P38631 (FKS1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
1,3-beta-glucan synthase component FKS1
EC=2.4.1.34

Alternative name(s):
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

Gene names

Name:	FKS1
Synonyms:	CND1, CWH53, ETG1, GLS1, GSC1, PBR1
Ordered Locus Names:	YLR342W
ORF Names:	L8300.6

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1876 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.14
Catalytic activity	UDP-glucose + ((1->3)-beta-D-glucosyl)(n) = UDP + ((1->3)-beta-D-glucosyl)(n+1). Ref.2 Ref.5 Ref.12 Ref.15 Ref.16
Subunit structure	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. Ref.12 Ref.13
Subcellular location	Mitochondrion. Cell membrane; Multi-pass membrane protein Potential. Note: Localizes to the sites of polarized growth. Co-localizes 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 co-localize 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. Ref.13 Ref.14 Ref.16 Ref.18 Ref.20
Induction	During vegetative growth. Expressed periodically during the cell cycle. Ref.11
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 Ca2+ 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. Ref.1 Ref.2 Ref.5 Ref.6 Ref.7 Ref.10
Sequence similarities	Belongs to the glycosyltransferase 48 family.

Ontologies

Keywords
Biological process	Cell shape Cell wall biogenesis/degradation
Cellular component	Cell membrane Membrane Mitochondrion
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	(1->3)-beta-D-glucan biosynthetic process Inferred from direct assay Ref.2. Source: SGD cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of endocytosis Inferred from mutant phenotype. Source: SGD regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell size Inferred from mutant phenotype. Source: SGD
Cellular component	1,3-beta-D-glucan synthase complex Inferred from direct assay. Source: SGD actin cap Traceable author statement. Source: SGD actin cortical patch Inferred from direct assay Ref.14. Source: SGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane fraction Inferred from direct assay. Source: SGD mitochondrion Inferred from direct assay Ref.20. Source: SGD
Molecular function	1,3-beta-D-glucan synthase activity Inferred from direct assay Ref.3. Source: SGD protein binding Inferred from physical interaction Ref.13. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RHO1	P06780	3	EBI-7708,EBI-15121

