ALS3_CANAL
ID ALS3_CANAL Reviewed; 1155 AA.
AC Q59L12; A0A1D8PTD3; Q874L2; Q874L3;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 3.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Agglutinin-like protein 3;
DE AltName: Full=3D9 antigen;
DE AltName: Full=Adhesin 3;
DE Flags: Precursor;
GN Name=ALS3; Synonyms=ALS10, ALS8; OrderedLocusNames=CAALFM_CR07070CA;
GN ORFNames=CaO19.1816, CaO19.2355, CaO19.9379, CaO19.9891;
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], INDUCTION, FUNCTION, DISRUPTION
RP PHENOTYPE, AND VARIANTS.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15256583; DOI=10.1099/mic.0.26943-0;
RA Zhao X., Oh S.H., Cheng G., Green C.B., Nuessen J.A., Yeater K., Leng R.P.,
RA Brown A.J., Hoyer L.L.;
RT "ALS3 and ALS8 represent a single locus that encodes a Candida albicans
RT adhesin; functional comparisons between Als3p and Als1p.";
RL Microbiology 150:2415-2428(2004).
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 SUBCELLULAR LOCATION.
RX PubMed=10417199; DOI=10.1128/iai.67.8.4251-4255.1999;
RA Hoyer L.L., Clevenger J., Hecht J.E., Ehrhart E.J., Poulet F.M.;
RT "Detection of Als proteins on the cell wall of Candida albicans in murine
RT tissues.";
RL Infect. Immun. 67:4251-4255(1999).
RN [6]
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 [7]
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 [8]
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 [9]
RP FUNCTION.
RX PubMed=16839200; DOI=10.1371/journal.ppat.0020063;
RA Nobile C.J., Andes D.R., Nett J.E., Smith F.J., Yue F., Phan Q.T.,
RA Edwards J.E., Filler S.G., Mitchell A.P.;
RT "Critical role of Bcr1-dependent adhesins in C. albicans biofilm formation
RT in vitro and in vivo.";
RL PLoS Pathog. 2:E63-E63(2006).
RN [10]
RP INDUCTION.
RX PubMed=17766464; DOI=10.1128/ec.00236-07;
RA Bauer J., Wendland J.;
RT "Candida albicans Sfl1 suppresses flocculation and filamentation.";
RL Eukaryot. Cell 6:1736-1744(2007).
RN [11]
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 [12]
RP FUNCTION.
RX PubMed=18635358; DOI=10.1016/j.cub.2008.06.034;
RA Nobile C.J., Schneider H.A., Nett J.E., Sheppard D.C., Filler S.G.,
RA Andes D.R., Mitchell A.P.;
RT "Complementary adhesin function in C. albicans biofilm formation.";
RL Curr. Biol. 18:1017-1024(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=18712765; DOI=10.1002/pmic.200800110;
RA Castillo L., Calvo E., Martinez A.I., Ruiz-Herrera J., Valentin E.,
RA Lopez J.A., Sentandreu R.;
RT "A study of the Candida albicans cell wall proteome.";
RL Proteomics 8:3871-3881(2008).
RN [14]
RP INDUCTION.
RX PubMed=18683080; DOI=10.1007/s11046-008-9148-6;
RA Nailis H., Vandenbroucke R., Tilleman K., Deforce D., Nelis H., Coenye T.;
RT "Monitoring ALS1 and ALS3 gene expression during in vitro Candida albicans
RT biofilm formation under continuous flow conditions.";
RL Mycopathologia 167:9-17(2009).
RN [15]
RP IDENTIFICATION AS THE 3D9 ANTIGEN, AND SUBCELLULAR LOCATION.
RX PubMed=19291169; DOI=10.1111/j.1574-695x.2008.00502.x;
RA Beucher B., Marot-Leblond A., Billaud-Nail S., Oh S.H., Hoyer L.L.,
RA Robert R.;
RT "Recognition of Candida albicans Als3 by the germ tube-specific monoclonal
RT antibody 3D9.3.";
RL FEMS Immunol. Med. Microbiol. 55:314-323(2009).
