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Agglutinin-like protein 3 (3D9 antigen) (Adhesin 3)

 ALS3_CANAL              Reviewed;        1155 AA.
Q59L12; A0A1D8PTD3; Q874L2; Q874L3;
28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
15-MAR-2017, sequence version 3.
13-FEB-2019, entry version 69.
RecName: Full=Agglutinin-like protein 3;
AltName: Full=3D9 antigen;
AltName: Full=Adhesin 3;
Flags: Precursor;
Name=ALS3; Synonyms=ALS10, ALS8; OrderedLocusNames=CAALFM_CR07070CA;
ORFNames=CaO19.1816, CaO19.2355, CaO19.9379, CaO19.9891;
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
Candida/Lodderomyces clade; Candida.
NCBI_TaxID=237561;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, FUNCTION, DISRUPTION
PHENOTYPE, AND VARIANTS.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=15256583; DOI=10.1099/mic.0.26943-0;
Zhao X., Oh S.H., Cheng G., Green C.B., Nuessen J.A., Yeater K.,
Leng R.P., Brown A.J., Hoyer L.L.;
"ALS3 and ALS8 represent a single locus that encodes a Candida
albicans adhesin; functional comparisons between Als3p and Als1p.";
Microbiology 150:2415-2428(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=15123810; DOI=10.1073/pnas.0401648101;
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
Davis R.W., Scherer S.;
"The diploid genome sequence of Candida albicans.";
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
[3]
GENOME REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
Chibana H., Nantel A., Magee P.T.;
"Assembly of the Candida albicans genome into sixteen supercontigs
aligned on the eight chromosomes.";
Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
"Assembly of a phased diploid Candida albicans genome facilitates
allele-specific measurements and provides a simple model for repeat
and indel structure.";
Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
[5]
SUBCELLULAR LOCATION.
PubMed=10417199;
Hoyer L.L., Clevenger J., Hecht J.E., Ehrhart E.J., Poulet F.M.;
"Detection of Als proteins on the cell wall of Candida albicans in
murine tissues.";
Infect. Immun. 67:4251-4255(1999).
[6]
PREDICTION OF GPI-ANCHOR.
PubMed=12845604; DOI=10.1002/yea.1007;
De Groot P.W., Hellingwerf K.J., Klis F.M.;
"Genome-wide identification of fungal GPI proteins.";
Yeast 20:781-796(2003).
[7]
FUNCTION, AND DOMAIN.
PubMed=15128742; DOI=10.1074/jbc.M401929200;
Sheppard D.C., Yeaman M.R., Welch W.H., Phan Q.T., Fu Y.,
Ibrahim A.S., Filler S.G., Zhang M., Waring A.J., Edwards J.E. Jr.;
"Functional and structural diversity in the Als protein family of
Candida albicans.";
J. Biol. Chem. 279:30480-30489(2004).
[8]
INDUCTION.
PubMed=15731087; DOI=10.1128/IAI.73.3.1852-1855.2005;
Green C.B., Zhao X., Hoyer L.L.;
"Use of green fluorescent protein and reverse transcription-PCR to
monitor Candida albicans agglutinin-like sequence gene expression in a
murine model of disseminated candidiasis.";
Infect. Immun. 73:1852-1855(2005).
[9]
FUNCTION.
PubMed=16839200; DOI=10.1371/journal.ppat.0020063;
Nobile C.J., Andes D.R., Nett J.E., Smith F.J., Yue F., Phan Q.T.,
Edwards J.E., Filler S.G., Mitchell A.P.;
"Critical role of Bcr1-dependent adhesins in C. albicans biofilm
formation in vitro and in vivo.";
PLoS Pathog. 2:E63-E63(2006).
[10]
INDUCTION.
PubMed=17766464; DOI=10.1128/EC.00236-07;
Bauer J., Wendland J.;
"Candida albicans Sfl1 suppresses flocculation and filamentation.";
Eukaryot. Cell 6:1736-1744(2007).
[11]
FUNCTION.
