ALS5_CANAL
ID ALS5_CANAL Reviewed; 1347 AA.
AC Q5A8T7; A0A1D8PQ81; Q5A8L3; Q874K9; Q874L0;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Agglutinin-like protein 5;
DE AltName: Full=Adhesin 5;
DE Flags: Precursor;
GN Name=ALS5; Synonyms=ALA1, ALS99; OrderedLocusNames=CAALFM_C603690WA;
GN ORFNames=CaO19.13158, CaO19.5736;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=14523127; DOI=10.1099/mic.0.26495-0;
RA Zhao X., Pujol C., Soll D.R., Hoyer L.L.;
RT "Allelic variation in the contiguous loci encoding Candida albicans ALS5,
RT ALS1 and ALS9.";
RL Microbiology 149:2947-2960(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [5]
RP FUNCTION.
RX PubMed=9393828; DOI=10.1128/iai.65.12.5289-5294.1997;
RA Gaur N.K., Klotz S.A.;
RT "Expression, cloning, and characterization of a Candida albicans gene,
RT ALA1, that confers adherence properties upon Saccharomyces cerevisiae for
RT extracellular matrix proteins.";
RL Infect. Immun. 65:5289-5294(1997).
RN [6]
RP FUNCTION.
RX PubMed=10531265; DOI=10.1128/iai.67.11.6040-6047.1999;
RA Gaur N.K., Klotz S.A., Henderson R.L.;
RT "Overexpression of the Candida albicans ALA1 gene in Saccharomyces
RT cerevisiae results in aggregation following attachment of yeast cells to
RT extracellular matrix proteins, adherence properties similar to those of
RT Candida albicans.";
RL Infect. Immun. 67:6040-6047(1999).
RN [7]
RP FUNCTION.
RX PubMed=12200964; DOI=10.1080/15419060212187;
RA Gaur N.K., Smith R.L., Klotz S.A.;
RT "Candida albicans and Saccharomyces cerevisiae expressing ALA1/ALS5 adhere
RT to accessible threonine, serine, or alanine patches.";
RL Cell Commun. Adhes. 9:45-57(2002).
RN [8]
RP PREDICTION OF GPI-ANCHOR.
RX PubMed=12845604; DOI=10.1002/yea.1007;
RA De Groot P.W., Hellingwerf K.J., Klis F.M.;
RT "Genome-wide identification of fungal GPI proteins.";
RL Yeast 20:781-796(2003).
RN [9]
RP FUNCTION.
RX PubMed=15039323; DOI=10.1128/iai.72.4.2029-2034.2004;
RA Klotz S.A., Gaur N.K., Lake D.F., Chan V., Rauceo J., Lipke P.N.;
RT "Degenerate peptide recognition by Candida albicans adhesins Als5p and
RT Als1p.";
RL Infect. Immun. 72:2029-2034(2004).
RN [10]
RP FUNCTION.
RX PubMed=15321986; DOI=10.1128/iai.72.9.4948-4955.2004;
RA Rauceo J.M., Gaur N.K., Lee K.G., Edwards J.E., Klotz S.A., Lipke P.N.;
RT "Global cell surface conformational shift mediated by a Candida albicans
RT adhesin.";
RL Infect. Immun. 72:4948-4955(2004).
RN [11]
RP FUNCTION, AND DOMAIN.
RX PubMed=15128742; DOI=10.1074/jbc.m401929200;
RA Sheppard D.C., Yeaman M.R., Welch W.H., Phan Q.T., Fu Y., Ibrahim A.S.,
RA Filler S.G., Zhang M., Waring A.J., Edwards J.E. Jr.;
RT "Functional and structural diversity in the Als protein family of Candida
RT albicans.";
RL J. Biol. Chem. 279:30480-30489(2004).
RN [12]
RP INDUCTION.
RX PubMed=15731087; DOI=10.1128/iai.73.3.1852-1855.2005;
RA Green C.B., Zhao X., Hoyer L.L.;
RT "Use of green fluorescent protein and reverse transcription-PCR to monitor
RT Candida albicans agglutinin-like sequence gene expression in a murine model
RT of disseminated candidiasis.";
RL Infect. Immun. 73:1852-1855(2005).
RN [13]
RP FUNCTION.