RN [16]
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 [17]
RP SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RX PubMed=20864472; DOI=10.1099/mic.0.044206-0;
RA Sosinska G.J., de Koning L.J., de Groot P.W., Manders E.M., Dekker H.L.,
RA Hellingwerf K.J., de Koster C.G., Klis F.M.;
RT "Mass spectrometric quantification of the adaptations in the wall proteome
RT of Candida albicans in response to ambient pH.";
RL Microbiology 157:136-146(2011).
RN [18]
RP INDUCTION.
RX PubMed=21456055; DOI=10.1002/yea.1839;
RA Giacometti R., Kronberg F., Biondi R.M., Passeron S.;
RT "Candida albicans Tpk1p and Tpk2p isoforms differentially regulate
RT pseudohyphal development, biofilm structure, cell aggregation and adhesins
RT expression.";
RL Yeast 28:293-308(2011).
RN [19]
RP SUBCELLULAR LOCATION.
RX PubMed=22106872; DOI=10.1111/j.1574-695x.2011.00914.x;
RA Coleman D.A., Oh S.H., Manfra-Maretta S.L., Hoyer L.L.;
RT "A monoclonal antibody specific for Candida albicans Als4 demonstrates
RT overlapping localization of Als family proteins on the fungal cell surface
RT and highlights differences between Als localization in vitro and in vivo.";
RL FEMS Immunol. Med. Microbiol. 64:321-333(2012).
RN [20]
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 [21]
RP FUNCTION, AND INDUCTION.
RX PubMed=22544909; DOI=10.1128/ec.00103-12;
RA Fanning S., Xu W., Solis N., Woolford C.A., Filler S.G., Mitchell A.P.;
RT "Divergent targets of Candida albicans biofilm regulator Bcr1 in vitro and
RT in vivo.";
RL Eukaryot. Cell 11:896-904(2012).
RN [22]
RP DISRUPTION PHENOTYPE.
RX PubMed=22428031; DOI=10.1371/journal.pone.0033362;
RA Murciano C., Moyes D.L., Runglall M., Tobouti P., Islam A., Hoyer L.L.,
RA Naglik J.R.;
RT "Evaluation of the role of Candida albicans agglutinin-like sequence (Als)
RT proteins in human oral epithelial cell interactions.";
RL PLoS ONE 7:E33362-E33362(2012).
RN [23]
RP INDUCTION.
RX PubMed=22545115; DOI=10.1371/journal.pone.0035543;
RA Li Y., Ma Y., Zhang L., Guo F., Ren L., Yang R., Li Y., Lou H.;
RT "In vivo inhibitory effect on the biofilm formation of Candida albicans by
RT liverwort derived riccardin D.";
RL PLoS ONE 7:E35543-E35543(2012).
RN [24]
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).
RN [25]
RP FUNCTION.
RX PubMed=23630968; DOI=10.1128/iai.00013-13;
RA Fu Y., Phan Q.T., Luo G., Solis N.V., Liu Y., Cormack B.P.,
RA Edwards J.E. Jr., Ibrahim A.S., Filler S.G.;
RT "Investigation of the function of Candida albicans Als3 by heterologous
RT expression in Candida glabrata.";
RL Infect. Immun. 81:2528-2535(2013).
RN [26]
RP FUNCTION.
RX PubMed=24152214; DOI=10.1021/la403237f;
RA Alsteens D., Van Dijck P., Lipke P.N., Dufrene Y.F.;
RT "Quantifying the forces driving cell-cell adhesion in a fungal pathogen.";
RL Langmuir 29:13473-13480(2013).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=23136884; DOI=10.1111/mmi.12087;
RA Rohm M., Lindemann E., Hiller E., Ermert D., Lemuth K., Trkulja D.,
RA Sogukpinar O., Brunner H., Rupp S., Urban C.F., Sohn K.;
RT "A family of secreted pathogenesis-related proteins in Candida albicans.";
RL Mol. Microbiol. 87:132-151(2013).
