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1,3-beta-glucan synthase component FKS1 (EC 2.4.1.34) (1,3-beta-D-glucan-UDP glucosyltransferase) (Calcineurin dependent protein 1) (Calcofluor white hypersensitivity protein 53) (Echinocandin target gene protein 1) (FK506 sensitivity protein 1) (Glucan synthase of cerevisiae protein 1) (Papulacandin B resistance protein 1)

 FKS1_YEAST              Reviewed;        1876 AA.
P38631; D6VYY0; Q53YZ4; Q6TKS9; Q6TKT0;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
11-DEC-2019, entry version 177.
RecName: Full=1,3-beta-glucan synthase component FKS1;
EC=2.4.1.34;
AltName: Full=1,3-beta-D-glucan-UDP glucosyltransferase;
AltName: Full=Calcineurin dependent protein 1;
AltName: Full=Calcofluor white hypersensitivity protein 53;
AltName: Full=Echinocandin target gene protein 1;
AltName: Full=FK506 sensitivity protein 1;
AltName: Full=Glucan synthase of cerevisiae protein 1;
AltName: Full=Papulacandin B resistance protein 1;
Name=FKS1; Synonyms=CND1, CWH53, ETG1, GLS1, GSC1, PBR1;
OrderedLocusNames=YLR342W; ORFNames=L8300.6;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], TOPOLOGY, AND DISRUPTION PHENOTYPE.
STRAIN=RC118D;
PubMed=7530227; DOI=10.1016/0378-1119(94)90633-5;
Eng W.-K., Faucette L., McLaughlin M.M., Cafferkey R., Koltin Y.,
Morris R.A., Young P.R., Johnson R.K., Livi G.P.;
"The yeast FKS1 gene encodes a novel membrane protein, mutations in which
confer FK506 and cyclosporin A hypersensitivity and calcineurin-dependent
growth.";
Gene 151:61-71(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME, ENZYME ACTIVITY, TOPOLOGY,
AND DISRUPTION PHENOTYPE.
STRAIN=S288c / GRF88;
PubMed=7528927; DOI=10.1073/pnas.91.26.12907;
Douglas C.M., Foor F., Marrinan J.A., Morin N., Nielsen J.B., Dahl A.M.,
Mazur P., Baginsky W., Li W., El-Sherbeini M., Clemas J.A., Mandala S.M.,
Frommer B.R., Kurtz M.B.;
"The Saccharomyces cerevisiae FKS1 (ETG1) gene encodes an integral membrane
protein which is a subunit of 1,3-beta-D-glucan synthase.";
Proc. Natl. Acad. Sci. U.S.A. 91:12907-12911(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND GENE NAME.
STRAIN=ATCC 200589 / A451;
PubMed=7649185; DOI=10.1111/j.1432-1033.1995.0845d.x;
Inoue S.B., Takewaki N., Takasuka T., Mio T., Adachi M., Fujii Y.,
Miyamoto C., Arisawa M., Furuichi Y., Watanabe T.;
"Characterization and gene cloning of 1,3-beta-D-glucan synthase from
Saccharomyces cerevisiae.";
Eur. J. Biochem. 231:845-854(1995).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND GENE NAME.
STRAIN=S288c / GRF88;
PubMed=7828729; DOI=10.1016/0014-5793(94)01418-z;
Ram A.F.J., Brekelmans S.S.C., Oehlen L.J.W.M., Klis F.M.;
"Identification of two cell cycle regulated genes affecting the beta 1,3-
glucan content of cell walls in Saccharomyces cerevisiae.";
FEBS Lett. 358:165-170(1995).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME, ENZYME ACTIVITY, AND
DISRUPTION PHENOTYPE.