RX PubMed=17510860; DOI=10.1080/13693780701299333;
RA Klotz S.A., Gaur N.K., De Armond R., Sheppard D., Khardori N.,
RA Edwards J.E. Jr., Lipke P.N., El-Azizi M.;
RT "Candida albicans Als proteins mediate aggregation with bacteria and
RT yeasts.";
RL Med. Mycol. 45:363-370(2007).
RN [14]
RP SUBUNIT.
RX PubMed=18083824; DOI=10.1128/ec.00309-07;
RA Otoo H.N., Lee K.G., Qiu W., Lipke P.N.;
RT "Candida albicans Als adhesins have conserved amyloid-forming sequences.";
RL Eukaryot. Cell 7:776-782(2008).
RN [15]
RP INDUCTION.
RX PubMed=20398368; DOI=10.1186/1471-2180-10-114;
RA Nailis H., Kucharikova S., Ricicova M., Van Dijck P., Deforce D., Nelis H.,
RA Coenye T.;
RT "Real-time PCR expression profiling of genes encoding potential virulence
RT factors in Candida albicans biofilms: identification of model-dependent and
RT -independent gene expression.";
RL BMC Microbiol. 10:114-114(2010).
RN [16]
RP DOMAIN, AND SUBUNIT.
RX PubMed=19820118; DOI=10.1128/ec.00235-09;
RA Frank A.T., Ramsook C.B., Otoo H.N., Tan C., Soybelman G., Rauceo J.M.,
RA Gaur N.K., Klotz S.A., Lipke P.N.;
RT "Structure and function of glycosylated tandem repeats from Candida
RT albicans Als adhesins.";
RL Eukaryot. Cell 9:405-414(2010).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=21059927; DOI=10.1073/pnas.1013893107;
RA Alsteens D., Garcia M.C., Lipke P.N., Dufrene Y.F.;
RT "Force-induced formation and propagation of adhesion nanodomains in living
RT fungal cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:20744-20749(2010).
RN [18]
RP FUNCTION, AND MUTAGENESIS OF VAL-326.
RX PubMed=21408122; DOI=10.1371/journal.pone.0017632;
RA Garcia M.C., Lee J.T., Ramsook C.B., Alsteens D., Dufrene Y.F., Lipke P.N.;
RT "A role for amyloid in cell aggregation and biofilm formation.";
RL PLoS ONE 6:E17632-E17632(2011).
RN [19]
RP FUNCTION.
RX PubMed=22321066; DOI=10.1111/j.1574-695x.2012.00941.x;
RA Aoki W., Kitahara N., Miura N., Morisaka H., Kuroda K., Ueda M.;
RT "Profiling of adhesive properties of the agglutinin-like sequence (ALS)
RT protein family, a virulent attribute of Candida albicans.";
RL FEMS Immunol. Med. Microbiol. 65:121-124(2012).
RN [20]
RP FUNCTION.
RX PubMed=22429754; DOI=10.1111/j.1439-0507.2012.02188.x;
RA Monroy-Perez E., Sainz-Espunes T., Paniagua-Contreras G.,
RA Negrete-Abascal E., Rodriguez-Moctezuma J.R., Vaca S.;
RT "Frequency and expression of ALS and HWP1 genotypes in Candida albicans
RT strains isolated from Mexican patients suffering from vaginal candidosis.";
RL Mycoses 55:E151-E157(2012).
CC -!- FUNCTION: Cell surface adhesion protein which mediates both yeast-to-
CC host tissue adherence and yeast aggregation. Plays an important role in
CC the pathogenesis of C.albicans infections. Forms amyloid structures,
CC essential for cell-cell association and cell-substrate adhesion to
CC polystyrene. {ECO:0000269|PubMed:10531265, ECO:0000269|PubMed:12200964,
CC ECO:0000269|PubMed:15039323, ECO:0000269|PubMed:15128742,
CC ECO:0000269|PubMed:15321986, ECO:0000269|PubMed:17510860,
CC ECO:0000269|PubMed:21408122, ECO:0000269|PubMed:22321066,
CC ECO:0000269|PubMed:22429754, ECO:0000269|PubMed:9393828}.
CC -!- SUBUNIT: Forms homodimers through the tandem repeats. Aggregates in
CC amyloid-like structures, with self-propagating secondary-structure
CC changes, amyloid-characteristic dye binding, and induced birefringence.
CC {ECO:0000269|PubMed:18083824, ECO:0000269|PubMed:19820118}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor
CC {ECO:0000305|PubMed:12845604}. Secreted, cell wall
CC {ECO:0000269|PubMed:21059927}. Note=Identified as covalently-linked
CC GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer.
