)" FT /evidence="ECO:0000305" FT /id="VSP_001979" FT VARIANT 82 FT /note="I -> M (in isoform 1950)" FT VARIANT 179 FT /note="E -> G (in isoform 1759)" FT VARIANT 233 FT /note="I -> T (in isoform 1950)" FT VARIANT 646 FT /note="G -> S (in isoform 1950)" FT MUTAGEN 409 FT /note="D->N: Significant reduction of binding." FT /evidence="ECO:0000269|PubMed:1714448" FT MUTAGEN 436 FT /note="D->N: No change in binding or cAMP production." FT /evidence="ECO:0000269|PubMed:1714448" FT MUTAGEN 455 FT /note="E->Q: No change in binding or cAMP production." FT /evidence="ECO:0000269|PubMed:1714448" FT MUTAGEN 582 FT /note="D->N: No change in binding or cAMP production." FT /evidence="ECO:0000269|PubMed:1714448" FT MUTAGEN 647 FT /note="C->A: Trapped intracellularly and does not appear to FT become mature; when associated with A-648." FT /evidence="ECO:0000269|PubMed:7776964" FT MUTAGEN 648 FT /note="C->A: Trapped intracellularly and does not appear to FT become mature; when associated with A-647." FT /evidence="ECO:0000269|PubMed:7776964" FT CONFLICT 33 FT /note="R -> L (in Ref. 9; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 700 AA; 78036 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 //