LSHR_HUMAN
ID LSHR_HUMAN Reviewed; 699 AA.
AC P22888; Q14751; Q15996; Q9UEW9;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 4.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=Lutropin-choriogonadotropic hormone receptor;
DE Short=LH/CG-R;
DE AltName: Full=Luteinizing hormone receptor;
DE Short=LHR;
DE Short=LSH-R;
DE Flags: Precursor;
GN Name=LHCGR; Synonyms=LCGR, LGR2, LHRHR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-312.
RC TISSUE=Ovary;
RX PubMed=2244890; DOI=10.1016/0006-291x(90)91552-4;
RA Minegish T., Nakamura K., Takakura Y., Miyamoto K., Hasegawa Y., Ibuki Y.,
RA Igarashi M.;
RT "Cloning and sequencing of human LH/hCG receptor cDNA.";
RL Biochem. Biophys. Res. Commun. 172:1049-1054(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=1922095; DOI=10.1210/mend-5-6-759;
RA Jia X.-C., Oikawa M., Bo M., Tanaka T., Ny T., Boime I., Hsueh A.J.W.;
RT "Expression of human luteinizing hormone (LH) receptor: interaction with LH
RT and chorionic gonadotropin from human but not equine, rat, and ovine
RT species.";
RL Mol. Endocrinol. 5:759-768(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thyroid;
RX PubMed=2293030; DOI=10.1210/mend-4-8-1264;
RA Frazier A.L., Robbins L.S., Stork P.J., Sprengel R., Segaloff D.L.,
RA Cone R.D.;
RT "Isolation of TSH and LH/CG receptor cDNAs from human thyroid: regulation
RT by tissue specific splicing.";
RL Mol. Endocrinol. 4:1264-1276(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-GLN-18 INS AND SER-312.
RX PubMed=7556872; DOI=10.1016/0303-7207(95)03557-n;
RA Atger M., Misrahi M., Sar S., Leflem L., Dessen P., Milgrom E.;
RT "Structure of the human luteinizing hormone-choriogonadotropin receptor
RT gene: unusual promoter and 5' non-coding regions.";
RL Mol. Cell. Endocrinol. 111:113-123(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54, AND VARIANT LEU-GLN-18 INS.
RX PubMed=9858858; DOI=10.1159/000022840;
RA Tsai-Morris C.-H., Geng Y., Buczko E., Dehejia A., Dufau M.L.;
RT "Genomic distribution and gonadal mRNA expression of two human luteinizing
RT hormone receptor exon 1 sequences in random populations.";
RL Hum. Hered. 49:48-51(1999).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, SULFATION AT TYR-331, AND MUTAGENESIS OF
RP TYR-331 AND TYR-333.
RX PubMed=11847099; DOI=10.1093/emboj/21.4.504;
RA Costagliola S., Panneels V., Bonomi M., Koch J., Many M.C., Smits G.,
RA Vassart G.;
RT "Tyrosine sulfation is required for agonist recognition by glycoprotein
RT hormone receptors.";
RL EMBO J. 21:504-513(2002).
RN [8]
RP PALMITOYLATION AT CYS-643 AND CYS-644, AND MUTAGENESIS OF CYS-643 AND
RP CYS-644.
RX PubMed=15539429; DOI=10.1210/me.2004-0335;
RA Munshi U.M., Clouser C.L., Peegel H., Menon K.M.;
RT "Evidence that palmitoylation of carboxyl terminus cysteine residues of the
RT human luteinizing hormone receptor regulates postendocytic processing.";
RL Mol. Endocrinol. 19:749-758(2005).
RN [9]
RP 3D-STRUCTURE MODELING OF 51-232.
RX PubMed=8747461; DOI=10.1016/s0969-2126(01)00272-6;
RA Jiang X., Dreano M., Buckler D.R., Cheng S., Ythier A., Wu H.,
RA Hendrickson W.A., el Tayar N.;
RT "Structural predictions for the ligand-binding region of glycoprotein
RT hormone receptors and the nature of hormone-receptor interactions.";
RL Structure 3:1341-1353(1995).
RN [10]
RP VARIANTS FMPP PRO-368 AND VAL-568, AND CHARACTERIZATION OF VARIANT FMPP
RP PRO-368.
RX PubMed=11134146; DOI=10.1210/jcem.85.12.7071;
RA Latronico A.C., Shinozaki H., Guerra G. Jr., Pereira M.A.A.,
RA Lemos Marini S.H.V., Baptista M.T.M., Arnhold I.J.P., Fanelli F.,
RA Mendonca B.B., Segaloff D.L.;
RT "Gonadotropin-independent precocious puberty due to luteinizing hormone
RT receptor mutations in Brazilian boys: a novel constitutively activating
RT mutation in the first transmembrane helix.";
RL J. Clin. Endocrinol. Metab. 85:4799-4805(2000).
RN [11]
RP VARIANT FMPP GLY-564.
RX PubMed=11391350; DOI=10.1067/mpd.2001.114477;
RA Leschek E.W., Chan W.-Y., Diamond D.A., Kaefer M., Jones J., Barnes K.M.,
RA Cutler G.B. Jr.;
RT "Nodular Leydig cell hyperplasia in a boy with familial male-limited
RT precocious puberty.";
RL J. Pediatr. 138:949-951(2001).
