ID   FUCO2_HUMAN             Reviewed;         467 AA.
AC   Q9BTY2; E9PEB6; Q7Z6V1; Q7Z6Y2; Q8NBK4;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   27-MAR-2024, entry version 169.
DE   RecName: Full=Plasma alpha-L-fucosidase;
DE            EC=3.2.1.51;
DE   AltName: Full=Alpha-L-fucoside fucohydrolase 2;
DE            Short=Alpha-L-fucosidase 2;
DE   Flags: Precursor;
GN   Name=FUCA2; ORFNames=PSEC0151, UNQ227/PRO260;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS VAL-356
RP   AND TYR-371.
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Thalamus;
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 1), AND VARIANTS VAL-356
RP   AND TYR-371.
RC   TISSUE=Placenta;
RX   PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA   Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA   Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA   Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA   Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA   Isogai T.;
RT   "Signal sequence and keyword trap in silico for selection of full-length
RT   human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT   libraries.";
RL   DNA Res. 12:117-126(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS VAL-356
RP   AND TYR-371.
RC   TISSUE=B-cell, and 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   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-239.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [7]
RP   PHOSPHORYLATION AT SER-301.
RX   PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA   Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA   Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA   Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT   "A single kinase generates the majority of the secreted phosphoproteome.";
RL   Cell 161:1619-1632(2015).
CC   -!- FUNCTION: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-
CC       1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the
CC       carbohydrate moieties of glycoproteins.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alpha-L-fucoside + H2O = an alcohol + L-fucose;
CC         Xref=Rhea:RHEA:12288, ChEBI:CHEBI:2181, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28349, ChEBI:CHEBI:30879; EC=3.2.1.51;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10054};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9BTY2; Q96NT3-2: GUCD1; NbExp=3; IntAct=EBI-9050116, EBI-11978177;
CC       Q9BTY2; P49639: HOXA1; NbExp=3; IntAct=EBI-9050116, EBI-740785;
CC       Q9BTY2; Q9BQ66: KRTAP4-12; NbExp=3; IntAct=EBI-9050116, EBI-739863;
CC       Q9BTY2; Q701N4: KRTAP5-2; NbExp=3; IntAct=EBI-9050116, EBI-11958178;
CC       Q9BTY2; Q6L8H2: KRTAP5-3; NbExp=3; IntAct=EBI-9050116, EBI-11974251;
CC       Q9BTY2; Q5T7P2: LCE1A; NbExp=3; IntAct=EBI-9050116, EBI-11962058;
CC       Q9BTY2; Q5T7P3: LCE1B; NbExp=3; IntAct=EBI-9050116, EBI-10245913;
CC       Q9BTY2; Q5T753: LCE1E; NbExp=3; IntAct=EBI-9050116, EBI-11955335;
CC       Q9BTY2; Q5TA78: LCE4A; NbExp=3; IntAct=EBI-9050116, EBI-10246358;
CC       Q9BTY2; P50222: MEOX2; NbExp=4; IntAct=EBI-9050116, EBI-748397;
CC       Q9BTY2; Q7Z417: NUFIP2; NbExp=3; IntAct=EBI-9050116, EBI-1210753;
CC       Q9BTY2; Q13526: PIN1; NbExp=3; IntAct=EBI-9050116, EBI-714158;
CC       Q9BTY2; O14787-2: TNPO2; NbExp=3; IntAct=EBI-9050116, EBI-12076664;
CC       Q9BTY2; Q2TAL6: VWC2; NbExp=3; IntAct=EBI-9050116, EBI-11957238;
CC       Q9BTY2; O96014: WNT11; NbExp=3; IntAct=EBI-9050116, EBI-8058160;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9BTY2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9BTY2-2; Sequence=VSP_057004, VSP_057005;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family. {ECO:0000305}.
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DR   EMBL; AY358551; AAQ88915.1; -; mRNA.
DR   EMBL; AK296485; BAG59123.1; -; mRNA.
DR   EMBL; AK075458; BAC11633.1; -; mRNA.
