SIA4B_HUMAN
ID SIA4B_HUMAN Reviewed; 350 AA.
AC Q16842; O00654;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2;
DE Short=Alpha 2,3-ST 2;
DE Short=Beta-galactoside alpha-2,3-sialyltransferase 2;
DE EC=2.4.99.4 {ECO:0000269|PubMed:25916169, ECO:0000269|PubMed:9266697};
DE AltName: Full=Gal-NAc6S;
DE AltName: Full=Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase {ECO:0000303|PubMed:9266697};
DE AltName: Full=Monosialoganglioside sialyltransferase;
DE EC=2.4.99.2 {ECO:0000305|PubMed:8920913, ECO:0000305|PubMed:9266697};
DE AltName: Full=ST3Gal II {ECO:0000303|PubMed:8920913};
DE Short=ST3GalII;
DE AltName: Full=ST3GalA.2;
DE AltName: Full=Sialyltransferase 4B;
DE Short=SIAT4-B;
GN Name=ST3GAL2 {ECO:0000312|HGNC:HGNC:10863}; Synonyms=SIAT4B;
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], TISSUE SPECIFICITY, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RC TISSUE=Liver;
RX PubMed=8920913; DOI=10.1006/bbrc.1996.1660;
RA Kim Y.-J., Kim K.-S., Kim S.-H., Kim C.-H., Ko J.H., Choe I.-S., Tsuji S.,
RA Lee Y.-C.;
RT "Molecular cloning and expression of human Gal beta 1,3GalNAc alpha 2,3-
RT sialyltransferase (hST3Gal II).";
RL Biochem. Biophys. Res. Commun. 228:324-327(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND TISSUE SPECIFICITY.
RX PubMed=9266697; DOI=10.1111/j.1432-1033.1997.00558.x;
RA Giordanengo V., Lefebvre J.-C.;
RT "Cloning and expression of cDNA for a human Gal(beta1-3)GalNAc alpha2,3-
RT sialyltransferase from the CEM T-cell line.";
RL Eur. J. Biochem. 247:558-566(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12716912; DOI=10.1074/jbc.m213223200;
RA Saito S., Aoki H., Ito A., Ueno S., Wada T., Mitsuzuka K., Satoh M.,
RA Arai Y., Miyagi T.;
RT "Human alpha2,3-sialyltransferase (ST3Gal II) is a stage-specific embryonic
RT antigen-4 synthase.";
RL J. Biol. Chem. 278:26474-26479(2003).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, GLYCOSYLATION AT ASN-211, AND
RP MUTAGENESIS OF ASN-92 AND ASN-211.
RX PubMed=25916169; DOI=10.1042/bj20150072;
RA Ruggiero F.M., Vilcaes A.A., Iglesias-Bartolome R., Daniotti J.L.;
RT "Critical role of evolutionarily conserved glycosylation at Asn211 in the
RT intracellular trafficking and activity of sialyltransferase ST3Gal-II.";
RL Biochem. J. 469:83-95(2015).
CC -!- FUNCTION: A beta-galactoside alpha2-3 sialyltransferase primarily
CC involved in terminal sialylation of ganglio and globo series
CC glycolipids (PubMed:8920913, PubMed:9266697). Catalyzes the transfer of
CC sialic acid (N-acetyl-neuraminic acid; Neu5Ac) from the nucleotide
CC sugar donor CMP-Neu5Ac onto acceptor Galbeta-(1->3)-GalNAc-terminated
CC glycoconjugates through an alpha2-3 linkage (PubMed:8920913,
CC PubMed:9266697, PubMed:25916169). Sialylates GM1/GM1a, GA1/asialo-GM1
CC and GD1b gangliosides to form GD1a, GM1b and GT1b, respectively
CC (PubMed:8920913, PubMed:9266697). Together with ST3GAL3, primarily
CC responsible for biosynthesis of brain GD1a and GT1b that function as
CC ligands for myelin-associated glycoprotein MAG on axons, regulating MAG
CC expression and axonal myelin stability and regeneration (By
CC similarity). Via GT1b regulates TLR2 signaling in spinal cord microglia
CC in response to nerve injury (By similarity). Responsible for the
CC sialylation of the pluripotent stem cell- and cancer stem cell-
CC associated antigen SSEA3, forming SSEA4 (PubMed:12716912). Sialylates
CC with low efficiency asialofetuin, presumably onto O-glycosidically
CC linked Galbeta-(1->3)-GalNAc-O-Ser (PubMed:9266697, PubMed:25916169).