RN [12]
RP VARIANTS LHR SER-343 AND ARG-543, AND CHARACTERIZATION OF VARIANTS LHR
RP SER-343 AND ARG-543.
RX PubMed=12050206; DOI=10.1210/jcem.87.6.8523;
RA Martens J.W.M., Lumbroso S., Verhoef-Post M., Georget V., Richter-Unruh A.,
RA Szarras-Czapnik M., Romer T.E., Brunner H.G., Themmen A.P.N., Sultan C.;
RT "Mutant luteinizing hormone receptors in a compound heterozygous patient
RT with complete Leydig cell hypoplasia: abnormal processing causes signaling
RT deficiency.";
RL J. Clin. Endocrinol. Metab. 87:2506-2513(2002).
RN [13]
RP ASSOCIATION OF VARIANT LEU-GLN-18 INS WITH AGE OF BREAST CANCER ONSET.
RX PubMed=12679452; DOI=10.1210/jc.2002-021585;
RA Powell B.L., Piersma D., Kevenaar M.E., van Staveren I.L., Themmen A.P.N.,
RA Iacopetta B.J., Berns E.M.J.J.;
RT "Luteinizing hormone signaling and breast cancer: polymorphisms and age of
RT onset.";
RL J. Clin. Endocrinol. Metab. 88:1653-1657(2003).
RN [14]
RP VARIANT FMPP GLY-578.
RX PubMed=7692306; DOI=10.1038/365652a0;
RA Shenker A., Laue L., Kosugi S., Merendino J.J. Jr., Minegishi T.,
RA Cutler G.B. Jr.;
RT "A constitutively activating mutation of the luteinizing hormone receptor
RT in familial male precocious puberty.";
RL Nature 365:652-654(1993).
RN [15]
RP VARIANTS FMPP ILE-571 AND GLY-578.
RX PubMed=8281137; DOI=10.1093/hmg/2.11.1779;
RA Kremer H., Mariman E., Otten B.J., Moll G.W. Jr., Stoelinga G.B.A.,
RA Wit J.M., Jansen M., Drop S.L., Faas B., Ropers H.-H., Brunner H.G.;
RT "Cosegregation of missense mutations of the luteinizing hormone receptor
RT gene with familial male-limited precocious puberty.";
RL Hum. Mol. Genet. 2:1779-1783(1993).
RN [16]
RP VARIANT FMPP ILE-577.
RX PubMed=7757065; DOI=10.1093/hmg/4.2.183;
RA Kosugi S., van Dop C., Geffner M.E., Rabl W., Carel J.-C., Chaussain J.-L.,
RA Mori T., Merendino J.J. Jr., Shenker A.;
RT "Characterization of heterogeneous mutations causing constitutive
RT activation of the luteinizing hormone receptor in familial male precocious
RT puberty.";
RL Hum. Mol. Genet. 4:183-188(1995).
RN [17]
RP VARIANT FMPP VAL-572.
RX PubMed=7714085; DOI=10.1210/jcem.80.4.7714085;
RA Yano K., Saji M., Hidaka A., Moriya N., Okuno A., Kohn L.D.,
RA Cutler G.B. Jr.;
RT "A new constitutively activating point mutation in the luteinizing
RT hormone/choriogonadotropin receptor gene in cases of male-limited
RT precocious puberty.";
RL J. Clin. Endocrinol. Metab. 80:1162-1168(1995).
RN [18]
RP VARIANT FMPP VAL-568.
RX PubMed=7629248; DOI=10.1210/jcem.80.8.7629248;
RA Latronico A.C., Anasti J., Arnhold I.J., Mendonca B.B., Domenice S.,
RA Albano M.C., Zachman K., Wajchenberg B.L., Tsigos C.;
RT "A novel mutation of the luteinizing hormone receptor gene causing male
RT gonadotropin-independent precocious puberty.";
RL J. Clin. Endocrinol. Metab. 80:2490-2494(1995).
RN [19]
RP VARIANT LHR PRO-593.
RX PubMed=7719343; DOI=10.1038/ng0295-160;
RA Kremer H., Kraaij R., Toledo S.P.A., Post M., Fridman J.B., Hayashida C.Y.,
RA van Reen M., Milgrom E., Ropers H.-H., Mariman E., Themmen A.P.N.,
RA Brunner H.G.;
RT "Male pseudohermaphroditism due to a homozygous missense mutation of the
RT luteinizing hormone receptor gene.";
RL Nat. Genet. 9:160-164(1995).
RN [20]
RP VARIANT FMPP ILE-577.
RX PubMed=8829636;
RX DOI=10.1002/(sici)1098-1004(1996)7:2<164::aid-humu13>3.0.co;2-0;
RA Cocco S., Meloni A., Marini M.G., Cao A., Moi P.;
RT "A missense (T577I) mutation in the luteinizing hormone receptor gene
RT associated with familial male-limited precocious puberty.";
RL Hum. Mutat. 7:164-166(1996).
RN [21]
RP VARIANT FMPP THR-398.
RX PubMed=8929952; DOI=10.1136/jmg.33.2.143;
RA Evans B.A.J., Bowen D.J., Smith P.J., Clayton P.E., Gregory J.W.;
RT "A new point mutation in the luteinising hormone receptor gene in familial
RT and sporadic male limited precocious puberty: genotype does not always
RT correlate with phenotype.";
RL J. Med. Genet. 33:143-147(1996).
