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
//
