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492 lines
23 KiB
Plaintext
492 lines
23 KiB
Plaintext
ID LSHR_RAT Reviewed; 700 AA.
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AC P16235; P70646; Q63807; Q63808; Q63809; Q6LDI7;
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DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
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DT 01-APR-1990, sequence version 1.
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DT 12-OCT-2022, entry version 184.
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DE RecName: Full=Lutropin-choriogonadotropic hormone receptor;
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DE Short=LH/CG-R;
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DE AltName: Full=Luteinizing hormone receptor;
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DE Short=LSH-R;
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DE Flags: Precursor;
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GN Name=Lhcgr;
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OS Rattus norvegicus (Rat).
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OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
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OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
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OC Murinae; Rattus.
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OX NCBI_TaxID=10116;
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RN [1]
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RP NUCLEOTIDE SEQUENCE [MRNA].
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RX PubMed=2502842; DOI=10.1126/science.2502842;
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RA McFarland K.C., Sprengel R., Phillips H.S., Koehler M., Rosemblit N.,
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RA Nikolics K., Segaloff D.L., Seeburg P.H.;
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RT "Lutropin-choriogonadotropin receptor: an unusual member of the G protein-
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RT coupled receptor family.";
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RL Science 245:494-499(1989).
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RN [2]
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RP NUCLEOTIDE SEQUENCE, AND ALTERNATIVE SPLICING.
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RC STRAIN=Sprague-Dawley; TISSUE=Ovary;
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RX PubMed=1353463; DOI=10.1016/0303-7207(92)90079-l;
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RA Aatsinki J.T., Pietila E.M., Lakkakorpi J.T., Rajaniemi H.J.;
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RT "Expression of the LH/CG receptor gene in rat ovarian tissue is regulated
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RT by an extensive alternative splicing of the primary transcript.";
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RL Mol. Cell. Endocrinol. 84:127-135(1992).
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RN [3]
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RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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RX PubMed=2019252; DOI=10.1210/endo-128-5-2297;
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RA Koo Y.B., Slaughter R.G., Ji T.H.;
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RT "Structure of the luteinizing hormone receptor gene and multiple exons of
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RT the coding sequence.";
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RL Endocrinology 128:2297-2308(1991).
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RN [4]
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RP NUCLEOTIDE SEQUENCE, AND ALTERNATIVE SPLICING.
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RX PubMed=1976554; DOI=10.1016/0303-7207(90)90034-6;
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RA Bernard M.P., Myers R.V., Moyle W.R.;
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RT "Cloning of rat lutropin (LH) receptor analogs lacking the soybean lectin
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RT domain.";
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RL Mol. Cell. Endocrinol. 71:R19-R23(1990).
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RN [5]
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RP NUCLEOTIDE SEQUENCE, AND ALTERNATIVE SPLICING.
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RX PubMed=2281186; DOI=10.1016/b978-0-12-571146-3.50014-6;
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RA Segaloff D.L., Sprengel R., Nikolics K., Ascoli M.;
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RT "Structure of the lutropin/choriogonadotropin receptor.";
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RL Recent Prog. Horm. Res. 46:261-301(1990).
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RN [6]
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RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-320.
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RC TISSUE=Liver;
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RX PubMed=2040640; DOI=10.1016/s0021-9258(18)99170-2;
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RA Tsai-Morris C.H., Buczko E., Wang W., Xie X.-Z., Dufau M.L.;
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RT "Structural organization of the rat luteinizing hormone (LH) receptor
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RT gene.";
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RL J. Biol. Chem. 266:11355-11359(1991).
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RN [7]
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RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 295-700.
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RX PubMed=2174034; DOI=10.1016/s0021-9258(17)45380-4;
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RA Tsai-Morris C.H., Buczko E., Wang W., Dufau M.L.;
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RT "Intronic nature of the rat luteinizing hormone receptor gene defines a
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RT soluble receptor subspecies with hormone binding activity.";
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RL J. Biol. Chem. 265:19385-19388(1990).
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RN [8]
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RP PROTEIN SEQUENCE OF 27-44.
