B3GA1_HUMAN
ID B3GA1_HUMAN Reviewed; 334 AA.
AC Q9P2W7; B7Z5Z8; Q96FS7;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1 {ECO:0000305};
DE EC=2.4.1.135 {ECO:0000250|UniProtKB:O35789};
DE AltName: Full=Beta-1,3-glucuronyltransferase 1;
DE AltName: Full=Glucuronosyltransferase P;
DE Short=GlcAT-P {ECO:0000250|UniProtKB:O35789};
DE AltName: Full=UDP-GlcUA:glycoprotein beta-1,3-glucuronyltransferase;
DE Short=GlcUAT-P;
GN Name=B3GAT1 {ECO:0000312|HGNC:HGNC:921}; Synonyms=GLCATP;
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 1).
RC TISSUE=Brain;
RX PubMed=10783264; DOI=10.1006/geno.2000.6152;
RA Mitsumoto Y., Oka S., Sakuma H., Inazawa J., Kawasaki T.;
RT "Cloning and chromosomal mapping of human glucuronyltransferase involved in
RT biosynthesis of the HNK-1 carbohydrate epitope.";
RL Genomics 65:166-173(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [6]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 83-334 IN COMPLEX WITH
RP UDP-GLUCURONIC ACID AND GALACTOSE MOIETY OF SUBSTRATE GLYCOPROTEIN.
RX PubMed=14993226; DOI=10.1074/jbc.m400622200;
RA Kakuda S., Shiba T., Ishiguro M., Tagawa H., Oka S., Kajihara Y.,
RA Kawasaki T., Wakatsuki S., Kato R.;
RT "Structural basis for acceptor substrate recognition of a human
RT glucuronyltransferase, GlcAT-P, an enzyme critical in the biosynthesis of
RT the carbohydrate epitope HNK-1.";
RL J. Biol. Chem. 279:22693-22703(2004).
CC -!- FUNCTION: Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope
CC on glycoproteins. Can also play a role in glycosaminoglycan
CC biosynthesis. Substrates include asialo-orosomucoid (ASOR), asialo-
CC fetuin, and asialo-neural cell adhesion molecule. Requires
CC sphingomyelin for activity: stearoyl-sphingomyelin was the most
CC effective, followed by palmitoyl-sphingomyelin and lignoceroyl-
CC sphingomyelin. Activity was demonstrated only for sphingomyelin with a
CC saturated fatty acid and not for that with an unsaturated fatty acid,
CC regardless of the length of the acyl group.
CC {ECO:0000250|UniProtKB:O35789}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-
CC xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-
CC GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-
CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:24168, Rhea:RHEA-COMP:12571,
CC Rhea:RHEA-COMP:12573, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:132090, ChEBI:CHEBI:132093;
CC EC=2.4.1.135; Evidence={ECO:0000250|UniProtKB:O35789};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Homodimer. Interacts with SAR1A.
CC {ECO:0000250|UniProtKB:O35789}.
CC -!- INTERACTION:
CC Q9P2W7; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-3918235, EBI-2807956;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O35789}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:O35789}. Secreted
CC {ECO:0000250|UniProtKB:O35789}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O35789}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:O35789}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O35789}. Secreted
CC {ECO:0000250|UniProtKB:O35789}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=sGlcAT-P {ECO:0000250|UniProtKB:O35789};
CC IsoId=Q9P2W7-1; Sequence=Displayed;
CC Name=2; Synonyms=lGlcAT-P {ECO:0000250|UniProtKB:O35789};
CC IsoId=Q9P2W7-2; Sequence=VSP_058538;
CC -!- TISSUE SPECIFICITY: Mainly expressed in the brain.
CC -!- PTM: The soluble form derives from the membrane form by proteolytic
CC processing. {ECO:0000250|UniProtKB:O35789}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 43 family.
CC {ECO:0000305}.
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DR EMBL; AB029396; BAA96077.1; -; mRNA.
DR EMBL; AK299637; BAH13084.1; -; mRNA.
