FUT1_MOUSE
ID FUT1_MOUSE Reviewed; 377 AA.
AC O09160; P97327;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2020, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Galactoside alpha-(1,2)-fucosyltransferase 1 {ECO:0000305};
DE AltName: Full=Alpha(1,2)FT 1;
DE AltName: Full=Fucosyltransferase 1;
DE Short=MFUT-1 {ECO:0000303|PubMed:11368156};
DE AltName: Full=GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 1;
DE AltName: Full=Type 1 galactoside alpha-(1,2)-fucosyltransferase FUT1 {ECO:0000305};
DE EC=2.4.1.69 {ECO:0000269|PubMed:14967068};
DE AltName: Full=Type 2 galactoside alpha-(1,2)-fucosyltransferase FUT1 {ECO:0000305};
DE EC=2.4.1.344 {ECO:0000250|UniProtKB:P19526};
GN Name=Fut1 {ECO:0000312|MGI:MGI:109375};
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=NIH Swiss;
RX PubMed=9355741; DOI=10.1042/bj3270105;
RA Domino S.E., Hiraiwa N., Lowe J.B.;
RT "Molecular cloning, chromosomal assignment and tissue-specific expression
RT of a murine alpha(1,2)fucosyltransferase expressed in thymic and epididymal
RT epithelial cells.";
RL Biochem. J. 327:105-115(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, CATALYTIC ACTIVITY,
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11368156; DOI=10.1006/abbi.2001.2303;
RA Lin B., Saito M., Sakakibara Y., Hayashi Y., Yanagisawa M., Iwamori M.;
RT "Characterization of three members of murine alpha1,2-fucosyltransferases:
RT change in the expression of the Se gene in the intestine of mice after
RT administration of microbes.";
RL Arch. Biochem. Biophys. 388:207-215(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ICR; TISSUE=Brain;
RA Hitoshi S., Kusunoki S., Kanazawa I., Tsuji S.;
RT "Molecular cloning and expression of a mouse GDP-L-Fucose: beta-D-
RT Galactoside 2-alpha-L-Fucosyltransferase.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Vagina;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/10;
RX PubMed=18379136; DOI=10.1266/ggs.83.77;
RA Liu Y., Takahashi A., Kitano T., Koide T., Shiroishi T., Moriwaki K.,
RA Saitou N.;
RT "Mosaic genealogy of the Mus musculus genome revealed by 21 nuclear genes
RT from its three subspecies.";
RL Genes Genet. Syst. 83:77-88(2008).
RN [6]
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 [7]
RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=14967068; DOI=10.1042/bj20031668;
RA Iwamori M., Domino S.E.;
RT "Tissue-specific loss of fucosylated glycolipids in mice with targeted
RT deletion of alpha(1,2)fucosyltransferase genes.";
RL Biochem. J. 380:75-81(2004).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=11713270; DOI=10.1128/mcb.21.24.8336-8345.2001;
RA Domino S.E., Zhang L., Gillespie P.J., Saunders T.L., Lowe J.B.;
RT "Deficiency of reproductive tract alpha(1,2)fucosylated glycans and normal
RT fertility in mice with targeted deletions of the FUT1 or FUT2
RT alpha(1,2)fucosyltransferase locus.";
RL Mol. Cell. Biol. 21:8336-8345(2001).
RN [9]
RP FUNCTION.
RX PubMed=16884711; DOI=10.1016/j.ydbio.2006.06.052;
RA St John J.A., Claxton C., Robinson M.W., Yamamoto F., Domino S.E., Key B.;
RT "Genetic manipulation of blood group carbohydrates alters development and
RT pathfinding of primary sensory axons of the olfactory systems.";
RL Dev. Biol. 298:470-484(2006).
