FUT10_HUMAN
ID FUT10_HUMAN Reviewed; 479 AA.
AC Q6P4F1; A8KAC8; Q70GG3; Q8IVI6; Q8IVI7; Q8IVJ3; Q8TE43; Q9BSR3;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Alpha-(1,3)-fucosyltransferase 10;
DE EC=2.4.1.- {ECO:0000269|PubMed:19088067};
DE AltName: Full=Fucosyltransferase X;
DE Short=Fuc-TX;
DE Short=FucT-X;
DE AltName: Full=Galactoside 3-L-fucosyltransferase 10;
DE Short=Fucosyltransferase 10;
GN Name=FUT10 {ECO:0000303|PubMed:19088067, ECO:0000312|HGNC:HGNC:19234};
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 6), AND VARIANTS PHE-59 AND VAL-368.
RC TISSUE=Brain;
RX PubMed=11698403; DOI=10.1074/jbc.m107927200;
RA Roos C., Kolmer M., Mattila P., Renkonen R.;
RT "Composition of Drosophila melanogaster proteome involved in fucosylated
RT glycan metabolism.";
RL J. Biol. Chem. 277:3168-3175(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4 AND 5).
RA Martinez-Duncker I., Candelier J.-J., Oriol R., Mollicone R.;
RT "Cloning, expression and genomic organization of two new human alpha3-
RT fucosyltransferases (FUT10 and FUT11).";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Trachea;
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 [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 7), AND VARIANTS
RP VAL-368 AND PRO-371.
RC TISSUE=Brain, and Ovary;
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 SUBCELLULAR LOCATION (ISOFORM 1).
RX PubMed=12370785; DOI=10.1007/s00335-001-2152-5;
RA Baboval T., Smith F.I.;
RT "Comparison of human and mouse Fuc-TX and Fuc-TXI genes, and expression
RT studies in the mouse.";
RL Mamm. Genome 13:538-541(2002).
RN [7]
RP FUNCTION (ISOFORMS 1; 4 AND 5), BIOPHYSICOCHEMICAL PROPERTIES (ISOFORMS 1
RP AND 4), PATHWAY, SUBCELLULAR LOCATION (ISOFORMS 1; 4 AND 5), TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE (ISOFORMS 4 AND 5).
RX PubMed=19088067; DOI=10.1074/jbc.m809312200;
RA Mollicone R., Moore S.E., Bovin N., Garcia-Rosasco M., Candelier J.J.,
RA Martinez-Duncker I., Oriol R.;
RT "Activity, splice variants, conserved peptide motifs, and phylogeny of two
RT new alpha1,3-fucosyltransferase families (FUT10 and FUT11).";
RL J. Biol. Chem. 284:4723-4738(2009).
CC -!- FUNCTION: Predominantly fucosylates the innermost N-acetyl glucosamine
CC (GlcNAc) residue in biantennary N-glycan acceptors. Postulated to
CC generate core alpha(1->3)-fucose epitope within the chitobiose unit of
CC biantennary N-glycans, providing for a recognition signal to reorient
CC aberrantly folded glycoproteins for degradation (PubMed:19088067).
CC Involved in biosynthesis of Lewis X-carrying biantennary N-glycans that
CC regulate neuron stem cell self-renewal during brain development (By
CC similarity). {ECO:0000250|UniProtKB:Q5F2L2,
CC ECO:0000269|PubMed:19088067}.
CC -!- FUNCTION: [Isoform 1]: Catalyzes the transfer of fucosyl moiety from
CC GDP-beta-L-fucose to the innermost GlcNAc residue in biantennary N-
CC glycan acceptors. Does not fucosylate GlcNAc within type 2 lactosamine
CC unit. {ECO:0000269|PubMed:19088067}.
CC -!- FUNCTION: [Isoform 4]: Catalyzes the transfer of fucosyl moiety from
CC GDP-beta-L-fucose to the innermost GlcNAc residue in biantennary N-
CC glycan acceptors. Does not fucosylate GlcNAc within type 2 lactosamine
CC unit. {ECO:0000269|PubMed:19088067}.
