ALS2_CANAL
ID ALS2_CANAL Reviewed; 2530 AA.
AC P0CU38; A0A1D8PQE1; O74657; Q59QW1;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=Agglutinin-like protein 2;
DE AltName: Full=Adhesin 2;
DE Flags: Precursor;
GN Name=ALS2; OrderedLocusNames=CAALFM_C604380WA;
GN ORFNames=CaO19.1097, CaO19.8699;
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 [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 [2]
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 [3]
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 [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=1161;
RX PubMed=9765564; DOI=10.1128/jb.180.20.5334-5343.1998;
RA Hoyer L.L., Payne T.L., Hecht J.E.;
RT "Identification of Candida albicans ALS2 and ALS4 and localization of als
RT proteins to the fungal cell surface.";
RL J. Bacteriol. 180:5334-5343(1998).
RN [5]
RP 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 [6]
RP FUNCTION.
RX PubMed=15870470; DOI=10.1099/mic.0.27763-0;
RA Zhao X., Oh S.H., Yeater K.M., Hoyer L.L.;
RT "Analysis of the Candida albicans Als2p and Als4p adhesins suggests the
RT potential for compensatory function within the Als family.";
RL Microbiology 151:1619-1630(2005).
RN [7]
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 [8]
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 [9]
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 [10]
RP FUNCTION, AND INDUCTION.
RX PubMed=22882910; DOI=10.1111/j.1365-2958.2012.08193.x;
RA Fanning S., Xu W., Beaurepaire C., Suhan J.P., Nantel A., Mitchell A.P.;
RT "Functional control of the Candida albicans cell wall by catalytic protein
RT kinase A subunit Tpk1.";
RL Mol. Microbiol. 86:284-302(2012).
RN [11]
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.
CC {ECO:0000269|PubMed:22321066, ECO:0000269|PubMed:22429754,
CC ECO:0000269|PubMed:22882910}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor
CC {ECO:0000255}. Secreted, cell wall {ECO:0000305|PubMed:9765564}.
CC Note=Identified as covalently-linked GPI-modified cell wall protein
CC (GPI-CWP) in the outer cell wall layer. {ECO:0000305}.
CC -!- INDUCTION: Highly expressed in biofilms with down-regulation during
CC later stages of biofilm formation. Expression is repressed by TPK1 and
CC SFL1, and induced by TPK2. Also under the control of TOR1. Expression
CC is down-regulated by Riccardin D, a macrocyclic bisbibenzyl isolated
CC from Chinese liverwort D.hirsute, which has an inhibitory effect on
CC biofilms and virulence. Induced by caspofungin.
CC {ECO:0000269|PubMed:15731087, ECO:0000269|PubMed:20398368,
CC ECO:0000269|PubMed:22882910}.
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:0000305|PubMed:15128742}.
CC -!- PTM: N-glycosylated and O-glycosylated. {ECO:0000305}.
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:9765564}.
CC -!- SIMILARITY: Belongs to the ALS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AOW30356.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CP017628; AOW30356.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; XP_712646.2; XM_707553.2.
DR AlphaFoldDB; P0CU38; -.
DR SMR; P0CU38; -.
DR STRING; 237561.P0CU38; -.
DR GeneID; 3645724; -.
DR KEGG; cal:CAALFM_C604380WA; -.
DR eggNOG; ENOG502RGCG; Eukaryota.
DR OrthoDB; 1428896at2759; -.
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; 12.
DR Pfam; PF05792; Candida_ALS; 50.
DR Pfam; PF11766; Candida_ALS_N; 1.
DR SMART; SM01056; Candida_ALS_N; 1.
DR SUPFAM; SSF49401; SSF49401; 1.