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1876	1876	1,3-beta-glucan synthase component FKS1		PRO_0000121725
Regions
	Topological domain	1 – 454	454	Cytoplasmic Potential
	Transmembrane	455 – 475	21	Helical; Potential
	Topological domain	476 – 492	17	Extracellular Potential
	Transmembrane	493 – 513	21	Helical; Potential
	Topological domain	514 – 531	18	Cytoplasmic Potential
	Transmembrane	532 – 552	21	Helical; Potential
	Topological domain	553 – 563	11	Extracellular Potential
	Transmembrane	564 – 584	21	Helical; Potential
	Topological domain	585 – 621	37	Cytoplasmic Potential
	Transmembrane	622 – 642	21	Helical; Potential
	Topological domain	643 – 678	36	Extracellular Potential
	Transmembrane	679 – 699	21	Helical; Potential
	Topological domain	700 – 1358	659	Cytoplasmic Potential
	Transmembrane	1359 – 1379	21	Helical; Potential
	Topological domain	1380 – 1444	65	Extracellular Potential
	Transmembrane	1445 – 1465	21	Helical; Potential
	Topological domain	1466 – 1469	4	Cytoplasmic Potential
	Transmembrane	1470 – 1490	21	Helical; Potential
	Topological domain	1491 – 1560	70	Extracellular Potential
	Transmembrane	1561 – 1581	21	Helical; Potential
	Topological domain	1582 – 1601	20	Cytoplasmic Potential
	Transmembrane	1602 – 1622	21	Helical; Potential
	Topological domain	1623 – 1643	21	Extracellular Potential
	Transmembrane	1644 – 1664	21	Helical; Potential
	Topological domain	1665 – 1672	8	Cytoplasmic Potential
	Transmembrane	1673 – 1695	23	Helical; Potential
	Topological domain	1696 – 1802	107	Extracellular Potential
	Transmembrane	1803 – 1823	21	Helical; Potential
	Topological domain	1824 – 1876	53	Cytoplasmic Potential
Amino acid modifications
	Modified residue	269	1	Phosphothreonine Ref.21
	Cross-link	910		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.17
Experimental info
	Mutagenesis	146	1	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. Ref.16
	Mutagenesis	302	1	V → N in 1082; temperature-sensitive mutant; no gross alteration in beta-glucan content of cells; when associated with DEL-GSC2. Ref.16
	Mutagenesis	329	1	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. Ref.16
	Mutagenesis	335	1	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. Ref.16
	Mutagenesis	470	1	N → K in ACR79-5; selectively resistant to antibiotic arborcandin C. Ref.7
	Mutagenesis	605	1	T → I in 1093; temperature-sensitive mutant; higher beta-glucan content of cells; when associated with T-761 and DEL-GSC2. Ref.16
	Mutagenesis	642	1	L → S in ACR1A3; selectively resistant to antibiotic arborcandin C. Ref.7
	Mutagenesis	713	1	I → L in 1163; temperature-sensitive mutant; no gross alteration in beta-glucan content of cells; when associated with V-722 and DEL-GSC2. Ref.16
	Mutagenesis	722	1	I → V in 1163; temperature-sensitive mutant; no gross alteration in beta-glucan content of cells; when associated with L-713 and DEL-GSC2. Ref.16
	Mutagenesis	761	1	M → T in 1093; temperature-sensitive mutant; higher beta-glucan content of cells; when associated with I-605 and DEL-GSC2. Ref.16
	Mutagenesis	823	1	A → V in 1104; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with E-920 and DEL-GSC2. Ref.16
	Mutagenesis	828	1	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. Ref.16
	Mutagenesis	853	1	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. Ref.16
	Mutagenesis	855	1	L → R in A6; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with DEL-GSC2. Ref.16
	Mutagenesis	872	1	L → F in 1144; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with K-907; S-982 and DEL-GSC2. Ref.16
	Mutagenesis	877	1	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. Ref.15 Ref.16
	Mutagenesis	899	1	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. Ref.15 Ref.16