PubMed=17510860; DOI=10.1080/13693780701299333;
Klotz S.A., Gaur N.K., De Armond R., Sheppard D., Khardori N.,
Edwards J.E. Jr., Lipke P.N., El-Azizi M.;
"Candida albicans Als proteins mediate aggregation with bacteria and
yeasts.";
Med. Mycol. 45:363-370(2007).
[12]
FUNCTION.
PubMed=18635358; DOI=10.1016/j.cub.2008.06.034;
Nobile C.J., Schneider H.A., Nett J.E., Sheppard D.C., Filler S.G.,
Andes D.R., Mitchell A.P.;
"Complementary adhesin function in C. albicans biofilm formation.";
Curr. Biol. 18:1017-1024(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=18712765; DOI=10.1002/pmic.200800110;
Castillo L., Calvo E., Martinez A.I., Ruiz-Herrera J., Valentin E.,
Lopez J.A., Sentandreu R.;
"A study of the Candida albicans cell wall proteome.";
Proteomics 8:3871-3881(2008).
[14]
INDUCTION.
PubMed=18683080; DOI=10.1007/s11046-008-9148-6;
Nailis H., Vandenbroucke R., Tilleman K., Deforce D., Nelis H.,
Coenye T.;
"Monitoring ALS1 and ALS3 gene expression during in vitro Candida
albicans biofilm formation under continuous flow conditions.";
Mycopathologia 167:9-17(2009).
[15]
IDENTIFICATION AS THE 3D9 ANTIGEN, AND SUBCELLULAR LOCATION.
PubMed=19291169; DOI=10.1111/j.1574-695X.2008.00502.x;
Beucher B., Marot-Leblond A., Billaud-Nail S., Oh S.H., Hoyer L.L.,
Robert R.;
"Recognition of Candida albicans Als3 by the germ tube-specific
monoclonal antibody 3D9.3.";
FEMS Immunol. Med. Microbiol. 55:314-323(2009).
[16]
INDUCTION.
PubMed=20398368; DOI=10.1186/1471-2180-10-114;
Nailis H., Kucharikova S., Ricicova M., Van Dijck P., Deforce D.,
Nelis H., Coenye T.;
"Real-time PCR expression profiling of genes encoding potential
virulence factors in Candida albicans biofilms: identification of
model-dependent and -independent gene expression.";
BMC Microbiol. 10:114-114(2010).
[17]
SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
INDUCTION.
PubMed=20864472; DOI=10.1099/mic.0.044206-0;
Sosinska G.J., de Koning L.J., de Groot P.W., Manders E.M.,
Dekker H.L., Hellingwerf K.J., de Koster C.G., Klis F.M.;
"Mass spectrometric quantification of the adaptations in the wall
proteome of Candida albicans in response to ambient pH.";
Microbiology 157:136-146(2011).
[18]
INDUCTION.
PubMed=21456055; DOI=10.1002/yea.1839;
Giacometti R., Kronberg F., Biondi R.M., Passeron S.;
"Candida albicans Tpk1p and Tpk2p isoforms differentially regulate
pseudohyphal development, biofilm structure, cell aggregation and
adhesins expression.";
Yeast 28:293-308(2011).
[19]
SUBCELLULAR LOCATION.
PubMed=22106872; DOI=10.1111/j.1574-695X.2011.00914.x;
Coleman D.A., Oh S.H., Manfra-Maretta S.L., Hoyer L.L.;
"A monoclonal antibody specific for Candida albicans Als4 demonstrates
overlapping localization of Als family proteins on the fungal cell
surface and highlights differences between Als localization in vitro
and in vivo.";
FEMS Immunol. Med. Microbiol. 64:321-333(2012).
[20]
FUNCTION.
PubMed=22321066; DOI=10.1111/j.1574-695X.2012.00941.x;
Aoki W., Kitahara N., Miura N., Morisaka H., Kuroda K., Ueda M.;
"Profiling of adhesive properties of the agglutinin-like sequence
(ALS) protein family, a virulent attribute of Candida albicans.";
FEMS Immunol. Med. Microbiol. 65:121-124(2012).
[21]
FUNCTION, AND INDUCTION.
