CHS2_YEAST
ID CHS2_YEAST Reviewed; 963 AA.
AC P14180; D6VQ38;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Chitin synthase 2;
DE EC=2.4.1.16;
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 2;
GN Name=CHS2; OrderedLocusNames=YBR038W; ORFNames=YBR0407;
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=2533436; DOI=10.1002/yea.320050605;
RA Silverman S.J.;
RT "Similar and different domains of chitin synthases 1 and 2 of S.
RT cerevisiae: two isozymes with distinct functions.";
RL Yeast 5:459-467(1989).
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 MUTAGENESIS.
RX PubMed=7775457; DOI=10.1074/jbc.270.23.13961;
RA Nagahashi S., Sudoh M., Ono N., Sawada R., Yamaguchi E., Uchida Y., Mio T.,
RA Takagi M., Arisawa M., Yamada-Okabe H.;
RT "Characterization of chitin synthase 2 of Saccharomyces cerevisiae.
RT Implication of two highly conserved domains as possible catalytic sites.";
RL J. Biol. Chem. 270:13961-13967(1995).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, 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-86 AND SER-133, 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-40; SER-82; SER-86; SER-100
RP AND SER-133, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 (Probable). Required for
CC septum formation (Probable). {ECO:0000305, ECO:0000305|PubMed:2533436}.
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: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the chitin synthase family. {ECO:0000305}.
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DR EMBL; M23865; AAA34493.1; -; Genomic_DNA.
DR EMBL; Z35907; CAA84980.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07158.1; -; Genomic_DNA.
DR PIR; S45167; S45167.
DR RefSeq; NP_009594.1; NM_001178386.1.
DR AlphaFoldDB; P14180; -.
DR BioGRID; 32739; 186.
DR DIP; DIP-3819N; -.
DR IntAct; P14180; 18.
DR MINT; P14180; -.
DR STRING; 4932.YBR038W; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR TCDB; 4.D.1.1.16; the putative vectorial glycosyl polymerization (vgp) family.
DR iPTMnet; P14180; -.
DR MaxQB; P14180; -.
DR PaxDb; P14180; -.
DR PRIDE; P14180; -.
DR EnsemblFungi; YBR038W_mRNA; YBR038W; YBR038W.
DR GeneID; 852326; -.
DR KEGG; sce:YBR038W; -.
DR SGD; S000000242; CHS2.
DR VEuPathDB; FungiDB:YBR038W; -.
DR eggNOG; KOG2571; Eukaryota.
DR HOGENOM; CLU_004760_3_2_1; -.
DR InParanoid; P14180; -.
DR OMA; FIISMGN; -.
DR BioCyc; MetaCyc:YBR038W-MON; -.
DR BioCyc; YEAST:YBR038W-MON; -.
DR BRENDA; 2.4.1.16; 984.
DR PRO; PR:P14180; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P14180; protein.
DR GO; GO:0071944; C:cell periphery; IBA:GO_Central.
DR GO; GO:0030428; C:cell septum; IBA:GO_Central.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0006031; P:chitin biosynthetic process; IMP:SGD.
