ID   SAG1_YEAST              Reviewed;         650 AA.
AC   P20840; D6VWH8;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   27-MAR-2024, entry version 182.
DE   RecName: Full=Alpha-agglutinin;
DE   AltName: Full=AG-alpha-1;
DE   Flags: Precursor;
GN   Name=SAG1; Synonyms=AGAL1; OrderedLocusNames=YJR004C; ORFNames=J1418;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=2676603; DOI=10.1016/0014-5793(89)81108-1;
RA   Hauser K., Tanner W.;
RT   "Purification of the inducible alpha-agglutinin of S. cerevisiae and
RT   molecular cloning of the gene.";
RL   FEBS Lett. 255:290-294(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2677666; DOI=10.1128/mcb.9.8.3155-3165.1989;
RA   Lipke P.N., Wojciechowicz D., Kurjan J.;
RT   "AG alpha 1 is the structural gene for the Saccharomyces cerevisiae alpha-
RT   agglutinin, a cell surface glycoprotein involved in cell-cell interactions
RT   during mating.";
RL   Mol. Cell. Biol. 9:3155-3165(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-248; SER-282; THR-289;
RP   THR-299; THR-303; ASN-306; THR-307; THR-308; THR-311; SER-314; THR-315;
RP   THR-316; THR-329; SER-331; SER-334; SER-335; SER-338; THR-339; THR-340;
RP   THR-341; THR-342; THR-345; SER-346; THR-349 AND SER-350, LACK OF
RP   GLYCOSYLATION AT ASN-348, AND DISULFIDE BONDS.
RX   PubMed=7592821; DOI=10.1074/jbc.270.44.26168;
RA   Chen M.-H., Shen Z.-M., Bobin S., Kahn P.C., Lipke P.N.;
RT   "Structure of Saccharomyces cerevisiae alpha-agglutinin. Evidence for a
RT   yeast cell wall protein with multiple immunoglobulin-like domains with
RT   atypical disulfides.";
RL   J. Biol. Chem. 270:26168-26177(1995).
RN   [6]
RP   GLYCOSYLATION, AND GPI-ANCHOR.
RX   PubMed=8455628; DOI=10.1128/mcb.13.4.2554-2563.1993;
RA   Wojciechowicz D., Lu C.F., Kurjan J., Lipke P.N.;
RT   "Cell surface anchorage and ligand-binding domains of the Saccharomyces
RT   cerevisiae cell adhesion protein alpha-agglutinin, a member of the
RT   immunoglobulin superfamily.";
RL   Mol. Cell. Biol. 13:2554-2563(1993).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=8007981; DOI=10.1128/mcb.14.7.4825-4833.1994;
RA   Lu C.-F., Kurjan J., Lipke P.N.;
RT   "A pathway for cell wall anchorage of Saccharomyces cerevisiae alpha-
RT   agglutinin.";
RL   Mol. Cell. Biol. 14:4825-4833(1994).
RN   [8]
RP   GPI-ANCHOR, AND CROSS-LINKING TO CELL WALL.
RX   PubMed=7844147; DOI=10.1083/jcb.128.3.333;
RA   Lu C.-F., Montijn R.C., Brown J.L., Klis F., Kurjan J., Bussey H.,
RA   Lipke P.N.;
RT   "Glycosyl phosphatidylinositol-dependent cross-linking of alpha-agglutinin
RT   and beta 1,6-glucan in the Saccharomyces cerevisiae cell wall.";
RL   J. Cell Biol. 128:333-340(1995).
RN   [9]
RP   FUNCTION, AND MUTAGENESIS OF ILE-214; ASP-215; TYR-216; ASP-217; THR-289;
RP   ILE-290; ASP-291; HIS-292; LEU-294; GLU-295; PHE-296; TYR-298; TYR-322;
RP   GLN-323; GLY-324 AND ARG-325.
RX   PubMed=8741846; DOI=10.1091/mbc.7.1.143;
RA   de Nobel H., Lipke P.N., Kurjan J.;
RT   "Identification of a ligand-binding site in an immunoglobulin fold domain
RT   of the Saccharomyces cerevisiae adhesion protein alpha-agglutinin.";
RL   Mol. Biol. Cell 7:143-153(1996).
RN   [10]
RP   SUBCELLULAR LOCATION.