PubMed=22544909; DOI=10.1128/EC.00103-12;
Fanning S., Xu W., Solis N., Woolford C.A., Filler S.G.,
Mitchell A.P.;
"Divergent targets of Candida albicans biofilm regulator Bcr1 in vitro
and in vivo.";
Eukaryot. Cell 11:896-904(2012).
[22]
DISRUPTION PHENOTYPE.
PubMed=22428031; DOI=10.1371/journal.pone.0033362;
Murciano C., Moyes D.L., Runglall M., Tobouti P., Islam A.,
Hoyer L.L., Naglik J.R.;
"Evaluation of the role of Candida albicans agglutinin-like sequence
(Als) proteins in human oral epithelial cell interactions.";
PLoS ONE 7:E33362-E33362(2012).
[23]
INDUCTION.
PubMed=22545115; DOI=10.1371/journal.pone.0035543;
Li Y., Ma Y., Zhang L., Guo F., Ren L., Yang R., Li Y., Lou H.;
"In vivo inhibitory effect on the biofilm formation of Candida
albicans by liverwort derived riccardin D.";
PLoS ONE 7:E35543-E35543(2012).
[24]
FUNCTION.
PubMed=22429754; DOI=10.1111/j.1439-0507.2012.02188.x;
Monroy-Perez E., Sainz-Espunes T., Paniagua-Contreras G.,
Negrete-Abascal E., Rodriguez-Moctezuma J.R., Vaca S.;
"Frequency and expression of ALS and HWP1 genotypes in Candida
albicans strains isolated from Mexican patients suffering from vaginal
candidosis.";
Mycoses 55:E151-E157(2012).
[25]
FUNCTION.
PubMed=23630968; DOI=10.1128/IAI.00013-13;
Fu Y., Phan Q.T., Luo G., Solis N.V., Liu Y., Cormack B.P.,
Edwards J.E. Jr., Ibrahim A.S., Filler S.G.;
"Investigation of the function of Candida albicans Als3 by
heterologous expression in Candida glabrata.";
Infect. Immun. 81:2528-2535(2013).
[26]
FUNCTION.
PubMed=24152214; DOI=10.1021/la403237f;
Alsteens D., Van Dijck P., Lipke P.N., Dufrene Y.F.;
"Quantifying the forces driving cell-cell adhesion in a fungal
pathogen.";
Langmuir 29:13473-13480(2013).
[27]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=23136884; DOI=10.1111/mmi.12087;
Rohm M., Lindemann E., Hiller E., Ermert D., Lemuth K., Trkulja D.,
Sogukpinar O., Brunner H., Rupp S., Urban C.F., Sohn K.;
"A family of secreted pathogenesis-related proteins in Candida
albicans.";
Mol. Microbiol. 87:132-151(2013).
[28]
INDUCTION.
PubMed=24514088; DOI=10.1128/AAC.01583-13;
Li D.D., Zhao L.X., Mylonakis E., Hu G.H., Zou Y., Huang T.K., Yan L.,
Wang Y., Jiang Y.Y.;
"In vitro and in vivo activities of pterostilbene against Candida
albicans biofilms.";
Antimicrob. Agents Chemother. 58:2344-2355(2014).
[29]
INDUCTION.
PubMed=24623107; DOI=10.1007/s10482-014-0135-2;
Rautela R., Singh A.K., Shukla A., Cameotra S.S.;
"Lipopeptides from Bacillus strain AR2 inhibits biofilm formation by
Candida albicans.";
Antonie Van Leeuwenhoek 105:809-821(2014).
[30]
INDUCTION.
PubMed=24673895; DOI=10.1186/1471-2180-14-80;
Ding X., Liu Z., Su J., Yan D.;
"Human serum inhibits adhesion and biofilm formation in Candida
albicans.";
BMC Microbiol. 14:80-80(2014).
