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FSHR_HUMAN
ID   FSHR_HUMAN              Reviewed;         695 AA.
AC   P23945; A0A0A0MSC5; A8K947; G5CBS7; G5E967; J3KQ00; Q05AH0; Q16225; Q4QRJ3;
AC   Q4ZFZ2; Q53RW2;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 3.
DT   03-AUG-2022, entry version 227.
DE   RecName: Full=Follicle-stimulating hormone receptor;
DE            Short=FSH-R;
DE   AltName: Full=Follitropin receptor;
DE   Flags: Precursor;
GN   Name=FSHR; Synonyms=LGR1;
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] (ISOFORM LONG), AND VARIANT SER-680.
RC   TISSUE=Ovary;
RX   PubMed=1709010; DOI=10.1016/0006-291x(91)91682-3;
RA   Minegish T., Nakamura K., Takakura Y., Ibuki Y., Igarashi M.;
RT   "Cloning and sequencing of human FSH receptor cDNA.";
RL   Biochem. Biophys. Res. Commun. 175:1125-1130(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT THR-307.
RX   PubMed=1322283; DOI=10.1210/endo.131.2.1322283;
RA   Tilly J.L., Aihara T., Nishimori K., Jia X.-C., Billig H., Kowalski K.I.,
RA   Perlas E.A., Hsueh A.J.;
RT   "Expression of recombinant human follicle-stimulating hormone receptor:
RT   species-specific ligand binding, signal transduction, and identification of
RT   multiple ovarian messenger ribonucleic acid transcripts.";
RL   Endocrinology 131:799-806(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT THR-307.
RC   TISSUE=Testis;
RX   PubMed=1301382; DOI=10.1016/0303-7207(92)90220-z;
RA   Kelton C.A., Cheng S.V., Nugent N.P., Schweickhardt R.L., Rosenthal J.L.,
RA   Overton S.A., Wands G.D., Kuzeja J.B., Luchette C.A., Chappel S.C.;
RT   "The cloning of the human follicle stimulating hormone receptor and its
RT   expression in COS-7, CHO, and Y-1 cells.";
RL   Mol. Cell. Endocrinol. 89:141-151(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC   TISSUE=Adipose tissue;
RA   Liu X., Huang H., Sheng J.;
RT   "FSHR expression in adipose tissue.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), AND VARIANT THR-307.
RC   TISSUE=Testis;
RA   Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT   "cDNA clones of human proteins involved in signal transduction sequenced by
RT   the Guthrie cDNA resource center (www.cdna.org).";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), AND VARIANT THR-307.
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-680.
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-680.
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND 3), AND VARIANTS
RP   THR-307 AND SER-680.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-342 (ISOFORM SHORT), AND VARIANT THR-307.
RC   TISSUE=Testis;
RX   PubMed=1359889; DOI=10.1016/0006-291x(92)91341-m;
RA   Gromoll J., Gudermann T., Nieschlag E.;
RT   "Molecular cloning of a truncated isoform of the human follicle stimulating
RT   hormone receptor.";
RL   Biochem. Biophys. Res. Commun. 188:1077-1083(1992).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51.
RX   PubMed=7926278; DOI=10.1016/0303-7207(94)90102-3;
RA   Gromoll J., Dankbar B., Gudermann T.;
RT   "Characterization of the 5' flanking region of the human follicle-
RT   stimulating hormone receptor gene.";
RL   Mol. Cell. Endocrinol. 102:93-102(1994).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 286-695, AND VARIANTS THR-307 AND
RP   SER-680.
RX   PubMed=7916967; DOI=10.1677/jme.0.0120265;
RA   Gromoll J., Ried T., Holtgreve-Grez H., Nieschlag E., Gudermann T.;
RT   "Localization of the human FSH receptor to chromosome 2p21 using a genomic
RT   probe comprising exon 10.";
RL   J. Mol. Endocrinol. 12:265-271(1994).
RN   [13]
RP   FUNCTION, SUBCELLULAR LOCATION, SULFATION AT TYR-335, AND MUTAGENESIS OF
RP   TYR-330 AND TYR-335.
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   [14]
RP   ALTERNATIVE SPLICING (ISOFORM 4).
RX   PubMed=11872202; DOI=10.1016/s0015-0282(01)03221-6;
RA   Song G.J., Park Y.S., Lee Y.S., Lee C.C., Kang I.S.;
RT   "Alternatively spliced variants of the follicle-stimulating hormone
RT   receptor gene in the testis of infertile men.";
RL   Fertil. Steril. 77:499-504(2002).
RN   [15]
RP   INTERACTION WITH APPL2.
RX   PubMed=17030088; DOI=10.1016/j.mce.2006.08.014;
RA   Nechamen C.A., Thomas R.M., Dias J.A.;
RT   "APPL1, APPL2, Akt2 and FOXO1a interact with FSHR in a potential signaling
RT   complex.";
RL   Mol. Cell. Endocrinol. 260:93-99(2007).
RN   [16]
RP   3D-STRUCTURE MODELING OF 49-228.
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   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) OF 17-268 IN COMPLEX WITH FSHA AND
RP   FSHB, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-191.