STRAIN=S288c / GRF88;
PubMed=7592316; DOI=10.1128/jb.177.20.5732-5739.1995;
Castro C., Ribas J.C., Valdivieso M.H., Varona R., del Rey F., Duran A.;
"Papulacandin B resistance in budding and fission yeasts: isolation and
characterization of a gene involved in (1,3)beta-D-glucan synthesis in
Saccharomyces cerevisiae.";
J. Bacteriol. 177:5732-5739(1995).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 204508 / S288c;
PubMed=7542741; DOI=10.1128/mcb.15.8.4103;
Garrett-Engele P., Moilanen B., Cyert M.S.;
"Calcineurin, the Ca2+/calmodulin-dependent protein phosphatase, is
essential in yeast mutants with cell integrity defects and in mutants that
lack a functional vacuolar H(+)-ATPase.";
Mol. Cell. Biol. 15:4103-4114(1995).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], TOPOLOGY, MUTAGENESIS OF ASN-470 AND
LEU-642, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC 96519 / YPH250;
PubMed=14693557; DOI=10.1128/aac.48.1.319-322.2004;
Ohyama T., Miyakoshi S., Isono F.;
"FKS1 mutations responsible for selective resistance of Saccharomyces
cerevisiae to the novel 1,3-beta-glucan synthase inhibitor arborcandin C.";
Antimicrob. Agents Chemother. 48:319-322(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
Zollner A., Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[9]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
G3 (Bethesda) 4:389-398(2014).
[10]
DISRUPTION PHENOTYPE.
PubMed=7510323; DOI=10.1099/00221287-139-12-2973;
Parent S.A., Nielsen J.B., Morin N., Chrebet G., Ramadan N., Dahl A.M.,
Hsu M.J., Bostian K.A., Foor F.;
"Calcineurin-dependent growth of an FK506- and CsA-hypersensitive mutant of
Saccharomyces cerevisiae.";
J. Gen. Microbiol. 139:2973-2984(1993).
[11]
INDUCTION.
PubMed=7565718; DOI=10.1128/mcb.15.10.5671;
Mazur P., Morin N., Baginsky W., el-Sherbeini M., Clemas J.A.,
Nielsen J.B., Foor F.;
"Differential expression and function of two homologous subunits of yeast
1,3-beta-D-glucan synthase.";
Mol. Cell. Biol. 15:5671-5681(1995).
[12]
ENZYME ACTIVITY, AND INTERACTION WITH RHO1.
PubMed=8662910; DOI=10.1074/jbc.271.24.14604;
Mazur P., Baginsky W.;
"In vitro activity of 1,3-beta-D-glucan synthase requires the GTP-binding
protein Rho1.";
J. Biol. Chem. 271:14604-14609(1996).
[13]
INTERACTION WITH RHO1, AND SUBCELLULAR LOCATION.
PubMed=8602515; DOI=10.1126/science.272.5259.279;
Qadota H., Python C.P., Inoue S.B., Arisawa M., Anraku Y., Zheng Y.,
Watanabe T., Levin D.E., Ohya Y.;
"Identification of yeast Rho1p GTPase as a regulatory subunit of 1,3-beta-
glucan synthase.";
Science 272:279-281(1996).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11856368; DOI=10.1046/j.1356-9597.2001.00495.x;
Utsugi T., Minemura M., Hirata A., Abe M., Watanabe D., Ohya Y.;
"Movement of yeast 1,3-beta-glucan synthase is essential for uniform cell
wall synthesis.";
Genes Cells 7:1-9(2002).
[15]
ENZYME ACTIVITY, AND MUTAGENESIS OF LYS-877; ALA-899 AND GLN-977.
PubMed=12399379;
Sekiya-Kawasaki M., Abe M., Saka A., Watanabe D., Kono K.,
Minemura-Asakawa M., Ishihara S., Watanabe T., Ohya Y.;
"Dissection of upstream regulatory components of the Rho1p effector, 1,3-
beta-glucan synthase, in Saccharomyces cerevisiae.";
Genetics 162:663-676(2002).
[16]
ENZYME ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-146; VAL-302;
TYR-329; TYR-335; THR-605; ILE-713; ILE-722; MET-761; ALA-823; THR-828;
ILE-853; LEU-855; LEU-872; LYS-877; ALA-899; GLU-907; ASP-920; ALA-932;
GLU-934; GLN-977; ASN-982; PHE-1020; ILE-1047; GLU-1111; PHE-1258 AND
ASN-1520.