	Mutagenesis	907	1	E → K in 1144; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with F-872; S-982 and DEL-GSC2. Ref.16
	Mutagenesis	920	1	D → E in 1104; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with V-823 and DEL-GSC2. Ref.16
	Mutagenesis	932	1	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. Ref.16
	Mutagenesis	934	1	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. Ref.16
	Mutagenesis	977	1	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. Ref.15 Ref.16
	Mutagenesis	982	1	N → S in 1144; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with F-872; K-907 and DEL-GSC2. Ref.16
	Mutagenesis	1020	1	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. Ref.16
	Mutagenesis	1047	1	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. Ref.16
	Mutagenesis	1111	1	E → G in F4; temperature-sensitive mutant; lower beta-glucan content of cells; when associated with DEL-GSC2. Ref.16
	Mutagenesis	1258	1	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. Ref.16
	Mutagenesis	1520	1	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. Ref.16
	Sequence conflict	19	1	G → D in AAC13763. Ref.1
	Sequence conflict	19	1	G → D in AAA79760. Ref.6
	Sequence conflict	19	1	G → D in AAR86935. Ref.7
	Sequence conflict	19	1	G → D in AAR86936. Ref.7
	Sequence conflict	19	1	G → D in AAR86937. Ref.7
	Sequence conflict	113	1	A → P in AAC13763. Ref.1
	Sequence conflict	113	1	A → P in AAA79760. Ref.6
	Sequence conflict	113	1	A → P in AAR86935. Ref.7
	Sequence conflict	113	1	A → P in AAR86936. Ref.7
	Sequence conflict	113	1	A → P in AAR86937. Ref.7
	Sequence conflict	236	1	I → V in AAC13763. Ref.1
	Sequence conflict	236	1	I → V in AAA79760. Ref.6
	Sequence conflict	236	1	I → V in AAR86935. Ref.7
	Sequence conflict	236	1	I → V in AAR86936. Ref.7
	Sequence conflict	236	1	I → V in AAR86937. Ref.7
	Sequence conflict	373	1	V → I in AAC13763. Ref.1
	Sequence conflict	373	1	V → I in AAA79760. Ref.6
	Sequence conflict	373	1	V → I in AAR86935. Ref.7
	Sequence conflict	373	1	V → I in AAR86936. Ref.7
	Sequence conflict	373	1	V → I in AAR86937. Ref.7
	Sequence conflict	437	1	K → T in AAC13763. Ref.1
	Sequence conflict	470	1	N → K in AAR86936. Ref.7
	Sequence conflict	492	1	K → R in AAC13763. Ref.1
	Sequence conflict	492	1	K → R in AAA79760. Ref.6
	Sequence conflict	492	1	K → R in AAR86935. Ref.7
	Sequence conflict	492	1	K → R in AAR86936. Ref.7
	Sequence conflict	492	1	K → R in AAR86937. Ref.7
	Sequence conflict	642	1	L → S in AAR86937. Ref.7
	Sequence conflict	1341	1	V → F in AAC13763. Ref.1
	Sequence conflict	1341	1	V → F in AAA79760. Ref.6
	Sequence conflict	1341	1	V → F in AAR86935. Ref.7
	Sequence conflict	1341	1	V → F in AAR86936. Ref.7
	Sequence conflict	1341	1	V → F in AAR86937. Ref.7
	Sequence conflict	1457	1	M → I in AAC13763. Ref.1
	Sequence conflict	1457	1	M → I in AAA79760. Ref.6
	Sequence conflict	1457	1	M → I in AAR86935. Ref.7
	Sequence conflict	1457	1	M → I in AAR86936. Ref.7
	Sequence conflict	1457	1	M → I in AAR86937. Ref.7
	Sequence conflict	1790	1	T → S in AAC13763. Ref.1
	Sequence conflict	1790	1	T → S in AAA79760. Ref.6
	Sequence conflict	1790	1	T → S in AAR86935. Ref.7
	Sequence conflict	1790	1	T → S in AAR86936. Ref.7
	Sequence conflict	1790	1	T → S in AAR86937. Ref.7
	Sequence conflict	1827 – 1828	2	KH → DQ in AAC13763. Ref.1
	Sequence conflict	1827 – 1828	2	KH → DQ in AAA79760. Ref.6
	Sequence conflict	1827 – 1828	2	KH → DQ in AAR86935. Ref.7
	Sequence conflict	1827 – 1828	2	KH → DQ in AAR86936. Ref.7
	Sequence conflict	1827 – 1828	2	KH → DQ in AAR86937. Ref.7
	Sequence conflict	1834	1	D → T in AAC13763. Ref.1
	Sequence conflict	1834	1	D → T in AAA79760. Ref.6