[31]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=24736223; DOI=10.1128/mBio.00911-14;
Dutton L.C., Nobbs A.H., Jepson K., Jepson M.A., Vickerman M.M.,
Aqeel Alawfi S., Munro C.A., Lamont R.J., Jenkinson H.F.;
"O-mannosylation in Candida albicans enables development of
interkingdom biofilm communities.";
MBio 5:E00911-E00911(2014).
[32]
INDUCTION.
PubMed=24466000; DOI=10.1371/journal.pone.0086270;
Delgado-Silva Y., Vaz C., Carvalho-Pereira J., Carneiro C.,
Nogueira E., Correia A., Carreto L., Silva S., Faustino A., Pais C.,
Oliveira R., Sampaio P.;
"Participation of Candida albicans transcription factor RLM1 in cell
wall biogenesis and virulence.";
PLoS ONE 9:E86270-E86270(2014).
[33]
INDUCTION.
PubMed=24796422; DOI=10.1371/journal.pone.0093225;
Feldman M., Al-Quntar A., Polacheck I., Friedman M., Steinberg D.;
"Therapeutic Potential of Thiazolidinedione-8 as an Antibiofilm Agent
against Candida albicans.";
PLoS ONE 9:E93225-E93225(2014).
[34]
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 18-330, AND DISULFIDE BONDS.
PubMed=24802757; DOI=10.1074/jbc.M114.547877;
Lin J., Oh S.H., Jones R., Garnett J.A., Salgado P.S., Rusnakova S.,
Matthews S.J., Hoyer L.L., Cota E.;
"The peptide-binding cavity is essential for Als3-mediated adhesion of
Candida albicans to human cells.";
J. Biol. Chem. 289:18401-18412(2014).
-!- FUNCTION: Cell surface adhesion protein which mediates both yeast-
to-host tissue adherence and yeast aggregation. Plays an important
role in the biofilm formation and pathogenesis of C.albicans
infections. Necessary for C.albicans to bind to N-cadherin on
endothelial cells and E-cadherin on oral epithelial cells and
subsequent endocytosis by these cells. During disseminated
infection, mediates initial trafficking to the brain and renal
cortex and contributes to fungal persistence in the kidneys.
{ECO:0000269|PubMed:15128742, ECO:0000269|PubMed:15256583,
ECO:0000269|PubMed:16839200, ECO:0000269|PubMed:17510860,
ECO:0000269|PubMed:18635358, ECO:0000269|PubMed:22321066,
ECO:0000269|PubMed:22429754, ECO:0000269|PubMed:22544909,
ECO:0000269|PubMed:23630968, ECO:0000269|PubMed:24152214,
ECO:0000269|PubMed:24736223}.
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor
{ECO:0000305|PubMed:12845604}. Secreted, cell wall
{ECO:0000269|PubMed:10417199, ECO:0000269|PubMed:18712765,
ECO:0000269|PubMed:19291169, ECO:0000269|PubMed:20864472,
ECO:0000269|PubMed:22106872, ECO:0000269|PubMed:23136884,
ECO:0000269|PubMed:24736223}. Note=Covers the surface of the germ
tube. {ECO:0000269|PubMed:19291169, ECO:0000269|PubMed:22106872}.
-!- INDUCTION: Expression is under the positive control of the biofilm
regulator BCR1, RLM1, TOR1 and TPK2; and under the negative
control of SFL1. Induced during germ tube formation. Highly
expressed in oropharyngeal candidiasis (OPC), a biofilm-like
infection of the oral mucosa. Induced in the initial stages of
biofilm formation. Down-regulated by human serum, as well as by
bacterial quorum sensing quencher thiazolidinedione-8,
pterostilbene, lipopeptides biosurfactant produced by
B.amyloliquefaciens, and Riccardin D, a macrocyclic bisbibenzyl
isolated from Chinese liverwort D.hirsute, which has an inhibitory
effect on biofilms and virulence. {ECO:0000269|PubMed:15256583,
ECO:0000269|PubMed:15731087, ECO:0000269|PubMed:17766464,
ECO:0000269|PubMed:18683080, ECO:0000269|PubMed:20398368,
ECO:0000269|PubMed:20864472, ECO:0000269|PubMed:21456055,
ECO:0000269|PubMed:22544909, ECO:0000269|PubMed:22545115,
ECO:0000269|PubMed:24466000, ECO:0000269|PubMed:24514088,
ECO:0000269|PubMed:24623107, ECO:0000269|PubMed:24673895,
ECO:0000269|PubMed:24796422}.
