SIA7C_HUMAN
ID SIA7C_HUMAN Reviewed; 305 AA.
AC Q8NDV1; Q6PCE0; Q6UX29; Q8N259;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 3;
DE EC=2.4.99.7 {ECO:0000269|PubMed:16169874, ECO:0000269|PubMed:17123352};
DE AltName: Full=GalNAc alpha-2,6-sialyltransferase III;
DE AltName: Full=ST6GalNAc III {ECO:0000303|PubMed:16169874, ECO:0000303|PubMed:17123352};
DE Short=ST6GalNAcIII;
DE AltName: Full=STY;
DE AltName: Full=Sialyltransferase 7C;
DE Short=SIAT7-C;
GN Name=ST6GALNAC3; Synonyms=SIAT7C; ORFNames=UNQ2787/PRO7177;
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).
RA Harduin-Lepers A.;
RT "Molecular cloning and expression of human ST6GALNAC III.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Tongue;
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 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-223.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-223.
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=16169874; DOI=10.1093/jb/mvi124;
RA Tsuchida A., Ogiso M., Nakamura Y., Kiso M., Furukawa K., Furukawa K.;
RT "Molecular cloning and expression of human ST6GalNAc III: restricted tissue
RT distribution and substrate specificity.";
RL J. Biochem. 138:237-243(2005).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=17123352; DOI=10.1042/bj20061118;
RA Senda M., Ito A., Tsuchida A., Hagiwara T., Kaneda T., Nakamura Y.,
RA Kasama K., Kiso M., Yoshikawa K., Katagiri Y., Ono Y., Ogiso M., Urano T.,
RA Furukawa K., Oshima S., Furukawa K.;
RT "Identification and expression of a sialyltransferase responsible for the
RT synthesis of disialylgalactosylgloboside in normal and malignant kidney
RT cells: downregulation of ST6GalNAc VI in renal cancers.";
RL Biochem. J. 402:459-470(2007).
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. ST6GalNAcIII prefers glycolipids to glycoproteins,
CC predominantly catalyzing the biosynthesis of ganglioside GD1alpha from
CC GM1b (PubMed:16169874, PubMed:17123352). GD1alpha is a critical
CC molecule in the communication and interaction between neuronal cells
CC and their supportive cells, particularly in brain tissues, and
CC functions as an adhesion molecule in the process of metastasis (By
CC similarity). Sialylation of glycoproteins or glycosphingolipids is very
CC important in tumor development, neuronal development, nerve repair,
CC immunological processes and regulation of hormone sensitivity
CC (PubMed:17123352). {ECO:0000250|UniProtKB:Q9QYJ1,
CC ECO:0000269|PubMed:16169874, ECO:0000269|PubMed:17123352}.
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:0000269|PubMed:16169874,
CC ECO:0000269|PubMed:17123352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53897;
CC Evidence={ECO:0000305|PubMed:16169874, ECO:0000305|PubMed:17123352};
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:16169874, ECO:0000269|PubMed:17123352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41969;
CC Evidence={ECO:0000305|PubMed:16169874, ECO:0000305|PubMed:17123352};
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:0000269|PubMed:17123352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56089;
CC Evidence={ECO:0000305|PubMed:17123352};
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:0000269|PubMed:16169874, ECO:0000269|PubMed:17123352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65281;
CC Evidence={ECO:0000305|PubMed:16169874, ECO:0000305|PubMed:17123352};
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:0000269|PubMed:16169874, ECO:0000269|PubMed:17123352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65285;
CC Evidence={ECO:0000305|PubMed:16169874, ECO:0000305|PubMed:17123352};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.02 mM for ganglioside GM1b {ECO:0000269|PubMed:16169874};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:16169874, ECO:0000305|PubMed:17123352}.
CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000305|PubMed:16169874,
CC ECO:0000305|PubMed:17123352}.
CC -!- INTERACTION:
CC Q8NDV1; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-12947081, EBI-10243654;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NDV1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NDV1-2; Sequence=VSP_013218, VSP_013219;
CC -!- TISSUE SPECIFICITY: Expressed in brain and kidney (PubMed:16169874,
CC PubMed:17123352). Observed in the epithelium of the proximal tubules,
CC marginal expression was also found in the distal tubules and collecting
CC tubules (PubMed:17123352). {ECO:0000269|PubMed:16169874,
CC ECO:0000269|PubMed:17123352}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST6GalNAc
CC III;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_632";
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DR EMBL; AJ507291; CAD45371.1; -; mRNA.
DR EMBL; AK091215; BAC03611.1; -; mRNA.
DR EMBL; AY358540; AAQ88904.1; -; mRNA.
DR EMBL; CH471059; EAX06388.1; -; Genomic_DNA.
DR EMBL; BC059363; AAH59363.1; -; mRNA.
DR CCDS; CCDS672.1; -. [Q8NDV1-1]
DR RefSeq; NP_001153483.1; NM_001160011.1. [Q8NDV1-2]
DR RefSeq; NP_694541.2; NM_152996.2. [Q8NDV1-1]
DR AlphaFoldDB; Q8NDV1; -.