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RX PubMed=2601325; DOI=10.1016/0022-4731(89)90482-2;
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RA Dufau M.L., Minegishi T., Buczko E.S., Delgado C.J., Zhang R.;
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RT "Characterization and structure of ovarian and testicular LH/hCG
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RT receptors.";
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RL J. Steroid Biochem. 33:715-720(1989).
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RN [9]
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RP PROTEIN SEQUENCE OF 27-37.
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RX PubMed=2925659; DOI=10.1016/s0021-9258(18)83790-5;
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RA Roche P.C., Ryan R.J.;
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RT "Purification, characterization, and amino-terminal sequence of rat ovarian
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RT receptor for luteinizing hormone/human choriogonadotropin.";
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RL J. Biol. Chem. 264:4636-4641(1989).
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RN [10]
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RP MUTAGENESIS OF ASP-409; ASP-436; GLU-455 AND ASP-582.
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RX PubMed=1714448; DOI=10.1016/s0021-9258(18)98570-4;
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RA Ji I., Ji T.H.;
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RT "Asp383 in the second transmembrane domain of the lutropin receptor is
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RT important for high affinity hormone binding and cAMP production.";
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RL J. Biol. Chem. 266:14953-14957(1991).
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RN [11]
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RP PALMITOYLATION AT CYS-647 AND CYS-648, AND MUTAGENESIS OF CYS-647 AND
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RP CYS-648.
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RX PubMed=7776964; DOI=10.1210/mend.9.2.7776964;
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RA Zhu H., Wang H., Ascoli M.;
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RT "The lutropin/choriogonadotropin receptor is palmitoylated at intracellular
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RT cysteine residues.";
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RL Mol. Endocrinol. 9:141-150(1995).
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CC -!- FUNCTION: Receptor for lutropin-choriogonadotropic hormone. The
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CC activity of this receptor is mediated by G proteins which activate
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CC adenylate cyclase. {ECO:0000250|UniProtKB:P22888}.
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CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P22888};
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CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P22888}. Secreted.
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CC Note=Some isoforms may be secreted.
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CC -!- ALTERNATIVE PRODUCTS:
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CC Event=Alternative splicing; Named isoforms=11;
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CC Comment=Additional isoforms seem to exist.;
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CC Name=1;
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CC IsoId=P16235-1; Sequence=Displayed;
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CC Name=1759;
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CC IsoId=P16235-2; Sequence=VSP_001969, VSP_001977, VSP_001978;
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CC Name=1834;
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CC IsoId=P16235-3; Sequence=VSP_001977, VSP_001978;
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CC Name=1950;
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CC IsoId=P16235-4; Sequence=VSP_001968;
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CC Name=2075;
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CC IsoId=P16235-5; Sequence=VSP_001971, VSP_001973;
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CC Name=C1;
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CC IsoId=P16235-6; Sequence=VSP_001975, VSP_001976;
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CC Name=C2;
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CC IsoId=P16235-7; Sequence=VSP_001970;
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CC Name=EA2;
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CC IsoId=P16235-8; Sequence=VSP_001972;
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CC Name=EB;
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CC IsoId=P16235-9; Sequence=VSP_001972, VSP_001977, VSP_001978;
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CC Name=B1;
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CC IsoId=P16235-10; Sequence=VSP_001972, VSP_001974, VSP_001979;
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CC Name=B3;
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CC IsoId=P16235-11; Sequence=VSP_001974, VSP_001979;
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CC -!- PTM: Sulfated. {ECO:0000250|UniProtKB:P22888}.
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CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
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CC FSH/LSH/TSH subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
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CC -!- WEB RESOURCE: Name=Sequence-structure-function-analysis of glycoprotein
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CC hormone receptors;
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CC URL="http://www.ssfa-gphr.de/";
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CC ---------------------------------------------------------------------------
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CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
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CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
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CC ---------------------------------------------------------------------------
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DR EMBL; M26199; AAA41528.1; -; mRNA.
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DR EMBL; M61212; AAA41527.1; -; Genomic_DNA.
