SKT5_YEAST
ID SKT5_YEAST Reviewed; 696 AA.
AC P34226; D6VPT8; Q02215;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Chitin synthase regulator SKT5 {ECO:0000303|PubMed:9234668};
DE Flags: Precursor;
GN Name=SKT5 {ECO:0000303|Ref.5, ECO:0000312|SGD:S000000157};
GN Synonyms=CAL2 {ECO:0000303|PubMed:9234668},
GN CHS4 {ECO:0000303|PubMed:9234668}, CSD4 {ECO:0000303|PubMed:9234668};
GN OrderedLocusNames=YBL061C; ORFNames=YBL0506, YBL0519;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8154187; DOI=10.1002/yea.320091210;
RA Scherens B., el Bakkoury M., Vierendeels F., Dubois E., Messenguy F.;
RT "Sequencing and functional analysis of a 32,560 bp segment on the left arm
RT of yeast chromosome II. Identification of 26 open reading frames, including
RT the KIP1 and SEC17 genes.";
RL Yeast 9:1355-1371(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-678.
RC STRAIN=KR13;
RX PubMed=7764021; DOI=10.1271/bbb.57.1391;
RA Kawamoto S., Sasaki T., Itahashi S., Hatsuyama Y., Ohno T.;
RT "A mutant allele skt5 affecting protoplast regeneration and killer toxin
RT resistance has double mutations in its wild-type structural gene in
RT Saccharomyces cerevisiae.";
RL Biosci. Biotechnol. Biochem. 57:1391-1393(1993).
RN [5]
RP PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE.
RA Kawamoto S., Nomura M., Ohno T.;
RT "Cloning and characterization of SKT5, a Saccharomyces cerevisiae gene that
RT affects protoplast regeneration and resistance to killer toxin of
RT Kluyveromyces lactis.";
RL J. Ferment. Bioeng. 74:199-208(1992).
RN [6]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=9314530; DOI=10.1083/jcb.139.1.75;
RA DeMarini D.J., Adams A.E., Fares H., De Virgilio C., Valle G., Chuang J.S.,
RA Pringle J.R.;
RT "A septin-based hierarchy of proteins required for localized deposition of
RT chitin in the Saccharomyces cerevisiae cell wall.";
RL J. Cell Biol. 139:75-93(1997).
RN [7]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9234668;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<795::aid-yea139>3.0.co;2-l;
RA Trilla J.A., Cos T., Duran A., Roncero C.;
RT "Characterization of CHS4 (CAL2), a gene of Saccharomyces cerevisiae
RT involved in chitin biosynthesis and allelic to SKT5 and CSD4.";
RL Yeast 13:795-807(1997).
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 SUBCELLULAR LOCATION, METHYLATION AT CYS-693, ISOPRENYLATION AT CYS-693,
RP AND MUTAGENESIS OF CYS-693 AND 695-ILE-MET-696.
RX PubMed=17142567; DOI=10.1128/ec.00203-06;
RA Grabinska K.A., Magnelli P., Robbins P.W.;
RT "Prenylation of Saccharomyces cerevisiae Chs4p Affects Chitin Synthase III
RT activity and chitin chain length.";
RL Eukaryot. Cell 6:328-336(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-561, 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 [11]
RP IDENTIFICATION BY 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-561; SER-563 AND THR-564, 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).
CC -!- FUNCTION: Activator of the chitin synthase CHS3 which polymerizes
CC chitin, a structural polymer of the fungal cell wall.
CC {ECO:0000269|PubMed:9234668}.
CC -!- SUBUNIT: May interact with CHS3 and seems to be an adapter (along with
CC BNI4) to link CHS3 to septins. {ECO:0000269|PubMed:9314530}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17142567};
CC Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC Note=Farnesylation is not required for cellular membrane localization.
CC {ECO:0000269|PubMed:17142567}.
CC -!- INDUCTION: Induced by Calcofluor White (PubMed:9234668). Repressed by
CC alpha-factor (PubMed:9234668). Unchanged during sporulation
CC (PubMed:9234668). {ECO:0000269|PubMed:9234668}.
CC -!- PTM: Farnesylation is required for chitin synthase CHS3 activity but is
CC not required for SKT5 membrane association.
CC {ECO:0000269|PubMed:17142567}.
CC -!- DISRUPTION PHENOTYPE: Decreases CHS3 chitin synthase activity
CC (PubMed:9234668). Decreases cellular chitin level (PubMed:9234668).
CC Resistance to Calcofluor White (cell wall stressor) (PubMed:9234668).
CC Normal CHS3 RNA level (PubMed:9234668). Decreases conjugation frequency
CC (PubMed:9234668). {ECO:0000269|PubMed:9234668}.
CC -!- MISCELLANEOUS: Present with 2580 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SKT5 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-15 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC60564.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z23261; CAA80786.1; -; Genomic_DNA.
DR EMBL; Z35823; CAA84882.1; -; Genomic_DNA.
DR EMBL; S65415; AAC60564.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006936; DAA07058.1; -; Genomic_DNA.
DR PIR; S39827; S39827.