CC -!- FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine
CC diphosphate-beta-L-fucose, to the terminal galactose residue of
CC glycoconjugates through an alpha(1,2) linkage leading to H antigen
CC synthesis that is an intermediate substrate in the synthesis of ABO
CC blood group antigens (PubMed:11368156, PubMed:14967068,
CC PubMed:16884711). H antigen is essential for maturation of the
CC glomerular layer of the main olfactory bulb, in cell migration and
CC early cell-cell contacts during tumor associated angiogenesis
CC (PubMed:16884711). Preferentially fucosylates soluble lactose and to a
CC lesser extent, fucosylates glycolipids gangliosides GA1 and GM1a
CC (PubMed:11368156, PubMed:14967068). {ECO:0000269|PubMed:11368156,
CC ECO:0000269|PubMed:14967068, ECO:0000269|PubMed:16884711}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC derivative + GDP-beta-L-fucose = an alpha-L-Fuc-(1->2)-beta-D-Gal-
CC (1->4)-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:50668,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:133507, ChEBI:CHEBI:133510; EC=2.4.1.344;
CC Evidence={ECO:0000250|UniProtKB:P19526};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GA1 + GDP-beta-L-fucose = ganglioside Fuc-GA1 +
CC GDP + H(+); Xref=Rhea:RHEA:48320, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:88069,
CC ChEBI:CHEBI:90262; Evidence={ECO:0000269|PubMed:11368156,
CC ECO:0000269|PubMed:14967068};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48321;
CC Evidence={ECO:0000305|PubMed:11368156};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-Glc-(1<->1')-Cer(d18:1(4E)) + GDP-beta-L-fucose = alpha-L-
CC fucosyl-(1->2)- beta-D-galactosyl-(1->3)-N-acetyl-beta-D-
CC glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-
CC (1<->1')-N-acylsphing-4-enine + GDP + H(+); Xref=Rhea:RHEA:32175,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17292, ChEBI:CHEBI:28743,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189; EC=2.4.1.69;
CC Evidence={ECO:0000269|PubMed:14967068};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32176;
CC Evidence={ECO:0000305|PubMed:14967068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside nLc4Cer(d18:1(4E)) + GDP-beta-L-fucose = a
CC neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:1(4E)) + GDP + H(+);
CC Xref=Rhea:RHEA:48304, ChEBI:CHEBI:15378, ChEBI:CHEBI:17006,
CC ChEBI:CHEBI:28691, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000269|PubMed:14967068};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48305;
CC Evidence={ECO:0000305|PubMed:14967068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GM1 + GDP-beta-L-fucose = ganglioside Fuc-GM1 +
CC GDP + H(+); Xref=Rhea:RHEA:48292, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:82639,
CC ChEBI:CHEBI:90189; Evidence={ECO:0000250|UniProtKB:F6Q1T7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48293;
CC Evidence={ECO:0000250|UniProtKB:F6Q1T7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine + GDP-beta-
CC L-fucose = alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-
CC D-galactosamine + GDP + H(+); Xref=Rhea:RHEA:62964,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:84728, ChEBI:CHEBI:546807;
CC Evidence={ECO:0000250|UniProtKB:F6Q1T7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62965;
CC Evidence={ECO:0000250|UniProtKB:F6Q1T7};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=28.85 mM for phenyl-beta-D-Galactoside
CC {ECO:0000269|PubMed:11368156};
CC KM=29.09 mM for lactose {ECO:0000269|PubMed:11368156};
CC KM=0.24 mM for ganglioside GA1 {ECO:0000269|PubMed:11368156};
CC KM=22.5 uM for ganglioside GA1 {ECO:0000269|PubMed:14967068};
CC KM=10.8 uM for nLc4Cer {ECO:0000269|PubMed:14967068};
CC KM=6.2 uM for Lc4Cer {ECO:0000269|PubMed:14967068};
CC KM=4.3 uM for GM1 {ECO:0000269|PubMed:14967068};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P19526}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000305}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:11368156}. Note=Membrane-bound form in trans
CC cisternae of Golgi. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In the adult, highly expressed in pancreas, testis
CC and epididymis and to a lesser extent in thymus, lung, stomach, small
CC intestine, colon, spleen and uterus. Not expressed in brain, heart,
CC skeletal muscle, kidney, liver and bone marrow (PubMed:9355741).
CC Expressed in epididymis and testis (PubMed:11368156).
CC {ECO:0000269|PubMed:11368156, ECO:0000269|PubMed:9355741}.
CC -!- DISRUPTION PHENOTYPE: Homozygous mutant knockout mice for Fut1 develop
CC normally, exhibit no gross phenotypic abnormalities and the
CC Fucalpha(1-->2)Galbeta epitope is absent from the epithelia of the
CC epididymis mice. {ECO:0000269|PubMed:11713270}.
CC -!- MISCELLANEOUS: In mouse, there are three genes (Fut1, Fut2 and Sec1)
CC which encode galactoside 2-L-fucosyltransferase.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 11 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Fucosyltransferase 1;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_611";
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DR EMBL; U90553; AAC53492.1; -; Genomic_DNA.
DR EMBL; AF113533; AAD25352.1; -; mRNA.
DR EMBL; Y09883; CAA71009.1; -; Genomic_DNA.
DR EMBL; AK137638; BAE23444.1; -; mRNA.