RX   PubMed=15662415; DOI=10.1038/nature03206;
RA   Fan Q.R., Hendrickson W.A.;
RT   "Structure of human follicle-stimulating hormone in complex with its
RT   receptor.";
RL   Nature 433:269-277(2005).
RN   [18] {ECO:0007744|PDB:4MQW}
RP   X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 16-366 OF HOMOTRIMER IN COMPLEX
RP   WITH CGA AND FSHB, FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION AT
RP   ASN-191, AND DISULFIDE BONDS.
RX   PubMed=24692546; DOI=10.1074/jbc.m114.549592;
RA   Jiang X., Fischer D., Chen X., McKenna S.D., Liu H., Sriraman V., Yu H.N.,
RA   Goutopoulos A., Arkinstall S., He X.;
RT   "Evidence for follicle-stimulating hormone receptor as a functional
RT   trimer.";
RL   J. Biol. Chem. 289:14273-14282(2014).
RN   [19]
RP   VARIANT ODG1 VAL-189.
RX   PubMed=7553856; DOI=10.1016/0092-8674(95)90275-9;
RA   Aittomaeki K., Lucena J.L.D., Pakarinen P., Sistonen P., Tapanainen J.,
RA   Gromoll J., Kaskikari R., Sankila E.-M., Lehvaslaiho H., Engel A.R.,
RA   Nieschlag E., Huhtaniemi I., de la Chapelle A.;
RT   "Mutation in the follicle-stimulating hormone receptor gene causes
RT   hereditary hypergonadotropic ovarian failure.";
RL   Cell 82:959-968(1995).
RN   [20]
RP   VARIANT OVARIAN SEX CORD TUMOR SER-591.
RX   PubMed=9100567; DOI=10.1210/jcem.82.4.3870;
RA   Kotlar T.J., Young R.H., Albanese C., Crowley W.F. Jr., Scully R.E.,
RA   Jameson J.L.;
RT   "A mutation in the follicle-stimulating hormone receptor occurs frequently
RT   in human ovarian sex cord tumors.";
RL   J. Clin. Endocrinol. Metab. 82:1020-1026(1997).
RN   [21]
RP   VARIANT FSHR ACTIVATION GLY-567, AND CHARACTERIZATION OF VARIANT FSHR
RP   ACTIVATION GLY-567.
RX   PubMed=8636335; DOI=10.1210/jcem.81.4.8636335;
RA   Gromoll J., Simoni M., Nieschlag E.;
RT   "An activating mutation of the follicle-stimulating hormone receptor
RT   autonomously sustains spermatogenesis in a hypophysectomized man.";
RL   J. Clin. Endocrinol. Metab. 81:1367-1370(1996).
RN   [22]
RP   VARIANT ODG1 VAL-189.
RX   PubMed=9851774; DOI=10.1210/jcem.83.12.5306;
RA   Jiang M., Aittomaeki K., Nilsson C., Pakarinen P., Iitia A., Torresani T.,
RA   Simonsen H., Goh V., Pettersson K., de la Chapelle A., Huhtaniemi I.;
RT   "The frequency of an inactivating point mutation (566C-->T) of the human
RT   follicle-stimulating hormone receptor gene in four populations using
RT   allele-specific hybridization and time-resolved fluorometry.";
RL   J. Clin. Endocrinol. Metab. 83:4338-4343(1998).
RN   [23]
RP   VARIANTS ODG1 THR-160 AND CYS-573.
RX   PubMed=9769327; DOI=10.1172/jci3795;
RA   Beau I., Touraine P., Meduri G., Gougeon A., Desroches A., Matuchansky C.,
RA   Milgrom E., Kuttenn F., Misrahi M.;
RT   "A novel phenotype related to partial loss of function mutations of the
RT   follicle stimulating hormone receptor.";
RL   J. Clin. Invest. 102:1352-1359(1998).
RN   [24]
RP   VARIANTS ODG1 VAL-224 AND VAL-601, AND CHARACTERIZATION OF VARIANTS ODG1
RP   VAL-224; CYS-573 AND VAL-601.
RX   PubMed=10551778; DOI=10.1210/mend.13.11.0370;
RA   Touraine P., Beau I., Gougeon A., Meduri G., Desroches A., Pichard C.,
RA   Detoeuf M., Paniel B., Prieur M., Zorn J.-R., Milgrom E., Kuttenn F.,
RA   Misrahi M.;
RT   "New natural inactivating mutations of the follicle-stimulating hormone
RT   receptor: correlations between receptor function and phenotype.";
RL   Mol. Endocrinol. 13:1844-1854(1999).
RN   [25]
RP   VARIANTS THR-307; ARG-524 AND SER-680.
RX   PubMed=10391209; DOI=10.1038/10290;
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RT   "Characterization of single-nucleotide polymorphisms in coding regions of
RT   human genes.";
RL   Nat. Genet. 22:231-238(1999).
RN   [26]
RP   ERRATUM OF PUBMED:10391209.
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RL   Nat. Genet. 23:373-373(1999).
RN   [27]
RP   VARIANTS THR-307 AND SER-680.