CC {ECO:0000305|PubMed:12845604}.
CC -!- INDUCTION: Highly expressed in biofilms and during candidiasis
CC infection dissemination. {ECO:0000269|PubMed:15731087,
CC ECO:0000269|PubMed:20398368}.
CC -!- DOMAIN: Each ALS protein has a similar three-domain structure,
CC including a N-ter domain of 433-436 amino acids that is 55-90 percent
CC identical across the family and which mediates adherence to various
CC materials; a central domain of variable numbers of tandemly repeated
CC copies of a 36 amino acid motif; and a C-ter domain that is relatively
CC variable in length and sequence across the family.
CC {ECO:0000269|PubMed:15128742, ECO:0000269|PubMed:19820118}.
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 {ECO:0000305|PubMed:12845604}.
CC -!- SIMILARITY: Belongs to the ALS family. {ECO:0000305}.
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DR EMBL; AY227439; AAO72528.1; -; Genomic_DNA.
DR EMBL; AY227440; AAO72529.1; -; Genomic_DNA.
DR EMBL; CP017628; AOW30296.1; -; Genomic_DNA.
DR RefSeq; XP_718074.2; XM_712981.2.
DR AlphaFoldDB; Q5A8T7; -.
DR SMR; Q5A8T7; -.
DR BioGRID; 1223371; 10.
DR GeneID; 3640277; -.
DR KEGG; cal:CAALFM_C603690WA; -.
DR CGD; CAL0000191115; ALS5.
DR VEuPathDB; FungiDB:C6_03690W_A; -.
DR HOGENOM; CLU_257941_0_0_1; -.
DR InParanoid; Q5A8T7; -.
DR OrthoDB; 1428896at2759; -.
DR PRO; PR:Q5A8T7; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0043710; P:cell adhesion involved in multi-species biofilm formation; IBA:GO_Central.
DR GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR Gene3D; 2.60.40.1280; -; 1.
DR Gene3D; 2.60.40.2430; -; 1.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR InterPro; IPR008440; Agglutinin-like_ALS_rpt.
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; PTHR33793; 3.
DR Pfam; PF05792; Candida_ALS; 6.
DR Pfam; PF11766; Candida_ALS_N; 1.
DR SMART; SM01056; Candida_ALS_N; 1.
DR SUPFAM; SSF49401; SSF49401; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Cell wall; Disulfide bond; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Reference proteome; Repeat; Secreted;
KW Signal; Virulence.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1326
FT /note="Agglutinin-like protein 5"
FT /id="PRO_0000420222"
FT PROPEP 1327..1347
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420223"
FT REPEAT 365..396
FT /note="ALS 1"
FT REPEAT 401..432
FT /note="ALS 2"
FT REPEAT 438..469
FT /note="ALS 3"
FT REPEAT 474..505
FT /note="ALS 4"
FT REPEAT 510..541
FT /note="ALS 5"
FT REPEAT 546..577
FT /note="ALS 6"
FT REGION 580..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1326
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 723
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 847
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 73..150
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
FT DISULFID 96..112
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
FT DISULFID 205..298
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
FT DISULFID 227..256
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
FT VARIANT 2
FT /note="I -> L (in allele ALS5-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 311
FT /note="K -> R (in allele ALS5-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 406
FT /note="E -> K (in allele ALS5-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 481
FT /note="S -> SESYATTETITTGPLGTDSVIIKEPHNPTVTTTVFWS (in
FT allele ALS5-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 492
FT /note="N -> T (in allele ALS5-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 495
FT /note="E -> L (in allele ALS5-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 502..503
FT /note="VR -> IK (in allele ALS5-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 514
FT /note="E -> K (in allele ALS5-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 526
FT /note="V -> I (in allele ALS5-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 539
FT /note="K -> R (in allele ALS5-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 542
FT /note="H -> Y (in allele ALS5-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1167
FT /note="A -> T (in allele ALS5-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1202
FT /note="T -> N (in allele ALS5-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1267..1269
FT /note="AQV -> SEA (in allele ALS5-1)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1271
FT /note="N -> S (in allele ALS5-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1273
FT /note="L -> S (in allele ALS5-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1278
FT /note="S -> L (in allele ALS5-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1283
FT /note="M -> T (in allele ALS5-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT VARIANT 1291
FT /note="I -> M (in allele ALS5-2)"
FT /evidence="ECO:0000269|PubMed:14523127"
FT MUTAGEN 326
FT /note="V->N: Impairs amyloid formation and decreases cell
FT aggregation."