PubMed=12185837; DOI=10.1002/yea.866;
Dijkgraaf G.J.P., Abe M., Ohya Y., Bussey H.;
"Mutations in Fks1p affect the cell wall content of beta-1,3- and beta-1,6-
glucan in Saccharomyces cerevisiae.";
Yeast 19:671-690(2002).
[17]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-910, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=14557538; DOI=10.1073/pnas.2135500100;
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
"A subset of membrane-associated proteins is ubiquitinated in response to
mutations in the endoplasmic reticulum degradation machinery.";
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
[18]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
STRAIN=ATCC 76625 / YPH499;
PubMed=14576278; DOI=10.1073/pnas.2135385100;
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
Pfanner N., Meisinger C.;
"The proteome of Saccharomyces cerevisiae mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
[19]
CASPOFUNGIN HYPERSENSITIVITY.
PubMed=15166135; DOI=10.1534/genetics.167.1.35;
Lesage G., Sdicu A.-M., Menard P., Shapiro J., Hussein S., Bussey H.;
"Analysis of beta-1,3-glucan assembly in Saccharomyces cerevisiae using a
synthetic interaction network and altered sensitivity to caspofungin.";
Genetics 167:35-49(2004).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome
analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-269 AND THR-272, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides insights
into evolution.";
Science 325:1682-1686(2009).
[22]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-259; LYS-275; LYS-386;
LYS-910; LYS-915; LYS-1539 AND LYS-1547, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
-!- FUNCTION: Alternate catalytic subunit of the 1,3-beta-glucan synthase
(GS). Synthesizes 1,3-beta-glucan, a major structural component of the
yeast cell wall. Involved in cell wall synthesis, maintenance and cell
wall remodeling. {ECO:0000269|PubMed:11856368}.
-!- CATALYTIC ACTIVITY:
Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-
COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378,
ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34;
Evidence={ECO:0000269|PubMed:12185837, ECO:0000269|PubMed:12399379,
ECO:0000269|PubMed:7528927, ECO:0000269|PubMed:7592316,
ECO:0000269|PubMed:8662910};
-!- SUBUNIT: Component of the 1,3-beta-glucan synthase (GS), composed of
two alternate catalytic subunits FKS1 or GSC2, and a regulatory subunit
RHO1. Interacts with RHO1, which is a GTP-binding protein.
{ECO:0000269|PubMed:8602515, ECO:0000269|PubMed:8662910}.
-!- INTERACTION:
P06780:RHO1; NbExp=3; IntAct=EBI-7708, EBI-15121;
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11856368,
ECO:0000269|PubMed:12185837, ECO:0000269|PubMed:14576278,
ECO:0000269|PubMed:8602515}. Cell membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000305}. Note=Localizes to the sites of
polarized growth. Colocalizes with cortical actin patches and moves on
the cell surface at the sites of cell wall remodeling. Actin patch
motility is required for the movement. Early at the cell cycle,
localizes at the presumed bud site of the mother cell and at the tip of
the small bud. As the bud enlarges, appears as discernible spots in the
medium-sized bud and these spots colocalize with actin patches. Late in
the cell cycle, disappears in large budded cells, while the actin
patches disperse over the cell. During cytokinesis, is concentrated in
the neck, overlapping with the location of cortical actin patches.
-!- INDUCTION: During vegetative growth. Expressed periodically during the
cell cycle. {ECO:0000269|PubMed:7565718}.
-!- DISRUPTION PHENOTYPE: Cells are hypersensitive to immunosuppressant
drugs FK506 and cyclosporin A (CsA) due to the inhibition of
calcineurin phosphatase activity by the receptor-drug complexes and is
dependent on calcineurin for vegetative growth. It confers a slow
growth phenotype which is partially suppressed by exogenously added
Ca(2+) and exacerbated by EGTA. Simultaneous disruption of CNA1 and
CNA2 or CNB1 is lethal in FKS1-1. Disruption of FPR1 or CPR1 results in
the loss of hypersensitivity. Overexpression of CNA1 or CNA2, in
conjunction with CNB1, results in a significant decrease in
hypersensitivity to FK506 and CsA. FKS1-8 mutant is sensitive to FK506
and cyclosporin A, has increased tendency to lyse and exhibits slow
growth that is improved by the addition of osmotic stabilizing agents.
