FKS3_YEAST
ID FKS3_YEAST Reviewed; 1785 AA.
AC Q04952; D6W0D3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=1,3-beta-glucan synthase component FKS3;
DE EC=2.4.1.34;
DE AltName: Full=1,3-beta-D-glucan-UDP glucosyltransferase;
DE AltName: Full=FK506 sensitivity protein 3;
GN Name=FKS3; OrderedLocusNames=YMR306W; ORFNames=YM9952.08;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [4]
RP FUNCTION.
RX PubMed=17158736; DOI=10.1128/ec.00200-06;
RA Ishihara S., Hirata A., Nogami S., Beauvais A., Latge J.-P., Ohya Y.;
RT "Homologous subunits of 1,3-beta-glucan synthase are important for spore
RT wall assembly in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 6:143-156(2007).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX PubMed=19756047; DOI=10.1038/msb.2009.64;
RA Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT new roles for protein glycosylation in eukaryotes.";
RL Mol. Syst. Biol. 5:308-308(2009).
CC -!- FUNCTION: Required for spore wall assembly.
CC {ECO:0000269|PubMed:17158736}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-
CC COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14576278}.
CC Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000305}.
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DR EMBL; Z49212; CAA89139.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10207.1; -; Genomic_DNA.
DR PIR; S53976; S53976.
DR RefSeq; NP_014036.1; NM_001182817.1.
DR AlphaFoldDB; Q04952; -.
DR BioGRID; 35486; 46.
DR ComplexPortal; CPX-3028; 1,3-beta-D-glucan synthase complex, FKS3-RHO1 variant.
DR DIP; DIP-7253N; -.
DR IntAct; Q04952; 3.
DR MINT; Q04952; -.
DR STRING; 4932.YMR306W; -.
DR CAZy; GT48; Glycosyltransferase Family 48.
DR iPTMnet; Q04952; -.
DR PaxDb; Q04952; -.
DR PRIDE; Q04952; -.
DR EnsemblFungi; YMR306W_mRNA; YMR306W; YMR306W.
DR GeneID; 855353; -.
DR KEGG; sce:YMR306W; -.
DR SGD; S000004923; FKS3.
DR VEuPathDB; FungiDB:YMR306W; -.
DR eggNOG; KOG0916; Eukaryota.
DR HOGENOM; CLU_000844_0_1_1; -.
DR InParanoid; Q04952; -.
DR OMA; LWFWITV; -.
DR BioCyc; YEAST:G3O-32970-MON; -.
DR PRO; PR:Q04952; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04952; protein.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; ISS:SGD.
DR GO; GO:0046527; F:glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
DR GO; GO:0051278; P:fungal-type cell wall polysaccharide biosynthetic process; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 1.
DR SMART; SM01205; FKS1_dom1; 1.
