SIA7D_HUMAN
ID SIA7D_HUMAN Reviewed; 302 AA.
AC Q9H4F1; Q5T9D0; Q9NWU6; Q9UKU1; Q9ULB9; Q9Y3G3; Q9Y3G4;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3-N-acetyl-galactosaminide alpha-2,6-sialyltransferase;
DE EC=2.4.99.7 {ECO:0000250|UniProtKB:Q9R2B6};
DE AltName: Full=NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc-alpha-2,6-sialyltransferase;
DE AltName: Full=ST6GalNAc IV;
DE Short=ST6GalNAcIV;
DE AltName: Full=Sialyltransferase 3C;
DE Short=SIAT3-C;
DE AltName: Full=Sialyltransferase 7D;
DE Short=SIAT7-D;
GN Name=ST6GALNAC4; Synonyms=SIAT3C, SIAT7D;
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 / MRNA].
RX PubMed=11062056; DOI=10.1042/bj3520037;
RA Harduin-Lepers A., Stokes D.C., Steelant W.F.A., Samyn-Petit B.,
RA Krzewinski-Recchi M.A., Vallejo-Ruiz V., Zanetta J.P., Auge C.,
RA Delannoy P.;
RT "Cloning, expression and gene organization of a human Neu5Ac alpha 2-3Gal
RT beta 1-3GalNAc alpha 2,6-sialyltransferase: hST6GalNAcIV.";
RL Biochem. J. 352:37-48(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal liver;
RA Kim K.-W., Kim K.-S., Do S.-I., Kim C.-H., Lee Y.-C.;
RT "Molecular cloning of NeuAcalpha2,3Galbeta1,3GalNAc alpha2,6-
RT sialyltransferase cDNA from human fetal liver.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RA Yoshida A.;
RT "N-acetylgalactosaminide alpha2,6-sialyltransferase.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell;
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 213-302.
RX PubMed=10369878; DOI=10.1093/hmg/8.7.1313;
RA Gilley J., Fried M.;
RT "Extensive gene order differences within regions of conserved synteny
RT between the Fugu and human genomes: implications for chromosomal evolution
RT and the cloning of disease genes.";
RL Hum. Mol. Genet. 8:1313-1320(1999).
CC -!- FUNCTION: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or
CC NeuAc) from CMP-NeuAc to the GalNAc residue on the NeuAc-alpha-2,3-Gal-
CC beta-1,3-GalNAc sequence of glycoproteins and glycolipids forming an
CC alpha-2,6-linkage. Produces branched type disialyl structures by
CC transfer of a sialyl group onto a GalNAc residue inside the backbone
CC core chains. Prefers O-glycans to glycoproteins or glycolipids.
CC {ECO:0000250|UniProtKB:Q9R2B6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-D-GlcNAc derivative +
CC CMP-N-acetyl-beta-neuraminate = an alpha-Neu5Ac-(2->3)-beta-D-Gal-
CC (1->3)-[alpha-Neu5Ac-(2->6)]-D-GlcNAc-R + CMP + H(+);
CC Xref=Rhea:RHEA:53896, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:146021, ChEBI:CHEBI:149714;
CC EC=2.4.99.7; Evidence={ECO:0000250|UniProtKB:Q9R2B6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + N-acetyl-alpha-neuraminosyl-
CC (2->3)-beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine = CMP + H(+)
CC + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1->3)-[N-
CC acetyl-alpha-neuraminosyl-(2->6)]-N-acetyl-D-galactosamine;
CC Xref=Rhea:RHEA:65288, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:156406, ChEBI:CHEBI:156407;
CC Evidence={ECO:0000250|UniProtKB:Q9R2B6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65289;
CC Evidence={ECO:0000250|UniProtKB:Q9R2B6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1b (d18:1(4E)) =
CC a ganglioside GD1alpha (d18:1(4E)) + CMP + H(+);
CC Xref=Rhea:RHEA:41968, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:78568, ChEBI:CHEBI:78569;
CC Evidence={ECO:0000250|UniProtKB:Q9R2B6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41969;
CC Evidence={ECO:0000250|UniProtKB:Q9R2B6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc]-L-
CC Ser-[protein] + CMP-N-acetyl-beta-neuraminate = 3-O-{alpha-Neu5Ac-
CC (2->3)-beta-D-Gal-(1->3)-[alpha-Neu5Ac-(2->6)]-alpha-D-GalNAc}-L-Ser-
CC [protein] + CMP + H(+); Xref=Rhea:RHEA:65280, Rhea:RHEA-COMP:16760,
CC Rhea:RHEA-COMP:16761, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:156395, ChEBI:CHEBI:156397;
CC Evidence={ECO:0000250|UniProtKB:Q9R2B6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65281;
CC Evidence={ECO:0000250|UniProtKB:Q9R2B6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc]-L-
CC Thr-[protein] + CMP-N-acetyl-beta-neuraminate = 3-O-{alpha-Neu5Ac-
CC (2->3)-beta-D-Gal-(1->3)-[alpha-Neu5Ac-(2->6)]-alpha-D-GalNAc}-L-Thr-
CC [protein] + CMP + H(+); Xref=Rhea:RHEA:65284, Rhea:RHEA-COMP:16762,
CC Rhea:RHEA-COMP:16763, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:156396, ChEBI:CHEBI:156398;
CC Evidence={ECO:0000250|UniProtKB:Q9R2B6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65285;
CC Evidence={ECO:0000250|UniProtKB:Q9R2B6};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q9R2B6}.
CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000250|UniProtKB:Q9R2B6}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST6GalNAc
CC IV;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_633";
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DR EMBL; AJ271734; CAC07404.1; -; mRNA.
DR EMBL; AF127142; AAF00102.1; -; mRNA.
DR EMBL; AB035172; BAA87034.1; -; mRNA.
DR EMBL; AK000600; BAA91281.1; -; mRNA.
DR EMBL; AL157935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87717.1; -; Genomic_DNA.
DR EMBL; BC036705; AAH36705.1; -; mRNA.
DR EMBL; Y17460; CAB44353.1; -; Genomic_DNA.
DR EMBL; Y17461; CAB44354.1; -; Genomic_DNA.
DR CCDS; CCDS6883.1; -.
DR RefSeq; NP_778204.1; NM_175039.3.
DR RefSeq; NP_778205.1; NM_175040.3.
DR AlphaFoldDB; Q9H4F1; -.
DR SMR; Q9H4F1; -.
DR BioGRID; 117992; 52.
DR IntAct; Q9H4F1; 3.
DR STRING; 9606.ENSP00000336733; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q9H4F1; 1 site.
DR iPTMnet; Q9H4F1; -.
DR PhosphoSitePlus; Q9H4F1; -.
DR BioMuta; ST6GALNAC4; -.
DR DMDM; 21759443; -.
DR EPD; Q9H4F1; -.
DR jPOST; Q9H4F1; -.
DR MassIVE; Q9H4F1; -.
DR MaxQB; Q9H4F1; -.
DR PaxDb; Q9H4F1; -.
DR PeptideAtlas; Q9H4F1; -.
DR PRIDE; Q9H4F1; -.
DR ProteomicsDB; 80828; -.
DR Antibodypedia; 2464; 87 antibodies from 17 providers.
DR DNASU; 27090; -.
DR Ensembl; ENST00000335791.10; ENSP00000336733.5; ENSG00000136840.19.
DR GeneID; 27090; -.
DR KEGG; hsa:27090; -.
DR MANE-Select; ENST00000335791.10; ENSP00000336733.5; NM_175039.4; NP_778204.1.
DR UCSC; uc004bss.3; human.
DR CTD; 27090; -.
DR DisGeNET; 27090; -.
DR GeneCards; ST6GALNAC4; -.
DR HGNC; HGNC:17846; ST6GALNAC4.
DR HPA; ENSG00000136840; Tissue enhanced (pancreas).
DR MIM; 606378; gene.
DR neXtProt; NX_Q9H4F1; -.
DR OpenTargets; ENSG00000136840; -.
DR PharmGKB; PA38250; -.
DR VEuPathDB; HostDB:ENSG00000136840; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT00940000157958; -.
DR HOGENOM; CLU_061099_1_0_1; -.
DR InParanoid; Q9H4F1; -.
DR OMA; NECRMYK; -.
DR OrthoDB; 817470at2759; -.
DR PhylomeDB; Q9H4F1; -.
DR TreeFam; TF352818; -.
DR BioCyc; MetaCyc:HS06223-MON; -.
DR BRENDA; 2.4.99.7; 2681.
DR PathwayCommons; Q9H4F1; -.
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; Q9H4F1; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 27090; 18 hits in 1075 CRISPR screens.
DR GeneWiki; ST6GALNAC4; -.
DR GenomeRNAi; 27090; -.
DR Pharos; Q9H4F1; Tbio.
DR PRO; PR:Q9H4F1; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9H4F1; protein.
DR Bgee; ENSG00000136840; Expressed in body of pancreas and 156 other tissues.
DR ExpressionAtlas; Q9H4F1; baseline and differential.
DR Genevisible; Q9H4F1; HS.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047290; F:(alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3)-N-acetyl-galactosaminide 6-alpha-sialyltransferase activity; TAS:Reactome.
DR GO; GO:0001665; F:alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase activity; IBA:GO_Central.
DR GO; GO:0008373; F:sialyltransferase activity; TAS:Reactome.
DR GO; GO:0001574; P:ganglioside biosynthetic process; IBA:GO_Central.
DR GO; GO:0006664; P:glycolipid metabolic process; TAS:ProtInc.
DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
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 Pfam; PF00777; Glyco_transf_29; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Lipid metabolism; Membrane; Reference proteome; Sialic acid; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..302
FT /note="Alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3-N-
FT acetyl-galactosaminide alpha-2,6-sialyltransferase"
FT /id="PRO_0000149278"
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..302
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 76..225
FT /evidence="ECO:0000250"
FT CONFLICT 119..120
FT /note="ST -> QA (in Ref. 2; AAF00102)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="S -> T (in Ref. 1; CAC07404)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="F -> L (in Ref. 4; BAA91281)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 302 AA; 34201 MW; 08A4CDC749A6D783 CRC64;
MKAPGRLVLI ILCSVVFSAV YILLCCWAGL PLCLATCLDH HFPTGSRPTV PGPLHFSGYS
SVPDGKPLVR EPCRSCAVVS SSGQMLGSGL GAEIDSAECV FRMNQAPTVG FEADVGQRST
LRVVSHTSVP LLLRNYSHYF QKARDTLYMV WGQGRHMDRV LGGRTYRTLL QLTRMYPGLQ
VYTFTERMMA YCDQIFQDET GKNRRQSGSF LSTGWFTMIL ALELCEEIVV YGMVSDSYCR
EKSHPSVPYH YFEKGRLDEC QMYLAHEQAP RSAHRFITEK AVFSRWAKKR PIVFAHPSWR
TE
