ID   GLHA_HUMAN              Reviewed;         116 AA.
AC   P01215;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 223.
DE   RecName: Full=Glycoprotein hormones alpha chain;
DE   AltName: Full=Anterior pituitary glycoprotein hormones common subunit alpha;
DE   AltName: Full=Choriogonadotropin alpha chain;
DE   AltName: Full=Chorionic gonadotrophin subunit alpha;
DE            Short=CG-alpha;
DE   AltName: Full=Follicle-stimulating hormone alpha chain;
DE            Short=FSH-alpha;
DE   AltName: Full=Follitropin alpha chain;
DE   AltName: Full=Luteinizing hormone alpha chain;
DE            Short=LSH-alpha;
DE   AltName: Full=Lutropin alpha chain;
DE   AltName: Full=Thyroid-stimulating hormone alpha chain;
DE            Short=TSH-alpha;
DE   AltName: Full=Thyrotropin alpha chain;
DE   Flags: Precursor;
GN   Name=CGA;
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 [GENOMIC DNA].
RX   PubMed=481597; DOI=10.1038/281351a0;
RA   Fiddes J.C., Goodman H.M.;
RT   "Isolation, cloning and sequence analysis of the cDNA for the alpha-subunit
RT   of human chorionic gonadotropin.";
RL   Nature 281:351-356(1979).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8196184;
RA   Miyoshi I., Kasai N., Hayashizaki Y.;
RT   "Structure and regulation of human thyroid-stimulating hormone (TSH)
RT   gene.";
RL   Nippon Rinsho 52:940-947(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98.
RX   PubMed=6286817;
RA   Fiddes J.C., Goodman H.M.;
RT   "The gene encoding the common alpha subunit of the four human glycoprotein
RT   hormones.";
RL   J. Mol. Appl. Genet. 1:3-18(1981).
RN   [5]
RP   PROTEIN SEQUENCE OF 1-24 (PRECURSOR PROTEIN).
RX   PubMed=7462224; DOI=10.1016/s0021-9258(19)69881-9;
RA   Birken S., Fetherston J., Canfield R.E., Boime I.;
RT   "The amino acid sequences of the prepeptides contained in the alpha and
RT   beta subunits of human choriogonadotropin.";
RL   J. Biol. Chem. 256:1816-1823(1981).
RN   [6]
RP   PROTEIN SEQUENCE OF 28-116.
RX   PubMed=890569; DOI=10.1139/o77-108;
RA   Sairam M.R., Li C.H.;
RT   "Human pituitary thyrotropin. The primary structure of the alpha and beta
RT   subunits.";
RL   Can. J. Biochem. 55:755-760(1977).
RN   [7]
RP   PROTEIN SEQUENCE OF 28-116.
RX   PubMed=5065401; DOI=10.1016/0006-291x(72)90380-4;
RA   Sairam M.R., Papkoff H., Li C.H.;
RT   "Human pituitary interstitial cell stimulating hormone: primary structure
RT   of the alpha-subunit.";
RL   Biochem. Biophys. Res. Commun. 48:530-537(1972).
RN   [8]
RP   PROTEIN SEQUENCE, AND SEQUENCE REVISION.
RA   Keutmann H.T., Williams R.M., Bishop W.H., Ryan R.J.;
RT   "Structure of human luteninizing hormone.";
RL   Fed. Proc. 37:1828-1828(1978).
RN   [9]
RP   PROTEIN SEQUENCE OF 25-116.
RC   TISSUE=Pituitary;
RX   PubMed=1158880; DOI=10.1016/s0021-9258(19)40994-0;
RA   Rathnam P., Saxena B.B.;
RT   "Primary amino acid sequence of follicle-stimulating hormone from human
RT   pituitary glands. I. alpha subunit.";
RL   J. Biol. Chem. 250:6735-6746(1975).
RN   [10]
RP   PROTEIN SEQUENCE OF 28-116.