FT /evidence="ECO:0000269|PubMed:21408122"
FT CONFLICT 538
FT /note="I -> V (in Ref. 1; AAO72528/AAO72529)"
FT /evidence="ECO:0000305"
FT CONFLICT 841
FT /note="T -> I (in Ref. 1; AAO72528/AAO72529)"
FT /evidence="ECO:0000305"
FT CONFLICT 911
FT /note="M -> I (in Ref. 1; AAO72528/AAO72529)"
FT /evidence="ECO:0000305"
FT CONFLICT 975
FT /note="S -> L (in Ref. 1; AAO72528/AAO72529)"
FT /evidence="ECO:0000305"
FT CONFLICT 1028
FT /note="M -> T (in Ref. 1; AAO72528/AAO72529)"
FT /evidence="ECO:0000305"
FT CONFLICT 1046
FT /note="T -> I (in Ref. 1; AAO72528/AAO72529)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1347 AA; 141787 MW; 9AB66EDE24480F83 CRC64;
MIQQFTLLFL YLSFATAKAI TGIFNSIDSL TWSNAGNYAF KGPGYPTWNA VLGWSLDGTS
ANPGDTFILN MPCVFKFTAS QKSVDLTADG VKYATCQFYS GEEFTTFSSL KCTVNNNLRS
SIKALGTVTL PIAFNVGGTG SSVDLEDSKC FTAGTNTVTF NDGSKKLSIA VNFEKSTVDQ
SGYLTTSRFM PSLNKIATLY VAPQCENGYT SGTMGFSTSY GDVAIDCSNV HIGISKGVND
WNHPVTSESF SYTKSCSSFG ISITYQNVPA GYRPFIDAYI SPSDNNQYQL SYKNDYTCVD
DYWQHAPFTL KWTGYKNSDA GSNGIVIVAT TRTVTDSTTA VTTLPFNPSV DKTKTIEILQ
PIPTTTITTS YVGVTTSYST KTAPIGETAT VIVDVPYHTT TTVTSEWTGT ITTTTTRTNP
TDSIDTVVVQ VPLPNPTTTT TQFWSESFTS TTTITNSLKG TDSVIVREPH NPTVTTTEFW
SESYATTETI TNGPEGTDSV IVREPHNPTV TTTEFWSESY ATTETVTNKP EGTDSVIIKE
PHNPTVTTTE FWSESYATTE TITTGPLGTD SIVIHDPLEE SSSTTAIESS DSNISSSAQE
SSSSVEQSSS IVGLSSSSDI PLSSDMPSSS STGLTSSESS TVSSYDSDSS SSSELSTFSS
SESYSSSISD TTNFWDSSSS DLESTSITWS SSIDAQSSQS VQSVSNSIST SQETTSSSGE
ESNTSVTDIL VSSDASSILN SDISSYYPSS TISLSDDFPH TIAGEPDSRS SSSIASTVEI
SSDLVSLTSD PTSSFDSSSS LNSDSSSSPF SDESDISASS SFSTLVAPSF SLSSSSSLSL
TYPHYVNSTT YHASESESSS VASPSMASES ANDDTHTLSE STDTTSSIGT DSSTVTFCRR
DNGDGCIVTG MPSSSIDSEQ TSDVTTTSSF VASSTPTSAE QSITDNPNID SSQTSASSST
KSSVSVSDTV VNSISLSETS TLSSDDSTSS DTSISSTTNS DTGNINAGSS HTSTASIKES
SIQKTGVMLS SSYLSTKLSS TSDITTELIT TELITTELTT IEDNEPNTFT STPSSHSEIF
SSDNSVLSKQ VDRESTIKTS PTTDVTTVSS LSVHSTEAST ATLGENSFSN VASTPSNIAT
SLRSTSSSSN HATESSGTVK SEASAEAIPS PPTSTDNRLS YSTEEAKGIT YANSGSTNNL
ITESQVAAPT DSTSVLIENP VVTSTFDDNS SAAVDQPSKT KSIEESIMNP DSTNETNNGF
IATLSQAQVP NSLIHSESIS TTMAKTTDAS INGDSAASNS QPTTLIQQVA TSSYNQPLIT
TYAGSSSATK HPSWLLKFIS VALFFFL