PE 1: Evidence at protein level;
KW Cell shape; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosyltransferase; Membrane; Mitochondrion; Reference proteome;
KW Sporulation; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1785
FT /note="1,3-beta-glucan synthase component FKS3"
FT /id="PRO_0000121727"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 508..528
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 572..592
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 712..732
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1215..1235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1268..1288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1303..1323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1370..1390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1394..1414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1475..1495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1514..1534
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1549..1569
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1585..1605
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1655..1675
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1713..1733
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 791..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 844
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 874
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 955
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1002
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1579
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1761
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1785 AA; 207483 MW; 3475446DA46C6120 CRC64;
MDFMSPKFSL TDVEYPAWCQ DDEVPITMQE IREIFVELMD KFGFQKSSME NMYQHLMGQL
DSRASRTGAQ NALVSLHVSY IGGEHANYRK WYFAAQLDLD EEIGFQNMRL HGKARQRNVK
MAKKRGVSIK EQIKQWNEKE QEFINNHPKI TLTQEQLEDQ TNLKSADYKW KLKMKKLTPE
NMIRQLALYL LCWGEANQVR FAPECLCFIF KCALDYDIST SSSEKTVKSP EYSYLNDVIT
PLYEFLRGQV YKKDAKGNWK RREKDHKNII GYDDINQLFW YPEGFERIIL NNGERLVDKP
LEERYLYFKD VAWSKVFYKT YRETRSWKHC FTNFNRFWII HFAPFWFFTT FNSPTLYTKN
YIQLLNNQPT PQVRLSVIAF GGTIACLVQI LATVFEWGFV PREWPGAQHL SSRMIGLLFC
LAINLGPSVY VLGFFEWDVH SKSAYIVSIV QLIIAFLTTF FFAVRPLGGL FRPYLNKDKK
HRRYISSQTF TASFPKLTGR SKWFSYGLWV FVYLAKYIES YFFLTLSLRD PIRVLSIMDL
SRCQGEYLLG PILCKWQAKI TLVLMLLSDL GLFFLDTYLW YIICNCIFSI VLSFSLGTSI
LTPWKNVYSR LPKRIYSKIL ATSEMDVKFK AKILISQVWN AIVISMYREH LLSIEHLQRL
LFQQVDSLMG DTRTLKSPTF FVAQDDSTFK SMEFFPSNSE AKRRISFFAQ SLATPISEPV
PVDCMPTFTV LVPHYSEKIL LGLKEIIREE SPKSKITVLE YLKHLHPTEW ECFVKDTKLL
SMEKSFLKEA ESSHDEDRLE IPDALYDPRS SPLSDHTESR KLPTEDDLIK EKINDLPFSY
FGFNSSEPSY TLRTRIWASL RTQTLYRTLS GFMNYSKAIK LLYRIENPSL VSLYRGNNEA
LENDLENMAS RKFRMVVAMQ RYAKFNKDEV EATELLLRAY PNMFISYLLE ELEQNESEKT
YYSCLTNGYA EFDEESGLRK PIFKIRLSGN PILGDGKSDN QNHSIIFYRG EYIQVIDANQ
DNYLEECLKI RSVLSEFEEL ELNPTIPYIP GIEYEEEPPP IAIVGSREYI FSENIGVLGD
IAAGKEQTFG TLFARTLAEI GGKLHYGHPD FLNGIFMTTR GGLSKAQRGL HLNEDIYAGM
NAICRGGKIK HSDYYQCGKG RDLGFGSILN FTTKIGAGMG EQLLSREYYY LGTQLPMDRF
LSFFYAHPGF HLNNLFISFS VQLFFVLLLN LGALNHEIIA CFYDKDAPIT NLETPVGCYN
IQPALHWVSI FVLSIFIVFF IAFAPLLIQE VLEKGIWRAA SRFLHHLLSM APLFEVFVCQ
VYSNSLLMDL TFGGAKYIST GRGFAITRLD FFTLYSRFVN ISIYSGFQVF FMLLFAIISM
WQPALLWFWI TVISMCFAPF IFNPHQFAFM DFFIDYKTFI HWLFSGNTKY QKESWANFVK
SSRSRFTGYK SKTVDDISED SGHDSKKARF WNVFFAELFL PFCVFLFNFT AFSFINAQTG
VSDSTPTSAV FRLLLVTFLP IFLNSIVLFL LFWVSLFVVP GLSYCCKDAG AVIAFIAHTF
SVLVYLLDFE LMWFLQGWNF TRTLILLITC INMHLILFKV FTTIFLTREY KNNKAHLAWW
NGKWYNTGMG WSIILQPIRE YFVKIMESSY FAADFFLGHF LLFIQTPIIL LPFIDYWHTM
VLFWMNPRSI IAHKRILTRK QRALRSRIVS KYFSLYFVML GVLLFMLIAP FFAGDFVSSP
QELLEGTLFE GIFQPNNQNN NDTGPNAPST ILTTTPTLPT FRTVA