-!- DOMAIN: Each ALS protein has a similar three-domain structure,
including a N-ter domain of 433-436 amino acids that is 55-90
percent identical across the family and which mediates adherence
to various materials; a central domain of variable numbers of
tandemly repeated copies of a 36 amino acid motif; and a C-ter;
domain that is relatively variable in length and sequence across
the family. {ECO:0000269|PubMed:15128742}.
-!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
reticulum and serves to target the protein to the cell surface.
There, the glucosamine-inositol phospholipid moiety is cleaved off
and the GPI-modified mannoprotein is covalently attached via its
lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer
cell wall layer. {ECO:0000305|PubMed:12845604}.
-!- DISRUPTION PHENOTYPE: Reduces adhesion and damage to both human
umbilical vein endothelial cells (HUVEC) and oral epithelial
cells. {ECO:0000269|PubMed:15256583, ECO:0000269|PubMed:22428031}.
-!- SIMILARITY: Belongs to the ALS family. {ECO:0000305}.
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EMBL; AY223552; AAO72959.1; -; Genomic_DNA.
EMBL; AY223551; AAO72958.1; -; Genomic_DNA.
EMBL; CP017630; AOW31402.1; -; Genomic_DNA.
RefSeq; XP_710435.2; XM_705343.2.
PDB; 4LE8; X-ray; 1.75 A; A/B=18-316.
PDB; 4LEB; X-ray; 1.40 A; A=18-316.
PDB; 4LEE; X-ray; 3.00 A; A/B/C/D=18-330.
PDBsum; 4LE8; -.
PDBsum; 4LEB; -.
PDBsum; 4LEE; -.
ProteinModelPortal; Q59L12; -.
SMR; Q59L12; -.
PRIDE; Q59L12; -.
GeneID; 3647965; -.
KEGG; cal:CAALFM_CR07070CA; -.
CGD; CAL0000183666; ALS3.
EuPathDB; FungiDB:CR_07070C_A; -.
InParanoid; Q59L12; -.
KO; K22493; -.
OrthoDB; 1428896at2759; -.
PRO; PR:Q59L12; -.
Proteomes; UP000000559; Chromosome R.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IDA:CGD.
GO; GO:0005618; C:cell wall; IBA:GO_Central.
GO; GO:0005576; C:extracellular region; IDA:CGD.
GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0030445; C:yeast-form cell wall; IDA:CGD.
GO; GO:0050839; F:cell adhesion molecule binding; IDA:CGD.
GO; GO:0030985; F:high molecular weight kininogen binding; IDA:CGD.
GO; GO:0044406; P:adhesion of symbiont to host; IMP:CGD.
GO; GO:0007155; P:cell adhesion; IDA:CGD.
GO; GO:0043708; P:cell adhesion involved in biofilm formation; IMP:CGD.
GO; GO:0043710; P:cell adhesion involved in multi-species biofilm formation; IMP:CGD.
GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IMP:CGD.
GO; GO:0098609; P:cell-cell adhesion; IDA:CGD.
GO; GO:0006878; P:cellular copper ion homeostasis; IMP:CGD.
GO; GO:0006897; P:endocytosis; IMP:CGD.
GO; GO:0030260; P:entry into host cell; IDA:CGD.
GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
GO; GO:0009405; P:pathogenesis; IMP:CGD.
GO; GO:0033215; P:reductive iron assimilation; IMP:CGD.
GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
Gene3D; 2.60.40.1280; -; 1.
InterPro; IPR008966; Adhesion_dom_sf.
InterPro; IPR008440; Agglutinin-like_ALS_rpt.
InterPro; IPR024672; Agglutinin-like_N.
InterPro; IPR033504; ALS.
InterPro; IPR011252; Fibrogen-bd_dom1.
