ALS1_CANAL
ID ALS1_CANAL Reviewed; 1260 AA.
AC Q5A8T4; A0A1D8PQ83; Q5A8L0;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Agglutinin-like protein 1;
DE AltName: Full=Adhesin 1;
DE Flags: Precursor;
GN Name=ALS1; OrderedLocusNames=CAALFM_C603700WA;
GN ORFNames=CaO19.13163, CaO19.5741;
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 DOMAIN.
RX PubMed=7752895; DOI=10.1111/j.1365-2958.1995.tb02219.x;
RA Hoyer L.L., Scherer S., Shatzman A.R., Livi G.P.;
RT "Candida albicans ALS1: domains related to a Saccharomyces cerevisiae
RT sexual agglutinin separated by a repeating motif.";
RL Mol. Microbiol. 15:39-54(1995).
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 FUNCTION.
RX PubMed=12183577; DOI=10.1128/iai.70.9.5256-5258.2002;
RA Kamai Y., Kubota M., Kamai Y., Hosokawa T., Fukuoka T., Filler S.G.;
RT "Contribution of Candida albicans ALS1 to the pathogenesis of experimental
RT oropharyngeal candidiasis.";
RL Infect. Immun. 70:5256-5258(2002).
RN [7]
RP FUNCTION.
RX PubMed=11967069; DOI=10.1046/j.1365-2958.2002.02873.x;
RA Fu Y., Ibrahim A.S., Sheppard D.C., Chen Y.C., French S.W., Cutler J.E.,
RA Filler S.G., Edwards J.E. Jr.;
RT "Candida albicans Als1p: an adhesin that is a downstream effector of the
RT EFG1 filamentation pathway.";
RL Mol. Microbiol. 44:61-72(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 IDENTIFICATION BY MASS SPECTROSCOPY, AND SUBCELLULAR LOCATION.
RX PubMed=15302828; DOI=10.1128/ec.3.4.955-965.2004;
RA de Groot P.W., de Boer A.D., Cunningham J., Dekker H.L., de Jong L.,
RA Hellingwerf K.J., de Koster C., Klis F.M.;
RT "Proteomic analysis of Candida albicans cell walls reveals covalently bound
RT carbohydrate-active enzymes and adhesins.";
RL Eukaryot. Cell 3:955-965(2004).
RN [10]
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 [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 FUNCTION.
RX PubMed=15116430; DOI=10.1002/yea.1111;
RA Loza L., Fu Y., Ibrahim A.S., Sheppard D.C., Filler S.G., Edwards J.E. Jr.;
RT "Functional analysis of the Candida albicans ALS1 gene product.";
RL Yeast 21:473-482(2004).
RN [13]
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 [14]
RP INDUCTION.
RX PubMed=15797814; DOI=10.1016/j.mcp.2004.10.007;
RA O'Connor L., Lahiff S., Casey F., Glennon M., Cormican M., Maher M.;
RT "Quantification of ALS1 gene expression in Candida albicans biofilms by RT-
RT PCR using hybridisation probes on the LightCycler.";
RL Mol. Cell. Probes 19:153-162(2005).
RN [15]
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 [16]
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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
RP INDUCTION.
RX PubMed=19197361; DOI=10.1371/journal.ppat.1000294;
RA Bastidas R.J., Heitman J., Cardenas M.E.;
RT "The protein kinase Tor1 regulates adhesin gene expression in Candida
RT albicans.";
RL PLoS Pathog. 5:E1000294-E1000294(2009).
RN [22]
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 [23]
RP DOMAIN.
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 [24]
RP SUBCELLULAR LOCATION.
RX PubMed=20705663; DOI=10.1099/mic.0.043851-0;
RA Coleman D.A., Oh S.H., Zhao X., Hoyer L.L.;
RT "Heterogeneous distribution of Candida albicans cell-surface antigens
RT demonstrated with an Als1-specific monoclonal antibody.";
RL Microbiology 156:3645-3659(2010).
RN [25]
RP FUNCTION, AND INDUCTION.
RX PubMed=22037180; DOI=10.1128/ec.05187-11;
RA Gregori C., Glaser W., Frohner I.E., Reinoso-Martin C., Rupp S.,
RA Schuller C., Kuchler K.;
RT "Efg1 Controls caspofungin-induced cell aggregation of Candida albicans
RT through the adhesin Als1.";
RL Eukaryot. Cell 10:1694-1704(2011).