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DR EMBL; M61211; AAA41527.1; JOINED; Genomic_DNA.
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DR EMBL; S40803; AAB22680.1; -; Genomic_DNA.
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DR EMBL; S40787; AAB22680.1; JOINED; Genomic_DNA.
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DR EMBL; S40903; AAB22680.1; JOINED; Genomic_DNA.
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DR EMBL; S40904; AAB22680.1; JOINED; Genomic_DNA.
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DR EMBL; S40905; AAB22680.1; JOINED; Genomic_DNA.
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DR EMBL; S40907; AAB22680.1; JOINED; Genomic_DNA.
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DR EMBL; S40909; AAB22680.1; JOINED; Genomic_DNA.
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DR EMBL; S40918; AAB22680.1; JOINED; Genomic_DNA.
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DR EMBL; S40920; AAB22680.1; JOINED; Genomic_DNA.
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DR EMBL; S40795; AAB22680.1; JOINED; Genomic_DNA.
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DR EMBL; S40798; AAB22680.1; JOINED; Genomic_DNA.
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DR EMBL; S40795; AAB22681.1; -; Genomic_DNA.
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DR EMBL; S40787; AAB22681.1; JOINED; Genomic_DNA.
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DR EMBL; S40903; AAB22681.1; JOINED; Genomic_DNA.
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DR EMBL; S40904; AAB22681.1; JOINED; Genomic_DNA.
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DR EMBL; S40905; AAB22681.1; JOINED; Genomic_DNA.
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DR EMBL; S40907; AAB22681.1; JOINED; Genomic_DNA.
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DR EMBL; S40909; AAB22681.1; JOINED; Genomic_DNA.
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DR EMBL; S40918; AAB22681.1; JOINED; Genomic_DNA.
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DR EMBL; S40920; AAB22681.1; JOINED; Genomic_DNA.
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DR EMBL; S40803; AAB22682.2; -; Genomic_DNA.
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DR EMBL; S40787; AAB22682.2; JOINED; Genomic_DNA.
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DR EMBL; S40903; AAB22682.2; JOINED; Genomic_DNA.
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DR EMBL; S40907; AAB22682.2; JOINED; Genomic_DNA.
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DR EMBL; S40909; AAB22682.2; JOINED; Genomic_DNA.
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DR EMBL; S40918; AAB22682.2; JOINED; Genomic_DNA.
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DR EMBL; S40920; AAB22682.2; JOINED; Genomic_DNA.
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DR EMBL; S40795; AAB22682.2; JOINED; Genomic_DNA.
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DR EMBL; S40798; AAB22682.2; JOINED; Genomic_DNA.
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DR EMBL; S40803; AAB22683.1; -; Genomic_DNA.
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DR EMBL; S40787; AAB22683.1; JOINED; Genomic_DNA.
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DR EMBL; S40903; AAB22683.1; JOINED; Genomic_DNA.
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DR EMBL; S40904; AAB22683.1; JOINED; Genomic_DNA.
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DR EMBL; S40905; AAB22683.1; JOINED; Genomic_DNA.
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DR EMBL; S40907; AAB22683.1; JOINED; Genomic_DNA.
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DR EMBL; S40909; AAB22683.1; JOINED; Genomic_DNA.
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DR EMBL; S40918; AAB22683.1; JOINED; Genomic_DNA.
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DR EMBL; S40920; AAB22683.1; JOINED; Genomic_DNA.
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DR EMBL; S40795; AAB22683.1; JOINED; Genomic_DNA.
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DR EMBL; S40798; AAB22683.1; JOINED; Genomic_DNA.
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DR EMBL; S40803; AAB22684.2; -; Genomic_DNA.
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DR EMBL; S40787; AAB22684.2; JOINED; Genomic_DNA.
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DR EMBL; S40903; AAB22684.2; JOINED; Genomic_DNA.
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DR EMBL; S40904; AAB22684.2; JOINED; Genomic_DNA.
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DR EMBL; S40905; AAB22684.2; JOINED; Genomic_DNA.
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DR EMBL; S40909; AAB22684.2; JOINED; Genomic_DNA.
