KRE6_YEAST
ID KRE6_YEAST Reviewed; 720 AA.
AC P32486; D6W4F9; Q06472;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Beta-glucan synthesis-associated protein KRE6;
DE AltName: Full=Killer toxin-resistance protein 6;
GN Name=KRE6; Synonyms=CWH48; OrderedLocusNames=YPR159W;
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 [GENOMIC DNA].
RX PubMed=1837148; DOI=10.1073/pnas.88.24.11295;
RA Roemer T., Bussey H.;
RT "Yeast beta-glucan synthesis: KRE6 encodes a predicted type II membrane
RT protein required for glucan synthesis in vivo and for glucan synthase
RT activity in vitro.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:11295-11299(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7871892; DOI=10.1002/yea.320101117;
RA Roemer T.D., Fortin N., Bussey H.;
RT "DNA sequence analysis of a 10.4 kbp region on the right arm of yeast
RT chromosome XVI positions GPH1 and SGV1 adjacent to KRE6, and identifies two
RT novel tRNA genes.";
RL Yeast 10:1527-1530(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [4]
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 [5]
RP CHARACTERIZATION.
RX PubMed=7929594; DOI=10.1083/jcb.127.2.567;
RA Roemer T., Paravicini G., Payton M.A., Bussey H.;
RT "Characterization of the yeast (1-->6)-beta-glucan biosynthetic components,
RT Kre6p and Skn1p, and genetic interactions between the PKC1 pathway and
RT extracellular matrix assembly.";
RL J. Cell Biol. 127:567-579(1994).
RN [6]
RP FUNCTION.
RX PubMed=10601196; DOI=10.1128/jb.181.24.7414-7420.1999;
RA Montijn R.C., Vink E., Mueller W.H., Verkleij A.J., Van Den Ende H.,
RA Henrissat B., Klis F.M.;
RT "Localization of synthesis of beta1,6-glucan in Saccharomyces cerevisiae.";
RL J. Bacteriol. 181:7414-7420(1999).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH LAS17 AND SLA1.
RX PubMed=12237851; DOI=10.1002/yea.904;
RA Li H., Page N., Bussey H.;
RT "Actin patch assembly proteins Las17p and Sla1p restrict cell wall growth
RT to daughter cells and interact with cis-Golgi protein Kre6p.";
RL Yeast 19:1097-1112(2002).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP FUNCTION.
RX PubMed=15093776; DOI=10.1016/j.femsyr.2004.02.006;
RA Bowen S., Wheals A.E.;
RT "Incorporation of Sed1p into the cell wall of Saccharomyces cerevisiae
RT involves KRE6.";
RL FEMS Yeast Res. 4:731-735(2004).
RN [10]
RP INTERACTION WITH KEG1.
RX PubMed=17893149; DOI=10.1074/jbc.m706486200;
RA Nakamata K., Kurita T., Bhuiyan M.S.A., Sato K., Noda Y., Yoda K.;
RT "KEG1/YFR042w encodes a novel Kre6-binding endoplasmic reticulum membrane
RT protein responsible for beta-1,6-glucan synthesis in Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 282:34315-34324(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81; SER-116; SER-133;
RP SER-134; SER-136 AND SER-139, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Involved in the synthesis of (1->6)- and (1->3)-beta-D-glucan
CC polymers of the yeast cell wall in vivo. It is required for full
CC activity of beta-glucan synthase in vitro. May be involved in the
CC maturation and transport of cell wall proteins (CWP) to the cell wall.
CC May act as a transglucosidase and contribute to the construction of a
CC protein-bound glucan-structure that acts as an acceptor site for the
CC addition of (1->6)-beta-D-glucan at the cell surface.
CC {ECO:0000269|PubMed:10601196, ECO:0000269|PubMed:12237851,
CC ECO:0000269|PubMed:15093776}.
CC -!- SUBUNIT: The cytoplasmic domain interacts with the actin patch assembly
CC proteins LAS17 and SLA1. Interacts with KEG1.
CC {ECO:0000269|PubMed:12237851, ECO:0000269|PubMed:17893149}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:12237851}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:12237851}.
CC -!- MISCELLANEOUS: Present with 4760 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SKN1/KRE6 family. {ECO:0000305}.