RN [28]
RP INDUCTION.
RX PubMed=24514088; DOI=10.1128/aac.01583-13;
RA Li D.D., Zhao L.X., Mylonakis E., Hu G.H., Zou Y., Huang T.K., Yan L.,
RA Wang Y., Jiang Y.Y.;
RT "In vitro and in vivo activities of pterostilbene against Candida albicans
RT biofilms.";
RL Antimicrob. Agents Chemother. 58:2344-2355(2014).
RN [29]
RP INDUCTION.
RX PubMed=24623107; DOI=10.1007/s10482-014-0135-2;
RA Rautela R., Singh A.K., Shukla A., Cameotra S.S.;
RT "Lipopeptides from Bacillus strain AR2 inhibits biofilm formation by
RT Candida albicans.";
RL Antonie Van Leeuwenhoek 105:809-821(2014).
RN [30]
RP INDUCTION.
RX PubMed=24673895; DOI=10.1186/1471-2180-14-80;
RA Ding X., Liu Z., Su J., Yan D.;
RT "Human serum inhibits adhesion and biofilm formation in Candida albicans.";
RL BMC Microbiol. 14:80-80(2014).
RN [31]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24736223; DOI=10.1128/mbio.00911-14;
RA Dutton L.C., Nobbs A.H., Jepson K., Jepson M.A., Vickerman M.M.,
RA Aqeel Alawfi S., Munro C.A., Lamont R.J., Jenkinson H.F.;
RT "O-mannosylation in Candida albicans enables development of interkingdom
RT biofilm communities.";
RL MBio 5:E00911-E00911(2014).
RN [32]
RP INDUCTION.
RX PubMed=24466000; DOI=10.1371/journal.pone.0086270;
RA Delgado-Silva Y., Vaz C., Carvalho-Pereira J., Carneiro C., Nogueira E.,
RA Correia A., Carreto L., Silva S., Faustino A., Pais C., Oliveira R.,
RA Sampaio P.;
RT "Participation of Candida albicans transcription factor RLM1 in cell wall
RT biogenesis and virulence.";
RL PLoS ONE 9:E86270-E86270(2014).
RN [33]
RP INDUCTION.
RX PubMed=24796422; DOI=10.1371/journal.pone.0093225;
RA Feldman M., Al-Quntar A., Polacheck I., Friedman M., Steinberg D.;
RT "Therapeutic Potential of Thiazolidinedione-8 as an Antibiofilm Agent
RT against Candida albicans.";
RL PLoS ONE 9:E93225-E93225(2014).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 18-330, AND DISULFIDE BONDS.
RX PubMed=24802757; DOI=10.1074/jbc.m114.547877;
RA Lin J., Oh S.H., Jones R., Garnett J.A., Salgado P.S., Rusnakova S.,
RA Matthews S.J., Hoyer L.L., Cota E.;
RT "The peptide-binding cavity is essential for Als3-mediated adhesion of
RT Candida albicans to human cells.";
RL J. Biol. Chem. 289:18401-18412(2014).
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 biofilm formation and pathogenesis of C.albicans infections.
CC Necessary for C.albicans to bind to N-cadherin on endothelial cells and
CC E-cadherin on oral epithelial cells and subsequent endocytosis by these
CC cells. During disseminated infection, mediates initial trafficking to
CC the brain and renal cortex and contributes to fungal persistence in the
CC kidneys. {ECO:0000269|PubMed:15128742, ECO:0000269|PubMed:15256583,
CC ECO:0000269|PubMed:16839200, ECO:0000269|PubMed:17510860,
CC ECO:0000269|PubMed:18635358, ECO:0000269|PubMed:22321066,
CC ECO:0000269|PubMed:22429754, ECO:0000269|PubMed:22544909,
CC ECO:0000269|PubMed:23630968, ECO:0000269|PubMed:24152214,
CC ECO:0000269|PubMed:24736223}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor
CC {ECO:0000305|PubMed:12845604}. Secreted, cell wall
CC {ECO:0000269|PubMed:10417199, ECO:0000269|PubMed:18712765,
CC ECO:0000269|PubMed:19291169, ECO:0000269|PubMed:20864472,
CC ECO:0000269|PubMed:22106872, ECO:0000269|PubMed:23136884,
CC ECO:0000269|PubMed:24736223}. Note=Covers the surface of the germ tube.