CC {ECO:0000250|UniProtKB:Q11204, ECO:0000269|PubMed:12716912,
CC ECO:0000269|PubMed:25916169, ECO:0000269|PubMed:8920913,
CC ECO:0000269|PubMed:9266697}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl
CC derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-
CC neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl derivative + CMP + H(+); Xref=Rhea:RHEA:21616,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:133470, ChEBI:CHEBI:139596; EC=2.4.99.4;
CC Evidence={ECO:0000269|PubMed:25916169, ECO:0000269|PubMed:9266697};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21617;
CC Evidence={ECO:0000305|PubMed:25916169, ECO:0000305|PubMed:9266697};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1 = CMP +
CC ganglioside GD1a + H(+); Xref=Rhea:RHEA:48260, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:82637,
CC ChEBI:CHEBI:82639; Evidence={ECO:0000269|PubMed:9266697};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48261;
CC Evidence={ECO:0000305|PubMed:9266697};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1 (d18:1(4E)) =
CC CMP + ganglioside GD1a (d18:1(4E)) + H(+); Xref=Rhea:RHEA:18021,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:77709, ChEBI:CHEBI:78445; EC=2.4.99.2;
CC Evidence={ECO:0000305|PubMed:8920913, ECO:0000305|PubMed:9266697};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18022;
CC Evidence={ECO:0000305|PubMed:8920913, ECO:0000305|PubMed:9266697};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1
CC (d18:1(4E)/18:0) = CMP + ganglioside GD1a (18:1(4E)/18:0) + H(+);
CC Xref=Rhea:RHEA:48248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:73110, ChEBI:CHEBI:90153;
CC Evidence={ECO:0000269|PubMed:8920913};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48249;
CC Evidence={ECO:0000305|PubMed:8920913};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GA1 = CMP +
CC ganglioside GM1b + H(+); Xref=Rhea:RHEA:48244, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:88069,
CC ChEBI:CHEBI:90151; Evidence={ECO:0000269|PubMed:8920913,
CC ECO:0000269|PubMed:9266697};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48245;
CC Evidence={ECO:0000305|PubMed:8920913, ECO:0000305|PubMed:9266697};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GA1 (d18:1(4E)) =
CC CMP + ganglioside GM1b (d18:1(4E)) + H(+); Xref=Rhea:RHEA:47560,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27938, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:78568;
CC Evidence={ECO:0000305|PubMed:8920913, ECO:0000305|PubMed:9266697};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47561;
CC Evidence={ECO:0000305|PubMed:8920913, ECO:0000305|PubMed:9266697};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GD1b = CMP +
CC ganglioside GT1b + H(+); Xref=Rhea:RHEA:48240, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:82939,
CC ChEBI:CHEBI:82940; Evidence={ECO:0000269|PubMed:9266697};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48241;
CC Evidence={ECO:0000305|PubMed:9266697};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GD1b (d18:1(4E)) =
CC CMP + ganglioside GT1b (d18:1(4E)) + H(+); Xref=Rhea:RHEA:47572,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:78452, ChEBI:CHEBI:87785;
CC Evidence={ECO:0000305|PubMed:9266697};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47573;
CC Evidence={ECO:0000305|PubMed:9266697};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + globoside GalGb4Cer = CMP +
CC globoside MSGG + H(+); Xref=Rhea:RHEA:65372, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:140623,
CC ChEBI:CHEBI:140691; Evidence={ECO:0000269|PubMed:12716912};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65373;
CC Evidence={ECO:0000305|PubMed:12716912};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.46 mM for ganglioside GA1 {ECO:0000269|PubMed:9266697};
CC KM=0.87 mM for ganglioside GM1 {ECO:0000269|PubMed:9266697};
CC KM=0.049 mM for asialofetuin {ECO:0000269|PubMed:9266697};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:9266697}.
CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000305|PubMed:9266697}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Homodimer formation occurs in the
CC endoplasmic reticulum. {ECO:0000269|PubMed:25916169}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:25916169}; Single-pass type II membrane protein
CC {ECO:0000255}. Secreted {ECO:0000250}. Note=Membrane-bound form
CC distributed along the Golgi cisternae, mainly in proximal compartments
CC (PubMed:25916169). Secreted into the body fluid. {ECO:0000250,
CC ECO:0000269|PubMed:25916169}.
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle and heart and
CC to a much lesser extent in brain, placenta, liver and pancreas.
CC Scarcely detectable in lung and kidney. {ECO:0000269|PubMed:8920913,
CC ECO:0000269|PubMed:9266697}.
CC -!- PTM: The soluble form derives from the membrane form by proteolytic
CC processing. {ECO:0000250}.
CC -!- PTM: N-glycosylated; necessary for proper exit from endoplasmic
CC reticulum and trafficking to the Golgi apparatus.
CC {ECO:0000269|PubMed:25916169}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST3Gal
CC II;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_623";
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DR EMBL; U63090; AAB40389.1; -; mRNA.
DR EMBL; X96667; CAA65447.1; -; mRNA.
DR EMBL; BC036777; AAH36777.1; -; mRNA.
DR CCDS; CCDS10890.1; -.
DR PIR; JC5251; JC5251.
DR RefSeq; NP_008858.1; NM_006927.3.
DR AlphaFoldDB; Q16842; -.
DR SMR; Q16842; -.
DR BioGRID; 112376; 28.
DR IntAct; Q16842; 9.
DR STRING; 9606.ENSP00000377257; -.
DR SwissLipids; SLP:000001388; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyConnect; 1119; 2 N-Linked glycans (1 site).
DR GlyGen; Q16842; 2 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q16842; -.
DR PhosphoSitePlus; Q16842; -.
DR SwissPalm; Q16842; -.
DR BioMuta; ST3GAL2; -.
DR DMDM; 21759433; -.
DR EPD; Q16842; -.
DR jPOST; Q16842; -.
DR MassIVE; Q16842; -.
DR MaxQB; Q16842; -.
DR PaxDb; Q16842; -.
DR PeptideAtlas; Q16842; -.
DR PRIDE; Q16842; -.
DR ProteomicsDB; 61098; -.
DR Antibodypedia; 2529; 144 antibodies from 25 providers.
DR DNASU; 6483; -.
DR Ensembl; ENST00000342907.3; ENSP00000345477.2; ENSG00000157350.13.
DR Ensembl; ENST00000393640.8; ENSP00000377257.4; ENSG00000157350.13.
DR GeneID; 6483; -.
DR KEGG; hsa:6483; -.
DR MANE-Select; ENST00000342907.3; ENSP00000345477.2; NM_006927.4; NP_008858.1.
DR UCSC; uc002eyw.3; human.
DR CTD; 6483; -.
DR DisGeNET; 6483; -.
DR GeneCards; ST3GAL2; -.
DR HGNC; HGNC:10863; ST3GAL2.
DR HPA; ENSG00000157350; Low tissue specificity.
DR MIM; 607188; gene.
DR neXtProt; NX_Q16842; -.
DR OpenTargets; ENSG00000157350; -.
DR PharmGKB; PA35765; -.
DR VEuPathDB; HostDB:ENSG00000157350; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT00940000156356; -.
DR HOGENOM; CLU_032020_2_0_1; -.
DR InParanoid; Q16842; -.
DR OMA; ISPVWTK; -.
DR OrthoDB; 891104at2759; -.
DR PhylomeDB; Q16842; -.
DR TreeFam; TF354325; -.
DR BioCyc; MetaCyc:HS08206-MON; -.