DR   EMBL; AL031320; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC003060; AAH03060.1; -; mRNA.
DR   EMBL; BC051268; AAH51268.1; -; mRNA.
DR   CCDS; CCDS5200.1; -. [Q9BTY2-1]
DR   RefSeq; NP_114409.2; NM_032020.4. [Q9BTY2-1]
DR   AlphaFoldDB; Q9BTY2; -.
DR   SMR; Q9BTY2; -.
DR   BioGRID; 108795; 57.
DR   IntAct; Q9BTY2; 34.
DR   MINT; Q9BTY2; -.
DR   STRING; 9606.ENSP00000002165; -.
DR   BindingDB; Q9BTY2; -.
DR   ChEMBL; CHEMBL2271; -.
DR   CAZy; GH29; Glycoside Hydrolase Family 29.
DR   GlyConnect; 1608; 3 N-Linked glycans (1 site).
DR   GlyCosmos; Q9BTY2; 3 sites, 2 glycans.
DR   GlyGen; Q9BTY2; 4 sites, 2 N-linked glycans (1 site).
DR   iPTMnet; Q9BTY2; -.
DR   PhosphoSitePlus; Q9BTY2; -.
DR   BioMuta; FUCA2; -.
DR   DMDM; 254763296; -.
DR   EPD; Q9BTY2; -.
DR   jPOST; Q9BTY2; -.
DR   MassIVE; Q9BTY2; -.
DR   MaxQB; Q9BTY2; -.
DR   PaxDb; 9606-ENSP00000002165; -.
DR   PeptideAtlas; Q9BTY2; -.
DR   ProteomicsDB; 69462; -.
DR   ProteomicsDB; 79030; -. [Q9BTY2-1]
DR   Pumba; Q9BTY2; -.
DR   Antibodypedia; 33149; 383 antibodies from 28 providers.
DR   DNASU; 2519; -.
DR   Ensembl; ENST00000002165.11; ENSP00000002165.5; ENSG00000001036.14. [Q9BTY2-1]
DR   GeneID; 2519; -.
DR   KEGG; hsa:2519; -.
DR   MANE-Select; ENST00000002165.11; ENSP00000002165.5; NM_032020.5; NP_114409.2.
DR   UCSC; uc003qjm.4; human. [Q9BTY2-1]
DR   AGR; HGNC:4008; -.
DR   CTD; 2519; -.
DR   DisGeNET; 2519; -.
DR   GeneCards; FUCA2; -.
DR   HGNC; HGNC:4008; FUCA2.
DR   HPA; ENSG00000001036; Tissue enhanced (parathyroid).
DR   MIM; 136820; gene+phenotype.
DR   neXtProt; NX_Q9BTY2; -.
DR   OpenTargets; ENSG00000001036; -.
DR   PharmGKB; PA28424; -.
DR   VEuPathDB; HostDB:ENSG00000001036; -.
DR   eggNOG; KOG3340; Eukaryota.
DR   GeneTree; ENSGT00440000035378; -.
DR   HOGENOM; CLU_002934_1_1_1; -.
DR   InParanoid; Q9BTY2; -.
DR   OMA; WESTDKH; -.
DR   OrthoDB; 2955544at2759; -.
DR   PhylomeDB; Q9BTY2; -.
DR   TreeFam; TF313034; -.
DR   BRENDA; 3.2.1.51; 2681.
DR   PathwayCommons; Q9BTY2; -.
DR   Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR   SABIO-RK; Q9BTY2; -.
DR   SignaLink; Q9BTY2; -.
DR   BioGRID-ORCS; 2519; 9 hits in 1159 CRISPR screens.
DR   ChiTaRS; FUCA2; human.
DR   GeneWiki; FUCA2; -.
DR   GenomeRNAi; 2519; -.
DR   Pharos; Q9BTY2; Tchem.
DR   PRO; PR:Q9BTY2; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9BTY2; Protein.