CC {ECO:0000269|PubMed:19291169, ECO:0000269|PubMed:22106872}.
CC -!- INDUCTION: Expression is under the positive control of the biofilm
CC regulator BCR1, RLM1, TOR1 and TPK2; and under the negative control of
CC SFL1. Induced during germ tube formation. Highly expressed in
CC oropharyngeal candidiasis (OPC), a biofilm-like infection of the oral
CC mucosa. Induced in the initial stages of biofilm formation. Down-
CC regulated by human serum, as well as by bacterial quorum sensing
CC quencher thiazolidinedione-8, pterostilbene, lipopeptides biosurfactant
CC produced by B.amyloliquefaciens, and Riccardin D, a macrocyclic
CC bisbibenzyl isolated from Chinese liverwort D.hirsute, which has an
CC inhibitory effect on biofilms and virulence.
CC {ECO:0000269|PubMed:15256583, ECO:0000269|PubMed:15731087,
CC ECO:0000269|PubMed:17766464, ECO:0000269|PubMed:18683080,
CC ECO:0000269|PubMed:20398368, ECO:0000269|PubMed:20864472,
CC ECO:0000269|PubMed:21456055, ECO:0000269|PubMed:22544909,
CC ECO:0000269|PubMed:22545115, ECO:0000269|PubMed:24466000,
CC ECO:0000269|PubMed:24514088, ECO:0000269|PubMed:24623107,
CC ECO:0000269|PubMed:24673895, ECO:0000269|PubMed:24796422}.
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}.
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 -!- DISRUPTION PHENOTYPE: Reduces adhesion and damage to both human
CC umbilical vein endothelial cells (HUVEC) and oral epithelial cells.
CC {ECO:0000269|PubMed:15256583, ECO:0000269|PubMed:22428031}.
CC -!- SIMILARITY: Belongs to the ALS family. {ECO:0000305}.
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DR EMBL; AY223552; AAO72959.1; -; Genomic_DNA.
DR EMBL; AY223551; AAO72958.1; -; Genomic_DNA.
DR EMBL; CP017630; AOW31402.1; -; Genomic_DNA.
DR RefSeq; XP_710435.2; XM_705343.2.
DR PDB; 4LE8; X-ray; 1.75 A; A/B=18-316.
DR PDB; 4LEB; X-ray; 1.40 A; A=18-316.
DR PDB; 4LEE; X-ray; 3.00 A; A/B/C/D=18-330.
DR PDBsum; 4LE8; -.
DR PDBsum; 4LEB; -.
DR PDBsum; 4LEE; -.
DR AlphaFoldDB; Q59L12; -.
DR SMR; Q59L12; -.
DR STRING; 237561.Q59L12; -.
DR GeneID; 3647965; -.
DR KEGG; cal:CAALFM_CR07070CA; -.
DR CGD; CAL0000183666; ALS3.
DR VEuPathDB; FungiDB:CR_07070C_A; -.
DR eggNOG; ENOG502RGCG; Eukaryota.
DR HOGENOM; CLU_011374_0_0_1; -.
DR InParanoid; Q59L12; -.
DR OrthoDB; 1428896at2759; -.
DR PHI-base; PHI:527; -.
DR PRO; PR:Q59L12; -.
DR Proteomes; UP000000559; Chromosome R.
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; 4.
DR Pfam; PF05792; Candida_ALS; 14.
