GLHA_HUMAN
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 03-AUG-2022, entry version 214.
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 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 AlphaFoldDB; P01215; -.
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 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 GlyGen; P01215; 3 sites, 97 N-linked glycans (3 sites), 13 O-linked glycans (1 site).
DR iPTMnet; P01215; -.
DR PhosphoSitePlus; P01215; -.
DR BioMuta; CGA; -.
DR DMDM; 121312; -.
DR jPOST; P01215; -.
DR MassIVE; P01215; -.
DR PaxDb; P01215; -.
DR PeptideAtlas; P01215; -.
DR PRIDE; P01215; -.
DR ProteomicsDB; 51346; -.
DR ABCD; P01215; 4 sequenced antibodies.
DR Antibodypedia; 18627; 1524 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 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; ATVMGNT; -.
DR OrthoDB; 913381at2759; -.
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-9660821; ADORA2B mediated anti-inflammatory cytokines production.
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; 12 hits in 1071 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 94 other tissues.
DR ExpressionAtlas; P01215; baseline and differential.
DR Genevisible; P01215; HS.
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; IC:ComplexPortal.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IC: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; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR000476; Glyco_hormone.
DR PANTHER; PTHR11509; PTHR11509; 1.
DR Pfam; PF00236; Hormone_6; 1.
DR PRINTS; PR00274; GLYCOHORMONE.
DR SMART; SM00067; GHA; 1.
DR SUPFAM; SSF57501; SSF57501; 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.
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:4AY9"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:4AY9"
FT STRAND 50..62
FT /evidence="ECO:0007829|PDB:4AY9"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:4AY9"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:4AY9"
FT STRAND 83..94
FT /evidence="ECO:0007829|PDB:4AY9"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:4AY9"
FT STRAND 98..109
FT /evidence="ECO:0007829|PDB:4AY9"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1DZ7"
SQ SEQUENCE 116 AA; 13075 MW; F0623CD8CC90CFCD CRC64;
MDYYRKYAAI FLVTLSVFLH VLHSAPDVQD CPECTLQENP FFSQPGAPIL QCMGCCFSRA
YPTPLRSKKT MLVQKNVTSE STCCVAKSYN RVTVMGGFKV ENHTACHCST CYYHKS