RX   PubMed=12059813; DOI=10.1046/j.1439-0272.2002.00493.x;
RA   Asatiani K., Gromoll J., Eckardstein S.V., Zitzmann M., Nieschlag E.,
RA   Simoni M.;
RT   "Distribution and function of FSH receptor genetic variants in normal
RT   men.";
RL   Andrologia 34:172-176(2002).
RN   [28]
RP   VARIANT ODG1 THR-419, AND CHARACTERIZATION OF VARIANT ODG1 THR-419.
RX   PubMed=11889179; DOI=10.1210/jcem.87.3.8319;
RA   Doherty E., Pakarinen P., Tiitinen A., Kiilavuori A., Huhtaniemi I.,
RA   Forrest S., Aittomaeki K.;
RT   "A novel mutation in the FSH receptor inhibiting signal transduction and
RT   causing primary ovarian failure.";
RL   J. Clin. Endocrinol. Metab. 87:1151-1155(2002).
RN   [29]
RP   VARIANT ODG1 ARG-348.
RX   PubMed=12571157; DOI=10.1093/humrep/deg046;
RA   Allen L.A., Achermann J.C., Pakarinen P., Kotlar T.J., Huhtaniemi I.T.,
RA   Jameson J.L., Cheetham T.D., Ball S.G.;
RT   "A novel loss of function mutation in exon 10 of the FSH receptor gene
RT   causing hypergonadotrophic hypogonadism: clinical and molecular
RT   characteristics.";
RL   Hum. Reprod. 18:251-256(2003).
RN   [30]
RP   VARIANT ODG1 THR-519, AND CHARACTERIZATION OF VARIANT ODG1 THR-519.
RX   PubMed=12915623; DOI=10.1210/jc.2003-030217;
RA   Meduri G., Touraine P., Beau I., Lahuna O., Desroches A.,
RA   Vacher-Lavenu M.C., Kuttenn F., Misrahi M.;
RT   "Delayed puberty and primary amenorrhea associated with a novel mutation of
RT   the human follicle-stimulating hormone receptor: clinical, histological,
RT   and molecular studies.";
RL   J. Clin. Endocrinol. Metab. 88:3491-3498(2003).
RN   [31]
RP   VARIANT OHSS ILE-449.
RX   PubMed=12930927; DOI=10.1056/nejmoa030065;
RA   Vasseur C., Rodien P., Beau I., Desroches A., Gerard C., de Poncheville L.,
RA   Chaplot S., Savagner F., Croue A., Mathieu E., Lahlou N., Descamps P.,
RA   Misrahi M.;
RT   "A chorionic gonadotropin-sensitive mutation in the follicle-stimulating
RT   hormone receptor as a cause of familial gestational spontaneous ovarian
RT   hyperstimulation syndrome.";
RL   N. Engl. J. Med. 349:753-759(2003).
RN   [32]
RP   VARIANT OHSS ASN-567.
RX   PubMed=12930928; DOI=10.1056/nejmoa030064;
RA   Smits G., Olatunbosun O., Delbaere A., Pierson R., Vassart G.,
RA   Costagliola S.;
RT   "Ovarian hyperstimulation syndrome due to a mutation in the follicle-
RT   stimulating hormone receptor.";
RL   N. Engl. J. Med. 349:760-766(2003).
RN   [33]
RP   VARIANT OHSS ALA-449, AND CHARACTERIZATION OF VARIANT OHSS ALA-449.
RX   PubMed=15080154; DOI=10.1210/jc.2003-031910;
RA   Montanelli L., Delbaere A., Di Carlo C., Nappi C., Smits G., Vassart G.,
RA   Costagliola S.;
RT   "A mutation in the follicle-stimulating hormone receptor as a cause of
RT   familial spontaneous ovarian hyperstimulation syndrome.";
RL   J. Clin. Endocrinol. Metab. 89:1255-1258(2004).
RN   [34]
RP   VARIANT OHSS THR-545, AND CHARACTERIZATION OF VARIANT OHSS THR-545.
RX   PubMed=16278261; DOI=10.1210/jc.2005-1580;
RA   De Leener A., Montanelli L., Van Durme J., Chae H., Smits G., Vassart G.,
RA   Costagliola S.;
RT   "Presence and absence of follicle-stimulating hormone receptor mutations
RT   provide some insights into spontaneous ovarian hyperstimulation syndrome
RT   physiopathology.";
RL   J. Clin. Endocrinol. Metab. 91:555-562(2006).
RN   [35]
RP   VARIANT OHSS TYR-128, AND CHARACTERIZATION OF VARIANT OHSS TYR-128.
RX   PubMed=17721928; DOI=10.1002/humu.20604;
RA   De Leener A., Caltabiano G., Erkan S., Idil M., Vassart G., Pardo L.,
RA   Costagliola S.;
RT   "Identification of the first germline mutation in the extracellular domain
RT   of the follitropin receptor responsible for spontaneous ovarian
RT   hyperstimulation syndrome.";
RL   Hum. Mutat. 29:91-98(2008).
RN   [36]
RP   VARIANT OHSS ILE-512, CHARACTERIZATION OF VARIANT OHSS ILE-512, AND
RP   FUNCTION.