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 3D-structure; Cell adhesion; Cell membrane; Cell wall; Disulfide bond;
KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Reference proteome;
KW Repeat; Secreted; Signal; Virulence.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..1134
FT /note="Agglutinin-like protein 3"
FT /id="PRO_0000420221"
FT PROPEP 1135..1155
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000429922"
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 REPEAT 582..613
FT /note="ALS 7"
FT REPEAT 618..649
FT /note="ALS 8"
FT REPEAT 654..685
FT /note="ALS 9"
FT REPEAT 690..721
FT /note="ALS 10"
FT REPEAT 726..757
FT /note="ALS 11"
FT REPEAT 762..793
FT /note="ALS 12"
FT REPEAT 798..829
FT /note="ALS 13"
FT REPEAT 834..863
FT /note="ALS 14"
FT REGION 936..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1134
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 615
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 651
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 723
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 759
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 795
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 881
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1023
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1099
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 73..150
FT /evidence="ECO:0000269|PubMed:24802757,
FT ECO:0007744|PDB:4LE8, ECO:0007744|PDB:4LEB,
FT ECO:0007744|PDB:4LEE"
FT DISULFID 96..112
FT /evidence="ECO:0000269|PubMed:24802757,
FT ECO:0007744|PDB:4LE8, ECO:0007744|PDB:4LEB,
FT ECO:0007744|PDB:4LEE"
FT DISULFID 205..298
FT /evidence="ECO:0000269|PubMed:24802757,
FT ECO:0007744|PDB:4LE8, ECO:0007744|PDB:4LEB,
FT ECO:0007744|PDB:4LEE"
FT DISULFID 227..256
FT /evidence="ECO:0000269|PubMed:24802757,
FT ECO:0007744|PDB:4LE8, ECO:0007744|PDB:4LEB,
FT ECO:0007744|PDB:4LEE"
FT VARIANT 628
FT /note="Y -> F (in allele ALS3-2)"
FT /evidence="ECO:0000269|PubMed:15256583"
FT VARIANT 634
FT /note="I -> V (in allele ALS3-2)"
FT /evidence="ECO:0000269|PubMed:15256583"
FT VARIANT 640
FT /note="E -> G (in allele ALS3-2)"
FT /evidence="ECO:0000269|PubMed:15256583"
FT VARIANT 645
FT /note="L -> I (in allele ALS3-2)"
FT /evidence="ECO:0000269|PubMed:15256583"
FT VARIANT 665..700
FT /note="Missing (in allele ALS3-2)"
FT /evidence="ECO:0000269|PubMed:15256583"
FT VARIANT 676
FT /note="G -> E (in allele ALS3-1)"
FT /evidence="ECO:0000269|PubMed:15256583"
FT VARIANT 743..814
FT /note="Missing (in allele ALS3-2)"
FT /evidence="ECO:0000269|PubMed:15256583"
FT VARIANT 814..815
FT /note="II -> VT (in allele ALS3-1)"
FT /evidence="ECO:0000269|PubMed:15256583"
FT VARIANT 820
FT /note="E -> G (in allele ALS3-1)"
FT /evidence="ECO:0000269|PubMed:15256583"
FT VARIANT 843
FT /note="S -> P (in allele ALS3-1)"
FT /evidence="ECO:0000269|PubMed:15256583"
FT VARIANT 847
FT /note="A -> T (in allele ALS3-1)"
FT /evidence="ECO:0000269|PubMed:15256583"
FT VARIANT 851
FT /note="T -> I (in allele ALS3-1)"
FT /evidence="ECO:0000269|PubMed:15256583"
FT VARIANT 935
FT /note="T -> S (in allele ALS3-1)"