RX   PubMed=4835135; DOI=10.1210/jcem-39-1-199;
RA   Shome B., Parlow A.F.;
RT   "Human follicle stimulating hormone (hFSH): first proposal for the amino
RT   acid sequence of the alpha-subunit (hFSHa) and first demonstration of its
RT   identity with the alpha-subunit of human luteinizing hormone (hLHa).";
RL   J. Clin. Endocrinol. Metab. 39:199-202(1974).
RN   [11]
RP   PROTEIN SEQUENCE OF 25-116.
RX   PubMed=1150658; DOI=10.1016/s0021-9258(19)41303-3;
RA   Morgan F.J., Birken S., Canfield R.E.;
RT   "The amino acid sequence of human chorionic gonadotropin. The alpha subunit
RT   and beta subunit.";
RL   J. Biol. Chem. 250:5247-5258(1975).
RN   [12]
RP   PROTEIN SEQUENCE OF 25-116.
RX   PubMed=4745444; DOI=10.1016/s0021-9258(19)43424-8;
RA   Bellisario R., Carlsen R.B., Bahl O.P.;
RT   "Human chorionic gonadotropin. Linear amino acid sequence of the alpha
RT   subunit.";
RL   J. Biol. Chem. 248:6796-6809(1973).
RN   [13]
RP   PRELIMINARY ASSIGNMENT OF DISULFIDE BONDS.
RX   PubMed=6774759; DOI=10.1016/0005-2795(80)90084-7;
RA   Fujiki Y., Rathnam P., Saxena B.B.;
RT   "Studies on the disulfide bonds in human pituitary follicle-stimulating
RT   hormone.";
RL   Biochim. Biophys. Acta 624:428-435(1980).
RN   [14]
RP   PRELIMINARY ASSIGNMENT OF DISULFIDE BONDS.
RX   PubMed=7410374; DOI=10.1016/s0021-9258(18)43527-2;
RA   Mise T., Bahl O.P.;
RT   "Assignment of disulfide bonds in the alpha subunit of human chorionic
RT   gonadotropin.";
RL   J. Biol. Chem. 255:8516-8522(1980).
RN   [15]
RP   STRUCTURE OF CARBOHYDRATES.
RX   PubMed=1991473; DOI=10.1111/j.1432-1033.1991.tb15702.x;
RA   Weisshaar G., Hiyama J., Renwick A.G.C., Nimtz M.;
RT   "NMR investigations of the N-linked oligosaccharides at individual
RT   glycosylation sites of human lutropin.";
RL   Eur. J. Biochem. 195:257-268(1991).
RN   [16]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=2494176; DOI=10.1016/s0021-9258(18)83656-0;
RA   Keene J.L., Matzuk M.M., Otani T., Fauser B.C.J.M., Galway A.B.,
RA   Hsueh A.J.W., Boime I.;
RT   "Expression of biologically active human follitropin in Chinese hamster
RT   ovary cells.";
RL   J. Biol. Chem. 264:4769-4775(1989).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=8202136; DOI=10.1038/369455a0;
RA   Lapthorn A.J., Harris D.C., Littlejohn A., Lustbader J.W., Canfield R.E.,
RA   Machin K.J., Morgan F.J., Isaacs N.W.;
RT   "Crystal structure of human chorionic gonadotropin.";
RL   Nature 369:455-461(1994).
RN   [18]
RP   STRUCTURE BY NMR.
RX   PubMed=8898911; DOI=10.1111/j.1432-1033.1996.0229t.x;
RA   de Beer T., van Zuylen C.W.E.M., Leeflang B.R., Haard K., Boelens R.,
RA   Kaptein R., Kamerling J.P., Vliegenthart J.F.G.;
RT   "NMR studies of the free alpha subunit of human chorionic gonadotropin.
RT   Structural influences of N-glycosylation and the beta subunit on the
RT   conformation of the alpha subunit.";
RL   Eur. J. Biochem. 241:229-242(1996).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) OF 25-116 IN COMPLEX WITH FSHB AND
RP   FSHR, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-76 AND ASN-102.