RN [22]
RP VARIANT LHR TYR-616.
RX PubMed=8559204; DOI=10.1056/nejm199602223340805;
RA Latronico A.C., Anasti J., Arnhold I.J.P., Rapaport R., Mendonca B.B.,
RA Bloise W., Castro M., Tsigos C., Chrousos G.P.;
RT "Testicular and ovarian resistance to luteinizing hormone caused by
RT inactivating mutations of the luteinizing hormone-receptor gene.";
RL N. Engl. J. Med. 334:507-512(1996).
RN [23]
RP VARIANT LHR ARG-131.
RX PubMed=9215288; DOI=10.1210/jcem.82.7.4039;
RA Misrahi M., Meduri G., Pissard S., Bouvattier C., Beau I., Loosfelt H.,
RA Jolivet A., Rappaport R., Milgrom E., Bougneres P.;
RT "Comparison of immunocytochemical and molecular features with the phenotype
RT in a case of incomplete male pseudohermaphroditism associated with a
RT mutation of the luteinizing hormone receptor.";
RL J. Clin. Endocrinol. Metab. 82:2159-2165(1997).
RN [24]
RP VARIANTS LEU-GLN-18 INS; SER-284 AND ASN-306.
RX PubMed=10215412;
RX DOI=10.1002/(sici)1098-1004(1998)11:4<333::aid-humu19>3.0.co;2-d;
RA Wu S.-M., Jose M., Hallermeier K., Rennert O.M., Chan W.-Y.;
RT "Polymorphisms in the coding exons of the human luteinizing hormone
RT receptor gene.";
RL Hum. Mutat. 11:333-334(1998).
RN [25]
RP VARIANT FMPP VAL-373.
RX PubMed=9467560; DOI=10.1210/jcem.83.2.4579;
RA Gromoll J., Partsch C.-J., Simoni M., Nordhoff V., Sippell W.G.,
RA Nieschlag E., Saxena B.B.;
RT "A mutation in the first transmembrane domain of the lutropin receptor
RT causes male precocious puberty.";
RL J. Clin. Endocrinol. Metab. 83:476-480(1998).
RN [26]
RP VARIANT LHR LYS-354.
RX PubMed=9626144; DOI=10.1210/jcem.83.6.4855;
RA Stavrou S.S., Zhu Y.S., Cai L.Q., Katz M.D., Herrera C., Defillo-Ricart M.,
RA Imperato-Mcginley J.;
RT "A novel mutation of the human luteinizing hormone receptor in 46XY and
RT 46XX sisters.";
RL J. Clin. Endocrinol. Metab. 83:2091-2098(1998).
RN [27]
RP VARIANT FMPP ARG-457.
RX PubMed=9661624; DOI=10.1210/jcem.83.7.4968;
RA Latronico A.C., Abell A.N., Arnhold I.J., Liu X., Lins T.S., Brito V.N.,
RA Billerbeck A.E., Segaloff D.L., Mendonca B.B.;
RT "A unique constitutively activating mutation in third transmembrane helix
RT of luteinizing hormone receptor causes sporadic male gonadotropin-
RT independent precocious puberty.";
RL J. Clin. Endocrinol. Metab. 83:2435-2440(1998).
RN [28]
RP VARIANT LEU-GLN-18 INS.
RX PubMed=9851790; DOI=10.1210/jcem.83.12.5325;
RA Rodien P., Cetani F., Costagliola S., Tonacchera M., Duprez L.,
RA Minegishi T., Govaerts C., Vassart G.;
RT "Evidences for an allelic variant of the human LC/CG receptor rather than a
RT gene duplication: functional comparison of wild-type and variant
RT receptors.";
RL J. Clin. Endocrinol. Metab. 83:4431-4434(1998).
RN [29]
RP VARIANT LHR 608-LEU-VAL-609 DEL.
RX PubMed=9514160; DOI=10.1210/mend.12.3.0077;
RA Latronico A.C., Chai Y., Arnhold I.J.P., Liu X., Mendonca B.B.,
RA Segaloff D.L.;
RT "A homozygous microdeletion in helix 7 of the luteinizing hormone receptor
RT associated with familial testicular and ovarian resistance is due to both
RT decreased cell surface expression and impaired effector activation by the
RT cell surface receptor.";
RL Mol. Endocrinol. 12:442-450(1998).
RN [30]
RP VARIANT LHR LYS-625.
RX PubMed=9626653; DOI=10.1210/mend.12.6.0124;
RA Martens J.W., Verhoef-Post M., Abelin N., Ezabella M., Toledo S.P.,
RA Brunner H.G., Themmen A.P.;
RT "A homozygous mutation in the luteinizing hormone receptor causes partial
RT Leydig cell hypoplasia: correlation between receptor activity and
RT phenotype.";
RL Mol. Endocrinol. 12:775-784(1998).
RN [31]
RP VARIANT LEYDIG CELL TUMOR HIS-578.
RX PubMed=10580072; DOI=10.1056/nejm199912023412304;
RA Liu G., Duranteau L., Carel J.-C., Monroe J., Doyle D.A., Shenker A.;
RT "Leydig-cell tumors caused by an activating mutation of the gene encoding
RT the luteinizing hormone receptor.";
RL N. Engl. J. Med. 341:1731-1736(1999).