RX   PubMed=24058690; DOI=10.1371/journal.pone.0075478;
RA   Uchida S., Uchida H., Maruyama T., Kajitani T., Oda H., Miyazaki K.,
RA   Kagami M., Yoshimura Y.;
RT   "Molecular analysis of a mutated FSH receptor detected in a patient with
RT   spontaneous ovarian hyperstimulation syndrome.";
RL   PLoS ONE 8:E75478-E75478(2013).
RN   [37]
RP   VARIANTS OHSS ALA-514 AND VAL-575, AND CHARACTERIZATION OF VARIANTS OHSS
RP   ALA-514 AND VAL-575.
RX   PubMed=25581598; DOI=10.1210/jc.2014-3662;
RA   Desai S.S., Achrekar S.K., Sahasrabuddhe K.A., Meharji P.K., Desai S.K.,
RA   Mangoli V.S., Mahale S.D.;
RT   "Functional characterization of two naturally occurring mutations
RT   (Val514Ala and Ala575Val) in follicle-stimulating hormone receptor.";
RL   J. Clin. Endocrinol. Metab. 100:E638-E645(2015).
CC   -!- FUNCTION: G protein-coupled receptor for follitropin, the follicle-
CC       stimulating hormone (PubMed:11847099, PubMed:24058690,
CC       PubMed:24692546). Through cAMP production activates the downstream
CC       PI3K-AKT and ERK1/ERK2 signaling pathways (PubMed:24058690).
CC       {ECO:0000269|PubMed:11847099, ECO:0000269|PubMed:24058690,
CC       ECO:0000269|PubMed:24692546}.
CC   -!- SUBUNIT: Homotrimer. Functions as a homotrimer binding the FSH hormone
CC       heterodimer composed of CGA and FSHB (PubMed:24692546). Interacts with
CC       ARRB2 (By similarity). Interacts with APPL2; interaction is independent
CC       of follicle stimulating hormone stimulation (PubMed:17030088).
CC       {ECO:0000250|UniProtKB:P20395, ECO:0000269|PubMed:17030088,
CC       ECO:0000269|PubMed:24692546}.
CC   -!- INTERACTION:
CC       P23945; P27348: YWHAQ; NbExp=4; IntAct=EBI-848239, EBI-359854;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11847099,
CC       ECO:0000269|PubMed:24692546}; Multi-pass membrane protein
CC       {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=Long; Synonyms=R1;
CC         IsoId=P23945-1; Sequence=Displayed;
CC       Name=Short; Synonyms=E9Del;
CC         IsoId=P23945-2; Sequence=VSP_001953;
CC       Name=3; Synonyms=E6Del;
CC         IsoId=P23945-3; Sequence=VSP_043181;
CC       Name=4; Synonyms=E8'Inc;
CC         IsoId=P23945-4; Sequence=VSP_053411;
CC   -!- TISSUE SPECIFICITY: Sertoli cells and ovarian granulosa cells.
CC   -!- PTM: Sulfated. {ECO:0000269|PubMed:11847099}.
CC   -!- PTM: N-glycosylated; indirectly required for FSH-binding, possibly via
CC       a conformational change that allows high affinity binding of hormone.
CC       {ECO:0000250|UniProtKB:P20395}.
CC   -!- DISEASE: Ovarian dysgenesis 1 (ODG1) [MIM:233300]: An autosomal
CC       recessive disease characterized by primary amenorrhea, variable
CC       development of secondary sex characteristics, poorly developed streak
CC       ovaries, and high serum levels of follicle-stimulating hormone (FSH)
CC       and luteinizing hormone (LH). {ECO:0000269|PubMed:10551778,
CC       ECO:0000269|PubMed:11889179, ECO:0000269|PubMed:12571157,
CC       ECO:0000269|PubMed:12915623, ECO:0000269|PubMed:7553856,
CC       ECO:0000269|PubMed:9769327, ECO:0000269|PubMed:9851774}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Ovarian hyperstimulation syndrome (OHSS) [MIM:608115]:
CC       Disorder which occurs either spontaneously or most often as an
CC       iatrogenic complication of ovarian stimulation treatments for in vitro
CC       fertilization. The clinical manifestations vary from abdominal
CC       distention and discomfort to potentially life-threatening, massive
CC       ovarian enlargement and capillary leak with fluid sequestration.
CC       Pathologic features of this syndrome include the presence of multiple
CC       serous and hemorrhagic follicular cysts lined by luteinized cells, a
CC       condition called hyperreactio luteinalis. {ECO:0000269|PubMed:12930927,
CC       ECO:0000269|PubMed:12930928, ECO:0000269|PubMed:15080154,
CC       ECO:0000269|PubMed:16278261, ECO:0000269|PubMed:17721928,
CC       ECO:0000269|PubMed:24058690, ECO:0000269|PubMed:25581598}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       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=Sequence-structure-function-analysis of glycoprotein
CC       hormone receptors;
CC       URL="http://www.ssfa-gphr.de/";
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DR   EMBL; M65085; AAA52477.1; -; mRNA.
DR   EMBL; M95489; AAA52478.1; -; mRNA.