DR EMBL; CR457098; CAG33379.1; -; mRNA.
DR EMBL; BC010466; AAH10466.1; -; mRNA.
DR CCDS; CCDS8500.1; -. [Q9P2W7-1]
DR RefSeq; NP_061114.2; NM_018644.3. [Q9P2W7-1]
DR RefSeq; NP_473366.1; NM_054025.2. [Q9P2W7-1]
DR RefSeq; XP_005271563.1; XM_005271506.3.
DR RefSeq; XP_011541053.1; XM_011542751.2. [Q9P2W7-2]
DR RefSeq; XP_011541055.1; XM_011542753.2. [Q9P2W7-2]
DR RefSeq; XP_016873039.1; XM_017017550.1. [Q9P2W7-1]
DR RefSeq; XP_016873040.1; XM_017017551.1. [Q9P2W7-2]
DR PDB; 1V82; X-ray; 1.85 A; A/B=83-334.
DR PDB; 1V83; X-ray; 1.90 A; A/B=83-334.
DR PDB; 1V84; X-ray; 1.82 A; A/B=83-334.
DR PDBsum; 1V82; -.
DR PDBsum; 1V83; -.
DR PDBsum; 1V84; -.
DR AlphaFoldDB; Q9P2W7; -.
DR SMR; Q9P2W7; -.
DR BioGRID; 117990; 391.
DR IntAct; Q9P2W7; 3.
DR STRING; 9606.ENSP00000433847; -.
DR DrugBank; DB01694; D-tartaric acid.
DR DrugBank; DB03435; Uridine-5'-Diphosphate.
DR CAZy; GT43; Glycosyltransferase Family 43.
DR GlyConnect; 1254; 1 N-Linked glycan (1 site).
DR GlyGen; Q9P2W7; 3 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9P2W7; -.
DR PhosphoSitePlus; Q9P2W7; -.
DR BioMuta; B3GAT1; -.
DR DMDM; 205830910; -.
DR jPOST; Q9P2W7; -.
DR MassIVE; Q9P2W7; -.
DR PaxDb; Q9P2W7; -.
DR PeptideAtlas; Q9P2W7; -.
DR PRIDE; Q9P2W7; -.
DR ProteomicsDB; 83905; -.
DR Antibodypedia; 3739; 1556 antibodies from 46 providers.
DR DNASU; 27087; -.
DR Ensembl; ENST00000312527.9; ENSP00000307875.4; ENSG00000109956.13. [Q9P2W7-1]
DR Ensembl; ENST00000392580.5; ENSP00000376359.1; ENSG00000109956.13. [Q9P2W7-1]
DR Ensembl; ENST00000524765.1; ENSP00000433847.1; ENSG00000109956.13. [Q9P2W7-1]
DR GeneID; 27087; -.
DR KEGG; hsa:27087; -.
DR MANE-Select; ENST00000312527.9; ENSP00000307875.4; NM_054025.3; NP_473366.1.
DR UCSC; uc001qhq.4; human. [Q9P2W7-1]
DR CTD; 27087; -.
DR DisGeNET; 27087; -.
DR GeneCards; B3GAT1; -.
DR HGNC; HGNC:921; B3GAT1.
DR HPA; ENSG00000109956; Tissue enriched (brain).
DR MIM; 151290; gene.
DR neXtProt; NX_Q9P2W7; -.
DR OpenTargets; ENSG00000109956; -.
DR PharmGKB; PA25215; -.
DR VEuPathDB; HostDB:ENSG00000109956; -.
DR eggNOG; KOG1476; Eukaryota.
DR GeneTree; ENSGT00940000157165; -.
DR HOGENOM; CLU_045177_1_0_1; -.
DR InParanoid; Q9P2W7; -.
DR OMA; DSREYCM; -.
DR OrthoDB; 901158at2759; -.
DR PhylomeDB; Q9P2W7; -.
DR TreeFam; TF313522; -.
DR BioCyc; MetaCyc:HS03272-MON; -.
DR BRENDA; 2.4.1.135; 2681.