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   [20] {ECO:0007744|PDB:4MQW}
RP   X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 25-116 IN COMPLEX WITH FSHB AND
RP   FSHR, FUNCTION, SUBCELLULAR LOCATION, DISULFIDE BONDS, GLYCOSYLATION AT
RP   ASN-76 AND ASN-102, AND MUTAGENESIS OF ASN-76.
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).
CC   -!- FUNCTION: Shared alpha chain of the active heterodimeric glycoprotein
CC       hormones thyrotropin/thyroid stimulating hormone/TSH,
CC       lutropin/luteinizing hormone/LH, follitropin/follicle stimulating
CC       hormone/FSH and choriogonadotropin/CG. These hormones bind specific
CC       receptors on target cells that in turn activate downstream signaling
CC       pathways. {ECO:0000269|PubMed:24692546, ECO:0000269|PubMed:2494176}.
CC   -!- SUBUNIT: Heterodimer. The active hormones thyrotropin, lutropin,
CC       follitropin and choriogonadotropin are heterodimers composed of CGA, a
CC       common alpha chain described here and a unique beta chain which confers
CC       their biological specificity to the hormones: TSHB for thyrotropin, LHB
CC       for lutropin, FSHB for follitropin and choriogonadotropin subunit
CC       beta/CGB for choriogonadotropin. {ECO:0000269|PubMed:15662415,
CC       ECO:0000269|PubMed:2494176}.
CC   -!- INTERACTION:
CC       P01215; P0DN86: CGB3; NbExp=2; IntAct=EBI-718913, EBI-8626304;
CC       P01215; P01225: FSHB; NbExp=4; IntAct=EBI-718913, EBI-1030645;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24692546,
CC       ECO:0000269|PubMed:2494176}.
CC   -!- SIMILARITY: Belongs to the glycoprotein hormones subunit alpha family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Proteic grace - Issue 77 of
CC       December 2006;
CC       URL="https://web.expasy.org/spotlight/back_issues/077";
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DR   EMBL; J00152; AAD13690.1; -; Genomic_DNA.
DR   EMBL; J00150; AAD13690.1; JOINED; Genomic_DNA.
DR   EMBL; J00151; AAD13690.1; JOINED; Genomic_DNA.
DR   EMBL; S70585; AAB30827.1; -; Genomic_DNA.
DR   EMBL; S70583; AAB30827.1; JOINED; Genomic_DNA.
DR   EMBL; S70584; AAB30827.1; JOINED; Genomic_DNA.
DR   EMBL; BC020782; AAH20782.1; -; mRNA.
DR   EMBL; BC055080; AAH55080.1; -; mRNA.
DR   EMBL; V00518; CAA23777.1; -; mRNA.
DR   CCDS; CCDS5007.1; -.
DR   PIR; A93213; TTHUAP.
DR   RefSeq; NP_000726.1; NM_000735.3.
DR   RefSeq; NP_001239312.1; NM_001252383.1.
DR   PDB; 1DZ7; NMR; -; A=25-116.
DR   PDB; 1E9J; NMR; -; A=25-116.
DR   PDB; 1FL7; X-ray; 3.00 A; A/C=25-116.
DR   PDB; 1HCN; X-ray; 2.60 A; A=25-116.
DR   PDB; 1HD4; NMR; -; A=25-116.
DR   PDB; 1HRP; X-ray; 3.00 A; A=25-116.
DR   PDB; 1QFW; X-ray; 3.50 A; A=25-116.
DR   PDB; 1XWD; X-ray; 2.92 A; A/D=25-116.
DR   PDB; 4AY9; X-ray; 2.50 A; A/D/G=25-116.
DR   PDB; 4MQW; X-ray; 2.90 A; A/D/G=25-116.