PANTHER; PTHR33793; PTHR33793; 3.
Pfam; PF05792; Candida_ALS; 14.
Pfam; PF11766; Candida_ALS_N; 1.
SMART; SM01056; Candida_ALS_N; 1.
SUPFAM; SSF49401; SSF49401; 1.
1: Evidence at protein level;
3D-structure; Cell adhesion; Cell membrane; Cell wall;
Complete proteome; Disulfide bond; Glycoprotein; GPI-anchor;
Lipoprotein; Membrane; Reference proteome; Repeat; Secreted; Signal;
Virulence.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 1134 Agglutinin-like protein 3.
/FTId=PRO_0000420221.
PROPEP 1135 1155 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000429922.
REPEAT 365 396 ALS 1.
REPEAT 401 432 ALS 2.
REPEAT 438 469 ALS 3.
REPEAT 474 505 ALS 4.
REPEAT 510 541 ALS 5.
REPEAT 546 577 ALS 6.
REPEAT 582 613 ALS 7.
REPEAT 618 649 ALS 8.
REPEAT 654 685 ALS 9.
REPEAT 690 721 ALS 10.
REPEAT 726 757 ALS 11.
REPEAT 762 793 ALS 12.
REPEAT 798 829 ALS 13.
REPEAT 834 863 ALS 14.
COMPBIAS 330 1130 Thr-rich.
LIPID 1134 1134 GPI-anchor amidated serine.
{ECO:0000255}.
CARBOHYD 471 471 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 543 543 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 615 615 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 651 651 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 723 723 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 759 759 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 795 795 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 881 881 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1023 1023 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1099 1099 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 73 150 {ECO:0000244|PDB:4LE8,
ECO:0000244|PDB:4LEB,
ECO:0000244|PDB:4LEE,
ECO:0000269|PubMed:24802757}.
DISULFID 96 112 {ECO:0000244|PDB:4LE8,
ECO:0000244|PDB:4LEB,
ECO:0000244|PDB:4LEE,
ECO:0000269|PubMed:24802757}.
DISULFID 205 298 {ECO:0000244|PDB:4LE8,
ECO:0000244|PDB:4LEB,
ECO:0000244|PDB:4LEE,
ECO:0000269|PubMed:24802757}.
DISULFID 227 256 {ECO:0000244|PDB:4LE8,
ECO:0000244|PDB:4LEB,
ECO:0000244|PDB:4LEE,
ECO:0000269|PubMed:24802757}.
VARIANT 628 628 Y -> F (in allele ALS3-2).
{ECO:0000269|PubMed:15256583}.
VARIANT 634 634 I -> V (in allele ALS3-2).
{ECO:0000269|PubMed:15256583}.
VARIANT 640 640 E -> G (in allele ALS3-2).
{ECO:0000269|PubMed:15256583}.
VARIANT 645 645 L -> I (in allele ALS3-2).
{ECO:0000269|PubMed:15256583}.
VARIANT 665 700 Missing (in allele ALS3-2).
{ECO:0000269|PubMed:15256583}.
VARIANT 676 676 G -> E (in allele ALS3-1).
{ECO:0000269|PubMed:15256583}.
VARIANT 743 814 Missing (in allele ALS3-2).
{ECO:0000269|PubMed:15256583}.
VARIANT 814 815 II -> VT (in allele ALS3-1).
{ECO:0000269|PubMed:15256583}.
VARIANT 820 820 E -> G (in allele ALS3-1).
{ECO:0000269|PubMed:15256583}.
VARIANT 843 843 S -> P (in allele ALS3-1).
{ECO:0000269|PubMed:15256583}.
VARIANT 847 847 A -> T (in allele ALS3-1).
{ECO:0000269|PubMed:15256583}.
VARIANT 851 851 T -> I (in allele ALS3-1).
{ECO:0000269|PubMed:15256583}.
VARIANT 935 935 T -> S (in allele ALS3-1).
{ECO:0000269|PubMed:15256583}.
VARIANT 963 963 F -> V (in allele ALS3-1).
{ECO:0000269|PubMed:15256583}.