DR   EMBL; S59900; AAB26480.1; -; mRNA.
DR   EMBL; JN003607; AEI86722.1; -; mRNA.
DR   EMBL; AY429104; AAR07899.1; -; mRNA.
DR   EMBL; AK292562; BAF85251.1; -; mRNA.
DR   EMBL; AC007189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC079394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC092533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471053; EAX00188.1; -; Genomic_DNA.
DR   EMBL; CH471053; EAX00189.1; -; Genomic_DNA.
DR   EMBL; BC096831; AAH96831.1; -; mRNA.
DR   EMBL; BC118548; AAI18549.1; -; mRNA.
DR   EMBL; BC125270; AAI25271.1; -; mRNA.
DR   EMBL; X68044; CAA48179.1; -; mRNA.
DR   EMBL; S73199; AAB32071.1; -; Genomic_DNA.
DR   EMBL; S73526; AAB32225.1; -; Genomic_DNA.
DR   CCDS; CCDS1843.1; -. [P23945-1]
DR   CCDS; CCDS1844.2; -. [P23945-3]
DR   PIR; I57661; QRHUFT.
DR   RefSeq; NP_000136.2; NM_000145.3.
DR   RefSeq; NP_852111.2; NM_181446.2.
DR   PDB; 1XWD; X-ray; 2.92 A; C/F=17-268.
DR   PDB; 4AY9; X-ray; 2.50 A; X/Y/Z=17-366.
DR   PDB; 4MQW; X-ray; 2.90 A; X/Y/Z=16-366.
DR   PDBsum; 1XWD; -.
DR   PDBsum; 4AY9; -.
DR   PDBsum; 4MQW; -.
DR   AlphaFoldDB; P23945; -.
DR   SMR; P23945; -.
DR   BioGRID; 108770; 36.
DR   DIP; DIP-35605N; -.
DR   IntAct; P23945; 21.
DR   MINT; P23945; -.
DR   STRING; 9606.ENSP00000384708; -.
DR   BindingDB; P23945; -.
DR   ChEMBL; CHEMBL2024; -.
DR   DrugBank; DB00097; Choriogonadotropin alfa.
DR   DrugBank; DB09066; Corifollitropin alfa.
DR   DrugBank; DB00066; Follitropin.
DR   DrugBank; DB00032; Menotropins.
DR   DrugBank; DB04786; Suramin.
DR   DrugBank; DB00094; Urofollitropin.
DR   DrugCentral; P23945; -.
DR   GuidetoPHARMACOLOGY; 253; -.
DR   TCDB; 9.A.14.1.5; the g-protein-coupled receptor (gpcr) family.
DR   GlyGen; P23945; 4 sites.
DR   iPTMnet; P23945; -.
DR   PhosphoSitePlus; P23945; -.
DR   BioMuta; FSHR; -.
DR   DMDM; 311033420; -.
DR   MassIVE; P23945; -.
DR   PaxDb; P23945; -.
DR   PeptideAtlas; P23945; -.
DR   PRIDE; P23945; -.
DR   Antibodypedia; 15300; 706 antibodies from 36 providers.
DR   DNASU; 2492; -.
DR   Ensembl; ENST00000304421.8; ENSP00000306780.4; ENSG00000170820.12.
DR   GeneID; 2492; -.
DR   KEGG; hsa:2492; -.
DR   UCSC; uc002rww.4; human.
DR   UCSC; uc010fbn.4; human. [P23945-1]
DR   CTD; 2492; -.
DR   DisGeNET; 2492; -.
DR   GeneCards; FSHR; -.
DR   HGNC; HGNC:3969; FSHR.
DR   HPA; ENSG00000170820; Tissue enhanced (ovary, testis).
DR   MalaCards; FSHR; -.
DR   MIM; 136435; gene.
DR   MIM; 233300; phenotype.
DR   MIM; 608115; phenotype.
DR   neXtProt; NX_P23945; -.
DR   Orphanet; 243; 46,XX gonadal dysgenesis.
DR   Orphanet; 619; NON RARE IN EUROPE: Primary ovarian failure.
DR   Orphanet; 64739; Ovarian hyperstimulation syndrome.
DR   PharmGKB; PA28386; -.
DR   VEuPathDB; HostDB:ENSG00000170820; -.
DR   eggNOG; KOG2087; Eukaryota.
DR   HOGENOM; CLU_006130_1_1_1; -.
DR   InParanoid; P23945; -.
DR   OrthoDB; 257031at2759; -.
DR   PhylomeDB; P23945; -.
DR   TreeFam; TF316814; -.
DR   PathwayCommons; P23945; -.
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; P23945; -.
DR   SIGNOR; P23945; -.
DR   BioGRID-ORCS; 2492; 10 hits in 1071 CRISPR screens.
DR   ChiTaRS; FSHR; human.
DR   EvolutionaryTrace; P23945; -.
DR   GeneWiki; Follicle-stimulating_hormone_receptor; -.
DR   GenomeRNAi; 2492; -.
DR   Pharos; P23945; Tclin.
DR   PRO; PR:P23945; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; P23945; protein.