DR   PDB; 7FIG; EM; 3.90 A; X=1-116.
DR   PDB; 7FIH; EM; 3.20 A; X=2-116.
DR   PDB; 7FII; EM; 4.30 A; X=1-116.
DR   PDB; 7T9I; EM; 2.90 A; A=25-116.
DR   PDB; 7UTZ; EM; 2.40 A; A=25-116.
DR   PDB; 7XW5; EM; 2.96 A; X=25-116.
DR   PDB; 8I2G; EM; 2.80 A; X=25-116.
DR   PDBsum; 1DZ7; -.
DR   PDBsum; 1E9J; -.
DR   PDBsum; 1FL7; -.
DR   PDBsum; 1HCN; -.
DR   PDBsum; 1HD4; -.
DR   PDBsum; 1HRP; -.
DR   PDBsum; 1QFW; -.
DR   PDBsum; 1XWD; -.
DR   PDBsum; 4AY9; -.
DR   PDBsum; 4MQW; -.
DR   PDBsum; 7FIG; -.
DR   PDBsum; 7FIH; -.
DR   PDBsum; 7FII; -.
DR   PDBsum; 7T9I; -.
DR   PDBsum; 7UTZ; -.
DR   PDBsum; 7XW5; -.
DR   PDBsum; 8I2G; -.
DR   AlphaFoldDB; P01215; -.
DR   EMDB; EMD-25758; -.
DR   EMDB; EMD-26795; -.
DR   EMDB; EMD-31596; -.
DR   EMDB; EMD-31597; -.
DR   EMDB; EMD-31598; -.
DR   EMDB; EMD-33491; -.
DR   EMDB; EMD-35135; -.
DR   SMR; P01215; -.
DR   BioGRID; 107507; 28.
DR   ComplexPortal; CPX-6096; Thyroid-stimulating hormone complex.
DR   ComplexPortal; CPX-6097; Luteinizing hormone complex.
DR   ComplexPortal; CPX-665; Follicle-stimulating hormone complex.
DR   ComplexPortal; CPX-748; Chorionic gonadotropin hormone complex.
DR   DIP; DIP-6182N; -.
DR   IntAct; P01215; 4.
DR   MINT; P01215; -.
DR   STRING; 9606.ENSP00000482232; -.
DR   ChEMBL; CHEMBL2146305; -.
DR   GlyConnect; 165; 10 N-Linked glycans.
DR   GlyConnect; 194; 33 N-Linked glycans (2 sites).
DR   GlyConnect; 88; 12 N-Linked glycans, 9 O-Linked glycans.
DR   GlyCosmos; P01215; 2 sites, 110 glycans.
DR   GlyGen; P01215; 5 sites, 97 N-linked glycans (3 sites), 15 O-linked glycans (3 sites).
DR   iPTMnet; P01215; -.
DR   PhosphoSitePlus; P01215; -.
DR   BioMuta; CGA; -.
DR   DMDM; 121312; -.
DR   jPOST; P01215; -.
DR   MassIVE; P01215; -.
DR   PeptideAtlas; P01215; -.
DR   ProteomicsDB; 51346; -.
DR   ABCD; P01215; 4 sequenced antibodies.
DR   Antibodypedia; 18627; 1604 antibodies from 39 providers.
DR   DNASU; 1081; -.
DR   Ensembl; ENST00000627148.3; ENSP00000486024.1; ENSG00000135346.9.
DR   GeneID; 1081; -.
DR   KEGG; hsa:1081; -.
DR   MANE-Select; ENST00000627148.3; ENSP00000486024.1; NM_000735.4; NP_000726.1.
DR   UCSC; uc063pyi.1; human.
DR   AGR; HGNC:1885; -.
DR   CTD; 1081; -.
DR   DisGeNET; 1081; -.
DR   GeneCards; CGA; -.
DR   HGNC; HGNC:1885; CGA.
DR   HPA; ENSG00000135346; Tissue enriched (pituitary).