RX   PubMed=9613572; DOI=10.1007/s004380050706;
RA   Hamada K., Fukuchi S., Arisawa M., Baba M., Kitada K.;
RT   "Screening for glycosylphosphatidylinositol (GPI)-dependent cell wall
RT   proteins in Saccharomyces cerevisiae.";
RL   Mol. Gen. Genet. 258:53-59(1998).
RN   [11]
RP   INTERACTION WITH AGA2.
RX   PubMed=11292808; DOI=10.1128/jb.183.9.2874-2880.2001;
RA   Zhao H., Shen Z.M., Kahn P.C., Lipke P.N.;
RT   "Interaction of alpha-agglutinin and a-agglutinin, Saccharomyces cerevisiae
RT   sexual cell adhesion molecules.";
RL   J. Bacteriol. 183:2874-2880(2001).
CC   -!- FUNCTION: Cell surface glycoprotein promoting cell-cell contact to
CC       facilitate mating. S.cerevisiae A and alpha cells express the
CC       complementary cell surface glycoproteins A-agglutinin and alpha-,
CC       respectively, which interact with one another to promote cellular
CC       aggregation during mating. {ECO:0000269|PubMed:8741846}.
CC   -!- SUBUNIT: Interacts with AGA2. {ECO:0000269|PubMed:11292808}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Lipid-anchor, GPI-
CC       anchor. Note=Covalently-linked GPI-modified cell wall protein (GPI-
CC       CWP).
CC   -!- INDUCTION: By exposition to pheromone (A-factor) secreted by the
CC       opposite mating type cells (type A).
CC   -!- PTM: N-glycosylated, and O-glycosylated by both PMT1 and PMT2.
CC       {ECO:0000269|PubMed:7592821, ECO:0000269|PubMed:8455628}.
CC   -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC       reticulum and serves to target the protein to the cell surface. There,
CC       the glucosamine-inositol phospholipid moiety is cleaved off and the
CC       GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC       glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
CC   -!- SIMILARITY: To C.albicans ALS1. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=Alpha-agglutinin;
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_oth_other_801";
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DR   EMBL; X16861; CAA34752.1; -; Genomic_DNA.
DR   EMBL; M28164; AAA34417.1; -; Genomic_DNA.
DR   EMBL; X87611; CAA60926.1; -; Genomic_DNA.
DR   EMBL; Z49504; CAA89526.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08794.1; -; Genomic_DNA.
DR   PIR; S22835; S22835.
DR   RefSeq; NP_012537.1; NM_001181661.1.
DR   AlphaFoldDB; P20840; -.
DR   SMR; P20840; -.
DR   BioGRID; 33760; 38.
DR   DIP; DIP-5692N; -.
DR   MINT; P20840; -.
DR   STRING; 4932.YJR004C; -.
DR   GlyCosmos; P20840; 33 sites, No reported glycans.
DR   GlyGen; P20840; 33 sites.
DR   iPTMnet; P20840; -.
DR   PaxDb; 4932-YJR004C; -.
DR   PeptideAtlas; P20840; -.
DR   EnsemblFungi; YJR004C_mRNA; YJR004C; YJR004C.
DR   GeneID; 853460; -.
DR   KEGG; sce:YJR004C; -.
DR   AGR; SGD:S000003764; -.
DR   SGD; S000003764; SAG1.
DR   VEuPathDB; FungiDB:YJR004C; -.
DR   eggNOG; ENOG502RGCG; Eukaryota.
DR   HOGENOM; CLU_019475_0_0_1; -.
DR   InParanoid; P20840; -.
DR   OMA; IIIHVET; -.
DR   OrthoDB; 2032179at2759; -.
DR   BioCyc; YEAST:G3O-31650-MONOMER; -.
DR   BioGRID-ORCS; 853460; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P20840; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P20840; Protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050839; F:cell adhesion molecule binding; IMP:SGD.
DR   GO; GO:0000752; P:agglutination involved in conjugation with cellular fusion; IMP:SGD.
DR   Gene3D; 2.60.40.1280; -; 1.
DR   Gene3D; 2.60.40.2430; Agglutinin-like protein, N-terminal domain, N2 subdomain; 1.
DR   InterPro; IPR008966; Adhesion_dom_sf.
DR   InterPro; IPR024672; Agglutinin-like_N.
DR   InterPro; IPR043063; Agglutinin-like_N_N2.
DR   InterPro; IPR033504; ALS.
DR   InterPro; IPR011252; Fibrogen-bd_dom1.
DR   PANTHER; PTHR33793:SF2; AGGLUTININ-LIKE PROTEIN 6; 1.