RN [26]
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 [27]
RP GLYCAN-BINDING.
RX PubMed=21585565; DOI=10.1111/j.1365-2958.2011.07676.x;
RA Donohue D.S., Ielasi F.S., Goossens K.V., Willaert R.G.;
RT "The N-terminal part of Als1 protein from Candida albicans specifically
RT binds fucose-containing glycans.";
RL Mol. Microbiol. 80:1667-1679(2011).
RN [28]
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 [29]
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 [30]
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 [31]
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 [32]
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 [33]
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 [34]
RP FUNCTION.
RX PubMed=22359502; DOI=10.1371/journal.ppat.1002525;
RA Finkel J.S., Xu W., Huang D., Hill E.M., Desai J.V., Woolford C.A.,
RA Nett J.E., Taff H., Norice C.T., Andes D.R., Lanni F., Mitchell A.P.;
RT "Portrait of Candida albicans adherence regulators.";
RL PLoS Pathog. 8:E1002525-E1002525(2012).
CC -!- FUNCTION: Major cell surface adhesion protein which mediates both
CC yeast-to-host tissue adherence and yeast aggregation. Acts as a
CC downstream effector of the EFG1 regulatory pathway. Required for
CC rapamycin-induced aggregation of C.albicans. Binds glycans and mediates
CC adherence to endothelial and epithelial cells, thereby playing an
CC important role in the pathogenesis of C.albicans infections.
CC {ECO:0000269|PubMed:11967069, ECO:0000269|PubMed:12183577,
CC ECO:0000269|PubMed:15039323, ECO:0000269|PubMed:15116430,
CC ECO:0000269|PubMed:15128742, ECO:0000269|PubMed:16839200,
CC ECO:0000269|PubMed:17510860, ECO:0000269|PubMed:18635358,
CC ECO:0000269|PubMed:22037180, ECO:0000269|PubMed:22321066,
CC ECO:0000269|PubMed:22359502, ECO:0000269|PubMed:22429754,
CC ECO:0000269|PubMed:22882910}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:15302828, ECO:0000305|PubMed:12845604}. Secreted,
CC cell wall {ECO:0000269|PubMed:18712765, ECO:0000269|PubMed:20705663,
CC ECO:0000269|PubMed:20864472, ECO:0000269|PubMed:22106872}.
CC Note=Identified as covalently-linked GPI-modified cell wall protein
CC (GPI-CWP) in the outer cell wall layer (Probable) (PubMed:15302828).
CC Covers the germ tube as well as the cell surface with the exception of
CC bud scars (PubMed:22106872). {ECO:0000269|PubMed:15302828,
CC ECO:0000269|PubMed:22106872, ECO:0000305|PubMed:12845604}.
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. Down-
CC regulated by Riccardin D, a macrocyclic bisbibenzyl isolated from
CC Chinese liverwort D.hirsute which has an inhibitory effect on biofilms
CC and virulence. Induced by caspofungin. {ECO:0000269|PubMed:15731087,
CC ECO:0000269|PubMed:15797814, ECO:0000269|PubMed:17766464,
CC ECO:0000269|PubMed:18683080, ECO:0000269|PubMed:19197361,
CC ECO:0000269|PubMed:20398368, ECO:0000269|PubMed:20864472,
CC ECO:0000269|PubMed:21456055, ECO:0000269|PubMed:22037180,
CC ECO:0000269|PubMed:22545115, 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:0000269|PubMed:15128742, ECO:0000269|PubMed:19820118,
CC ECO:0000269|PubMed:7752895}.
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; CP017628; AOW30297.1; -; Genomic_DNA.
DR RefSeq; XP_718077.1; XM_712984.2.
DR AlphaFoldDB; Q5A8T4; -.
DR SMR; Q5A8T4; -.
DR BioGRID; 1223374; 10.
DR STRING; 237561.Q5A8T4; -.
DR GeneID; 3640280; -.
DR KEGG; cal:CAALFM_C603700WA; -.
DR CGD; CAL0000199010; ALS1.
DR VEuPathDB; FungiDB:C6_03700W_A; -.
DR HOGENOM; CLU_003114_0_0_1; -.
DR InParanoid; Q5A8T4; -.
DR OrthoDB; 1428896at2759; -.
DR PRO; PR:Q5A8T4; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005576; C:extracellular region; IDA:CGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030445; C:yeast-form cell wall; IDA:CGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0001968; F:fibronectin binding; IDA:CGD.