RN [32]
RP VARIANT LHR PRO-502, AND CHARACTERIZATION OF VARIANT LCH PRO-502.
RX PubMed=15372531; DOI=10.1002/ajmg.a.20681;
RA Leung M.Y.-K., Al-Muslim O., Wu S.-M., Aziz A., Inam S., Awadh M.,
RA Rennert O.M., Chan W.-Y.;
RT "A novel missense homozygous inactivating mutation in the fourth
RT transmembrane helix of the luteinizing hormone receptor in Leydig cell
RT hypoplasia.";
RL Am. J. Med. Genet. A 130:146-153(2004).
RN [33]
RP VARIANT LHR PHE-144, AND CHARACTERIZATION OF VARIANT LCH PHE-144.
RX PubMed=15472221; DOI=10.1210/jc.2004-0298;
RA Richter-Unruh A., Verhoef-Post M., Malak S., Homoki J., Hauffa B.P.,
RA Themmen A.P.N.;
RT "Leydig cell hypoplasia: absent luteinizing hormone receptor cell surface
RT expression caused by a novel homozygous mutation in the extracellular
RT domain.";
RL J. Clin. Endocrinol. Metab. 89:5161-5167(2004).
RN [34]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-564.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [35]
RP VARIANT LHR THR-152, AND CHARACTERIZATION OF VARIANT LHR THR-152.
RX PubMed=19551906; DOI=10.1002/humu.21072;
RA Qiao J., Han B., Liu B.-L., Chen X., Ru Y., Cheng K.-X., Chen F.-G.,
RA Zhao S.-X., Liang J., Lu Y.-L., Tang J.-F., Wu Y.-X., Wu W.-L., Chen J.-L.,
RA Chen M.-D., Song H.-D.;
RT "A splice site mutation combined with a novel missense mutation of LHCGR
RT cause male pseudohermaphroditism.";
RL Hum. Mutat. 30:E855-E865(2009).
CC -!- FUNCTION: Receptor for lutropin-choriogonadotropic hormone
CC (PubMed:11847099). The activity of this receptor is mediated by G
CC proteins which activate adenylate cyclase (PubMed:11847099).
CC {ECO:0000269|PubMed:11847099}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11847099};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=Long;
CC IsoId=P22888-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P22888-2; Sequence=VSP_001962;
CC -!- TISSUE SPECIFICITY: Gonadal and thyroid cells.
CC -!- PTM: Sulfated. {ECO:0000269|PubMed:11847099}.
CC -!- DISEASE: Familial male precocious puberty (FMPP) [MIM:176410]: In FMPP
CC the receptor is constitutively activated. {ECO:0000269|PubMed:11134146,
CC ECO:0000269|PubMed:11391350, ECO:0000269|PubMed:7629248,
CC ECO:0000269|PubMed:7692306, ECO:0000269|PubMed:7714085,
CC ECO:0000269|PubMed:7757065, ECO:0000269|PubMed:8281137,
CC ECO:0000269|PubMed:8829636, ECO:0000269|PubMed:8929952,
CC ECO:0000269|PubMed:9467560, ECO:0000269|PubMed:9661624}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Luteinizing hormone resistance (LHR) [MIM:238320]: An
CC autosomal recessive disorder characterized by unresponsiveness to
CC luteinizing hormone, defective sexual development in males, and
CC defective follicular development and ovulation, amenorrhea and
CC infertility in females. Two forms of the disorder have been defined in
CC males. Type 1 is a severe form characterized by complete 46,XY male
CC pseudohermaphroditism, low testosterone and high luteinizing hormone
CC levels, total lack of responsiveness to luteinizing and chorionic
CC gonadotropin hormones, lack of breast development, and absent
CC development of secondary male sex characteristics. Type 2, a milder
CC form, displays a broader range of phenotypic expression ranging from
CC micropenis to severe hypospadias. {ECO:0000269|PubMed:12050206,
CC ECO:0000269|PubMed:15372531, ECO:0000269|PubMed:15472221,
CC ECO:0000269|PubMed:19551906, ECO:0000269|PubMed:7719343,
CC ECO:0000269|PubMed:8559204, ECO:0000269|PubMed:9215288,
CC ECO:0000269|PubMed:9514160, ECO:0000269|PubMed:9626144,
CC ECO:0000269|PubMed:9626653}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/LHRID288.html";
CC -!- WEB RESOURCE: Name=Sequence-structure-function-analysis of glycoprotein
CC hormone receptors;
CC URL="http://www.ssfa-gphr.de/";
CC ---------------------------------------------------------------------------
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DR EMBL; M63108; AAA59515.1; -; mRNA.
DR EMBL; S57793; AAB19917.2; -; mRNA.
DR EMBL; M73746; AAA70231.1; -; mRNA.
DR EMBL; X84753; CAA59234.1; -; Genomic_DNA.
DR EMBL; X84754; CAA59234.1; JOINED; Genomic_DNA.
DR EMBL; X84755; CAA59234.1; JOINED; Genomic_DNA.
DR EMBL; X84756; CAA59234.1; JOINED; Genomic_DNA.
DR EMBL; X84757; CAA59234.1; JOINED; Genomic_DNA.
DR EMBL; X84758; CAA59234.1; JOINED; Genomic_DNA.
DR EMBL; X84759; CAA59234.1; JOINED; Genomic_DNA.