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DR EMBL; M80657; AAA34726.1; -; Genomic_DNA.
DR EMBL; L33835; AAB59312.1; -; Genomic_DNA.
DR EMBL; U28371; AAB68056.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11575.1; -; Genomic_DNA.
DR PIR; S61143; S61143.
DR RefSeq; NP_015485.1; NM_001184256.1.
DR AlphaFoldDB; P32486; -.
DR BioGRID; 36331; 86.
DR DIP; DIP-1850N; -.
DR IntAct; P32486; 14.
DR MINT; P32486; -.
DR STRING; 4932.YPR159W; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR iPTMnet; P32486; -.
DR MaxQB; P32486; -.
DR PaxDb; P32486; -.
DR PRIDE; P32486; -.
DR EnsemblFungi; YPR159W_mRNA; YPR159W; YPR159W.
DR GeneID; 856287; -.
DR KEGG; sce:YPR159W; -.
DR SGD; S000006363; KRE6.
DR VEuPathDB; FungiDB:YPR159W; -.
DR eggNOG; ENOG502QR13; Eukaryota.
DR GeneTree; ENSGT00940000176454; -.
DR HOGENOM; CLU_010811_4_3_1; -.
DR InParanoid; P32486; -.
DR OMA; RIDYIRI; -.
DR BioCyc; YEAST:YPR159W-MON; -.
DR PRO; PR:P32486; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P32486; protein.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0030427; C:site of polarized growth; IDA:SGD.
DR GO; GO:0030133; C:transport vesicle; IDA:SGD.
DR GO; GO:0015926; F:glucosidase activity; IMP:SGD.
DR GO; GO:0006078; P:(1->6)-beta-D-glucan biosynthetic process; IMP:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR CDD; cd02180; GH16_fungal_KRE6_glucanase; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR InterPro; IPR005629; Skn1/Kre6/Sbg1.
DR PANTHER; PTHR31361; PTHR31361; 1.
DR Pfam; PF03935; SKN1_KRE6_Sbg1; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Glycoprotein; Golgi apparatus; Membrane;
KW Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..720
FT /note="Beta-glucan synthesis-associated protein KRE6"
FT /id="PRO_0000084331"
FT TOPO_DOM 1..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..720
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 289..664
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 691
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 310
FT /note="D -> E (in Ref. 1; AAA34726 and 2; AAB59312)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="G -> V (in Ref. 1; AAA34726 and 2; AAB59312)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 720 AA; 80123 MW; A7A91D0C40805106 CRC64;
MPLRNLTETH NFSSTNLDTD GTGDDHDGAP LSSSPSFGQQ NDNSTNDNAG LTNPFMGSDE
ESNARDGESL SSSVHYQPQG SDSSLLHDNS RLDLSQNKGV SDYKGYYSRN NSRAVSTAND
NSFLQPPHRA IASSPSLNSN LSKNDILSPP EFDRYPLVGS RVTSMTQLNH HGRSPTSSPG
NESSASFSSN PFLGEQDFSP FGGYPASSFP LMIDEKEEDD YLHNPDPEEE ARLDRRRFID
DFKYMDKRSA SGLAGVLLLF LAAIFIFIVL PALTFTGAID HESNTEEVTY LTQYQYPQLS
AIRTSLVDPD TPDTAKTREA MDGSKWELVF SDEFNAEGRT FYDGDDPYWT APDVHYDATK
DLEWYSPDAS TTVNGTLQLR MDAFKNHGLY YRSGMLQSWN KVCFTQGALE ISANLPNYGR
VSGLWPGLWT MGNLGRPGYL ASTQGVWPYS YESCDAGITP NQSSPDGISY LPGQKLSICT
CDGEDHPNQG VGRGAPEIDV LEGETDTKIG VGIASQSLQI APFDIWYMPD YDFIEVYNFT
TTTMNTYAGG PFQQAVSAVS TLNVTWYEFG EYGGYFQKYA IEYLNDDDNG YIRWFVGDTP
TYTIHAKALH PDGNIGWRRI SKEPMSIILN LGISNNWAYI DWQYIFFPVV MSIDYVRIYQ
PSNAISVTCD PSDYPTYDYI QSHLNAFQNA NLTTWEDAGY TFPKNILTGK CTSSKFKLSS