DR GO; GO:0043236; F:laminin binding; IDA:CGD.
DR GO; GO:0042277; F:peptide binding; IDA:CGD.
DR GO; GO:0044406; P:adhesion of symbiont to host; IMP: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:0006878; P:cellular copper ion homeostasis; IMP:CGD.
DR GO; GO:0036244; P:cellular response to neutral pH; IMP:CGD.
DR GO; GO:0044409; P:entry into host; IDA:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0036178; P:filamentous growth of a population of unicellular organisms in response to neutral pH; IMP:CGD.
DR GO; GO:0000128; P:flocculation; IMP:CGD.
DR GO; GO:0030448; P:hyphal growth; IMP:CGD.
DR GO; GO:0044416; P:induction by symbiont of host defense response; IMP:CGD.
DR GO; GO:1900735; P:positive regulation of flocculation; IMP:CGD.
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; 12.
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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..1238
FT /note="Agglutinin-like protein 1"
FT /id="PRO_0000420218"
FT PROPEP 1239..1260
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420219"
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..791
FT /note="ALS 12"
FT REGION 896..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..1066
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1238
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
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 579
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 687
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 820
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 886
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 918
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 973
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1045
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1068
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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"
SQ SEQUENCE 1260 AA; 132913 MW; C025873111ECF06D CRC64;
MLQQFTLLFL YLSIASAKTI TGVFDSFNSL TWSNAANYAF KGPGYPTWNA VLGWSLDGTS
ANPGDTFTLN MPCVFKYTTS QTSVDLTADG VKYATCQFYS GEEFTTFSTL TCTVNDALKS
SIKAFGTVTL PIAFNVGGTG SSTDLEDSKC FTAGTNTVTF NDGDKDISID VEFEKSTVDP
SGYLYASRVM PSLNKVTTLF VAPQCENGYT SGTMGFSSSN GDVAIDCSNI HIGITKGLND
WNYPVSSESF SYTKTCTSNG IQIKYQNVPA GYRPFIDAYI SATDVNQYTL AYTNDYTCAG
SRSQSKPFTL RWTGYKNSDA GSNGIVIVAT TRTVTDSTTA VTTLPFNPSV DKTKTIEILQ
PIPTTTITTS YVGVTTSYST KTAPIGETAT VIVDVPYHTT TTVTSEWTGT ITTTTTRTNP
TDSIDTVVVQ VPSPNPTVST TEYWSQSYAT TTTVTAPPGG TDTVIIREPP NHTVTTTEYW
SQSFATTTTV TAPPGETDTV IIREPPNHTV TTTEYWSQSY ATTTTVTAPP GGTDTVLIRE
PPNHTVTTTE YWSQSYATTT TVTAPPGGTD TVIIREPPNY TVTTTEYWSQ SYATTTTITA
PPGETDTVII REPPNHTVTT TEYWSQSYAT TTTVTAPPGG TDTVLIREPP NHTVTTTEYW
SQSYATTTTV TAPPGGTDTV LIREPPNHTV TTTEYWSQSY ATTTTVTAPP GGTDTVIIRE
PPNHTVTTTE YWSQSYATTT TVTAPPGGTD TVIIREPPNY TVTTTEYWSQ SFATTTTVTA
PPGGTDTVII YESMSSSKIS TSSNDITSII PSFSRPHYVN STTSDLSTFE SSSMNTPTSI
SSDGMLLSST TLVTESETTT ESICSDGKEC SRLSSSSGIV TNPDSNESSI VTSTVPTAST
MSDSLSSTDG ISATSSDNVS KSGVSVTTET SVTTIQTTPN PLSSSVTSLT QLSSIPSVSE
SESKVTFTSN GDNQSGTHDS QSTSTEIEIV TTSSTKVLPP VVSSNTDLTS EPTNTREQPT
TLSTTSNSIT EDITTSQPTG DNGDNTSSTN PVPTVATSTL ASASEEDNKS GSHESASTSL
KPSMGENSGL TTSTEIEATT TSPTEAPSPA VSSGTDVTTE PTDTREQPTT LSTTSKTNSE
SVATTQATNE NGGKSPSTDL TSSLTTGTSA STSANSELVT SGSVTGGAVA SASNDQSHST
SVTNSNSIVS NTPQTTLSQQ VTSSSPSTNT FIASTYDGSG SIIQHSTWLY GLITLLSLFI