PE 2: Evidence at transcript 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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..2507
FT /note="Agglutinin-like protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000020692"
FT PROPEP 2508..2530
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000439163"
FT REPEAT 364..395
FT /note="ALS 1"
FT REPEAT 400..431
FT /note="ALS 2"
FT REPEAT 437..468
FT /note="ALS 3"
FT REPEAT 473..504
FT /note="ALS 4"
FT REPEAT 509..540
FT /note="ALS 5"
FT REPEAT 545..576
FT /note="ALS 6"
FT REPEAT 581..612
FT /note="ALS 7"
FT REPEAT 617..648
FT /note="ALS 8"
FT REPEAT 653..684
FT /note="ALS 9"
FT REPEAT 689..720
FT /note="ALS 10"
FT REPEAT 725..756
FT /note="ALS 11"
FT REPEAT 761..792
FT /note="ALS 12"
FT REPEAT 797..828
FT /note="ALS 13"
FT REPEAT 833..864
FT /note="ALS 14"
FT REPEAT 869..900
FT /note="ALS 15"
FT REPEAT 905..936
FT /note="ALS 16"
FT REPEAT 941..972
FT /note="ALS 17"
FT REPEAT 977..1008
FT /note="ALS 18"
FT REPEAT 1013..1044
FT /note="ALS 19"
FT REPEAT 1049..1077
FT /note="ALS 20"
FT REPEAT 1085..1116
FT /note="ALS 21"
FT REPEAT 1121..1152
FT /note="ALS 22"
FT REPEAT 1157..1188
FT /note="ALS 23"
FT REPEAT 1193..1224
FT /note="ALS 24"
FT REPEAT 1229..1260
FT /note="ALS 25"
FT REPEAT 1265..1296
FT /note="ALS 26"
FT REPEAT 1301..1332
FT /note="ALS 27"
FT REPEAT 1337..1368
FT /note="ALS 28"
FT REPEAT 1373..1404
FT /note="ALS 29"
FT REPEAT 1409..1440
FT /note="ALS 30"
FT REPEAT 1445..1476
FT /note="ALS 31"
FT REPEAT 1481..1512
FT /note="ALS 32"
FT REPEAT 1517..1548
FT /note="ALS 33"
FT REPEAT 1553..1584
FT /note="ALS 34"
FT REPEAT 1589..1620
FT /note="ALS 35"
FT REPEAT 1625..1656
FT /note="ALS 36"
FT REPEAT 1661..1692
FT /note="ALS 37"
FT REPEAT 1697..1728
FT /note="ALS 38"
FT REPEAT 1733..1764
FT /note="ALS 39"
FT REPEAT 1769..1800
FT /note="ALS 40"
FT REPEAT 1805..1836
FT /note="ALS 41"
FT REPEAT 1841..1872
FT /note="ALS 42"
FT REPEAT 1877..1907
FT /note="ALS 43"
FT REPEAT 1913..1944
FT /note="ALS 44"
FT REPEAT 1949..1980
FT /note="ALS 45"
FT REPEAT 1985..2016
FT /note="ALS 46"
FT REPEAT 2021..2052
FT /note="ALS 47"
FT REPEAT 2057..2088
FT /note="ALS 48"
FT REPEAT 2093..2124
FT /note="ALS 49"
FT REPEAT 2129..2157
FT /note="ALS 50"
FT REGION 954..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2200..2235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2274..2494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2274..2315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2326..2494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2507
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 866
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1010
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1586
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1730
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1766
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1838
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1910
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1982
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2090