It is more sensitive to the drugs when grown on galactose compared to
dextrose. ETG1-1 mutant is resistant to the cell wall active
echinocandins, which are inhibitors of 1,3-beta-D-glucan synthase.
ETG1-4 mutant is hypersensitive to the chitin synthase inhibitor
nikkomycin Z. Deletion of FKS1 leads to hypersensitivity to
echinocandin-like antifungal lipopeptide caspofungin, a 1,3-beta-glucan
synthase inhibitor. Deletion mutant also displays a 30% reduction in
1,3-beta-glucan and 15% reduction in alkali-insoluble 1,6-beta-glucan
compared to wild-type. {ECO:0000269|PubMed:14693557,
ECO:0000269|PubMed:7510323, ECO:0000269|PubMed:7528927,
ECO:0000269|PubMed:7530227, ECO:0000269|PubMed:7542741,
ECO:0000269|PubMed:7592316}.
-!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
{ECO:0000305}.
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EMBL; U08459; AAC13763.1; -; Genomic_DNA.
EMBL; U12893; AAC48981.1; -; Genomic_DNA.
EMBL; D42126; BAA07706.1; -; Genomic_DNA.
EMBL; X80817; CAA56783.1; -; Genomic_DNA.
EMBL; Z46262; CAA86404.1; -; Genomic_DNA.
EMBL; L35923; AAA79760.1; -; Genomic_DNA.
EMBL; AY395693; AAR86935.1; -; Genomic_DNA.
EMBL; AY395694; AAR86936.1; -; Genomic_DNA.
EMBL; AY395695; AAR86937.1; -; Genomic_DNA.
EMBL; U19028; AAB67256.1; -; Genomic_DNA.
EMBL; BK006945; DAA09646.1; -; Genomic_DNA.
PIR; S50235; S50235.
RefSeq; NP_013446.1; NM_001182231.1.
BioGrid; 31604; 516.
ComplexPortal; CPX-1812; 1,3-beta-D-glucan synthase complex.
DIP; DIP-5749N; -.
IntAct; P38631; 68.
MINT; P38631; -.
STRING; 4932.YLR342W; -.
CAZy; GT48; Glycosyltransferase Family 48.
TCDB; 9.B.119.1.1; the glycan synthase, fks1 (fks1) family.
iPTMnet; P38631; -.
MaxQB; P38631; -.
PaxDb; P38631; -.
PRIDE; P38631; -.
EnsemblFungi; YLR342W_mRNA; YLR342W; YLR342W.
GeneID; 851055; -.
KEGG; sce:YLR342W; -.
EuPathDB; FungiDB:YLR342W; -.
SGD; S000004334; FKS1.
HOGENOM; HOG000216604; -.
InParanoid; P38631; -.
KO; K00706; -.
OMA; YHQVDAG; -.
BioCyc; YEAST:YLR342W-MONOMER; -.
PRO; PR:P38631; -.
Proteomes; UP000002311; Chromosome XII.
RNAct; P38631; protein.
GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IDA:SGD.
GO; GO:0030479; C:actin cortical patch; IDA:SGD.
GO; GO:0071944; C:cell periphery; HDA:SGD.
GO; GO:0005933; C:cellular bud; HDA:SGD.
GO; GO:0005935; C:cellular bud neck; IDA:SGD.
GO; GO:0005934; C:cellular bud tip; IDA:SGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005739; C:mitochondrion; HDA:SGD.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IDA:SGD.
GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IDA:SGD.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0045807; P:positive regulation of endocytosis; IMP:SGD.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
GO; GO:0008361; P:regulation of cell size; IMP:SGD.
InterPro; IPR026899; FKS1-like_dom1.
InterPro; IPR003440; Glyco_trans_48.
Pfam; PF14288; FKS1_dom1; 1.
Pfam; PF02364; Glucan_synthase; 1.
SMART; SM01205; FKS1_dom1; 1.
1: Evidence at protein level;
Cell membrane; Cell shape; Cell wall biogenesis/degradation;
Glycosyltransferase; Isopeptide bond; Membrane; Mitochondrion;
Phosphoprotein; Reference proteome; Transferase; Transmembrane;
Transmembrane helix; Ubl conjugation.