DR SMR; Q8NDV1; -.
DR BioGRID; 129166; 82.
DR IntAct; Q8NDV1; 13.
DR STRING; 9606.ENSP00000329214; -.
DR SwissLipids; SLP:000001364; -. [Q8NDV1-1]
DR SwissLipids; SLP:000001373; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q8NDV1; 3 sites.
DR PhosphoSitePlus; Q8NDV1; -.
DR BioMuta; ST6GALNAC3; -.
DR DMDM; 48428651; -.
DR EPD; Q8NDV1; -.
DR MassIVE; Q8NDV1; -.
DR MaxQB; Q8NDV1; -.
DR PaxDb; Q8NDV1; -.
DR PeptideAtlas; Q8NDV1; -.
DR PRIDE; Q8NDV1; -.
DR ProteomicsDB; 73055; -. [Q8NDV1-1]
DR ProteomicsDB; 73056; -. [Q8NDV1-2]
DR Antibodypedia; 33477; 53 antibodies from 15 providers.
DR DNASU; 256435; -.
DR Ensembl; ENST00000328299.4; ENSP00000329214.3; ENSG00000184005.11. [Q8NDV1-1]
DR GeneID; 256435; -.
DR KEGG; hsa:256435; -.
DR MANE-Select; ENST00000328299.4; ENSP00000329214.3; NM_152996.4; NP_694541.2.
DR UCSC; uc001dhh.3; human. [Q8NDV1-1]
DR CTD; 256435; -.
DR DisGeNET; 256435; -.
DR GeneCards; ST6GALNAC3; -.
DR HGNC; HGNC:19343; ST6GALNAC3.
DR HPA; ENSG00000184005; Tissue enhanced (brain).
DR MIM; 610133; gene.
DR neXtProt; NX_Q8NDV1; -.
DR OpenTargets; ENSG00000184005; -.
DR PharmGKB; PA134984080; -.
DR VEuPathDB; HostDB:ENSG00000184005; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT00940000159735; -.
DR HOGENOM; CLU_061099_2_0_1; -.
DR InParanoid; Q8NDV1; -.
DR OMA; PGAKWIP; -.
DR OrthoDB; 817470at2759; -.
DR PhylomeDB; Q8NDV1; -.
DR TreeFam; TF352818; -.
DR BRENDA; 2.4.99.7; 2681.
DR PathwayCommons; Q8NDV1; -.
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; Q8NDV1; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 256435; 9 hits in 1067 CRISPR screens.
DR ChiTaRS; ST6GALNAC3; human.
DR GenomeRNAi; 256435; -.
DR Pharos; Q8NDV1; Tbio.
DR PRO; PR:Q8NDV1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8NDV1; protein.
DR Bgee; ENSG00000184005; Expressed in corpus callosum and 142 other tissues.
DR ExpressionAtlas; Q8NDV1; baseline and differential.
DR Genevisible; Q8NDV1; 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:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0047290; F:(alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3)-N-acetyl-galactosaminide 6-alpha-sialyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0001665; F:alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase activity; IBA:GO_Central.
DR GO; GO:0008373; F:sialyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0001574; P:ganglioside biosynthetic process; IBA:GO_Central.
DR GO; GO:0009100; P:glycoprotein metabolic process; IDA:BHF-UCL.
DR GO; GO:0006687; P:glycosphingolipid metabolic process; IDA:BHF-UCL.
DR GO; GO:0006677; P:glycosylceramide metabolic process; IDA:BHF-UCL.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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 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..305
FT /note="Alpha-N-acetylgalactosaminide alpha-2,6-
FT sialyltransferase 3"
FT /id="PRO_0000149275"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..305
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80..229
FT /evidence="ECO:0000250"
FT VAR_SEQ 208..210
FT /note="RVQ -> STE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_013218"
FT VAR_SEQ 211..305
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_013219"
FT VARIANT 223
FT /note="L -> I (in dbSNP:rs1184626)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4"
FT /id="VAR_055846"
FT CONFLICT 169
FT /note="V -> I (in Ref. 2; BAC03611)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 305 AA; 35395 MW; 700BFC6A48F8AD3A CRC64;
MACILKRKSV IAVSFIAAFL FLLVVRLVNE VNFPLLLNCF GQPGTKWIPF SYTYRRPLRT
HYGYINVKTQ EPLQLDCDLC AIVSNSGQMV GQKVGNEIDR SSCIWRMNNA PTKGYEEDVG
RMTMIRVVSH TSVPLLLKNP DYFFKEANTT IYVIWGPFRN MRKDGNGIVY NMLKKTVGIY
PNAQIYVTTE KRMSYCDGVF KKETGKDRVQ SGSYLSTGWF TFLLAMDACY GIHVYGMIND
TYCKTEGYRK VPYHYYEQGR DECDEYFLHE HAPYGGHRFI TEKKVFAKWA KKHRIIFTHP
NWTLS