DR   Bgee; ENSG00000170820; Expressed in lower esophagus mucosa and 70 other tissues.
DR   ExpressionAtlas; P23945; baseline and differential.
DR   Genevisible; P23945; HS.
DR   GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0043235; C:receptor complex; IDA:UniProtKB.
DR   GO; GO:0004963; F:follicle-stimulating hormone receptor activity; IDA:UniProtKB.
DR   GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR   GO; GO:0007190; P:activation of adenylate cyclase activity; IBA:GO_Central.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IMP:UniProtKB.
DR   GO; GO:0007292; P:female gamete generation; TAS:ProtInc.
DR   GO; GO:0008585; P:female gonad development; TAS:ProtInc.
DR   GO; GO:0042699; P:follicle-stimulating hormone signaling pathway; IDA:UniProtKB.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0008406; P:gonad development; TAS:ProtInc.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0008584; P:male gonad development; IEP:UniProtKB.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR   GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:UniProtKB.
DR   GO; GO:0010738; P:regulation of protein kinase A signaling; IMP:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR002272; FSH_rcpt.
DR   InterPro; IPR024635; GnHR_TM.
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; IPR000372; LRRNT.
DR   PANTHER; PTHR24372:SF5; PTHR24372:SF5; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   Pfam; PF12369; GnHR_trans; 1.
DR   Pfam; PF13306; LRR_5; 2.
DR   Pfam; PF01462; LRRNT; 1.
DR   PRINTS; PR01143; FSHRECEPTOR.
DR   PRINTS; PR00373; GLYCHORMONER.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SMART; SM00013; LRRNT; 1.
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; Membrane; Receptor; Reference proteome; Repeat;
KW   Signal; Sulfation; Transducer; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..695
FT                   /note="Follicle-stimulating hormone receptor"
FT                   /id="PRO_0000012771"
FT   TOPO_DOM        18..366
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        367..387
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        388..398
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        399..421
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        422..443
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        444..465
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        466..485
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        486..508
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        509..528
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        529..550
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        551..573
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        574..597
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        598..608
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        609..630
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        631..695
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          18..46
FT                   /note="LRRNT"
FT   REPEAT          49..72
FT                   /note="LRR 1"
FT   REPEAT          73..97
FT                   /note="LRR 2"
FT   REPEAT          98..118
FT                   /note="LRR 3"
FT   REPEAT          119..143
FT                   /note="LRR 4"
FT   REPEAT          144..169
FT                   /note="LRR 5"
FT   REPEAT          170..192
FT                   /note="LRR 6"
FT   REPEAT          193..216
FT                   /note="LRR 7"
FT   REPEAT          217..240
FT                   /note="LRR 8"
FT   REPEAT          241..259
FT                   /note="LRR 9"
FT   MOD_RES         335
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000305|PubMed:11847099"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15662415,
FT                   ECO:0000269|PubMed:24692546, ECO:0007744|PDB:4MQW"
FT   CARBOHYD        199
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        318
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        18..25
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT                   ECO:0000269|PubMed:15662415, ECO:0000269|PubMed:24692546,
FT                   ECO:0007744|PDB:4MQW"
FT   DISULFID        23..32
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT                   ECO:0000269|PubMed:15662415, ECO:0000269|PubMed:24692546,
FT                   ECO:0007744|PDB:4MQW"
FT   DISULFID        275..346
FT                   /evidence="ECO:0000269|PubMed:24692546,
FT                   ECO:0007744|PDB:4MQW"
FT   DISULFID        276..356
FT                   /evidence="ECO:0000269|PubMed:24692546,
FT                   ECO:0007744|PDB:4MQW"
FT   DISULFID        276..292
FT                   /evidence="ECO:0000269|PubMed:24692546,
FT                   ECO:0007744|PDB:4MQW"
FT   DISULFID        292..338
FT                   /evidence="ECO:0000269|PubMed:24692546,
FT                   ECO:0007744|PDB:4MQW"
FT   DISULFID        442..517
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VAR_SEQ         149..174
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_043181"
FT   VAR_SEQ         223
FT                   /note="L -> LNRRTRTPTEPNVLLAKYPSGQGVLEEPESLSSSI (in isoform
FT                   4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_053411"
FT   VAR_SEQ         224..285
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:1359889"
FT                   /id="VSP_001953"
FT   VARIANT         128
FT                   /note="S -> Y (in OHSS; displays increase in affinity and
FT                   sensitivity toward hCG and does not show any constitutive
FT                   activity nor promiscuous activation by TSH;
FT                   dbSNP:rs121909665)"
FT                   /evidence="ECO:0000269|PubMed:17721928"
FT                   /id="VAR_039279"
FT   VARIANT         160
FT                   /note="I -> T (in ODG1; impairs cell surface expression)"
