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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
//
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