CC -!- FUNCTION: [Isoform 5]: Catalyzes the transfer of fucosyl moiety from
CC GDP-beta-L-fucose to the innermost GlcNAc residue in biantennary N-
CC glycan acceptors. Does not fucosylate GlcNAc within type 2 lactosamine
CC unit. {ECO:0000269|PubMed:19088067}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 1]:
CC Kinetic parameters:
CC KM=15 uM for GDP-beta-L-fucose {ECO:0000269|PubMed:19088067};
CC Vmax=146 pmol/h/mg enzyme toward GDP-beta-L-fucose
CC {ECO:0000269|PubMed:19088067};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 4]:
CC Kinetic parameters:
CC KM=13 uM for GDP-beta-L-fucose {ECO:0000269|PubMed:19088067};
CC Vmax=285 pmol/h/mg enzyme toward GDP-beta-L-fucose
CC {ECO:0000269|PubMed:19088067};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:19088067}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:19088067}; Single-pass type II membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000305|PubMed:12370785,
CC ECO:0000305|PubMed:19088067}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Golgi apparatus
CC {ECO:0000269|PubMed:19088067}. Lysosome {ECO:0000269|PubMed:19088067}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19088067}; Single-pass type II membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000305|PubMed:19088067};
CC Single-pass type II membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q6P4F1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P4F1-2; Sequence=VSP_027501;
CC Name=3;
CC IsoId=Q6P4F1-3; Sequence=VSP_027498, VSP_027502, VSP_027505,
CC VSP_027506;
CC Name=4;
CC IsoId=Q6P4F1-4; Sequence=VSP_027500, VSP_027505, VSP_027506;
CC Name=5;
CC IsoId=Q6P4F1-5; Sequence=VSP_027505, VSP_027506;
CC Name=6;
CC IsoId=Q6P4F1-6; Sequence=VSP_027500;
CC Name=7;
CC IsoId=Q6P4F1-7; Sequence=VSP_027499, VSP_027503, VSP_027504;
CC -!- TISSUE SPECIFICITY: Expressed in lung, digestive tract, gall bladder,
CC placenta, kidney, uterus and brain. Not detected in spleen, heart,
CC muscle, liver and pancreas. {ECO:0000269|PubMed:19088067}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal tissues including skin, small
CC intestine, liver, kidney, lung, muscle, heart and brain.
CC {ECO:0000269|PubMed:19088067}.
CC -!- DEVELOPMENTAL STAGE: [Isoform 4]: Expressed in 50 day old embryo.
CC {ECO:0000269|PubMed:19088067}.
CC -!- DEVELOPMENTAL STAGE: [Isoform 5]: Expressed in 50 day old embryo.
CC {ECO:0000269|PubMed:19088067}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD24023.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ431184; CAD24023.1; ALT_INIT; mRNA.
DR EMBL; AJ512465; CAD54669.1; -; mRNA.
DR EMBL; AJ535838; CAD59771.1; -; mRNA.
DR EMBL; AJ535839; CAD59772.1; -; mRNA.
DR EMBL; AJ582015; CAE46499.1; -; mRNA.
DR EMBL; AK292993; BAF85682.1; -; mRNA.
DR EMBL; CH471080; EAW63404.1; -; Genomic_DNA.
DR EMBL; BC004884; AAH04884.2; -; mRNA.
DR EMBL; BC063462; AAH63462.1; -; mRNA.
DR CCDS; CCDS6088.1; -. [Q6P4F1-1]
DR RefSeq; NP_116053.3; NM_032664.3. [Q6P4F1-1]
DR AlphaFoldDB; Q6P4F1; -.
DR BioGRID; 124239; 11.
DR IntAct; Q6P4F1; 2.
DR STRING; 9606.ENSP00000332757; -.
DR BindingDB; Q6P4F1; -.
DR ChEMBL; CHEMBL2926; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR GlyGen; Q6P4F1; 4 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q6P4F1; -.
DR PhosphoSitePlus; Q6P4F1; -.
DR BioMuta; FUT10; -.
DR DMDM; 156630455; -.
DR EPD; Q6P4F1; -.
DR MassIVE; Q6P4F1; -.
DR PaxDb; Q6P4F1; -.
DR PeptideAtlas; Q6P4F1; -.
DR PRIDE; Q6P4F1; -.
DR Antibodypedia; 23343; 177 antibodies from 24 providers.
DR DNASU; 84750; -.
DR Ensembl; ENST00000327671.10; ENSP00000332757.5; ENSG00000172728.16. [Q6P4F1-1]
DR Ensembl; ENST00000518672.5; ENSP00000430428.1; ENSG00000172728.16. [Q6P4F1-6]
DR Ensembl; ENST00000524021.1; ENSP00000429870.1; ENSG00000172728.16. [Q6P4F1-6]
DR GeneID; 84750; -.
DR KEGG; hsa:84750; -.
DR MANE-Select; ENST00000327671.10; ENSP00000332757.5; NM_032664.3; NP_116053.3.
DR UCSC; uc003xjd.4; human. [Q6P4F1-1]
DR CTD; 84750; -.
DR DisGeNET; 84750; -.
DR GeneCards; FUT10; -.
DR HGNC; HGNC:19234; FUT10.
DR HPA; ENSG00000172728; Low tissue specificity.
DR neXtProt; NX_Q6P4F1; -.
DR OpenTargets; ENSG00000172728; -.
DR PharmGKB; PA134872572; -.
DR VEuPathDB; HostDB:ENSG00000172728; -.
DR eggNOG; KOG2619; Eukaryota.
DR GeneTree; ENSGT00940000160287; -.
DR HOGENOM; CLU_032075_0_2_1; -.
DR InParanoid; Q6P4F1; -.
DR OMA; FTAQEFW; -.
DR OrthoDB; 551308at2759; -.
DR PhylomeDB; Q6P4F1; -.
DR TreeFam; TF316348; -.
DR BRENDA; 2.4.1.65; 2681.
DR PathwayCommons; Q6P4F1; -.
DR Reactome; R-HSA-9037629; Lewis blood group biosynthesis.