DR EMBL; X84760; CAA59234.1; JOINED; Genomic_DNA.
DR EMBL; X84761; CAA59234.1; JOINED; Genomic_DNA.
DR EMBL; X84762; CAA59234.1; JOINED; Genomic_DNA.
DR EMBL; X84763; CAA59234.1; JOINED; Genomic_DNA.
DR EMBL; AC073082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF082076; AAC98291.1; -; Genomic_DNA.
DR EMBL; AF024642; AAB88417.1; -; Genomic_DNA.
DR CCDS; CCDS1842.1; -. [P22888-1]
DR PIR; A36243; QRHUUT.
DR RefSeq; NP_000224.2; NM_000233.3. [P22888-1]
DR PDB; 7FIG; EM; 3.90 A; R=28-699.
DR PDB; 7FIH; EM; 3.20 A; R=28-699.
DR PDB; 7FII; EM; 4.30 A; R=28-699.
DR PDB; 7FIJ; EM; 3.80 A; R=28-699.
DR PDBsum; 7FIG; -.
DR PDBsum; 7FIH; -.
DR PDBsum; 7FII; -.
DR PDBsum; 7FIJ; -.
DR AlphaFoldDB; P22888; -.
DR SMR; P22888; -.
DR BioGRID; 110161; 12.
DR CORUM; P22888; -.
DR MINT; P22888; -.
DR STRING; 9606.ENSP00000294954; -.
DR BindingDB; P22888; -.
DR ChEMBL; CHEMBL1854; -.
DR DrugBank; DB06719; Buserelin.
DR DrugBank; DB00050; Cetrorelix.
DR DrugBank; DB00097; Choriogonadotropin alfa.
DR DrugBank; DB09126; Chorionic Gonadotropin (Human).
DR DrugBank; DB00014; Goserelin.
DR DrugBank; DB00044; Lutropin alfa.
DR DrugBank; DB00032; Menotropins.
DR DrugCentral; P22888; -.
DR GuidetoPHARMACOLOGY; 254; -.
DR GlyGen; P22888; 6 sites.
DR iPTMnet; P22888; -.
DR PhosphoSitePlus; P22888; -.
DR SwissPalm; P22888; -.
DR BioMuta; LHCGR; -.
DR DMDM; 281185513; -.
DR MassIVE; P22888; -.
DR PaxDb; P22888; -.
DR PeptideAtlas; P22888; -.
DR PRIDE; P22888; -.
DR Antibodypedia; 4073; 611 antibodies from 37 providers.
DR DNASU; 3973; -.
DR Ensembl; ENST00000294954.12; ENSP00000294954.6; ENSG00000138039.15. [P22888-1]
DR GeneID; 3973; -.
DR KEGG; hsa:3973; -.
DR MANE-Select; ENST00000294954.12; ENSP00000294954.6; NM_000233.4; NP_000224.2.
DR UCSC; uc002rwu.5; human. [P22888-1]
DR CTD; 3973; -.
DR DisGeNET; 3973; -.
DR GeneCards; LHCGR; -.
DR HGNC; HGNC:6585; LHCGR.
DR HPA; ENSG00000138039; Tissue enhanced (brain, ovary, testis).
DR MalaCards; LHCGR; -.
DR MIM; 152790; gene+phenotype.
DR MIM; 176410; phenotype.
DR MIM; 238320; phenotype.
DR neXtProt; NX_P22888; -.
DR OpenTargets; ENSG00000138039; -.
DR Orphanet; 3000; Familial male-limited precocious puberty.
DR Orphanet; 96265; Leydig cell hypoplasia due to complete LH resistance.
DR Orphanet; 96266; Leydig cell hypoplasia due to partial LH resistance.
DR Orphanet; 619; NON RARE IN EUROPE: Primary ovarian failure.
DR PharmGKB; PA30357; -.
DR VEuPathDB; HostDB:ENSG00000138039; -.
DR eggNOG; KOG2087; Eukaryota.
DR GeneTree; ENSGT00940000157364; -.
DR InParanoid; P22888; -.
DR OMA; CNTGIRQ; -.
DR OrthoDB; 257031at2759; -.
DR PhylomeDB; P22888; -.
DR TreeFam; TF316814; -.
DR PathwayCommons; P22888; -.
DR Reactome; R-HSA-375281; Hormone ligand-binding receptors.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR SignaLink; P22888; -.
DR SIGNOR; P22888; -.
DR BioGRID-ORCS; 3973; 8 hits in 1073 CRISPR screens.
DR ChiTaRS; LHCGR; human.
DR GeneWiki; Luteinizing_hormone/choriogonadotropin_receptor; -.
DR GenomeRNAi; 3973; -.
DR Pharos; P22888; Tclin.
DR PRO; PR:P22888; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P22888; protein.
DR Bgee; ENSG00000138039; Expressed in sural nerve and 87 other tissues.
DR ExpressionAtlas; P22888; baseline and differential.
DR Genevisible; P22888; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005768; C:endosome; TAS:ProtInc.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:BHF-UCL.
DR GO; GO:0031233; C:intrinsic component of external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:0038106; F:choriogonadotropin hormone binding; ISS:BHF-UCL.
DR GO; GO:0035472; F:choriogonadotropin hormone receptor activity; ISS:BHF-UCL.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0004964; F:luteinizing hormone receptor activity; IMP:UniProtKB.