DR   MIM; 118850; gene.
DR   neXtProt; NX_P01215; -.
DR   OpenTargets; ENSG00000135346; -.
DR   PharmGKB; PA26433; -.
DR   VEuPathDB; HostDB:ENSG00000135346; -.
DR   GeneTree; ENSGT00390000012242; -.
DR   InParanoid; P01215; -.
DR   OMA; MMQGCPE; -.
DR   OrthoDB; 4182331at2759; -.
DR   PhylomeDB; P01215; -.
DR   TreeFam; TF332733; -.
DR   PathwayCommons; P01215; -.
DR   Reactome; R-HSA-193048; Androgen biosynthesis.
DR   Reactome; R-HSA-193993; Mineralocorticoid biosynthesis.
DR   Reactome; R-HSA-209822; Glycoprotein hormones.
DR   Reactome; R-HSA-209968; Thyroxine biosynthesis.
DR   Reactome; R-HSA-375281; Hormone ligand-binding receptors.
DR   Reactome; R-HSA-418555; G alpha (s) signalling events.
DR   Reactome; R-HSA-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
DR   Reactome; R-HSA-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR   SABIO-RK; P01215; -.
DR   SignaLink; P01215; -.
DR   SIGNOR; P01215; -.
DR   BioGRID-ORCS; 1081; 13 hits in 1147 CRISPR screens.
DR   ChiTaRS; CGA; human.
DR   EvolutionaryTrace; P01215; -.
DR   GeneWiki; Chorionic_gonadotropin_alpha; -.
DR   GenomeRNAi; 1081; -.
DR   Pharos; P01215; Tbio.
DR   PRO; PR:P01215; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; P01215; Protein.
DR   Bgee; ENSG00000135346; Expressed in adenohypophysis and 96 other cell types or tissues.
DR   ExpressionAtlas; P01215; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0016914; C:follicle-stimulating hormone complex; IDA:UniProtKB.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0061696; C:pituitary gonadotropin complex; IPI:ComplexPortal.
DR   GO; GO:0016913; F:follicle-stimulating hormone activity; IDA:UniProtKB.
DR   GO; GO:0005179; F:hormone activity; IMP:AgBase.
DR   GO; GO:0046884; P:follicle-stimulating hormone secretion; IEA:Ensembl.
DR   GO; GO:0042699; P:follicle-stimulating hormone signaling pathway; NAS:ComplexPortal.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; NAS:ComplexPortal.
DR   GO; GO:0032275; P:luteinizing hormone secretion; IEA:Ensembl.
DR   GO; GO:0046621; P:negative regulation of organ growth; IEA:Ensembl.
DR   GO; GO:0035265; P:organ growth; IEA:Ensembl.
DR   GO; GO:0030335; P:positive regulation of cell migration; NAS:BHF-UCL.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; NAS:BHF-UCL.
DR   GO; GO:0010893; P:positive regulation of steroid biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; NAS:BHF-UCL.
DR   GO; GO:0010469; P:regulation of signaling receptor activity; IDA:UniProtKB.
DR   GO; GO:0030878; P:thyroid gland development; IEA:Ensembl.
DR   GO; GO:0006590; P:thyroid hormone generation; IBA:GO_Central.
DR   DisProt; DP02922; -.
DR   Gene3D; 2.10.90.10; Cystine-knot cytokines; 1.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR000476; Glyco_hormone.
DR   PANTHER; PTHR11509; GLYCOPROTEIN HORMONE ALPHA CHAIN; 1.
DR   PANTHER; PTHR11509:SF0; GLYCOPROTEIN HORMONES ALPHA CHAIN; 1.
DR   Pfam; PF00236; Hormone_6; 1.
DR   PRINTS; PR00274; GLYCOHORMONE.
DR   SMART; SM00067; GHA; 1.
DR   SUPFAM; SSF57501; Cystine-knot cytokines; 1.