CHAIN 1..1876
/note="1,3-beta-glucan synthase component FKS1"
/id="PRO_0000121725"
TOPO_DOM 1..454
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 455..475
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 476..492
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 493..513
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 514..531
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 532..552
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 553..563
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 564..584
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 585..621
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 622..642
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 643..678
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 679..699
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 700..1358
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 1359..1379
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1380..1444
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 1445..1465
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1466..1469
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 1470..1490
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1491..1560
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 1561..1581
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1582..1601
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 1602..1622
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1623..1643
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 1644..1664
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1665..1672
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 1673..1695
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1696..1802
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 1803..1823
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1824..1876
/note="Cytoplasmic"
/evidence="ECO:0000255"
MOD_RES 269
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:19779198"
MOD_RES 272
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:19779198"
CROSSLNK 259
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000244|PubMed:22106047"
CROSSLNK 275
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000244|PubMed:22106047"
CROSSLNK 386
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000244|PubMed:22106047"
CROSSLNK 910
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000244|PubMed:22106047"
CROSSLNK 915
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000244|PubMed:22106047"
CROSSLNK 1539
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000244|PubMed:22106047"
CROSSLNK 1547
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000244|PubMed:22106047"
MUTAGEN 146
/note="E->V: In 1132; temperature-sensitive mutant; no
gross alteration in beta-glucan content of cells; when
associated with N-329; N-335 and DEL-GSC2."
/evidence="ECO:0000269|PubMed:12185837"
MUTAGEN 302
/note="V->N: In 1082; temperature-sensitive mutant; no
gross alteration in beta-glucan content of cells; when
associated with DEL-GSC2."
/evidence="ECO:0000269|PubMed:12185837"
MUTAGEN 329
/note="Y->N: In 1132; temperature-sensitive mutant; no
gross alteration in beta-glucan content of cells; when
associated with V-146; N-335 and DEL-GSC2."
/evidence="ECO:0000269|PubMed:12185837"
MUTAGEN 335
/note="Y->N: In 1132; temperature-sensitive mutant; no
gross alteration in beta-glucan content of cells; when
associated with V-146; N-329 and DEL-GSC2."
/evidence="ECO:0000269|PubMed:12185837"
MUTAGEN 470
/note="N->K: In ACR79-5; selectively resistant to
antibiotic arborcandin C."
/evidence="ECO:0000269|PubMed:14693557"
MUTAGEN 605
/note="T->I: In 1093; temperature-sensitive mutant; higher
beta-glucan content of cells; when associated with T-761
and DEL-GSC2."
/evidence="ECO:0000269|PubMed:12185837"
MUTAGEN 642
/note="L->S: In ACR1A3; selectively resistant to antibiotic
arborcandin C."
/evidence="ECO:0000269|PubMed:14693557"
MUTAGEN 713
/note="I->L: In 1163; temperature-sensitive mutant; no
gross alteration in beta-glucan content of cells; when
associated with V-722 and DEL-GSC2."
/evidence="ECO:0000269|PubMed:12185837"
MUTAGEN 722
/note="I->V: In 1163; temperature-sensitive mutant; no
gross alteration in beta-glucan content of cells; when
associated with L-713 and DEL-GSC2."
/evidence="ECO:0000269|PubMed:12185837"
MUTAGEN 761
/note="M->T: In 1093; temperature-sensitive mutant; higher
beta-glucan content of cells; when associated with I-605
and DEL-GSC2."
/evidence="ECO:0000269|PubMed:12185837"
MUTAGEN 823
/note="A->V: In 1104; temperature-sensitive mutant; lower
beta-glucan content of cells; when associated with E-920
and DEL-GSC2."
/evidence="ECO:0000269|PubMed:12185837"
MUTAGEN 828
/note="T->A: In 1014; temperature-sensitive mutant; no
gross alteration in beta-glucan content of cells; partially
K1 killer toxin-sensitive; when associated with DEL-GSC2."