DR GO; GO:0017046; F:peptide hormone binding; IEA:Ensembl.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; ISS:BHF-UCL.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:Ensembl.
DR GO; GO:0071371; P:cellular response to gonadotropin stimulus; ISS:BHF-UCL.
DR GO; GO:0071373; P:cellular response to luteinizing hormone stimulus; IMP:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; IEA:Ensembl.
DR GO; GO:0050890; P:cognition; IMP:UniProtKB.
DR GO; GO:0046544; P:development of secondary male sexual characteristics; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; TAS:ProtInc.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0042700; P:luteinizing hormone signaling pathway; IMP:UniProtKB.
DR GO; GO:0030539; P:male genitalia development; TAS:ProtInc.
DR GO; GO:0008584; P:male gonad development; IBA:GO_Central.
DR GO; GO:0001541; P:ovarian follicle development; IBA:GO_Central.
DR GO; GO:0022602; P:ovulation cycle process; IBA:GO_Central.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IEA:Ensembl.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IEA:Ensembl.
DR GO; GO:0046886; P:positive regulation of hormone biosynthetic process; IEA:Ensembl.
DR GO; GO:0032962; P:positive regulation of inositol trisphosphate biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR GO; GO:0006622; P:protein targeting to lysosome; IEA:Ensembl.
DR GO; GO:0090030; P:regulation of steroid hormone biosynthetic process; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0072520; P:seminiferous tubule development; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0060065; P:uterus development; IEA:Ensembl.
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 3D-structure; Alternative splicing; Cell membrane; Disease variant;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Leucine-rich repeat; Lipoprotein; Membrane; Palmitate; Receptor;
KW Reference proteome; Repeat; Signal; Sulfation; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..699
FT /note="Lutropin-choriogonadotropic hormone receptor"
FT /id="PRO_0000012780"
FT TOPO_DOM 27..363
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..385
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 417..439
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..462
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..482
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..505
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 506..525
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 526..549
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..570
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 571..594
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 595..605
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..627
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 628..699
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..66
FT /note="LRRNT"
FT REPEAT 96..115
FT /note="LRR 1"
FT REPEAT 124..145
FT /note="LRR 2"
FT REPEAT 149..171
FT /note="LRR 3"
FT REPEAT 175..196
FT /note="LRR 4"
FT REPEAT 198..220
FT /note="LRR 5"
FT REPEAT 223..244
FT /note="LRR 6"
FT MOD_RES 331
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000305|PubMed:11847099"
FT LIPID 643
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:15539429"
FT LIPID 644
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:15539429"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 439..514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 227..289
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_001962"
FT VARIANT 18
FT /note="Q -> QLQ (may be associated with earlier age of
FT onset of breast cancer and poor prognosis)"
FT /evidence="ECO:0000269|PubMed:9851790,
FT ECO:0000269|PubMed:9858858"
FT /id="VAR_003549"
FT VARIANT 131
FT /note="C -> R (in LHR; Leydig cell hypoplasia type 2;
FT dbSNP:rs121912527)"
FT /evidence="ECO:0000269|PubMed:9215288"
FT /id="VAR_010154"
FT VARIANT 144
FT /note="V -> F (in LHR; Leydig cell hypoplasia type 1;
FT exhibits a marked impairment of human chorionic
FT gonadotropin binding; shows the absence of the glycosylated
FT cell surface form; the mutant receptor is retained in the
FT endoplasmic reticulum; mutant receptors do not migrate to
FT the cell surface; dbSNP:rs121912539)"
FT /evidence="ECO:0000269|PubMed:15472221"
FT /id="VAR_062336"
FT VARIANT 152
FT /note="I -> T (in LHR; reveals a marked impairment of human
FT chorionic gonadotropin binding and signal transduction)"
FT /evidence="ECO:0000269|PubMed:19551906"
FT /id="VAR_062337"
FT VARIANT 284
FT /note="N -> S"
FT /evidence="ECO:0000269|PubMed:10215412"
FT /id="VAR_003550"
FT VARIANT 291
FT /note="N -> S (in dbSNP:rs12470652)"
FT /id="VAR_055922"
FT VARIANT 306
