CHS1_YEAST
ID CHS1_YEAST Reviewed; 1131 AA.
AC P08004; D6W0Z5;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Chitin synthase 1;
DE EC=2.4.1.16;
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 1;
GN Name=CHS1; OrderedLocusNames=YNL192W; ORFNames=N1404;
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], AND FUNCTION.
RX PubMed=2941152; DOI=10.1016/0092-8674(86)90738-5;
RA Bulawa C.E., Slater M., Cabib E., Au-Young J., Sburlati A., Adair W.L. Jr.,
RA Robbins P.W.;
RT "The S. cerevisiae structural gene for chitin synthase is not required for
RT chitin synthesis in vivo.";
RL Cell 46:213-225(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 815.
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 FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=2523889; DOI=10.1083/jcb.108.5.1665;
RA Cabib E., Sburlati A., Bowers B., Silverman S.J.;
RT "Chitin synthase 1, an auxiliary enzyme for chitin synthesis in
RT Saccharomyces cerevisiae.";
RL J. Cell Biol. 108:1665-1672(1989).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-270; SER-299; SER-318
RP AND THR-328, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270 AND SER-358, AND
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-35 AND SER-270, 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: Polymerizes chitin, a structural polymer of the cell wall and
CC septum, by transferring the sugar moiety of UDP-GlcNAc to the non-
CC reducing end of the growing chitin polymer (PubMed:2941152). Required
CC for mitotic division septum formation during adverse conditions
CC (PubMed:2523889). {ECO:0000269|PubMed:2523889,
CC ECO:0000269|PubMed:2941152}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-
CC D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) +
CC UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9595,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17029, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223; EC=2.4.1.16;
CC -!- ACTIVITY REGULATION: Requires proteolytic activation.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:2523889};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Cell lysis during cytokinesis.
CC {ECO:0000269|PubMed:2523889}.
CC -!- SIMILARITY: Belongs to the chitin synthase family. {ECO:0000305}.
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DR EMBL; M14045; AAA34491.1; -; Genomic_DNA.
DR EMBL; Z71468; CAA96086.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10361.2; -; Genomic_DNA.
DR PIR; A23944; A23944.
DR RefSeq; NP_014207.2; NM_001183030.2.
DR AlphaFoldDB; P08004; -.
DR BioGRID; 35641; 133.
DR DIP; DIP-4680N; -.
DR IntAct; P08004; 8.
DR MINT; P08004; -.
DR STRING; 4932.YNL192W; -.
DR BindingDB; P08004; -.
DR ChEMBL; CHEMBL3827; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR TCDB; 4.D.1.1.17; the putative vectorial glycosyl polymerization (vgp) family.
DR iPTMnet; P08004; -.
DR MaxQB; P08004; -.
DR PaxDb; P08004; -.
DR PRIDE; P08004; -.
DR EnsemblFungi; YNL192W_mRNA; YNL192W; YNL192W.
DR GeneID; 855529; -.
DR KEGG; sce:YNL192W; -.
DR SGD; S000005136; CHS1.
DR VEuPathDB; FungiDB:YNL192W; -.
DR eggNOG; KOG2571; Eukaryota.
DR HOGENOM; CLU_004760_3_1_1; -.
DR InParanoid; P08004; -.
DR OMA; NTIMSWF; -.
DR BioCyc; YEAST:YNL192W-MON; -.
DR PRO; PR:P08004; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P08004; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0030428; C:cell septum; IBA:GO_Central.
DR GO; GO:0045009; C:chitosome; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0004100; F:chitin synthase activity; IDA:SGD.
DR GO; GO:0006038; P:cell wall chitin biosynthetic process; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IMP:SGD.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR004834; Chitin_synth_fun.
DR InterPro; IPR013616; Chitin_synth_N.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; PTHR22914; 1.
DR Pfam; PF01644; Chitin_synth_1; 1.
DR Pfam; PF08407; Chitin_synth_1N; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Glycosyltransferase;
KW Membrane; Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1131
FT /note="Chitin synthase 1"
FT /id="PRO_0000193727"
FT TRANSMEM 795..815
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 833..853
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 866..886
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 914..934
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 942..962
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1042..1062
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1101..1121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 328
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 815
FT /note="V -> F (in Ref. 1; AAA34491 and 2; CAA96086)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1131 AA; 129871 MW; C1856F3C0C857E07 CRC64;
MSDQNNRSRN EYHSNRKNEP SYELQNAHSG LFHSSNEELT NRNQRYTNQN ASMGSFTPVQ
SLQFPEQSQQ TNMLYNGDDG NNNTINDNER DIYGGFVNHH RQRPPPATAE YNDVFNTNSQ
QLPSEHQYNN VPSYPLPSIN VIQTTPELIH NGSQTMATPI ERPFFNENDY YYNNRNSRTS
PSIASSSDGY ADQEARPILE QPNNNMNSGN IPQYHDQPFG YNNGYHGLQA KDYYDDPEGG
YIDQRGDDYQ INSYLGRNGE MVDPYDYENS LRHMTPMERR EYLHDDSRPV NDGKEELDSV
KSGYSHRDLG EYDKDDFSRD DEYDDLNTID KLQFQANGVP ASSSVSSIGS KESDIIVSND
NLTANRALKR SGTEIRKFKL WNGNFVFDSP ISKTLLDQYA TTTENANTLP NEFKFMRYQA
VTCEPNQLAE KNFTVRQLKY LTPRETELML VVTMYNEDHI LLGRTLKGIM DNVKYMVKKK
NSSTWGPDAW KKIVVCIISD GRSKINERSL ALLSSLGCYQ DGFAKDEINE KKVAMHVYEH
TTMINITNIS ESEVSLECNQ GTVPIQLLFC LKEQNQKKIN SHRWAFEGFA ELLRPNIVTL
LDAGTMPGKD SIYQLWREFR NPNVGGACGE IRTDLGKRFV KLLNPLVASQ NFEYKMSNIL
DKTTESNFGF ITVLPGAFSA YRFEAVRGQP LQKYFYGEIM ENEGFHFFSS NMYLAEDRIL
CFEVVTKKNC NWILKYCRSS YASTDVPERV PEFILQRRRW LNGSFFASVY SFCHFYRVWS
SGHNIGRKLL LTVEFFYLFF NTLISWFSLS SFFLVFRILT VSIALAYHSA FNVLSVIFLW
LYGICTLSTF ILSLGNKPKS TEKFYVLTCV IFAVMMIYMI FCSIFMSVKS FQNILKNDTI
SFEGLITTEA FRDIVISLGS TYCLYLISSI IYLQPWHMLT SFIQYILLSP SYINVLNIYA
FCNVHDLSWG TKGAMANPLG KINTTEDGTF KMEVLVSSSE IQANYDKYLK VLNDFDPKSE
SRPTEPSYDE KKTGYYANVR SLVIIFWVIT NFIIVAVVLE TGGIADYIAM KSISTDDTLE
TAKKAEIPLM TSKASIYFNV ILWLVALSAL IRFIGCSIYM IVRFFKKVTF R