DR SignaLink; Q6P4F1; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 84750; 9 hits in 1077 CRISPR screens.
DR ChiTaRS; FUT10; human.
DR GenomeRNAi; 84750; -.
DR Pharos; Q6P4F1; Tdark.
DR PRO; PR:Q6P4F1; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q6P4F1; protein.
DR Bgee; ENSG00000172728; Expressed in pancreatic ductal cell and 121 other tissues.
DR Genevisible; Q6P4F1; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
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:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0046920; F:alpha-(1->3)-fucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008417; F:fucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IEA:Ensembl.
DR GO; GO:0009566; P:fertilization; NAS:UniProtKB.
DR GO; GO:0036065; P:fucosylation; IBA:GO_Central.
DR GO; GO:0030097; P:hemopoiesis; NAS:UniProtKB.
DR GO; GO:0042355; P:L-fucose catabolic process; NAS:UniProtKB.
DR GO; GO:0036071; P:N-glycan fucosylation; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; NAS:UniProtKB.
DR GO; GO:0036445; P:neuronal stem cell division; ISS:UniProtKB.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; NAS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; TAS:UniProtKB.
DR GO; GO:0006605; P:protein targeting; NAS:UniProtKB.
DR GO; GO:0042060; P:wound healing; NAS:UniProtKB.
DR Gene3D; 3.40.50.11660; -; 1.
DR InterPro; IPR017176; Alpha-1_3-FUT_met.
DR InterPro; IPR031481; Glyco_tran_10_N.
DR InterPro; IPR001503; Glyco_trans_10.
DR InterPro; IPR038577; GT10-like_C_sf.
DR PANTHER; PTHR11929; PTHR11929; 1.
DR Pfam; PF17039; Glyco_tran_10_N; 1.
DR Pfam; PF00852; Glyco_transf_10; 1.
DR PIRSF; PIRSF037332; Alpha1_3FUT_met; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Lysosome; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..479
FT /note="Alpha-(1,3)-fucosyltransferase 10"
FT /id="PRO_0000299002"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..479
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..62
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_027498"
FT VAR_SEQ 1..51
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027499"
FT VAR_SEQ 1..28
FT /note="Missing (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:11698403, ECO:0000303|Ref.2"
FT /id="VSP_027500"
FT VAR_SEQ 27
FT /note="Q -> ALDTVENLMKVTGPPQGVTDSMQCFNDQRPLSNTRSSEHIKE (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027501"
FT VAR_SEQ 63..126
FT /note="LKKEGLTFNRKRKWELDSYPIMLWWSPLTGETGRLGQCGADACFFTINRTYL
FT HHHMTKAFLFYG -> MGIGQLPHYALVVPADGGDWEVRPMWSRCLFLHHQPDLPPSSH
FT DQSIPLLWSQEESPPLAENDG (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_027502"
FT VAR_SEQ 127..143
FT /note="TDFNIDSLPLPRKAHHD -> KQDFRLSPLFAVVFLQS (in isoform
FT 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027503"
FT VAR_SEQ 144..479
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027504"
FT VAR_SEQ 405..419
FT /note="GLPPKRWEAEDTHLS -> VSKSKVGIEPAGWPS (in isoform 3,
FT isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_027505"
FT VAR_SEQ 420..479
FT /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_027506"
FT VARIANT 59
FT /note="L -> F (in dbSNP:rs16880994)"
FT /evidence="ECO:0000269|PubMed:11698403"
FT /id="VAR_034759"
FT VARIANT 268
FT /note="Y -> H (in dbSNP:rs16880853)"
FT /id="VAR_034760"
FT VARIANT 368
FT /note="L -> V (in dbSNP:rs17855838)"
FT /evidence="ECO:0000269|PubMed:11698403,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_034761"
FT VARIANT 371
FT /note="R -> P (in dbSNP:rs17855839)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_034762"
SQ SEQUENCE 479 AA; 56094 MW; 205594E0CE587208 CRC64;
MVRIQRRKLL ASCLCVTATV FLLVTLQVMV ELGKFERKEF KSSSLQDGHT KMEEAPTHLN
SFLKKEGLTF NRKRKWELDS YPIMLWWSPL TGETGRLGQC GADACFFTIN RTYLHHHMTK
AFLFYGTDFN IDSLPLPRKA HHDWAVFHEE SPKNNYKLFH KPVITLFNYT ATFSRHSHLP
LTTQYLESIE VLKSLRYLVP LQSKNKLRKR LAPLVYVQSD CDPPSDRDSY VRELMTYIEV
DSYGECLRNK DLPQQLKNPA SMDADGFYRI IAQYKFILAF ENAVCDDYIT EKFWRPLKLG
VVPVYYGSPS ITDWLPSNKS AILVSEFSHP RELASYIRRL DSDDRLYEAY VEWKLKGEIS
NQRLLTALRE RKWGVQDVNQ DNYIDAFECM VCTKVWANIR LQEKGLPPKR WEAEDTHLSC
PEPTVFAFSP LRTPPLSSLR EMWISSFEQS KKEAQALRWL VDRNQNFSSQ EFWGLVFKD
