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   27-MAR-2024, entry version 189.
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; 96.
DR   DIP; DIP-1850N; -.
DR   IntAct; P32486; 14.
DR   MINT; P32486; -.
DR   STRING; 4932.YPR159W; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   GlyCosmos; P32486; 5 sites, No reported glycans.
DR   GlyGen; P32486; 5 sites.
DR   iPTMnet; P32486; -.
DR   MaxQB; P32486; -.
DR   PaxDb; 4932-YPR159W; -.
DR   PeptideAtlas; P32486; -.
DR   EnsemblFungi; YPR159W_mRNA; YPR159W; YPR159W.
DR   GeneID; 856287; -.
DR   KEGG; sce:YPR159W; -.
DR   AGR; SGD:S000006363; -.
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; PYNYQYE; -.
DR   OrthoDB; 2785251at2759; -.
DR   BioCyc; YEAST:YPR159W-MONOMER; -.
DR   BioGRID-ORCS; 856287; 3 hits in 10 CRISPR screens.
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:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C: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   Gene3D; 2.60.120.200; -; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   InterPro; IPR005629; Skn1/Kre6/Sbg1.
DR   PANTHER; PTHR31361; BETA-GLUCAN SYNTHESIS-ASSOCIATED PROTEIN KRE6-RELATED; 1.
DR   PANTHER; PTHR31361:SF1; BETA-GLUCAN SYNTHESIS-ASSOCIATED PROTEIN KRE6-RELATED; 1.
DR   Pfam; PF03935; SKN1_KRE6_Sbg1; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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
//