DR RefSeq; NP_009492.1; NM_001178301.1.
DR AlphaFoldDB; P34226; -.
DR SMR; P34226; -.
DR BioGRID; 32637; 226.
DR DIP; DIP-2481N; -.
DR IntAct; P34226; 16.
DR MINT; P34226; -.
DR STRING; 4932.YBL061C; -.
DR iPTMnet; P34226; -.
DR MaxQB; P34226; -.
DR PaxDb; P34226; -.
DR PRIDE; P34226; -.
DR EnsemblFungi; YBL061C_mRNA; YBL061C; YBL061C.
DR GeneID; 852218; -.
DR KEGG; sce:YBL061C; -.
DR SGD; S000000157; SKT5.
DR VEuPathDB; FungiDB:YBL061C; -.
DR eggNOG; KOG1550; Eukaryota.
DR GeneTree; ENSGT00940000176440; -.
DR HOGENOM; CLU_000288_126_4_1; -.
DR InParanoid; P34226; -.
DR OMA; YEHGKGC; -.
DR BioCyc; YEAST:G3O-28959-MON; -.
DR PRO; PR:P34226; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P34226; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008047; F:enzyme activator activity; IMP:SGD.
DR GO; GO:0034221; P:fungal-type cell wall chitin biosynthetic process; IMP:SGD.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR006597; Sel1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF08238; Sel1; 7.
DR SMART; SM00671; SEL1; 7.
PE 1: Evidence at protein level;
KW Cell membrane; Lipoprotein; Membrane; Methylation; Phosphoprotein;
KW Prenylation; Reference proteome; Repeat.
FT CHAIN 1..693
FT /note="Chitin synthase regulator SKT5"
FT /id="PRO_0000071940"
FT PROPEP 694..696
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:17142567"
FT /id="PRO_0000396725"
FT REPEAT 271..306
FT /note="Sel1-like 1"
FT REPEAT 307..342
FT /note="Sel1-like 2"
FT REPEAT 343..382
FT /note="Sel1-like 3"
FT REPEAT 386..423
FT /note="Sel1-like 4"
FT REPEAT 424..460
FT /note="Sel1-like 5"
FT REPEAT 461..498
FT /note="Sel1-like 6"
FT REPEAT 499..534
FT /note="Sel1-like 7"
FT REGION 37..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 564
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 693
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305|PubMed:17142567"
FT LIPID 693
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:17142567"
FT MUTAGEN 693
FT /note="C->S: Abolishes SKT5 prenylation. Decreases chitin
FT synthase CHS3 activity. Decreases chitin chain length.
FT Decreases cellular chitin level. Normal SKT5 localization
FT to cellular membranes. Resistance to Calcofluor White (cell
FT wall stressor)."
FT /evidence="ECO:0000269|PubMed:17142567"
FT MUTAGEN 695..696
FT /note="IM->LL: Decreases chitin synthase CHS3 activity,
FT resistance to Calcofluor White (cell wall stressor),
FT decreases cellular chitin level."
FT /evidence="ECO:0000269|PubMed:17142567"
FT CONFLICT 350
FT /note="G -> E (in Ref. 4; AAC60564)"
FT /evidence="ECO:0000305"
FT CONFLICT 643
FT /note="Q -> T (in Ref. 4; AAC60564)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 696 AA; 77066 MW; D50DE825E175D165 CRC64;
MASSPQVHPY KKHLMQSQHI NFDNRGLQFQ NSSLKVGQDF SDNKENRENR DNEDFSTADL
PKRSANQPLI NEHLRAASVP LLSNDIGNSQ EEDFVPVPPP QLHLNNSNNT SLSSLGSTPT
NSPSPGALRQ TNSSTSLTKE QIKKRTRSVD LSHMYLLNGS SDTQLTATNE SVADLSHQMI
SRYLGGKNNT SLVPRLKTIE MYRQNVKKSK DPEVLFQYAQ YMLQTALTIE SSNALVQDSD
KEGNVSQSDL KLQFLKEAQS YLKKLSIKGY SDAQYLLADG YSSGAFGKIE NKEAFVLFQA
AAKHGHIESA YRASHCLEEG LGTTRDSRKS VNFLKFAASR NHPSAMYKLG LYSFYGRMGL
PTDVNTKLNG VKWLSRAAAR ANELTAAAPY ELAKIYHEGF LDVVIPDEKY AMELYIQAAS
LGHVPSATLL AQIYETGNDT VGQDTSLSVH YYTQAALKGD SVAMLGLCAW YLLGAEPAFE
KDENEAFQWA LRAANAGLPK AQFTLGYFYE HGKGCDRNME YAWKWYEKAA GNEDKRAINK
LRSRDGGLAS IGKKQHKKNK SISTLNLFST VDSQTSNVGS NSRVSSKSET FFTGNPKRDR
EPQGLQINMN SNTNRNGIKT GSDTSIRKSS SSAKGMSREV AEQSMAAKQE VSLSNMGSSN
MIRKDFPAVK TESKKPTSLK NKKDKQGKKK KDCVIM