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DR EMBL; S40918; AAB22684.2; JOINED; Genomic_DNA.
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DR EMBL; S40920; AAB22684.2; JOINED; Genomic_DNA.
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DR EMBL; S40795; AAB22684.2; JOINED; Genomic_DNA.
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DR EMBL; S40798; AAB22684.2; JOINED; Genomic_DNA.
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DR EMBL; M68928; AAA41529.1; -; Genomic_DNA.
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DR EMBL; M68917; AAA41529.1; JOINED; Genomic_DNA.
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DR EMBL; M68918; AAA41529.1; JOINED; Genomic_DNA.
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DR EMBL; M68919; AAA41529.1; JOINED; Genomic_DNA.
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DR EMBL; M68920; AAA41529.1; JOINED; Genomic_DNA.
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DR EMBL; M68921; AAA41529.1; JOINED; Genomic_DNA.
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DR EMBL; M68922; AAA41529.1; JOINED; Genomic_DNA.
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DR EMBL; M68923; AAA41529.1; JOINED; Genomic_DNA.
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DR EMBL; M68925; AAA41529.1; JOINED; Genomic_DNA.
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DR EMBL; M68926; AAA41529.1; JOINED; Genomic_DNA.
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DR EMBL; M68927; AAA41529.1; JOINED; Genomic_DNA.
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DR EMBL; AH004953; AAB42193.1; -; Genomic_DNA.
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DR PIR; A49744; A49744.
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DR PIR; I57668; I57668.
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DR PIR; I77461; I77461.
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DR RefSeq; NP_037110.1; NM_012978.1. [P16235-1]
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DR AlphaFoldDB; P16235; -.
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DR SMR; P16235; -.
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DR STRING; 10116.ENSRNOP00000022481; -.
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DR BindingDB; P16235; -.
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DR ChEMBL; CHEMBL2456; -.
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DR DrugCentral; P16235; -.
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DR GlyGen; P16235; 6 sites.
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DR iPTMnet; P16235; -.
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DR PhosphoSitePlus; P16235; -.
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DR SwissPalm; P16235; -.
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DR PaxDb; P16235; -.
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DR Ensembl; ENSRNOT00000022481; ENSRNOP00000022481; ENSRNOG00000016712. [P16235-1]
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DR Ensembl; ENSRNOT00000096915; ENSRNOP00000089069; ENSRNOG00000016712. [P16235-2]
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DR Ensembl; ENSRNOT00000098297; ENSRNOP00000079785; ENSRNOG00000016712. [P16235-8]
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DR GeneID; 25477; -.
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DR KEGG; rno:25477; -.
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DR UCSC; RGD:3007; rat. [P16235-1]
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DR CTD; 3973; -.
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DR RGD; 3007; Lhcgr.
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DR eggNOG; KOG2087; Eukaryota.
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DR GeneTree; ENSGT00940000157364; -.
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DR InParanoid; P16235; -.
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DR OrthoDB; 257031at2759; -.
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DR PhylomeDB; P16235; -.
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DR Reactome; R-RNO-375281; Hormone ligand-binding receptors.
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DR PRO; PR:P16235; -.
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DR Proteomes; UP000002494; Chromosome 6.
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DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
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DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
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DR GO; GO:0005768; C:endosome; IDA:RGD.
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DR GO; GO:0005615; C:extracellular space; IDA:RGD.
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DR GO; GO:0005887; C:integral component of plasma membrane; IDA:RGD.
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DR GO; GO:0031233; C:intrinsic component of external side of plasma membrane; IDA:RGD.
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DR GO; GO:0005764; C:lysosome; IDA:RGD.
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DR GO; GO:0005634; C:nucleus; IDA:RGD.
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DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
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DR GO; GO:0043235; C:receptor complex; IDA:RGD.
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DR GO; GO:0051117; F:ATPase binding; IPI:RGD.
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DR GO; GO:0038106; F:choriogonadotropin hormone binding; ISO:RGD.
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DR GO; GO:0035472; F:choriogonadotropin hormone receptor activity; ISO:RGD.