DR PathwayCommons; Q9P2W7; -.
DR Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR SignaLink; Q9P2W7; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 27087; 9 hits in 1068 CRISPR screens.
DR ChiTaRS; B3GAT1; human.
DR EvolutionaryTrace; Q9P2W7; -.
DR GeneWiki; B3GAT1; -.
DR GenomeRNAi; 27087; -.
DR Pharos; Q9P2W7; Tbio.
DR PRO; PR:Q9P2W7; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9P2W7; protein.
DR Bgee; ENSG00000109956; Expressed in cortical plate and 133 other tissues.
DR Genevisible; Q9P2W7; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0015018; F:galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; IEA:Ensembl.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0050650; P:chondroitin sulfate proteoglycan biosynthetic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR CDD; cd00218; GlcAT-I; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005027; Glyco_trans_43.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR10896; PTHR10896; 1.
DR Pfam; PF03360; Glyco_transf_43; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Golgi apparatus; Manganese; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Secreted; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..334
FT /note="Galactosylgalactosylxylosylprotein 3-beta-
FT glucuronosyltransferase 1"
FT /id="PRO_0000195167"
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..334
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 3..5
FT /note="Essential for transport from endoplasmic reticulum
FT to Golgi apparatus and interaction with SAR1A"
FT /evidence="ECO:0000250|UniProtKB:O35789"
FT REGION 37..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..254
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT ACT_SITE 284
FT /note="Proton donor/acceptor"
FT BINDING 91..93
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT BINDING 122
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT BINDING 165
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT BINDING 170
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 195..197
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT BINDING 197
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 311..313
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT SITE 228
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT SITE 321
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT /evidence="ECO:0000250"
FT MOD_RES 103
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O35789"
FT MOD_RES 108
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O35789"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1
FT /note="M -> MGNEEPWVQPALEM (in isoform 2)"
FT /id="VSP_058538"
FT VARIANT 131
FT /note="A -> T (in dbSNP:rs35434644)"
FT /id="VAR_044538"
FT CONFLICT 240
FT /note="G -> R (in Ref. 1; BAA96077)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="Q -> K (in Ref. 2; BAH13084)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="K -> R (in Ref. 2; BAH13084)"
FT /evidence="ECO:0000305"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:1V84"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:1V84"
FT STRAND 112..125
FT /evidence="ECO:0007829|PDB:1V84"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:1V84"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:1V84"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:1V84"
FT HELIX 167..180
FT /evidence="ECO:0007829|PDB:1V84"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:1V84"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:1V84"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:1V84"
FT HELIX 202..209
FT /evidence="ECO:0007829|PDB:1V84"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:1V84"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:1V84"
FT STRAND 225..232
FT /evidence="ECO:0007829|PDB:1V84"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:1V84"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:1V83"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:1V84"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:1V84"
FT HELIX 262..267
FT /evidence="ECO:0007829|PDB:1V84"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:1V84"
FT HELIX 283..291
FT /evidence="ECO:0007829|PDB:1V84"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:1V84"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:1V84"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:1V84"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:1V84"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:1V84"
SQ SEQUENCE 334 AA; 38256 MW; 0DF42399D19701B3 CRC64;
MPKRRDILAI VLIVLPWTLL ITVWHQSTLA PLLAVHKDEG SDPRRETPPG ADPREYCTSD
RDIVEVVRTE YVYTRPPPWS DTLPTIHVVT PTYSRPVQKA ELTRMANTLL HVPNLHWLVV
EDAPRRTPLT ARLLRDTGLN YTHLHVETPR NYKLRGDARD PRIPRGTMQR NLALRWLRET
FPRNSSQPGV VYFADDDNTY SLELFEEMRS TRRVSVWPVA FVGGLRYEAP RVNGAGKVVG
WKTVFDPHRP FAIDMAGFAV NLRLILQRSQ AYFKLRGVKG GYQESSLLRE LVTLNDLEPK
AANCTKILVW HTRTEKPVLV NEGKKGFTDP SVEI