	Sequence conflict	1834	1	D → T in AAR86935. Ref.7
	Sequence conflict	1834	1	D → T in AAR86936. Ref.7
	Sequence conflict	1834	1	D → T in AAR86937. Ref.7
	Sequence conflict	1844	1	I → V in AAC13763. Ref.1
	Sequence conflict	1844	1	I → V in AAA79760. Ref.6
	Sequence conflict	1844	1	I → V in AAR86935. Ref.7
	Sequence conflict	1844	1	I → V in AAR86936. Ref.7
	Sequence conflict	1844	1	I → V in AAR86937. Ref.7
	Sequence conflict	1853	1	S → F in AAC13763. Ref.1
	Sequence conflict	1853	1	S → F in AAA79760. Ref.6
	Sequence conflict	1853	1	S → F in AAR86935. Ref.7
	Sequence conflict	1853	1	S → F in AAR86936. Ref.7
	Sequence conflict	1853	1	S → F in AAR86937. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P38631 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: AD4B4CB8CB28B5D8	FASTA	1,876	214,851
	10 20 30 40 50 60 MNTDQQPYQG QTDYTQGPGN GQSQEQDYDQ YGQPLYPSQA DGYYDPNVAA GTEADMYGQQ 70 80 90 100 110 120 PPNESYDQDY TNGEYYGQPP NMAAQDGENF SDFSSYGPPG TPGYDSYGGQ YTASQMSYGE 130 140 150 160 170 180 PNSSGTSTPI YGNYDPNAIA MALPNEPYPA WTADSQSPVS IEQIEDIFID LTNRLGFQRD 190 200 210 220 230 240 SMRNMFDHFM VLLDSRSSRM SPDQALLSLH ADYIGGDTAN YKKWYFAAQL DMDDEIGFRN 250 260 270 280 290 300 MSLGKLSRKA RKAKKKNKKA MEEANPEDTE ETLNKIEGDN SLEAADFRWK AKMNQLSPLE 310 320 330 340 350 360 RVRHIALYLL CWGEANQVRF TAECLCFIYK CALDYLDSPL CQQRQEPMPE GDFLNRVITP 370 380 390 400 410 420 IYHFIRNQVY EIVDGRFVKR ERDHNKIVGY DDLNQLFWYP EGIAKIVLED GTKLIELPLE 430 440 450 460 470 480 ERYLRLGDVV WDDVFFKTYK ETRTWLHLVT NFNRIWVMHI SIFWMYFAYN SPTFYTHNYQ 490 500 510 520 530 540 QLVDNQPLAA YKWASCALGG TVASLIQIVA TLCEWSFVPR KWAGAQHLSR RFWFLCIIFG 550 560 570 580 590 600 INLGPIIFVF AYDKDTVYST AAHVVAAVMF FVAVATIIFF SIMPLGGLFT SYMKKSTRRY 610 620 630 640 650 660 VASQTFTAAF APLHGLDRWM SYLVWVTVFA AKYSESYYFL VLSLRDPIRI LSTTAMRCTG 670 680 690 700 710 720 EYWWGAVLCK VQPKIVLGLV IATDFILFFL DTYLWYIIVN TIFSVGKSFY LGISILTPWR 730 740 750 760 770 780 NIFTRLPKRI YSKILATTDM EIKYKPKVLI SQVWNAIIIS MYREHLLAID HVQKLLYHQV 790 800 810 820 830 840 PSEIEGKRTL RAPTFFVSQD DNNFETEFFP RDSEAERRIS FFAQSLSTPI PEPLPVDNMP 850 860 870 880 890 900 TFTVLTPHYA ERILLSLREI IREDDQFSRV TLLEYLKQLH PVEWECFVKD TKILAEETAA 910 920 930 940 950 960 YEGNENEAEK EDALKSQIDD LPFYCIGFKS AAPEYTLRTR IWASLRSQTL YRTISGFMNY 970 980 990 1000 1010 1020 SRAIKLLYRV ENPEIVQMFG GNAEGLEREL EKMARRKFKF LVSMQRLAKF KPHELENAEF 1030 1040 1050 1060 1070 1080 LLRAYPDLQI AYLDEEPPLT EGEEPRIYSA LIDGHCEILD NGRRRPKFRV QLSGNPILGD 1090 1100 1110 1120 1130 1140 GKSDNQNHAL IFYRGEYIQL IDANQDNYLE ECLKIRSVLA EFEELNVEQV NPYAPGLRYE 1150 1160 1170 1180 1190 1200 EQTTNHPVAI VGAREYIFSE NSGVLGDVAA GKEQTFGTLF ARTLSQIGGK LHYGHPDFIN 1210 1220 1230 1240 1250 1260 ATFMTTRGGV SKAQKGLHLN EDIYAGMNAM LRGGRIKHCE YYQCGKGRDL GFGTILNFTT 1270 1280 1290 1300 1310 1320 KIGAGMGEQM LSREYYYLGT QLPVDRFLTF YYAHPGFHLN NLFIQLSLQM FMLTLVNLSS 1330 1340 1350 1360 1370 1380 LAHESIMCIY DRNKPKTDVL VPIGCYNFQP AVDWVRRYTL SIFIVFWIAF VPIVVQELIE 1390 1400 1410 1420 1430 1440 RGLWKATQRF FCHLLSLSPM FEVFAGQIYS SALLSDLAIG GARYISTGRG FATSRIPFSI 1450 1460 1470 1480 1490 1500 LYSRFAGSAI YMGARSMLML LFGTVAHWQA PLLWFWASLS SLIFAPFVFN PHQFAWEDFF 1510 1520 1530 1540 1550 1560 LDYRDYIRWL SRGNNQYHRN SWIGYVRMSR ARITGFKRKL VGDESEKAAG DASRAHRTNL 1570 1580 1590 1600 1610 1620 IMAEIIPCAI YAAGCFIAFT FINAQTGVKT TDDDRVNSVL RIIICTLAPI AVNLGVLFFC 1630 1640 1650 1660 1670 1680 MGMSCCSGPL FGMCCKKTGS VMAGIAHGVA VIVHIAFFIV MWVLESFNFV RMLIGVVTCI 1690 1700 1710 1720 1730 1740 QCQRLIFHCM TALMLTREFK NDHANTAFWT GKWYGKGMGY MAWTQPSREL TAKVIELSEF 1750 1760 1770 1780 1790 1800 AADFVLGHVI LICQLPLIII PKIDKFHSIM LFWLKPSRQI RPPIYSLKQT RLRKRMVKKY 1810 1820 1830 1840 1850 1860 CSLYFLVLAI FAGCIIGPAV ASAKIHKHIG DSLDGVVHNL FQPINTTNND TGSQMSTYQS 1870 HYYTHTPSLK TWSTIK