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DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IDA:RGD.
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DR GO; GO:0042802; F:identical protein binding; IDA:RGD.
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DR GO; GO:0004964; F:luteinizing hormone receptor activity; ISS:UniProtKB.
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DR GO; GO:0017046; F:peptide hormone binding; IDA:RGD.
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DR GO; GO:0007190; P:activation of adenylate cyclase activity; IDA:RGD.
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DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:RGD.
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DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IDA:RGD.
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DR GO; GO:0050482; P:arachidonic acid secretion; IDA:RGD.
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DR GO; GO:0071371; P:cellular response to gonadotropin stimulus; ISO:RGD.
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DR GO; GO:0071373; P:cellular response to luteinizing hormone stimulus; ISS:UniProtKB.
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DR GO; GO:0007417; P:central nervous system development; IEP:RGD.
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DR GO; GO:0050890; P:cognition; ISO:RGD.
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DR GO; GO:0046544; P:development of secondary male sexual characteristics; ISO:RGD.
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DR GO; GO:0008585; P:female gonad development; ISO:RGD.
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DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
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DR GO; GO:0009755; P:hormone-mediated signaling pathway; IDA:RGD.
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DR GO; GO:0042700; P:luteinizing hormone signaling pathway; IDA:RGD.
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DR GO; GO:0008584; P:male gonad development; ISO:RGD.
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DR GO; GO:0001541; P:ovarian follicle development; ISO:RGD.
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DR GO; GO:0022602; P:ovulation cycle process; ISO:RGD.
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DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:RGD.
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DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IDA:RGD.
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DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IDA:RGD.
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DR GO; GO:0046886; P:positive regulation of hormone biosynthetic process; IDA:RGD.
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DR GO; GO:0032962; P:positive regulation of inositol trisphosphate biosynthetic process; ISO:RGD.
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DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IDA:RGD.
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DR GO; GO:0006622; P:protein targeting to lysosome; IMP:RGD.
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DR GO; GO:0050810; P:regulation of steroid biosynthetic process; IEP:RGD.
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DR GO; GO:0090030; P:regulation of steroid hormone biosynthetic process; ISO:RGD.
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DR GO; GO:0034699; P:response to luteinizing hormone; IDA:CAFA.
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DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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DR GO; GO:0072520; P:seminiferous tubule development; ISO:RGD.
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DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
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DR GO; GO:0060065; P:uterus development; ISO:RGD.
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DR Gene3D; 3.80.10.10; -; 1.
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DR InterPro; IPR000276; GPCR_Rhodpsn.
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DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
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DR InterPro; IPR002131; Gphrmn_rcpt_fam.
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DR InterPro; IPR026906; LRR_5.
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DR InterPro; IPR032675; LRR_dom_sf.
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DR InterPro; IPR002273; LSH_rcpt.
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DR Pfam; PF00001; 7tm_1; 1.
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DR Pfam; PF13306; LRR_5; 2.
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DR PRINTS; PR00373; GLYCHORMONER.
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DR PRINTS; PR00237; GPCRRHODOPSN.
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DR PRINTS; PR01144; LSHRECEPTOR.
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DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
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DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
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PE 1: Evidence at protein level;
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KW Alternative splicing; Cell membrane; Direct protein sequencing;
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KW Disulfide bond; G-protein coupled receptor; Glycoprotein;
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KW Leucine-rich repeat; Lipoprotein; Membrane; Palmitate; Receptor;
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KW Reference proteome; Repeat; Secreted; Signal; Sulfation; Transducer;
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KW Transmembrane; Transmembrane helix.
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FT SIGNAL 1..26
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FT /evidence="ECO:0000269|PubMed:2601325,
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FT ECO:0000269|PubMed:2925659"
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FT CHAIN 27..700
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FT /note="Lutropin-choriogonadotropic hormone receptor"
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FT /id="PRO_0000012783"
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FT TOPO_DOM 27..362
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FT /note="Extracellular"
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FT /evidence="ECO:0000255"
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FT TRANSMEM 363..390
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FT /note="Helical; Name=1"
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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
|
|
//
|