DR   PANTHER; PTHR33793; ALPHA-AGGLUTININ; 1.
DR   Pfam; PF11766; Candida_ALS_N; 1.
DR   SMART; SM01056; Candida_ALS_N; 1.
DR   SUPFAM; SSF49401; Bacterial adhesins; 1.
PE   1: Evidence at protein level;
KW   Cell adhesion; Cell wall; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Reference proteome;
KW   Repeat; Secreted; Signal.
FT   SIGNAL          1..19
FT   CHAIN           20..627
FT                   /note="Alpha-agglutinin"
FT                   /id="PRO_0000022265"
FT   PROPEP          628..650
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000022266"
FT   REPEAT          339..378
FT                   /note="1"
FT   REPEAT          384..423
FT                   /note="2"
FT   REGION          216..322
FT                   /note="Ig-like fold domain important for alpha-agglutinin
FT                   activity, contributing to a functional binding site for a-
FT                   agglutinin"
FT   REGION          339..423
FT                   /note="2 X 40 AA tandem repeats"
FT   SITE            348
FT                   /note="Not glycosylated"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   LIPID           627
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        282
FT                   /note="O-linked (Man...) serine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        289
FT                   /note="O-linked (Man...) threonine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        299
FT                   /note="O-linked (Man...) threonine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        303
FT                   /note="O-linked (Man...) threonine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        306
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        307
FT                   /note="O-linked (Man...) threonine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        308
FT                   /note="O-linked (Man...) threonine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        311
FT                   /note="O-linked (Man...) threonine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        314
FT                   /note="O-linked (Man...) serine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        315
FT                   /note="O-linked (Man...) threonine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        316
FT                   /note="O-linked (Man...) threonine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        329
FT                   /note="O-linked (Man...) threonine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        331
FT                   /note="O-linked (Man...) serine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        334
FT                   /note="O-linked (Man...) serine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        335
FT                   /note="O-linked (Man...) serine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        338
FT                   /note="O-linked (Man...) serine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        339
FT                   /note="O-linked (Man...) threonine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        340
FT                   /note="O-linked (Man...) threonine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        341
FT                   /note="O-linked (Man...) threonine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        342
FT                   /note="O-linked (Man...) threonine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        345
FT                   /note="O-linked (Man...) threonine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        346
FT                   /note="O-linked (Man...) serine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        349
FT                   /note="O-linked (Man...) threonine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        350
FT                   /note="O-linked (Man...) serine"
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   CARBOHYD        364
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        402
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        485
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        501
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        614
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        97..114
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   DISULFID        202..300
FT                   /evidence="ECO:0000269|PubMed:7592821"
FT   MUTAGEN         211
FT                   /note="T->I: Little effect on secreted alpha-agglutinin
FT                   activity."
FT   MUTAGEN         214
FT                   /note="I->M: No effect on secreted alpha-agglutinin
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:8741846"
FT   MUTAGEN         215
FT                   /note="D->A,N: Little or no effect on secreted
FT                   alpha-agglutinin activity."
FT                   /evidence="ECO:0000269|PubMed:8741846"
FT   MUTAGEN         216
FT                   /note="Y->D: Complete loss of alpha-agglutinin activity."
FT                   /evidence="ECO:0000269|PubMed:8741846"
FT   MUTAGEN         216
FT                   /note="Y->F: No effect on secreted alpha-agglutinin
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:8741846"
FT   MUTAGEN         216
FT                   /note="Y->S: Decreases secreted alpha-agglutinin activity
FT                   by 100-fold."
FT                   /evidence="ECO:0000269|PubMed:8741846"
FT   MUTAGEN         216
FT                   /note="Y->V: Decreases secreted alpha-agglutinin activity
FT                   by 10-fold."
FT                   /evidence="ECO:0000269|PubMed:8741846"
FT   MUTAGEN         217
FT                   /note="D->A: Little effect on secreted alpha-agglutinin
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:8741846"
FT   MUTAGEN         217
FT                   /note="D->N: Decreases secreted alpha-agglutinin activity
FT                   by 10-fold."
FT                   /evidence="ECO:0000269|PubMed:8741846"
FT   MUTAGEN         289
FT                   /note="T->A: Decreases secreted alpha-agglutinin activity
FT                   by less than 2-fold."
FT                   /evidence="ECO:0000269|PubMed:8741846"
FT   MUTAGEN         290
FT                   /note="I->M: Decreases secreted alpha-agglutinin activity
FT                   by less than 2-fold."