References

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[1]	"The yeast FKS1 gene encodes a novel membrane protein, mutations in which confer FK506 and cyclosporin A hypersensitivity and calcineurin-dependent growth." Eng W.-K., Faucette L., McLaughlin M.M., Cafferkey R., Koltin Y., Morris R.A., Young P.R., Johnson R.K., Livi G.P. Gene 151:61-71(1994) [PubMed: 7530227] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TOPOLOGY, DISRUPTION PHENOTYPE. Strain: RC118D.
[2]	"The Saccharomyces cerevisiae FKS1 (ETG1) gene encodes an integral membrane protein which is a subunit of 1,3-beta-D-glucan synthase." 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. Proc. Natl. Acad. Sci. U.S.A. 91:12907-12911(1994) [PubMed: 7528927] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME, ENZYME ACTIVITY, TOPOLOGY, DISRUPTION PHENOTYPE. Strain: S288c / GRF88.
[3]	"Characterization and gene cloning of 1,3-beta-D-glucan synthase from Saccharomyces cerevisiae." Inoue S.B., Takewaki N., Takasuka T., Mio T., Adachi M., Fujii Y., Miyamoto C., Arisawa M., Furuichi Y., Watanabe T. Eur. J. Biochem. 231:845-854(1995) [PubMed: 7649185] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME. Strain: ATCC 200589 / A451.
[4]	"Identification of two cell cycle regulated genes affecting the beta 1,3-glucan content of cell walls in Saccharomyces cerevisiae." Ram A.F.J., Brekelmans S.S.C., Oehlen L.J.W.M., Klis F.M. FEBS Lett. 358:165-170(1995) [PubMed: 7828729] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME. Strain: S288c / GRF88.
[5]	"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." Castro C., Ribas J.C., Valdivieso M.H., Varona R., del Rey F., Duran A. J. Bacteriol. 177:5732-5739(1995) [PubMed: 7592316] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME, ENZYME ACTIVITY, DISRUPTION PHENOTYPE. Strain: S288c / GRF88.
[6]	"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." Garrett-Engele P., Moilanen B., Cyert M.S. Mol. Cell. Biol. 15:4103-4114(1995) [PubMed: 7542741] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME, DISRUPTION PHENOTYPE. Strain: ATCC 204508 / S288c.
[7]	"FKS1 mutations responsible for selective resistance of Saccharomyces cerevisiae to the novel 1,3-beta-glucan synthase inhibitor arborcandin C." Ohyama T., Miyakoshi S., Isono F. Antimicrob. Agents Chemother. 48:319-322(2004) [PubMed: 14693557] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TOPOLOGY, MUTAGENESIS OF ASN-470 AND LEU-642, DISRUPTION PHENOTYPE. Strain: ATCC 96519 / YPH250.
[8]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." 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. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[9]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[10]	"Calcineurin-dependent growth of an FK506- and CsA-hypersensitive mutant of Saccharomyces cerevisiae." Parent S.A., Nielsen J.B., Morin N., Chrebet G., Ramadan N., Dahl A.M., Hsu M.J., Bostian K.A., Foor F. J. Gen. Microbiol. 139:2973-2984(1993) [PubMed: 7510323] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[11]	"Differential expression and function of two homologous subunits of yeast 1,3-beta-D-glucan synthase." Mazur P., Morin N., Baginsky W., el-Sherbeini M., Clemas J.A., Nielsen J.B., Foor F. Mol. Cell. Biol. 15:5671-5681(1995) [PubMed: 7565718] [Abstract] Cited for: INDUCTION.
[12]	"In vitro activity of 1,3-beta-D-glucan synthase requires the GTP-binding protein Rho1." Mazur P., Baginsky W. J. Biol. Chem. 271:14604-14609(1996) [PubMed: 8662910] [Abstract] Cited for: ENZYME ACTIVITY, INTERACTION WITH RHO1.
[13]	"Identification of yeast Rho1p GTPase as a regulatory subunit of 1,3-beta-glucan synthase." Qadota H., Python C.P., Inoue S.B., Arisawa M., Anraku Y., Zheng Y., Watanabe T., Levin D.E., Ohya Y. Science 272:279-281(1996) [PubMed: 8602515] [Abstract] Cited for: INTERACTION WITH RHO1, SUBCELLULAR LOCATION.