FT                   /evidence="ECO:0000269|PubMed:9769327"
FT                   /id="VAR_018045"
FT   VARIANT         189
FT                   /note="A -> V (in ODG1; very frequent in the Finnish
FT                   population)"
FT                   /evidence="ECO:0000269|PubMed:7553856,
FT                   ECO:0000269|PubMed:9851774"
FT                   /id="VAR_018046"
FT   VARIANT         224
FT                   /note="D -> V (in ODG1; FSH binding is barely detectable;
FT                   impaired targeting to the cell membrane; adenylate cyclase
FT                   stimulation by FSH is 4 +-2% residual activity)"
FT                   /evidence="ECO:0000269|PubMed:10551778"
FT                   /id="VAR_039280"
FT   VARIANT         307
FT                   /note="A -> T (in dbSNP:rs6165)"
FT                   /evidence="ECO:0000269|PubMed:10391209,
FT                   ECO:0000269|PubMed:12059813, ECO:0000269|PubMed:1301382,
FT                   ECO:0000269|PubMed:1322283, ECO:0000269|PubMed:1359889,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:7916967, ECO:0000269|Ref.5"
FT                   /id="VAR_013903"
FT   VARIANT         348
FT                   /note="P -> R (in ODG1)"
FT                   /evidence="ECO:0000269|PubMed:12571157"
FT                   /id="VAR_039281"
FT   VARIANT         419
FT                   /note="A -> T (in ODG1)"
FT                   /evidence="ECO:0000269|PubMed:11889179"
FT                   /id="VAR_018047"
FT   VARIANT         449
FT                   /note="T -> A (in OHSS; increase of receptor sensitivity to
FT                   both hCG and TSH together with an increase in basal
FT                   activity)"
FT                   /evidence="ECO:0000269|PubMed:15080154"
FT                   /id="VAR_039282"
FT   VARIANT         449
FT                   /note="T -> I (in OHSS; dbSNP:rs28928870)"
FT                   /evidence="ECO:0000269|PubMed:12930927"
FT                   /id="VAR_017244"
FT   VARIANT         512
FT                   /note="M -> I (in OHSS; inhibits activation of PI3K/AKT
FT                   signaling pathway; reduces cAMP production; no effect on
FT                   ERK1/2 signaling pathway activation)"
FT                   /evidence="ECO:0000269|PubMed:24058690"
FT                   /id="VAR_074535"
FT   VARIANT         514
FT                   /note="V -> A (in OHSS; increases cell surface expression;
FT                   no effect on hormone binding; increases signaling
FT                   activity)"
FT                   /evidence="ECO:0000269|PubMed:25581598"
FT                   /id="VAR_074536"
FT   VARIANT         519
FT                   /note="P -> T (in ODG1; totally impairs adenylate cyclase
FT                   stimulation in vitro; alters the cell surface targeting of
FT                   the receptor which remains trapped intracellularly)"
FT                   /evidence="ECO:0000269|PubMed:12915623"
FT                   /id="VAR_039283"
FT   VARIANT         524
FT                   /note="S -> R (in dbSNP:rs6167)"
FT                   /evidence="ECO:0000269|PubMed:10391209"
FT                   /id="VAR_013904"
FT   VARIANT         545
FT                   /note="I -> T (in OHSS; displays promiscuous activation by
FT                   both hCG and TSH together with detectable constitutive
FT                   activity)"
FT                   /evidence="ECO:0000269|PubMed:16278261"
FT                   /id="VAR_039284"
FT   VARIANT         567
FT                   /note="D -> G (activating mutation resulting in 1.5-fold
FT                   increase in basal cAMP production compared to the wild-type
FT                   receptor)"
FT                   /evidence="ECO:0000269|PubMed:8636335"
FT                   /id="VAR_039285"
FT   VARIANT         567
FT                   /note="D -> N (in OHSS; dbSNP:rs28928871)"
FT                   /evidence="ECO:0000269|PubMed:12930928"
FT                   /id="VAR_017245"
FT   VARIANT         573
FT                   /note="R -> C (in ODG1; alters signal transduction of the
FT                   receptor; adenylate cyclase stimulation by FSH is 24 +-4%
FT                   residual activity)"
FT                   /evidence="ECO:0000269|PubMed:10551778,
FT                   ECO:0000269|PubMed:9769327"
FT                   /id="VAR_018048"
FT   VARIANT         575
FT                   /note="A -> V (in OHSS; decreases cell surface expression;
FT                   no effect on hormone binding; increases levels of
FT                   internalized hormone receptor complex; cAMP levels are
FT                   similar to basal levels even at high doses of FSH
FT                   stimulation indicating reduced signaling)"
FT                   /evidence="ECO:0000269|PubMed:25581598"
FT                   /id="VAR_074537"
FT   VARIANT         591
FT                   /note="F -> S (in ovarian sex cord tumor; loss of
FT                   function)"
FT                   /evidence="ECO:0000269|PubMed:9100567"
FT                   /id="VAR_018049"
FT   VARIANT         601
FT                   /note="L -> V (in ODG1; binds FSH with a similar affinity
FT                   than the wild-type receptor; adenylate cyclase stimulation
FT                   by FSH is 12 +-3% residual activity)"
FT                   /evidence="ECO:0000269|PubMed:10551778"
FT                   /id="VAR_039286"
FT   VARIANT         680
FT                   /note="N -> S (associated with longer menstrual cycles;
FT                   dbSNP:rs6166)"
FT                   /evidence="ECO:0000269|PubMed:10391209,
FT                   ECO:0000269|PubMed:12059813, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:15815621, ECO:0000269|PubMed:1709010,
FT                   ECO:0000269|PubMed:7916967, ECO:0000269|Ref.8"
FT                   /id="VAR_013905"
FT   MUTAGEN         330
FT                   /note="Y->F: No change in intracellular cAMP accumulation."