DR   PROSITE; PS00779; GLYCO_HORMONE_ALPHA_1; 1.
DR   PROSITE; PS00780; GLYCO_HORMONE_ALPHA_2; 1.
DR   PROSITE; PS50277; GLYCO_HORMONE_ALPHA_3; 1.
DR   Genevisible; P01215; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Hormone; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:1150658,
FT                   ECO:0000269|PubMed:1158880, ECO:0000269|PubMed:4745444,
FT                   ECO:0000269|PubMed:481597"
FT   CHAIN           25..116
FT                   /note="Glycoprotein hormones alpha chain"
FT                   /id="PRO_0000011640"
FT   CARBOHYD        76
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15662415,
FT                   ECO:0000269|PubMed:24692546, ECO:0007744|PDB:4MQW"
FT                   /id="CAR_000036"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15662415,
FT                   ECO:0000269|PubMed:24692546, ECO:0007744|PDB:4MQW"
FT                   /id="CAR_000037"
FT   DISULFID        31..55
FT                   /evidence="ECO:0000269|PubMed:15662415,
FT                   ECO:0000269|PubMed:24692546, ECO:0000269|PubMed:8202136,
FT                   ECO:0007744|PDB:4MQW"
FT   DISULFID        34..84
FT                   /evidence="ECO:0000269|PubMed:15662415,
FT                   ECO:0000269|PubMed:24692546, ECO:0000269|PubMed:8202136,
FT                   ECO:0007744|PDB:4MQW"
FT   DISULFID        52..106
FT                   /evidence="ECO:0000269|PubMed:15662415,
FT                   ECO:0000269|PubMed:24692546, ECO:0000269|PubMed:8202136,
FT                   ECO:0007744|PDB:4MQW"
FT   DISULFID        56..108
FT                   /evidence="ECO:0000269|PubMed:15662415,
FT                   ECO:0000269|PubMed:24692546, ECO:0000269|PubMed:8202136,
FT                   ECO:0007744|PDB:4MQW"
FT   DISULFID        83..111
FT                   /evidence="ECO:0000269|PubMed:15662415,
FT                   ECO:0000269|PubMed:24692546, ECO:0000269|PubMed:8202136,
FT                   ECO:0007744|PDB:4MQW"
FT   MUTAGEN         76
FT                   /note="N->D: Increases from 1 to 3 the number of FSH
FT                   binding a single FSHR receptor."
FT                   /evidence="ECO:0000269|PubMed:24692546"
FT   CONFLICT        29
FT                   /note="Q -> E (in Ref. 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        108..109
FT                   /note="CS -> SC (in Ref. 6; AA sequence and 7; AA
FT                   sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          33..38
FT                   /evidence="ECO:0007829|PDB:7UTZ"
FT   STRAND          40..42
FT                   /evidence="ECO:0007829|PDB:7UTZ"
FT   STRAND          50..62
FT                   /evidence="ECO:0007829|PDB:7UTZ"
FT   HELIX           65..68
FT                   /evidence="ECO:0007829|PDB:7UTZ"
FT   STRAND          76..81
FT                   /evidence="ECO:0007829|PDB:7UTZ"
FT   STRAND          83..93
FT                   /evidence="ECO:0007829|PDB:7UTZ"
FT   HELIX           95..97
FT                   /evidence="ECO:0007829|PDB:7UTZ"
FT   STRAND          99..109
FT                   /evidence="ECO:0007829|PDB:7UTZ"
FT   STRAND          112..115
FT                   /evidence="ECO:0007829|PDB:7T9I"
SQ   SEQUENCE   116 AA;  13075 MW;  F0623CD8CC90CFCD CRC64;
     MDYYRKYAAI FLVTLSVFLH VLHSAPDVQD CPECTLQENP FFSQPGAPIL QCMGCCFSRA
     YPTPLRSKKT MLVQKNVTSE STCCVAKSYN RVTVMGGFKV ENHTACHCST CYYHKS
//