DR   Bgee; ENSG00000001036; Expressed in decidua and 167 other cell types or tissues.
DR   ExpressionAtlas; Q9BTY2; baseline and differential.
DR   GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0004560; F:alpha-L-fucosidase activity; IDA:UniProtKB.
DR   GO; GO:0006004; P:fucose metabolic process; IDA:UniProtKB.
DR   GO; GO:0016139; P:glycoside catabolic process; IDA:UniProtKB.
DR   GO; GO:2000535; P:regulation of entry of bacterium into host cell; IMP:UniProtKB.
DR   GO; GO:0009617; P:response to bacterium; IMP:UniProtKB.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR016286; FUC_metazoa-typ.
DR   InterPro; IPR031919; Fucosidase_C.
DR   InterPro; IPR000933; Glyco_hydro_29.
DR   InterPro; IPR018526; Glyco_hydro_29_CS.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10030; ALPHA-L-FUCOSIDASE; 1.
DR   PANTHER; PTHR10030:SF45; PLASMA ALPHA-L-FUCOSIDASE; 1.
DR   Pfam; PF01120; Alpha_L_fucos; 1.
DR   Pfam; PF16757; Fucosidase_C; 1.
DR   PIRSF; PIRSF001092; Alpha-L-fucosidase; 1.
DR   PRINTS; PR00741; GLHYDRLASE29.
DR   SMART; SM00812; Alpha_L_fucos; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00385; ALPHA_L_FUCOSIDASE; 1.
DR   Genevisible; Q9BTY2; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Glycoprotein; Glycosidase; Hydrolase; Phosphoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..467
FT                   /note="Plasma alpha-L-fucosidase"
FT                   /id="PRO_0000010312"
FT   SITE            294
FT                   /note="May be important for catalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10054"
FT   MOD_RES         301
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218"
FT   CARBOHYD        377
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         138..165
FT                   /note="GFTLWGSEYSWNWNAIDEGPKRDIVKEL -> ATCRDSFMWRKSFDEYWAHT
FT                   RWHHFCSF (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_057004"
FT   VAR_SEQ         166..467
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_057005"
FT   VARIANT         233
FT                   /note="A -> E (in dbSNP:rs11155297)"
FT                   /id="VAR_055822"
FT   VARIANT         356
FT                   /note="M -> V (in dbSNP:rs3762002)"
FT                   /evidence="ECO:0000269|PubMed:12975309,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16303743"
FT                   /id="VAR_022444"
FT   VARIANT         371
FT                   /note="H -> Y (in dbSNP:rs3762001)"
FT                   /evidence="ECO:0000269|PubMed:12975309,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16303743"
FT                   /id="VAR_022445"
FT   CONFLICT        400
FT                   /note="L -> P (in Ref. 3; BAC11633)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   467 AA;  54067 MW;  A42AA6B369A3AC39 CRC64;
     MRPQELPRLA FPLLLLLLLL LPPPPCPAHS ATRFDPTWES LDARQLPAWF DQAKFGIFIH
     WGVFSVPSFG SEWFWWYWQK EKIPKYVEFM KDNYPPSFKY EDFGPLFTAK FFNANQWADI
     FQASGAKYIV LTSKHHEGFT LWGSEYSWNW NAIDEGPKRD IVKELEVAIR NRTDLRFGLY
     YSLFEWFHPL FLEDESSSFH KRQFPVSKTL PELYELVNNY QPEVLWSDGD GGAPDQYWNS
     TGFLAWLYNE SPVRGTVVTN DRWGAGSICK HGGFYTCSDR YNPGHLLPHK WENCMTIDKL
     SWGYRREAGI SDYLTIEELV KQLVETVSCG GNLLMNIGPT LDGTISVVFE ERLRQMGSWL
     KVNGEAIYET HTWRSQNDTV TPDVWYTSKP KEKLVYAIFL KWPTSGQLFL GHPKAILGAT
     EVKLLGHGQP LNWISLEQNG IMVELPQLTI HQMPCKWGWA LALTNVI
//