/evidence="ECO:0000269|PubMed:12185837"
MUTAGEN 853
/note="I->T: In 1114; temperature-sensitive mutant; lower
beta-glucan content of cells; when associated with G-932;
D-934; Y-1020; N-1047 and DEL-GSC2."
/evidence="ECO:0000269|PubMed:12185837"
MUTAGEN 855
/note="L->R: In A6; temperature-sensitive mutant; lower
beta-glucan content of cells; when associated with DEL-
GSC2."
/evidence="ECO:0000269|PubMed:12185837"
MUTAGEN 872
/note="L->F: In 1144; temperature-sensitive mutant; lower
beta-glucan content of cells; when associated with K-907;
S-982 and DEL-GSC2."
/evidence="ECO:0000269|PubMed:12185837"
MUTAGEN 877
/note="K->N: In 1154; temperature-sensitive mutant which is
able to grow at 25 degrees Celsius but fails to grow at
temperatures above 35 degrees Celsius; defective in 1,3-
beta-glucan synthesis and thus has lower beta-glucan
content; hypersensitive to echinocandin B and to a chitin-
binding reagent, Calcofluor white; fails to grow in a low
glucose medium; when associated with S-899; P-977 and DEL-
GSC2."
/evidence="ECO:0000269|PubMed:12185837,
ECO:0000269|PubMed:12399379"
MUTAGEN 899
/note="A->S: In 1154; temperature-sensitive mutant which is
able to grow at 25 degrees Celsius but fails to grow at
temperatures above 35 degrees Celsius; defective in 1,3-
beta-glucan synthesis and thus has lower beta-glucan
content; hypersensitive to echinocandin B and to a chitin-
binding reagent, Calcofluor white; fails to grow in a low
glucose medium; when associated with N-877; P-977 and DEL-
GSC2."
/evidence="ECO:0000269|PubMed:12185837,
ECO:0000269|PubMed:12399379"
MUTAGEN 907
/note="E->K: In 1144; temperature-sensitive mutant; lower
beta-glucan content of cells; when associated with F-872;
S-982 and DEL-GSC2."
/evidence="ECO:0000269|PubMed:12185837"
MUTAGEN 920
/note="D->E: In 1104; temperature-sensitive mutant; lower
beta-glucan content of cells; when associated with V-823
and DEL-GSC2."
/evidence="ECO:0000269|PubMed:12185837"
MUTAGEN 932
/note="A->G: In 1114; temperature-sensitive mutant; lower
beta-glucan content of cells; when associated with T-853;
D-934; Y-1020; N-1047 and DEL-GSC2."
/evidence="ECO:0000269|PubMed:12185837"
MUTAGEN 934
/note="E->D: In 1114; temperature-sensitive mutant; lower
beta-glucan content of cells; when associated with T-853;
G-932; Y-1020; N-1047 and DEL-GSC2."
/evidence="ECO:0000269|PubMed:12185837"
MUTAGEN 977
/note="Q->P: In 1154; temperature-sensitive mutant which is
able to grow at 25 degrees Celsius but fails to grow at
temperatures above 35 degrees Celsius; defective in 1,3-
beta-glucan synthesis and thus has lower beta-glucan
content; hypersensitive to echinocandin B and to a chitin-
binding reagent, Calcofluor white; fails to grow in a low
glucose medium; when associated with N-877; S-899 and DEL-
GSC2."
/evidence="ECO:0000269|PubMed:12185837,
ECO:0000269|PubMed:12399379"
MUTAGEN 982
/note="N->S: In 1144; temperature-sensitive mutant; lower
beta-glucan content of cells; when associated with F-872;
K-907 and DEL-GSC2."
/evidence="ECO:0000269|PubMed:12185837"
MUTAGEN 1020
/note="F->Y: In 1114; temperature-sensitive mutant; lower
beta-glucan content of cells; when associated with T-853;
G-932; D-934; N-1047 and DEL-GSC2."
/evidence="ECO:0000269|PubMed:12185837"
MUTAGEN 1047
/note="I->N: In 1114; temperature-sensitive mutant; lower
beta-glucan content of cells; when associated with T-853;
G-932; D-934; Y-1020 and DEL-GSC2."
