SKN1_YEAST
ID SKN1_YEAST Reviewed; 771 AA.
AC P33336; D6VUS3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Beta-glucan synthesis-associated protein SKN1;
GN Name=SKN1; OrderedLocusNames=YGR143W;
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.
RX PubMed=8321211; DOI=10.1128/mcb.13.7.4039-4048.1993;
RA Roemer T., Delaney S., Bussey H.;
RT "SKN1 and KRE6 define a pair of functional homologs encoding putative
RT membrane proteins involved in beta-glucan synthesis.";
RL Mol. Cell. Biol. 13:4039-4048(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
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 [4]
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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; SER-65 AND SER-67, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Required for synthesis of the major beta-glucans of the yeast
CC cell wall.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- MISCELLANEOUS: Present with 468 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; L18859; AAA02557.1; -; Unassigned_DNA.
DR EMBL; Z72928; CAA97156.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08234.1; -; Genomic_DNA.
DR PIR; S40966; S40966.
DR RefSeq; NP_011659.3; NM_001181272.3.
DR AlphaFoldDB; P33336; -.
DR BioGRID; 33390; 169.
DR DIP; DIP-6666N; -.
DR IntAct; P33336; 2.
DR STRING; 4932.YGR143W; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR iPTMnet; P33336; -.
DR MaxQB; P33336; -.
DR PaxDb; P33336; -.
DR PRIDE; P33336; -.
DR EnsemblFungi; YGR143W_mRNA; YGR143W; YGR143W.
DR GeneID; 853045; -.
DR KEGG; sce:YGR143W; -.
DR SGD; S000003375; SKN1.
DR VEuPathDB; FungiDB:YGR143W; -.
DR eggNOG; ENOG502QR13; Eukaryota.
DR GeneTree; ENSGT00940000176454; -.
DR HOGENOM; CLU_010811_4_3_1; -.
DR InParanoid; P33336; -.
DR OMA; YGYEWWS; -.
DR BioCyc; YEAST:G3O-30847-MON; -.
DR PRO; PR:P33336; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P33336; protein.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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 GO; GO:0030148; P:sphingolipid biosynthetic process; 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; Membrane; Phosphoprotein;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..771
FT /note="Beta-glucan synthesis-associated protein SKN1"
FT /id="PRO_0000097780"
FT TOPO_DOM 1..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..771
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 353..716
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32486"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32486"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32486"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32486"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32486"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 590
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 615
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 743
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 771 AA; 86241 MW; E074632279C794BD CRC64;
MSVRNLTNNR HSNSENSVSG SENSFYSSNE QSRQSSSLEP ADGQNVRVSG NPFLGSEEFD
EDYNSPSGDD ERRGANEYSS SSSINYNNDP NSDTSLLANE KNSPERNGQR MSDYKGYYAK
TNLTSANNLN NHNNNNYKNI ISSSNDNSFA SHLQPPDRNL PSHPSSNNMS SFSNNSLIKS
PPPFDRYPLV GTRHISAAQS QSQNLINEKK RANMTGSSSS AHDSSLSSTN LYMGEQDFSP
FGGYPASFFP LTLDEKEDDD YIHNPNVEEE AKLDRRRFVD DFKHMDRRSF LGLLGILFLF
MAGIFIFIVL PAITFSGVVY HHEHVHAANS AGSSSSNTTS KSLTEYQYPQ LAAIRTTLVD
PDTPDSAKTR VAKDGSKWQL VFSDEFNAEG RTFYDGDDQF WTAPDIHYDA TKDLEWYSPD
AVTTTNGTLT LRMDAFRNHD LYYRSGMVQS WNKLCFTEGA LEVSANLPNY GRVTGLWPGM
WTMGNLGRPG YLASTQGVWP YSYEACDAGI TPNQSSPDGI SYLPGQKLSV CTCDNEDHPN
QGVGRGAPEI DILEGEADTI LGVGVASQSL QIAPFDIWYM PDYDFIEVYN FTTTTMNTYA
GGPFQQAVSA ISTLNVTWYE FGEEAGYFQK YAIEYLNDDD NGYIRWFVGE NPTFTLYATS
LHPSGNIDWR RISKEPMSAI LNLGISNNWA YIDWQYIFFP VTMSIDYVRL YQPKGSTSIT
CDPEDYPTYD YIQSHLNAYY NANLTDWEQA GYTFPKNILT GGCSSSKFSL S