FT /evidence="ECO:0000269|PubMed:15256583"
FT VARIANT 963
FT /note="F -> V (in allele ALS3-1)"
FT /evidence="ECO:0000269|PubMed:15256583"
FT VARIANT 1062
FT /note="Q -> P (in allele ALS3-1)"
FT /evidence="ECO:0000269|PubMed:15256583"
FT CONFLICT 942
FT /note="L -> S (in Ref. 1; AAO72958/AAO72959)"
FT /evidence="ECO:0000305"
FT STRAND 24..32
FT /evidence="ECO:0007829|PDB:4LEB"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:4LEB"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:4LEB"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:4LEB"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:4LEB"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:4LEB"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:4LEB"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:4LEB"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:4LEB"
FT STRAND 123..134
FT /evidence="ECO:0007829|PDB:4LEB"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:4LEB"
FT HELIX 142..147
FT /evidence="ECO:0007829|PDB:4LEB"
FT STRAND 153..164
FT /evidence="ECO:0007829|PDB:4LEB"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:4LEB"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:4LEB"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:4LEB"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:4LEB"
FT STRAND 209..238
FT /evidence="ECO:0007829|PDB:4LEB"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:4LEB"
FT STRAND 260..268
FT /evidence="ECO:0007829|PDB:4LEB"
FT STRAND 272..284
FT /evidence="ECO:0007829|PDB:4LEB"
FT STRAND 287..298
FT /evidence="ECO:0007829|PDB:4LEB"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:4LEB"
FT STRAND 308..313
FT /evidence="ECO:0007829|PDB:4LEB"
FT STRAND 321..328
FT /evidence="ECO:0007829|PDB:4LEE"
SQ SEQUENCE 1155 AA; 123759 MW; 698CC6E64D739A6C CRC64;
MLQQYTLLLI YLSVATAKTI TGVFNSFNSL TWSNAATYNY KGPGTPTWNA VLGWSLDGTS
ASPGDTFTLN MPCVFKFTTS QTSVDLTAHG VKYATCQFQA GEEFMTFSTL TCTVSNTLTP
SIKALGTVTL PLAFNVGGTG SSVDLEDSKC FTAGTNTVTF NDGGKKISIN VDFERSNVDP
KGYLTDSRVI PSLNKVSTLF VAPQCANGYT SGTMGFANTY GDVQIDCSNI HVGITKGLND
WNYPVSSESF SYTKTCSSNG IFITYKNVPA GYRPFVDAYI SATDVNSYTL SYANEYTCAG
GYWQRAPFTL RWTGYRNSDA GSNGIVIVAT TRTVTDSTTA VTTLPFDPNR DKTKTIEILK
PIPTTTITTS YVGVTTSYST KTAPIGETAT VIVDIPYHTT TTVTSKWTGT ITSTTTHTNP
TDSIDTVIVQ VPSPNPTVTT TEYWSQSFAT TTTITGPPGN TDTVLIREPP NHTVTTTEYW
SESYTTTSTF TAPPGGTDSV IIKEPPNPTV TTTEYWSESY TTTTTVTAPP GGTDTVIIRE
PPNHTVTTTE YWSQSYTTTT TVIAPPGGTD SVIIREPPNP TVTTTEYWSQ SYATTTTITA
PPGETDTVLI REPPNHTVTT TEYWSQSYAT TTTITAPPGE TDTVLIREPP NHTVTTTEYW
SQSYTTTTTV IAPPGGTDSV IIKEPPNPTV TTTEYWSQSY ATTTTITAPP GETDTVLIRE
PPNHTVTTTE YWSQSYATTT TITAPPGETD TVLIREPPNH TVTTTEYWSQ SFATTTTVTA
PPGGTDTVII REPPNHTVTT TEYWSQSFAT TTTIIAPPGE TDTVLIREPP NPTVTTTEYW
SQSYTTATTV TAPPGGTDTV IIYDTMSSSE ISSFSRPHYT NHTTLWSTTW VIETKTITET
SCEGDKGCSW VSVSTRIVTI PNNIETPMVT NTVDTTTTES TLQSPSGIFS ESGVSVETES
STFTTAQTNP SVPTTESEVV FTTKGNNGNG PYESPSTNVK SSMDENSEFT TSTAASTSTD
IENETIATTG SVEASSPIIS SSADETTTVT TTAESTSVIE QQTNNNGGGN APSATSTSSP
STTTTANSDS VITSTTSTNQ SQSQSNSDTQ QTTLSQQMTS SLVSLHMLTT FDGSGSVIQH
STWLCGLITL LSLFI