FT /note="S -> N"
FT /evidence="ECO:0000269|PubMed:10215412"
FT /id="VAR_003551"
FT VARIANT 312
FT /note="N -> S (in dbSNP:rs2293275)"
FT /evidence="ECO:0000269|PubMed:2244890,
FT ECO:0000269|PubMed:7556872"
FT /id="VAR_060737"
FT VARIANT 343
FT /note="C -> S (in LHR; Leydig cell hypoplasia type 1;
FT completely devoided of hormone-induced cAMP reporter gene
FT activation; although initial translocation to the
FT endoplasmic reticulum is normal translocation is halted or
FT misrouted and the mutant does not reach the cell surface
FT and cannot bind hormone; dbSNP:rs121912536)"
FT /evidence="ECO:0000269|PubMed:12050206"
FT /id="VAR_010155"
FT VARIANT 354
FT /note="E -> K (in LHR; Leydig cell hypoplasia type 1;
FT dbSNP:rs121912529)"
FT /evidence="ECO:0000269|PubMed:9626144"
FT /id="VAR_003552"
FT VARIANT 368
FT /note="L -> P (in FMPP; cells expressing the mutation
FT display up to a 12-fold increase in basal cAMP production
FT compared with cells expressing the same number of cell
FT surface wild-type receptor indicating constitutive
FT activation of the mutant receptor; dbSNP:rs121912533)"
FT /evidence="ECO:0000269|PubMed:11134146"
FT /id="VAR_062338"
FT VARIANT 373
FT /note="A -> V (in FMPP; dbSNP:rs121912528)"
FT /evidence="ECO:0000269|PubMed:9467560"
FT /id="VAR_003553"
FT VARIANT 398
FT /note="M -> T (in FMPP; dbSNP:rs121912526)"
FT /evidence="ECO:0000269|PubMed:8929952"
FT /id="VAR_003554"
FT VARIANT 457
FT /note="L -> R (in FMPP; dbSNP:rs121912535)"
FT /evidence="ECO:0000269|PubMed:9661624"
FT /id="VAR_010156"
FT VARIANT 502
FT /note="L -> P (in LHR; Leydig cell hypoplasia type 1; shows
FT reduced cAMP production and ligand binding; receptor
FT trafficking is not affected by the mutation;
FT dbSNP:rs121912538)"
FT /evidence="ECO:0000269|PubMed:15372531"
FT /id="VAR_062339"
FT VARIANT 542
FT /note="I -> L (in FMPP; dbSNP:rs121912531)"
FT /id="VAR_010157"
FT VARIANT 543
FT /note="C -> R (in LHR; Leydig cell hypoplasia type 1;
FT completely devoided of hormone-induced cAMP reporter gene
FT activation; although initial translocation to the
FT endoplasmic reticulum is normal translocation is halted or
FT misrouted and the mutant does not reach the cell surface
FT and cannot bind hormone; dbSNP:rs121912537)"
FT /evidence="ECO:0000269|PubMed:12050206"
FT /id="VAR_010158"
FT VARIANT 564
FT /note="D -> G (in FMPP; dbSNP:rs121912540)"
FT /evidence="ECO:0000269|PubMed:11391350"
FT /id="VAR_010159"
FT VARIANT 564
FT /note="D -> N (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035764"
FT VARIANT 568
FT /note="A -> V (in FMPP; dbSNP:rs121912534)"
FT /evidence="ECO:0000269|PubMed:11134146,
FT ECO:0000269|PubMed:7629248"
FT /id="VAR_003555"
FT VARIANT 571
FT /note="M -> I (in FMPP; dbSNP:rs121912519)"
FT /evidence="ECO:0000269|PubMed:8281137"
FT /id="VAR_003556"
FT VARIANT 572
FT /note="A -> V (in FMPP; dbSNP:rs121912522)"
FT /evidence="ECO:0000269|PubMed:7714085"
FT /id="VAR_003557"
FT VARIANT 575
FT /note="I -> L (in FMPP; dbSNP:rs767343825)"
FT /id="VAR_010160"
FT VARIANT 577
FT /note="T -> I (in FMPP; dbSNP:rs121912521)"
FT /evidence="ECO:0000269|PubMed:7757065,
FT ECO:0000269|PubMed:8829636"
FT /id="VAR_003558"
FT VARIANT 578
FT /note="D -> E (in FMPP)"
FT /id="VAR_010161"
FT VARIANT 578
FT /note="D -> G (in FMPP; dbSNP:rs121912518)"
FT /evidence="ECO:0000269|PubMed:7692306,
FT ECO:0000269|PubMed:8281137"
FT /id="VAR_003559"
FT VARIANT 578
FT /note="D -> H (in Leydig cell tumor; somatic mutation;
FT causes receptor activation and precocious puberty;
FT dbSNP:rs121912532)"
FT /evidence="ECO:0000269|PubMed:10580072"
FT /id="VAR_010162"
FT VARIANT 578
FT /note="D -> Y (in FMPP; dbSNP:rs121912532)"
FT /id="VAR_010163"
FT VARIANT 581
FT /note="C -> R (in FMPP)"
FT /id="VAR_010164"
FT VARIANT 593
FT /note="A -> P (in LHR; Leydig cell hypoplasia type 1;
FT abolishes signal transduction; dbSNP:rs121912520)"
FT /evidence="ECO:0000269|PubMed:7719343"
FT /id="VAR_003560"
FT VARIANT 608..609
FT /note="Missing (in LHR; Leydig cell hypoplasia type 1)"
FT /evidence="ECO:0000269|PubMed:9514160"
FT /id="VAR_003561"
FT VARIANT 616
FT /note="S -> Y (in LHR; Leydig cell hypoplasia type 1;
FT micropenis; dbSNP:rs121912525)"
FT /evidence="ECO:0000269|PubMed:8559204"
FT /id="VAR_003562"
FT VARIANT 625
FT /note="I -> K (in LHR; Leydig cell hypoplasia type 2;
FT dbSNP:rs121912530)"
FT /evidence="ECO:0000269|PubMed:9626653"
FT /id="VAR_003563"
FT MUTAGEN 331
FT /note="Y->F: Reduces intracellular cAMP accumulation."
FT /evidence="ECO:0000269|PubMed:11847099"
FT MUTAGEN 333
FT /note="Y->F: No change in intracellular cAMP accumulation."
FT /evidence="ECO:0000269|PubMed:11847099"
FT MUTAGEN 643
FT /note="C->G: Loss of palmitoylation."
