SIA7F_MOUSE
ID SIA7F_MOUSE Reviewed; 333 AA.
AC Q9JM95; A2AK72; A2AK76; A2AK77; A2AK78; A2AK79; Q05CN1; Q8CDC3; Q9R0G9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 6;
DE EC=2.4.99.- {ECO:0000269|PubMed:10702226};
DE AltName: Full=GalNAc alpha-2,6-sialyltransferase VI;
DE AltName: Full=ST6GalNAc VI {ECO:0000303|PubMed:10702226};
DE Short=ST6GalNAcVI;
DE AltName: Full=Sialyltransferase 7F;
DE Short=SIAT7-F;
GN Name=St6galnac6; Synonyms=Siat7f;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Liver;
RX PubMed=10702226; DOI=10.1074/jbc.275.10.6717;
RA Okajima T., Chen H.-H., Ito H., Kiso M., Tai T., Furukawa K., Urano T.,
RA Furukawa K.;
RT "Molecular cloning and expression of mouse GD1alpha/GT1aalpha/GQ1balpha
RT synthase (ST6GalNAc VI) gene.";
RL J. Biol. Chem. 275:6717-6723(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Colon;
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 [5]
RP INDUCTION.
RX PubMed=15858074; DOI=10.1093/glycob/cwi068;
RA Yasukawa Z., Sato C., Kitajima K.;
RT "Inflammation-dependent changes in alpha2,3-, alpha2,6-, and alpha2,8-
RT sialic acid glycotopes on serum glycoproteins in mice.";
RL Glycobiology 15:827-837(2005).
CC -!- FUNCTION: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or
CC NeuAc) from CMP-NeuAc onto glycolipids, forming an alpha-2,6-linkage.
CC Produces branched type disialyl structures by transfer of a sialyl
CC group onto the GalNAc or GlcNAc residue inside backbone core chains
CC having a terminal sialic acid with an alpha-2,3-linkage on Gal.
CC ST6GalNAcVI prefers glycolipids to glycoproteins, predominantly
CC catalyzing the biosynthesis of ganglioside GD1alpha from GM1b. Also has
CC activity toward GD1a and GT1b, and can generate DSGG
CC (disialylgalactosylgloboside) from MSGG (monosialylgalactosylgloboside)
CC (PubMed:10702226). Besides GMb1, MSGG and other glycolipids, it shows
CC activity towards sialyl Lc4Cer generating disialyl Lc4Cer, which can
CC lead to the synthesis of disialyl Lewis a (Le(a)), suggested to be a
CC cancer-associated antigen (By similarity).
CC {ECO:0000250|UniProtKB:Q969X2, ECO:0000269|PubMed:10702226}.
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:0000269|PubMed:10702226};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41969;
CC Evidence={ECO:0000305|PubMed:10702226};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GD1a (d18:1(4E)) =
CC CMP + ganglioside GT1aalpha (d18:1(4E)) + H(+); Xref=Rhea:RHEA:41972,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:78445, ChEBI:CHEBI:78571;
CC Evidence={ECO:0000269|PubMed:10702226};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41973;
CC Evidence={ECO:0000305|PubMed:10702226};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GT1b (d18:1(4E)) =
CC CMP + ganglioside GQ1b alpha (d18:1(4E)) + H(+);
CC Xref=Rhea:RHEA:41976, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:78452, ChEBI:CHEBI:78572;
CC Evidence={ECO:0000269|PubMed:10702226};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41977;
CC Evidence={ECO:0000305|PubMed:10702226};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + N-acetyl-alpha-neuraminosyl-
CC (2->3)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-
CC beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acyl-sphing-4-
CC enine = CMP + H(+) + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-
CC galactosyl-(1->3)-[N-acetyl-alpha-neuraminosyl-(2->6)]-N-acetyl-beta-
CC D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-
CC (1<->1')-N-acyl-sphing-4-enine; Xref=Rhea:RHEA:47884,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:88073, ChEBI:CHEBI:88079;
CC Evidence={ECO:0000250|UniProtKB:Q969X2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47885;
CC Evidence={ECO:0000250|UniProtKB:Q969X2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + globoside MSGG = CMP +
CC globoside DSGG + H(+); Xref=Rhea:RHEA:56088, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:140623,
CC ChEBI:CHEBI:140624; Evidence={ECO:0000250|UniProtKB:Q969X2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56089;
CC Evidence={ECO:0000250|UniProtKB:Q969X2};
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:Q969X2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65281;
CC Evidence={ECO:0000250|UniProtKB:Q969X2};
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:Q969X2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65285;
CC Evidence={ECO:0000250|UniProtKB:Q969X2};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9JM95-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JM95-2; Sequence=VSP_030360;
CC Name=3;
CC IsoId=Q9JM95-3; Sequence=VSP_030361, VSP_030362;
CC -!- TISSUE SPECIFICITY: Widely expressed, the gene expression is most
CC abundant in colon, brain, liver, and heart.
CC {ECO:0000269|PubMed:10702226}.
CC -!- INDUCTION: After inflammation stimulus. {ECO:0000269|PubMed:15858074}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM16604.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM16608.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM16609.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM16610.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM16611.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB035123; BAA95940.1; -; mRNA.
DR EMBL; AB035174; BAA87036.1; -; mRNA.