DR GO; GO:1902406; P:mitotic actomyosin contractile ring maintenance; 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 wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW Membrane; Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..963
FT /note="Chitin synthase 2"
FT /id="PRO_0000193728"
FT TOPO_DOM 1..643
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 644..664
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 665..677
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 678..698
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 699..711
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 712..732
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 733..743
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 744..764
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 765..775
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 776..796
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 797..875
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 876..896
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 897..905
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 906..926
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 927..963
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 197
FT /note="N->A: 30% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 312
FT /note="S->A: 20% increase of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 355
FT /note="D->A: 10% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 393
FT /note="D->A: 5% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 441
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 441
FT /note="D->E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 447
FT /note="N->A: 80% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 490
FT /note="Q->A: 70% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 492
FT /note="F->A: 80% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 493
FT /note="E->A: 90% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 494
FT /note="Y->A: 95% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 497
FT /note="S->A: 95% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 502
FT /note="K->A: 90% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 505
FT /note="E->A: 80% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 506
FT /note="S->A: 20% increase of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 508
FT /note="F->A: 60% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 509
FT /note="G->A: 70% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 514
FT /note="L->A: 80% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 515
FT /note="P->A: 90% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 516
FT /note="G->A: 95% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 521
FT /note="Y->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 522
FT /note="R->A: 60% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 537
FT /note="R->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 550
FT /note="H->A: 85% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 556
FT /note="N->A: 95% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 559
FT /note="L->A: 95% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 561
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 561
FT /note="E->D: 65% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 561
FT /note="E->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 562
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 562
FT /note="D->E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 562
FT /note="D->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 563
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 563
FT /note="R->K: 94% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 565
FT /note="L->A: 95% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 589
FT /note="T->A: 70% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 592
FT /note="P->A: 70% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 601
FT /note="Q->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 601
FT /note="Q->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 602..603
FT /note="RR->KK: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 602
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 602
FT /note="R->K: 95% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 603
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 603
FT /note="R->K: 57% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 604
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 604
FT /note="R->K: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 605
FT /note="W->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 605
FT /note="W->Y: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
FT MUTAGEN 607
FT /note="N->A: 95% decrease of activity."
FT /evidence="ECO:0000269|PubMed:7775457"
SQ SEQUENCE 963 AA; 109882 MW; 4D44A287C0B65B5B CRC64;
MTRNPFMVEP SNGSPNRRGA SNLSKFYANA NSNSRWANPS EESLEDSYDQ SNVFQGLPAS
PSRAALRYSP DRRHRTQFYR DSAHNSPVAP NRYAANLQES PKRAGEAVIH LSEGSNLYPR
DNADLPVDPY HLSPQQQPSN NLFGSGRLYS QSSKYTMSTT STTAPSLAEA DDEKEKYLTS
TTSYDDQSTI FSADTFNETK FELNHPTRQQ YVRRANSESK RRMVSDLPPP SKKKALLKLD
NPIPKGLLDT LPRRNSPEFT EMRYTACTVE PDDFLREGYT LRFAEMNREC QIAICITMYN
EDKYSLARTI HSIMKNVAHL CKREKSHVWG PNGWKKVSVI LISDGRAKVN QGSLDYLAAL
GVYQEDMAKA SVNGDPVKAH IFELTTQVSI NADLDYVSKD IVPVQLVFCL KEENKKKINS
HRWLFNAFCP VLQPTVVTLV DVGTRLNNTA IYRLWKVFDM DSNVAGAAGQ IKTMKGKWGL
KLFNPLVASQ NFEYKISNIL DKPLESVFGY ISVLPGALSA YRYRALKNHE DGTGPLRSYF
LGETQEGRDH DVFTANMYLA EDRILCWELV AKRDAKWVLK YVKEATGETD VPEDVSEFIS
QRRRWLNGAM FAAIYAQLHF YQIWKTKHSV VRKFFLHVEF LYQFIQMLFS WFSIANFVLT
FYYLAGSMNL VIKHGEALFI FFKYLIFCDL ASLFIISMGN RPQGAKHLFI TSMVILSICA
TYSLICGFVF AFKSLASGTE SHKIFVDIVI SLLSTYGLYF FSSLMYLDPW HMFTSSIQYF
LTLPAFTCTL QIFAFCNTHD VSWGTKGSTQ ESKQLSKAIV VQGPDGKQIV ETDWPQEVDK
KFLEIKSRLK EPEFEESSGN EKQSKNDYYR DIRTRIVMIW MLSNLILIMS IIQVFTPQDT
DNGYLIFILW SVAALAAFRV VGSMAFLFMK YLRIIVSYRN KVEGSGSWEV SKLDLPNVFH
KKG
