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Database: UniProt
Entry: ALS5_CANAL
LinkDB: ALS5_CANAL
Original site: 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   24-JAN-2024, entry version 103.
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   STRING; 237561.Q5A8T7; -.
DR   GlyCosmos; Q5A8T7; 5 sites, No reported glycans.
DR   EnsemblFungi; C6_03690W_A-T; C6_03690W_A-T-p1; C6_03690W_A.
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; 2056365at2759; -.
DR   PHI-base; PHI:11394; -.
DR   PRO; PR:Q5A8T7; -.
DR   Proteomes; UP000000559; Chromosome 6.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR   GO; GO:0001968; F:fibronectin binding; IDA:CGD.
DR   GO; GO:0042277; F:peptide binding; IDA:CGD.
DR   GO; GO:0044406; P:adhesion of symbiont to host; IDA:CGD.
DR   GO; GO:0007155; P:cell adhesion; IDA:CGD.
DR   GO; GO:0043710; P:cell adhesion involved in multi-species biofilm formation; IMP:CGD.
DR   GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IMP:CGD.
DR   GO; GO:0098609; P:cell-cell adhesion; IDA:CGD.
DR   GO; GO:0007160; P:cell-matrix adhesion; IDA:CGD.
DR   GO; GO:0044409; P:entry into host; IDA:CGD.
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; 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:SF2; AGGLUTININ-LIKE PROTEIN 6; 1.
DR   PANTHER; PTHR33793; ALPHA-AGGLUTININ; 1.
DR   Pfam; PF05792; Candida_ALS; 6.
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 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
//
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