FT                   /evidence="ECO:0000269|PubMed:11847099"
FT   MUTAGEN         335
FT                   /note="Y->F: Reduces intracellular cAMP accumulation."
FT                   /evidence="ECO:0000269|PubMed:11847099"
FT   CONFLICT        13
FT                   /note="S -> R (in Ref. 10; CAA48179)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        112
FT                   /note="N -> T (in Ref. 1; AAA52477)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        197..198
FT                   /note="EL -> AV (in Ref. 1; AAA52477)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        295
FT                   /note="S -> P (in Ref. 10; CAA48179)"
FT                   /evidence="ECO:0000305"
FT   STRAND          21..26
FT                   /evidence="ECO:0007829|PDB:4AY9"
FT   STRAND          29..34
FT                   /evidence="ECO:0007829|PDB:4AY9"
FT   STRAND          49..55
FT                   /evidence="ECO:0007829|PDB:4AY9"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:4AY9"
FT   TURN            63..68
FT                   /evidence="ECO:0007829|PDB:1XWD"
FT   STRAND          74..78
FT                   /evidence="ECO:0007829|PDB:4AY9"
FT   TURN            88..90
FT                   /evidence="ECO:0007829|PDB:4MQW"
FT   STRAND          99..105
FT                   /evidence="ECO:0007829|PDB:4AY9"
FT   STRAND          115..117
FT                   /evidence="ECO:0007829|PDB:1XWD"
FT   STRAND          124..130
FT                   /evidence="ECO:0007829|PDB:4AY9"
FT   STRAND          143..145
FT                   /evidence="ECO:0007829|PDB:4AY9"
FT   STRAND          147..153
FT                   /evidence="ECO:0007829|PDB:4AY9"
FT   STRAND          168..171
FT                   /evidence="ECO:0007829|PDB:4AY9"
FT   STRAND          173..176
FT                   /evidence="ECO:0007829|PDB:4AY9"
FT   TURN            187..192
FT                   /evidence="ECO:0007829|PDB:4MQW"
FT   STRAND          193..199
FT                   /evidence="ECO:0007829|PDB:4AY9"
FT   TURN            211..216
FT                   /evidence="ECO:0007829|PDB:4AY9"
FT   STRAND          221..224
FT                   /evidence="ECO:0007829|PDB:4AY9"
FT   STRAND          235..237
FT                   /evidence="ECO:0007829|PDB:4AY9"
FT   STRAND          243..245
FT                   /evidence="ECO:0007829|PDB:4AY9"
FT   TURN            258..260
FT                   /evidence="ECO:0007829|PDB:4AY9"
FT   STRAND          266..268
FT                   /evidence="ECO:0007829|PDB:4AY9"
FT   HELIX           272..280
FT                   /evidence="ECO:0007829|PDB:4AY9"
FT   STRAND          345..348
FT                   /evidence="ECO:0007829|PDB:4AY9"
FT   STRAND          351..353
FT                   /evidence="ECO:0007829|PDB:4MQW"
SQ   SEQUENCE   695 AA;  78265 MW;  766BC421014CD5A4 CRC64;
     MALLLVSLLA FLSLGSGCHH RICHCSNRVF LCQESKVTEI PSDLPRNAIE LRFVLTKLRV
     IQKGAFSGFG DLEKIEISQN DVLEVIEADV FSNLPKLHEI RIEKANNLLY INPEAFQNLP
     NLQYLLISNT GIKHLPDVHK IHSLQKVLLD IQDNINIHTI ERNSFVGLSF ESVILWLNKN
     GIQEIHNCAF NGTQLDELNL SDNNNLEELP NDVFHGASGP VILDISRTRI HSLPSYGLEN
     LKKLRARSTY NLKKLPTLEK LVALMEASLT YPSHCCAFAN WRRQISELHP ICNKSILRQE
     VDYMTQARGQ RSSLAEDNES SYSRGFDMTY TEFDYDLCNE VVDVTCSPKP DAFNPCEDIM
     GYNILRVLIW FISILAITGN IIVLVILTTS QYKLTVPRFL MCNLAFADLC IGIYLLLIAS
     VDIHTKSQYH NYAIDWQTGA GCDAAGFFTV FASELSVYTL TAITLERWHT ITHAMQLDCK
     VQLRHAASVM VMGWIFAFAA ALFPIFGISS YMKVSICLPM DIDSPLSQLY VMSLLVLNVL
     AFVVICGCYI HIYLTVRNPN IVSSSSDTRI AKRMAMLIFT DFLCMAPISF FAISASLKVP
     LITVSKAKIL LVLFHPINSC ANPFLYAIFT KNFRRDFFIL LSKCGCYEMQ AQIYRTETSS
     TVHNTHPRNG HCSSAPRVTN GSTYILVPLS HLAQN
 
 
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