/evidence="ECO:0000269|PubMed:12185837"
MUTAGEN 1111
/note="E->G: In F4; temperature-sensitive mutant; lower
beta-glucan content of cells; when associated with DEL-
GSC2."
/evidence="ECO:0000269|PubMed:12185837"
MUTAGEN 1258
/note="F->Y: In 1125; temperature-sensitive mutant; lower
beta-glucan content of cells and partially K1 killer toxin-
resistant; when associated with D-1520 and DEL-GSC2."
/evidence="ECO:0000269|PubMed:12185837"
MUTAGEN 1520
/note="N->D: In 1125; temperature-sensitive mutant; lower
beta-glucan content of cells and partial K1 killer toxin-
resistant phenotype; when associated with Y-1258 and DEL-
GSC2."
/evidence="ECO:0000269|PubMed:12185837"
CONFLICT 19
/note="G -> D (in Ref. 1; AAC13763, 6; AAA79760 and 7;
AAR86935/AAR86936/AAR86937)"
/evidence="ECO:0000305"
CONFLICT 113
/note="A -> P (in Ref. 1; AAC13763, 6; AAA79760 and 7;
AAR86935/AAR86936/AAR86937)"
/evidence="ECO:0000305"
CONFLICT 236
/note="I -> V (in Ref. 1; AAC13763, 6; AAA79760 and 7;
AAR86935/AAR86936/AAR86937)"
/evidence="ECO:0000305"
CONFLICT 373
/note="V -> I (in Ref. 1; AAC13763, 6; AAA79760 and 7;
AAR86935/AAR86936/AAR86937)"
/evidence="ECO:0000305"
CONFLICT 437
/note="K -> T (in Ref. 1; AAC13763)"
/evidence="ECO:0000305"
CONFLICT 470
/note="N -> K (in Ref. 7; AAR86936)"
/evidence="ECO:0000305"
CONFLICT 492
/note="K -> R (in Ref. 1; AAC13763, 6; AAA79760 and 7;
AAR86935/AAR86936/AAR86937)"
/evidence="ECO:0000305"
CONFLICT 642
/note="L -> S (in Ref. 7; AAR86937)"
/evidence="ECO:0000305"
CONFLICT 1341
/note="V -> F (in Ref. 1; AAC13763, 6; AAA79760 and 7;
AAR86935/AAR86936/AAR86937)"
/evidence="ECO:0000305"
CONFLICT 1457
/note="M -> I (in Ref. 1; AAC13763, 6; AAA79760 and 7;
AAR86935/AAR86936/AAR86937)"
/evidence="ECO:0000305"
CONFLICT 1790
/note="T -> S (in Ref. 1; AAC13763, 6; AAA79760 and 7;
AAR86935/AAR86936/AAR86937)"
/evidence="ECO:0000305"
CONFLICT 1827..1828
/note="KH -> DQ (in Ref. 1; AAC13763, 6; AAA79760 and 7;
AAR86935/AAR86936/AAR86937)"
/evidence="ECO:0000305"
CONFLICT 1834
/note="D -> T (in Ref. 1; AAC13763, 6; AAA79760 and 7;
AAR86935/AAR86936/AAR86937)"
/evidence="ECO:0000305"
CONFLICT 1844
/note="I -> V (in Ref. 1; AAC13763, 6; AAA79760 and 7;
AAR86935/AAR86936/AAR86937)"
/evidence="ECO:0000305"
CONFLICT 1853