DR EMBL; AB039104; BAB68628.1; -; Genomic_DNA.
DR EMBL; AB039112; BAB68636.1; -; Genomic_DNA.
DR EMBL; AB039111; BAB68635.1; -; Genomic_DNA.
DR EMBL; AB039109; BAB68633.1; -; Genomic_DNA.
DR EMBL; AB039105; BAB68629.1; -; Genomic_DNA.
DR EMBL; AC149057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS21254.1; -.
DR RefSeq; NP_001258910.1; NM_001271981.1.
DR RefSeq; NP_032077.2; NM_008051.6.
DR RefSeq; XP_006540679.1; XM_006540616.3.
DR AlphaFoldDB; O09160; -.
DR STRING; 10090.ENSMUSP00000008605; -.
DR SwissLipids; SLP:000001425; -.
DR CAZy; GT11; Glycosyltransferase Family 11.
DR GlyGen; O09160; 3 sites.
DR iPTMnet; O09160; -.
DR PhosphoSitePlus; O09160; -.
DR PaxDb; O09160; -.
DR PRIDE; O09160; -.
DR ProteomicsDB; 271650; -.
DR ProteomicsDB; 328835; -.
DR Antibodypedia; 31803; 137 antibodies from 24 providers.
DR DNASU; 14343; -.
DR Ensembl; ENSMUST00000008605; ENSMUSP00000008605; ENSMUSG00000008461.
DR GeneID; 14343; -.
DR KEGG; mmu:14343; -.
DR UCSC; uc009gwg.2; mouse.
DR CTD; 2523; -.
DR MGI; MGI:109375; Fut1.
DR VEuPathDB; HostDB:ENSMUSG00000008461; -.
DR eggNOG; ENOG502S316; Eukaryota.
DR GeneTree; ENSGT00390000001450; -.
DR HOGENOM; CLU_043399_0_1_1; -.
DR InParanoid; O09160; -.
DR OMA; MWPPSHR; -.
DR OrthoDB; 1006406at2759; -.
DR PhylomeDB; O09160; -.
DR TreeFam; TF315810; -.
DR BRENDA; 2.4.1.69; 3474.
DR Reactome; R-MMU-9033807; ABO blood group biosynthesis.
DR SABIO-RK; O09160; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 14343; 0 hits in 74 CRISPR screens.
DR PRO; PR:O09160; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O09160; protein.
DR Bgee; ENSMUSG00000008461; Expressed in lip and 29 other tissues.
DR ExpressionAtlas; O09160; baseline and differential.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031127; F:alpha-(1,2)-fucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008107; F:galactoside 2-alpha-L-fucosyltransferase activity; IDA:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0036065; P:fucosylation; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0021772; P:olfactory bulb development; IMP:UniProtKB.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISS:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:1904906; P:positive regulation of endothelial cell-matrix adhesion via fibronectin; ISS:UniProtKB.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IDA:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; IDA:UniProtKB.
DR GO; GO:0001936; P:regulation of endothelial cell proliferation; IMP:UniProtKB.
DR InterPro; IPR002516; Glyco_trans_11.
DR PANTHER; PTHR11927; PTHR11927; 1.
DR Pfam; PF01531; Glyco_transf_11; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..377
FT /note="Galactoside alpha-(1,2)-fucosyltransferase 1"
FT /id="PRO_0000149098"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..377
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 12
FT /note="A -> T (in Ref. 1; AAC53492)"
FT /evidence="ECO:0000305"
FT CONFLICT 210..213
FT /note="GIRP -> SPA (in Ref. 1; AAC53492)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 42394 MW; 9B17542B1F7A969A CRC64;
MWTPSRRQLC LAFLLVCVLS AGSFFFHLNG GNFFRNGLTL SVLCSDYHLL KSPVAMVCLP
HPLQTSNGSP SCPEQSSSLS GTWTITPGGR FGNQMGQYAT LLALAQLNGR QAFIQPEMHA
ALAPVFRISL PVLDPEVDSL TPWQHLVLHD WMSEEYSHLE DPFLKLSGFP CSWTFFHHLR
EQIRREFTLH NHLREGAQYL LSGLRIGPAG IRPHTFVGVH VRRGDYLEVM PNRWKGVVGD
RAYLQQAMDW FRARHKDPIF VVTSNGMKWC LENIDTSHGD VVFAGNGQEG TPGKDFALLT
QCNHTIMTIG TFGFWAAYLA GGDTVYLANF TLPDSEFLKI FRPEAAFLPE WVGINADLSP
LQAQFDPWKP DSLFRLV