[14]	"Movement of yeast 1,3-beta-glucan synthase is essential for uniform cell wall synthesis." Utsugi T., Minemura M., Hirata A., Abe M., Watanabe D., Ohya Y. Genes Cells 7:1-9(2002) [PubMed: 11856368] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[15]	"Dissection of upstream regulatory components of the Rho1p effector, 1,3-beta-glucan synthase, in Saccharomyces cerevisiae." Sekiya-Kawasaki M., Abe M., Saka A., Watanabe D., Kono K., Minemura-Asakawa M., Ishihara S., Watanabe T., Ohya Y. Genetics 162:663-676(2002) [PubMed: 12399379] [Abstract] Cited for: ENZYME ACTIVITY, MUTAGENESIS OF LYS-877; ALA-899 AND GLN-977.
[16]	"Mutations in Fks1p affect the cell wall content of beta-1,3- and beta-1,6-glucan in Saccharomyces cerevisiae." Dijkgraaf G.J.P., Abe M., Ohya Y., Bussey H. Yeast 19:671-690(2002) [PubMed: 12185837] [Abstract] Cited for: ENZYME ACTIVITY, SUBCELLULAR LOCATION, 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.
[17]	"A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery." Hitchcock A.L., Auld K., Gygi S.P., Silver P.A. Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed: 14557538] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-910, MASS SPECTROMETRY.
[18]	"The proteome of Saccharomyces cerevisiae mitochondria." 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. Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed: 14576278] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Strain: ATCC 76625 / YPH499.
[19]	"Analysis of beta-1,3-glucan assembly in Saccharomyces cerevisiae using a synthetic interaction network and altered sensitivity to caspofungin." Lesage G., Sdicu A.-M., Menard P., Shapiro J., Hussein S., Bussey H. Genetics 167:35-49(2004) [PubMed: 15166135] [Abstract] Cited for: CASPOFUNGIN HYPERSENSITIVITY.
[20]	"Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics." Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A. J. Proteome Res. 5:1543-1554(2006) [PubMed: 16823961] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[21]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-269, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U08459 Genomic DNA. Translation: AAC13763.1. U12893 Genomic DNA. Translation: AAC48981.1. D42126 Genomic DNA. Translation: BAA07706.1. X80817 Genomic DNA. Translation: CAA56783.1. Z46262 Genomic DNA. Translation: CAA86404.1. L35923 Genomic DNA. Translation: AAA79760.1. AY395693 Genomic DNA. Translation: AAR86935.1. AY395694 Genomic DNA. Translation: AAR86936.1. AY395695 Genomic DNA. Translation: AAR86937.1. U19028 Genomic DNA. Translation: AAB67256.1. BK006945 Genomic DNA. Translation: DAA09646.1.
PIR	S50235.
RefSeq	NP_013446.1. NM_001182231.1.
3D structure databases
ProteinModelPortal	P38631.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5749N.
IntAct	P38631. 64 interactions.
MINT	MINT-619820.
STRING	P38631.
Protein family/group databases
CAZy	GT48. Glycosyltransferase Family 48.
Proteomic databases
PeptideAtlas	P38631.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR342W; YLR342W; YLR342W.
GeneID	851055.
KEGG	sce:YLR342W.
NMPDR	fig|4932.3.peg.4466.
Organism-specific databases
CYGD	YLR342w.
SGD	S000004334. FKS1.
Phylogenomic databases
eggNOG	fuNOG07261.
GeneTree	EFGT00050000001535.
HOGENOM	HBG332273.
OMA	ARALAWI.
OrthoDB	EOG49PF6H.
Gene expression databases
ArrayExpress	P38631.
Genevestigator	P38631.
GermOnline	YLR342W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR003440. Glyco_trans_48. [Graphical view]
KO	K00706.
Pfam	PF02364. Glucan_synthase. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	967673.

Entry information

Entry name

FKS1_YEAST

Accession

Primary (citable) accession number: P38631
Secondary accession number(s): D6VYY0 , Q53YZ4, Q6TKS9, Q6TKT0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	February 1, 1996
Last modified:	January 25, 2012
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program