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2466
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..297
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
FT DISULFID 227..256
FT /evidence="ECO:0000250|UniProtKB:A0A1D8PQ86"
SQ SEQUENCE 2530 AA; 267652 MW; 751F7089B29B4547 CRC64;
MLLQFLLLSL CVSVATAKVI TGVFNSFDSL TWTRAGNYAY KGPNRPTWNA VLGWSLDGTS
ANPGDTFTLN MPCVFKFITD QTSVDLTADG VKYATCQFYS GEEFTTFSSL KCTVSNTLTS
SIKALGTVTL PISFNVGGTG SLVDLESSKC FKAGTNTVTF NDGDKKISID VDFEKTNEDA
SGYFIASRLI PSINKASITY VAPQCANGYT SGAMGFTIGS GDTTIDCSNV HVGITKGLND
WNFPVSSDSL SYNKTCSSTG ISITYENVPA GYRPFFDVYT SVSDQNRQLK YTNDYACVGS
SLQSKPFNLR LRGYNNSEAN SNGFVIVATT RTVTDSTTAV TTLPFNPSVD KTKTIEILQP
IPTTTITTSY VGVTTSYSTK TAPIGETATV IVDVPYHTTT TVTSEWTGTI TTTTTRTNPT
DSIDTVVVQV PSPNPTVTTT EYWSQSYATT TTVTAPPGGT DSVIIREPPN PTVTTTEYWS
QSYATSSTVT APPGGTDTVI IREPPNPTVT TTEYWSQSYA TTTTVTAPPG GTDSVIIREP
PNPTVTTTEY WSQSFATTTT ITAPPGETDT VLIREPPNHT VTTTEYWSQS YVTTSTITAP
PGGTDTVIIR EPPNYTVTTT EYWSQSYATT TTVTAPPGGT DTVIIREPPN PTVTTTEYWS
QSYATTTTVT GPPGGTDTVI IREPPNPTVT TTEYWSQSYA TTTTVTAPPG GTDTVIIREP
PNPTVTTTEY WSQSYATTTT VTGPPGGTDT VIIREPPNPT VTTTEYWSQS YATTTTVTAP
PGGTATVIIR EPPNPTVTTT EYWSQSYATT TTVTGPPGGT DTVIIREPPN PTVTTTEYWS
QSYATTTTVT APPGGTATVI IREPPNYTVT TTEYWSQSYA TTTTVTGPPG GTDTVIIREP
PSPTVTTTEY WSQSYATTTT VTAPPGGTAT VIIREPPNPT VTTTEYWSQS YATTTTVTGP
PGGTDTVIIR EPPNPTVTTT EYWSQSYATT TTVTAPPGGT ATVIIREPPN YTVTTTEYWS
QSYATTTTVT GPPGGTDTVI IREPPSPTVT TTEYWSQSYA TTTTVTAPPG GTATVIIREP
PNPTVTTTEY WSQSYATTTT VTGPPGGTDT VIIREPPSPT VTTTEYWSQS YATTTTVTAP
PGGTATVIIR EPPNYTVTTT EYWSQSYATT TTVTGPPGGT DTVIIREPPN PTVTTTEYWS
QSFATTTTVT APPGGTDSVI IREPPNPTVT TTEYWSQSYA TTTTVTAPPG GTDSVIIREP
PNPTVTTTEY WSQSFATTTT VTAPPGGTDS VIIREPPNPT VTTTEYWSQS YATTTTVTAP
PGGTDSVIIR EPPNPTVTTT EYWSQSYATT TTVTAPPGGT ATVIIREPPN YTVTTTEYWS
QSYATTTTVT APPGGTATVI IREPPNYTVT TTEYWSQSYA TTTTITAPPG DTDTVIIREP
PNYTVTTTEY WSQSFATTTT VTAPPGGTDS VIIREPPNPT VTTTEYWSQS YATTTTVTAP
PGGTATVIIR EPPNYTVTTT EYWSQSYATT TTVTAPPGGT ATVIIREPPN YTVTTTEYWS
QSYATTTTIT APPGDTDTVI IREPPNYTVT TTEYWSQSYA TTTTVTAPPG GTDTVIIREP
PNYTVTTTEY WSQSYATTTT VTAPPGGTAT VIIREPPNYT VTTTEYWSQS YATTTTVTGP
PGSTDTVIIR EPPNPTVTTT EYWSQSYATT TTVTAPPGGT ATVIIREPPN YTVTTTEYWS
QSYATTTTVT APPGGTDTVI IREPPNYTVT TTEYWSQSYA TTTTVTAPPG GTDTVIIREP
PSPTVTTTEY WSQSYATTTT VTAPPGGTAT VIIREPPNYT VTTTEYWSES YATTTTVTGP
PGGTDVILIR EPPNPTVTTT EYWSESYATT TTITAPPGAT DSVRIREPPN YTVTTTEYWS
QSYATTTTVT APPGGTDSVI IREPPNPTVT TTEYWSQSYA TTTTVTAPPG GTATVIIREP
PNYTVTTTEY WSQSYATTTT VTAPPGGTDT VIIREPPSPT VTTTEYWSQS YATTTTVTAP
PGGTATVIIR EPPSPTVTTT EYWSQSYATT TTVTAPPGGT ATVIIREPPN YTVTTTEYWS
QSYATTTTVT GPPGGTDTVI IREPPNPTVT TTEYWSQSYA TTLTITAPPG GTNSVIIRVH
SSTNDESSES TFSTLSVPSF SGSISVVSTV SRPHYVNSTV THLPSSSSKP VDIPSSDVVT
STNDNSLTSL TGSENGKTSV AISTTFCDDE NGCQTSIPQG SVVRTTATTT ATTTTIIGDN
NGSGKSKSGE LSSTGSVTTN TATPDVPSTK VPSNPGAPGT GVPPPLAPST ETQTTNNVPG
SPNIPATGTT DIIRESTTVS HTVTGNGNTG VPMNPNPVLT TSTSLTGATN SATNPSHETS
VNTGSGGSTN IVTPPSSATA TVVIPGTDNG ATTKGQDTAG GNSNGSTATT NIQGGNNEPG
NQPGTNTTGE PVGTTDTQSV ESISQPTTLS QQTTSSLIST PLASTFDGSG SIVQHSGWLY
VLLTAISIFF