VARIANT 1062 1062 Q -> P (in allele ALS3-1).
{ECO:0000269|PubMed:15256583}.
CONFLICT 942 942 L -> S (in Ref. 1; AAO72958/AAO72959).
{ECO:0000305}.
STRAND 24 32 {ECO:0000244|PDB:4LEB}.
STRAND 48 57 {ECO:0000244|PDB:4LEB}.
TURN 58 60 {ECO:0000244|PDB:4LEB}.
STRAND 66 72 {ECO:0000244|PDB:4LEB}.
STRAND 74 80 {ECO:0000244|PDB:4LEB}.
STRAND 82 88 {ECO:0000244|PDB:4LEB}.
STRAND 91 99 {ECO:0000244|PDB:4LEB}.
TURN 102 104 {ECO:0000244|PDB:4LEB}.
STRAND 106 114 {ECO:0000244|PDB:4LEB}.
STRAND 123 134 {ECO:0000244|PDB:4LEB}.
STRAND 139 141 {ECO:0000244|PDB:4LEB}.
HELIX 142 147 {ECO:0000244|PDB:4LEB}.
STRAND 153 164 {ECO:0000244|PDB:4LEB}.
STRAND 166 173 {ECO:0000244|PDB:4LEB}.
STRAND 184 190 {ECO:0000244|PDB:4LEB}.
HELIX 191 193 {ECO:0000244|PDB:4LEB}.
STRAND 195 201 {ECO:0000244|PDB:4LEB}.
STRAND 209 238 {ECO:0000244|PDB:4LEB}.
STRAND 251 257 {ECO:0000244|PDB:4LEB}.
STRAND 260 268 {ECO:0000244|PDB:4LEB}.
STRAND 272 284 {ECO:0000244|PDB:4LEB}.
STRAND 287 298 {ECO:0000244|PDB:4LEB}.
STRAND 303 305 {ECO:0000244|PDB:4LEB}.
STRAND 308 313 {ECO:0000244|PDB:4LEB}.
STRAND 321 328 {ECO:0000244|PDB:4LEE}.
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


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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1424: Globo Sphingolipid Metabolism
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining

Related Genes :
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[tat] Protein Tat (Transactivating regulatory protein)
[tat] Protein Tat (Transactivating regulatory protein)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[vpr] Protein Vpr (R ORF protein) (Viral protein R)
[vpr] Protein Vpr (R ORF protein) (Viral protein R)
[vpu] Protein Vpu (U ORF protein) (Viral protein U)
[vif] Virion infectivity factor (Vif) (SOR protein) [Cleaved into: p17; p7]
[vpu] Protein Vpu (U ORF protein) (Viral protein U)
[vif] Virion infectivity factor (Vif) (SOR protein) [Cleaved into: p17; p7]
[rev] Protein Rev (ART/TRS) (Anti-repression transactivator) (Regulator of expression of viral proteins)
[POLR2A POLR2] DNA-directed RNA polymerase II subunit RPB1 (RNA polymerase II subunit B1) (EC 2.7.7.6) (DNA-directed RNA polymerase II subunit A) (DNA-directed RNA polymerase III largest subunit) (RNA-directed RNA polymerase II subunit RPB1) (EC 2.7.7.48)
[rev] Protein Rev (ART/TRS) (Anti-repression transactivator) (Regulator of expression of viral proteins)
[vpr] Protein Vpr (R ORF protein) (Viral protein R)
[vif] Virion infectivity factor (Vif) (SOR protein) [Cleaved into: p17; p7]
[BIRC2 API1 MIHB RNF48] Baculoviral IAP repeat-containing protein 2 (EC 2.3.2.27) (Cellular inhibitor of apoptosis 1) (C-IAP1) (IAP homolog B) (Inhibitor of apoptosis protein 2) (hIAP-2) (hIAP2) (RING finger protein 48) (RING-type E3 ubiquitin transferase BIRC2) (TNFR2-TRAF-signaling complex protein 2)
[vpu] Protein Vpu (U ORF protein) (Viral protein U)

Bibliography :
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