DR EMBL; AK030648; BAC27064.1; -; mRNA.
DR EMBL; AL772271; CAM16604.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL772271; CAM16606.1; -; Genomic_DNA.
DR EMBL; AL772271; CAM16607.1; -; Genomic_DNA.
DR EMBL; AL772271; CAM16608.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL772271; CAM16609.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL772271; CAM16610.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL772271; CAM16611.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC022924; AAH22924.1; -; mRNA.
DR CCDS; CCDS15923.1; -. [Q9JM95-1]
DR RefSeq; NP_001020481.1; NM_001025310.2.
DR RefSeq; NP_001020482.1; NM_001025311.2.
DR RefSeq; NP_001276476.1; NM_001289547.1.
DR RefSeq; NP_001276477.1; NM_001289548.1.
DR RefSeq; NP_001276478.1; NM_001289549.1.
DR RefSeq; NP_058669.1; NM_016973.3. [Q9JM95-1]
DR AlphaFoldDB; Q9JM95; -.
DR SMR; Q9JM95; -.
DR STRING; 10090.ENSMUSP00000080555; -.
DR SwissLipids; SLP:000000778; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q9JM95; 1 site.
DR iPTMnet; Q9JM95; -.
DR PhosphoSitePlus; Q9JM95; -.
DR MaxQB; Q9JM95; -.
DR PaxDb; Q9JM95; -.
DR PRIDE; Q9JM95; -.
DR ProteomicsDB; 257173; -. [Q9JM95-1]
DR ProteomicsDB; 257174; -. [Q9JM95-2]
DR ProteomicsDB; 257175; -. [Q9JM95-3]
DR DNASU; 50935; -.
DR Ensembl; ENSMUST00000072111; ENSMUSP00000071983; ENSMUSG00000026811. [Q9JM95-1]
DR Ensembl; ENSMUST00000081879; ENSMUSP00000080555; ENSMUSG00000026811. [Q9JM95-2]
DR Ensembl; ENSMUST00000095044; ENSMUSP00000092654; ENSMUSG00000026811. [Q9JM95-1]
DR Ensembl; ENSMUST00000183538; ENSMUSP00000138916; ENSMUSG00000026811. [Q9JM95-3]
DR GeneID; 50935; -.
DR KEGG; mmu:50935; -.
DR UCSC; uc008jgb.2; mouse. [Q9JM95-1]
DR CTD; 30815; -.
DR MGI; MGI:1355316; St6galnac6.
DR VEuPathDB; HostDB:ENSMUSG00000026811; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT00940000160114; -.
DR InParanoid; Q9JM95; -.
DR OrthoDB; 817470at2759; -.
DR PhylomeDB; Q9JM95; -.
DR TreeFam; TF323961; -.
DR Reactome; R-MMU-4085001; Sialic acid metabolism.
DR Reactome; R-MMU-9037629; Lewis blood group biosynthesis.
DR BioGRID-ORCS; 50935; 2 hits in 75 CRISPR screens.
DR ChiTaRS; St6galnac6; mouse.
DR PRO; PR:Q9JM95; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9JM95; protein.
DR Bgee; ENSMUSG00000026811; Expressed in left colon and 250 other tissues.
DR ExpressionAtlas; Q9JM95; baseline and differential.
DR Genevisible; Q9JM95; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0001665; F:alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase activity; IDA:MGI.
DR GO; GO:0008373; F:sialyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0009988; P:cell-cell recognition; IC:BHF-UCL.
DR GO; GO:0001574; P:ganglioside biosynthetic process; IDA:MGI.
DR GO; GO:0009100; P:glycoprotein metabolic process; ISO:MGI.
DR GO; GO:0006687; P:glycosphingolipid metabolic process; ISO:MGI.
DR GO; GO:0006677; P:glycosylceramide metabolic process; ISO:MGI.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
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 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Lipid metabolism; Membrane; Reference proteome;
KW Sialic acid; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..333
FT /note="Alpha-N-acetylgalactosaminide alpha-2,6-
FT sialyltransferase 6"
FT /id="PRO_0000314796"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..333
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 108..256
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..9
FT /note="MACSRPPSQ -> MAQGNHEAWGW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030360"
FT VAR_SEQ 230..235
FT /note="ETGKDR -> KSPIPG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030361"
FT VAR_SEQ 236..333
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030362"
FT CONFLICT 103
FT /note="S -> A (in Ref. 4; AAH22924)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 38167 MW; D3841828D389CDEA CRC64;
MACSRPPSQC DPTTLPPGPP AGRWPLPFSR RRREMSSNKE QRSAVFVILF ALITILILYS
SNSANEVFHY GSLRGRTRRP VNLKKWSFSS AYFPILGNKT LPSRCNQCVI ITSSSHLLGT
KLGPEIERAE CTIRMNDAPT SGYSADVGNK TTFRVVAHSS VFRVLRKPQE FVNRTPETVF
IFWGPPNKMQ KPQGSLLRVI QRAGLMFPNM EAYAVSPARM QQFDDLFRGE TGKDREKSHS
WLSTGWFTMV IAVELCDHVH VYGMVPPDYC SQRPRLQRMP YHYYEPKGPD ECVTYIQNEH
SRKGNHHRFI TEKRVFSSWA QLYGITFSHP SWT