/note="S -> F (in Ref. 1; AAC13763, 6; AAA79760 and 7;
AAR86935/AAR86936/AAR86937)"
/evidence="ECO:0000305"
SEQUENCE 1876 AA; 214851 MW; AD4B4CB8CB28B5D8 CRC64;
MNTDQQPYQG QTDYTQGPGN GQSQEQDYDQ YGQPLYPSQA DGYYDPNVAA GTEADMYGQQ
PPNESYDQDY TNGEYYGQPP NMAAQDGENF SDFSSYGPPG TPGYDSYGGQ YTASQMSYGE
PNSSGTSTPI YGNYDPNAIA MALPNEPYPA WTADSQSPVS IEQIEDIFID LTNRLGFQRD
SMRNMFDHFM VLLDSRSSRM SPDQALLSLH ADYIGGDTAN YKKWYFAAQL DMDDEIGFRN
MSLGKLSRKA RKAKKKNKKA MEEANPEDTE ETLNKIEGDN SLEAADFRWK AKMNQLSPLE
RVRHIALYLL CWGEANQVRF TAECLCFIYK CALDYLDSPL CQQRQEPMPE GDFLNRVITP
IYHFIRNQVY EIVDGRFVKR ERDHNKIVGY DDLNQLFWYP EGIAKIVLED GTKLIELPLE
ERYLRLGDVV WDDVFFKTYK ETRTWLHLVT NFNRIWVMHI SIFWMYFAYN SPTFYTHNYQ
QLVDNQPLAA YKWASCALGG TVASLIQIVA TLCEWSFVPR KWAGAQHLSR RFWFLCIIFG
INLGPIIFVF AYDKDTVYST AAHVVAAVMF FVAVATIIFF SIMPLGGLFT SYMKKSTRRY
VASQTFTAAF APLHGLDRWM SYLVWVTVFA AKYSESYYFL VLSLRDPIRI LSTTAMRCTG
EYWWGAVLCK VQPKIVLGLV IATDFILFFL DTYLWYIIVN TIFSVGKSFY LGISILTPWR
NIFTRLPKRI YSKILATTDM EIKYKPKVLI SQVWNAIIIS MYREHLLAID HVQKLLYHQV
PSEIEGKRTL RAPTFFVSQD DNNFETEFFP RDSEAERRIS FFAQSLSTPI PEPLPVDNMP
TFTVLTPHYA ERILLSLREI IREDDQFSRV TLLEYLKQLH PVEWECFVKD TKILAEETAA
YEGNENEAEK EDALKSQIDD LPFYCIGFKS AAPEYTLRTR IWASLRSQTL YRTISGFMNY
SRAIKLLYRV ENPEIVQMFG GNAEGLEREL EKMARRKFKF LVSMQRLAKF KPHELENAEF
LLRAYPDLQI AYLDEEPPLT EGEEPRIYSA LIDGHCEILD NGRRRPKFRV QLSGNPILGD
GKSDNQNHAL IFYRGEYIQL IDANQDNYLE ECLKIRSVLA EFEELNVEQV NPYAPGLRYE
EQTTNHPVAI VGAREYIFSE NSGVLGDVAA GKEQTFGTLF ARTLSQIGGK LHYGHPDFIN
ATFMTTRGGV SKAQKGLHLN EDIYAGMNAM LRGGRIKHCE YYQCGKGRDL GFGTILNFTT
KIGAGMGEQM LSREYYYLGT QLPVDRFLTF YYAHPGFHLN NLFIQLSLQM FMLTLVNLSS
LAHESIMCIY DRNKPKTDVL VPIGCYNFQP AVDWVRRYTL SIFIVFWIAF VPIVVQELIE
RGLWKATQRF FCHLLSLSPM FEVFAGQIYS SALLSDLAIG GARYISTGRG FATSRIPFSI
LYSRFAGSAI YMGARSMLML LFGTVAHWQA PLLWFWASLS SLIFAPFVFN PHQFAWEDFF
LDYRDYIRWL SRGNNQYHRN SWIGYVRMSR ARITGFKRKL VGDESEKAAG DASRAHRTNL
IMAEIIPCAI YAAGCFIAFT FINAQTGVKT TDDDRVNSVL RIIICTLAPI AVNLGVLFFC
MGMSCCSGPL FGMCCKKTGS VMAGIAHGVA VIVHIAFFIV MWVLESFNFV RMLIGVVTCI
QCQRLIFHCM TALMLTREFK NDHANTAFWT GKWYGKGMGY MAWTQPSREL TAKVIELSEF
AADFVLGHVI LICQLPLIII PKIDKFHSIM LFWLKPSRQI RPPIYSLKQT RLRKRMVKKY
CSLYFLVLAI FAGCIIGPAV ASAKIHKHIG DSLDGVVHNL FQPINTTNND TGSQMSTYQS
HYYTHTPSLK TWSTIK


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