FT /evidence="ECO:0000269|PubMed:15539429"
FT MUTAGEN 644
FT /note="C->G: Loss of palmitoylation."
FT /evidence="ECO:0000269|PubMed:15539429"
FT CONFLICT 7
FT /note="A -> P (in Ref. 3; AAA70231)"
FT /evidence="ECO:0000305"
FT CONFLICT 19
FT /note="P -> A (in Ref. 3; AAA70231)"
FT /evidence="ECO:0000305"
FT CONFLICT 27..28
FT /note="EA -> R (in Ref. 3; AAA70231)"
FT /evidence="ECO:0000305"
FT CONFLICT 44..51
FT /note="CPGPTAGL -> APAPRPS (in Ref. 3; AAA70231)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="A -> S (in Ref. 3; AAA70231)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="R -> G (in Ref. 1; AAA59515 and 4; CAA59234)"
FT /evidence="ECO:0000305"
FT CONFLICT 262..263
FT /note="RE -> KQ (in Ref. 3; AAA70231)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="E -> R (in Ref. 3; AAA70231)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="T -> H (in Ref. 3; AAA70231)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="Q -> L (in Ref. 3; AAA70231)"
FT /evidence="ECO:0000305"
FT CONFLICT 311..323
FT /note="Missing (in Ref. 3; AAA70231)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="F -> L (in Ref. 3; AAA70231)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="F -> L (in Ref. 3; AAA70231)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="E -> DP (in Ref. 3; AAA70231)"
FT /evidence="ECO:0000305"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:7FIH"
FT TURN 66..71
FT /evidence="ECO:0007829|PDB:7FIH"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:7FIH"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:7FIH"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:7FIH"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:7FIH"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:7FIH"
FT TURN 166..171
FT /evidence="ECO:0007829|PDB:7FIH"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:7FIH"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:7FIH"
FT STRAND 193..203
FT /evidence="ECO:0007829|PDB:7FIH"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:7FIH"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:7FIH"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:7FIH"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:7FIH"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:7FIH"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:7FIH"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:7FIH"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:7FIH"
FT HELIX 276..282
FT /evidence="ECO:0007829|PDB:7FIH"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:7FIH"
FT HELIX 360..372
FT /evidence="ECO:0007829|PDB:7FIH"
FT HELIX 375..385
FT /evidence="ECO:0007829|PDB:7FIH"
FT HELIX 393..421
FT /evidence="ECO:0007829|PDB:7FIH"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:7FIH"
FT HELIX 426..434
FT /evidence="ECO:0007829|PDB:7FIH"
FT HELIX 437..469
FT /evidence="ECO:0007829|PDB:7FIH"
FT HELIX 480..497
FT /evidence="ECO:0007829|PDB:7FIH"
FT HELIX 500..503
FT /evidence="ECO:0007829|PDB:7FIH"
FT HELIX 522..553
FT /evidence="ECO:0007829|PDB:7FIH"
FT STRAND 556..559
FT /evidence="ECO:0007829|PDB:7FIH"
FT TURN 561..563
FT /evidence="ECO:0007829|PDB:7FIH"
FT HELIX 564..593
FT /evidence="ECO:0007829|PDB:7FIH"
FT HELIX 601..611
FT /evidence="ECO:0007829|PDB:7FIH"
FT HELIX 614..623
FT /evidence="ECO:0007829|PDB:7FIH"
FT TURN 624..626
FT /evidence="ECO:0007829|PDB:7FIH"
FT HELIX 628..641
FT /evidence="ECO:0007829|PDB:7FIH"
SQ SEQUENCE 699 AA; 78643 MW; 2E3D93F4621BA842 CRC64;
MKQRFSALQL LKLLLLLQPP LPRALREALC PEPCNCVPDG ALRCPGPTAG LTRLSLAYLP
VKVIPSQAFR GLNEVIKIEI SQIDSLERIE ANAFDNLLNL SEILIQNTKN LRYIEPGAFI
NLPRLKYLSI CNTGIRKFPD VTKVFSSESN FILEICDNLH ITTIPGNAFQ GMNNESVTLK
LYGNGFEEVQ SHAFNGTTLT SLELKENVHL EKMHNGAFRG ATGPKTLDIS STKLQALPSY
GLESIQRLIA TSSYSLKKLP SRETFVNLLE ATLTYPSHCC AFRNLPTKEQ NFSHSISENF
SKQCESTVRK VNNKTLYSSM LAESELSGWD YEYGFCLPKT PRCAPEPDAF NPCEDIMGYD
FLRVLIWLIN ILAIMGNMTV LFVLLTSRYK LTVPRFLMCN LSFADFCMGL YLLLIASVDS
QTKGQYYNHA IDWQTGSGCS TAGFFTVFAS ELSVYTLTVI TLERWHTITY AIHLDQKLRL
RHAILIMLGG WLFSSLIAML PLVGVSNYMK VSICFPMDVE TTLSQVYILT ILILNVVAFF
IICACYIKIY FAVRNPELMA TNKDTKIAKK MAILIFTDFT CMAPISFFAI SAAFKVPLIT
VTNSKVLLVL FYPINSCANP FLYAIFTKTF QRDFFLLLSK FGCCKRRAEL YRRKDFSAYT
SNCKNGFTGS NKPSQSTLKL STLHCQGTAL LDKTRYTEC