FT                   /evidence="ECO:0000269|PubMed:8741846"
FT   MUTAGEN         291
FT                   /note="D->A,N: Decreases secreted alpha-agglutinin activity
FT                   by 4-fold."
FT                   /evidence="ECO:0000269|PubMed:8741846"
FT   MUTAGEN         292
FT                   /note="H->L,R: Almost complete loss of secreted
FT                   alpha-agglutinin activity."
FT                   /evidence="ECO:0000269|PubMed:8741846"
FT   MUTAGEN         294
FT                   /note="L->S: Decreases secreted alpha-agglutinin activity
FT                   by more than 20-fold."
FT                   /evidence="ECO:0000269|PubMed:8741846"
FT   MUTAGEN         295
FT                   /note="E->A,Q: Decreases secreted alpha-agglutinin activity
FT                   by 2-fold."
FT                   /evidence="ECO:0000269|PubMed:8741846"
FT   MUTAGEN         296
FT                   /note="F->Y: Decreases secreted alpha-agglutinin activity
FT                   by more than 20-fold."
FT                   /evidence="ECO:0000269|PubMed:8741846"
FT   MUTAGEN         298
FT                   /note="Y->H: Decreases secreted alpha-agglutinin activity
FT                   by less than 2-fold."
FT                   /evidence="ECO:0000269|PubMed:8741846"
FT   MUTAGEN         322
FT                   /note="Y->A: Decreases secreted alpha-agglutinin activity
FT                   by 60-fold."
FT                   /evidence="ECO:0000269|PubMed:8741846"
FT   MUTAGEN         322
FT                   /note="Y->C: Almost complete loss of secreted
FT                   alpha-agglutinin activity by 10-fold."
FT                   /evidence="ECO:0000269|PubMed:8741846"
FT   MUTAGEN         322
FT                   /note="Y->F: Decreases secreted alpha-agglutinin activity
FT                   by 15-fold."
FT                   /evidence="ECO:0000269|PubMed:8741846"
FT   MUTAGEN         323
FT                   /note="Q->L: Decreases secreted alpha-agglutinin activity
FT                   by 2-fold."
FT                   /evidence="ECO:0000269|PubMed:8741846"
FT   MUTAGEN         324
FT                   /note="G->A: Little effect on secreted alpha-agglutinin
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:8741846"
FT   MUTAGEN         325
FT                   /note="R->G: Little effect on secreted alpha-agglutinin
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:8741846"
FT   CONFLICT        449
FT                   /note="S -> P (in Ref. 1; AAA34417)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        556
FT                   /note="K -> E (in Ref. 1; AAA34417)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        581
FT                   /note="V -> L (in Ref. 1; AAA34417)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   650 AA;  70340 MW;  8BBF7A1C44C93C2B CRC64;
     MFTFLKIILW LFSLALASAI NINDITFSNL EITPLTANKQ PDQGWTATFD FSIADASSIR
     EGDEFTLSMP HVYRIKLLNS SQTATISLAD GTEAFKCYVS QQAAYLYENT TFTCTAQNDL
     SSYNTIDGSI TFSLNFSDGG SSYEYELENA KFFKSGPMLV KLGNQMSDVV NFDPAAFTEN
     VFHSGRSTGY GSFESYHLGM YCPNGYFLGG TEKIDYDSSN NNVDLDCSSV QVYSSNDFND
     WWFPQSYNDT NADVTCFGSN LWITLDEKLY DGEMLWVNAL QSLPANVNTI DHALEFQYTC
     LDTIANTTYA TQFSTTREFI VYQGRNLGTA SAKSSFISTT TTDLTSINTS AYSTGSISTV
     ETGNRTTSEV ISHVVTTSTK LSPTATTSLT IAQTSIYSTD SNITVGTDIH TTSEVISDVE
     TISRETASTV VAAPTSTTGW TGAMNTYISQ FTSSSFATIN STPIISSSAV FETSDASIVN
     VHTENITNTA AVPSEEPTFV NATRNSLNSF CSSKQPSSPS SYTSSPLVSS LSVSKTLLST
     SFTPSVPTSN TYIKTKNTGY FEHTALTTSS VGLNSFSETA VSSQGTKIDT FLVSSLIAYP
     SSASGSQLSG IQQNFTSTSL MISTYEGKAS IFFSAELGSI IFLLLSYLLF
//