DR BRENDA; 2.4.99.2; 2681.
DR PathwayCommons; Q16842; -.
DR Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-HSA-4085001; Sialic acid metabolism.
DR Reactome; R-HSA-9683673; Maturation of protein 3a.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR Reactome; R-HSA-9694719; Maturation of protein 3a.
DR Reactome; R-HSA-977068; Termination of O-glycan biosynthesis.
DR SignaLink; Q16842; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 6483; 17 hits in 1076 CRISPR screens.
DR ChiTaRS; ST3GAL2; human.
DR GenomeRNAi; 6483; -.
DR Pharos; Q16842; Tbio.
DR PRO; PR:Q16842; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q16842; protein.
DR Bgee; ENSG00000157350; Expressed in blood and 180 other tissues.
DR ExpressionAtlas; Q16842; baseline and differential.
DR Genevisible; Q16842; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0003836; F:beta-galactoside (CMP) alpha-2,3-sialyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047288; F:monosialoganglioside sialyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0008373; F:sialyltransferase activity; TAS:Reactome.
DR GO; GO:0010706; P:ganglioside biosynthetic process via lactosylceramide; IDA:UniProtKB.
DR GO; GO:0010707; P:globoside biosynthetic process via lactosylceramide; IDA:UniProtKB.
DR GO; GO:0009247; P:glycolipid biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0009101; P:glycoprotein biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0018146; P:keratan sulfate biosynthetic process; TAS:Reactome.
DR GO; GO:0030259; P:lipid glycosylation; IDA:BHF-UCL.
DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0006486; P:protein glycosylation; IDA:BHF-UCL.
DR GO; GO:1990743; P:protein sialylation; IDA:BHF-UCL.
DR GO; GO:0097503; P:sialylation; IDA:BHF-UCL.
DR GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR Gene3D; 3.90.1480.20; -; 1.
DR InterPro; IPR001675; Glyco_trans_29.
DR InterPro; IPR038578; GT29-like_sf.
DR InterPro; IPR012163; Sialyl_trans.
DR Pfam; PF00777; Glyco_transf_29; 1.
DR PIRSF; PIRSF005557; Sialyl_trans; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Lipid metabolism; Membrane; Reference proteome; Secreted; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..350
FT /note="CMP-N-acetylneuraminate-beta-galactosamide-alpha-
FT 2,3-sialyltransferase 2"
FT /id="PRO_0000149258"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..350
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:25916169"
FT DISULFID 70..75
FT /evidence="ECO:0000250"
FT DISULFID 72..149
FT /evidence="ECO:0000250"
FT DISULFID 152..291
FT /evidence="ECO:0000250"
FT MUTAGEN 92
FT /note="N->Q: Has a moderate effect on N-glycosylation and
FT sialyltransferase activity; when associated with Q-211."
FT /evidence="ECO:0000269|PubMed:25916169"
FT MUTAGEN 211
FT /note="N->Q: Impairs N-glycosylation. Impairs exit from the
FT endoplasmic reticulum. Decreases sialyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:25916169"
SQ SEQUENCE 350 AA; 40173 MW; E7E40CF26D9CB725 CRC64;
MKCSLRVWFL SVAFLLVFIM SLLFTYSHHS MATLPYLDSG ALDGTHRVKL VPGYAGLQRL
SKERLSGKSC ACRRCMGDAG ASDWFDSHFD GNISPVWTRE NMDLPPDVQR WWMMLQPQFK
SHNTNEVLEK LFQIVPGENP YRFRDPHQCR RCAVVGNSGN LRGSGYGQDV DGHNFIMRMN
QAPTVGFEQD VGSRTTHHFM YPESAKNLPA NVSFVLVPFK VLDLLWIASA LSTGQIRFTY
APVKSFLRVD KEKVQIYNPA FFKYIHDRWT EHHGRYPSTG MLVLFFALHV CDEVNVYGFG
ADSRGNWHHY WENNRYAGEF RKTGVHDADF EAHIIDMLAK ASKIEVYRGN
