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Protein

Chitin synthase 3

Gene

CHS3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Appears to be responsible for the synthesis of the majority of the chitin found in the cell wall periphery. It is involved in the synthesis of the chitin ring that forms in the cell wall just before bud emergence. This ring remains at the base of the bud as the bud grows and ultimately forms part of the bud scar marking the division site on the mother cell. Also catalyzes the synthesis of chitin laid down during mating and spore cell-wall synthesis.3 Publications

Catalytic activityi

UDP-N-acetyl-alpha-D-glucosamine + (1,4-(N-acetyl-beta-D-glucosaminyl))(n) = UDP + (1,4-(N-acetyl-beta-D-glucosaminyl))(n+1).1 Publication

GO - Molecular functioni

  • chitin synthase activity Source: SGD

GO - Biological processi

  • ascospore wall assembly Source: SGD
  • fungal-type cell wall chitin biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciYEAST:YBR023C-MONOMER.
BRENDAi2.4.1.16. 984.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.

Names & Taxonomyi

Protein namesi
Recommended name:
Chitin synthase 31 Publication (EC:2.4.1.161 Publication)
Alternative name(s):
Chitin-UDP acetyl-glucosaminyl transferase 3
Class-IV chitin synthase 3
Gene namesi
Name:CHS31 Publication
Synonyms:CAL11 Publication, CSD21 Publication, DIT1011 Publication, KIT2
Ordered Locus Names:YBR023CImported
ORF Names:YBR0305
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR023C.
SGDiS000000227. CHS3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 170170Extracellular1 PublicationAdd
BLAST
Transmembranei171 – 19121HelicalSequence analysisAdd
BLAST
Topological domaini192 – 20211Cytoplasmic1 PublicationAdd
BLAST
Transmembranei203 – 22321HelicalSequence analysisAdd
BLAST
Topological domaini224 – 452229Extracellular1 PublicationAdd
BLAST
Transmembranei453 – 47321HelicalSequence analysisAdd
BLAST
Topological domaini474 – 1006533Cytoplasmic1 PublicationAdd
BLAST
Transmembranei1007 – 102721HelicalSequence analysisAdd
BLAST
Topological domaini1028 – 10292Extracellular1 Publication
Transmembranei1030 – 105021HelicalSequence analysisAdd
BLAST
Topological domaini1051 – 10555Cytoplasmic1 Publication
Transmembranei1056 – 107621HelicalSequence analysisAdd
BLAST
Topological domaini1077 – 10804Extracellular1 Publication
Transmembranei1081 – 110121HelicalSequence analysisAdd
BLAST
Topological domaini1102 – 116564Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  • cellular bud neck Source: SGD
  • chitosome Source: SGD
  • cytoplasm Source: SGD
  • cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  • incipient cellular bud site Source: SGD
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: UniProtKB-SubCell
  • prospore membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi991 – 9911S → A: Reduces catalytic activity by 67%. 1 Publication
Mutagenesisi993 – 9931R → A: Reduces catalytic activity by 89%. 1 Publication
Mutagenesisi994 – 9941R → A: Completely abolishes catalytic activity. 1 Publication
Mutagenesisi995 – 9951R → A: Reduces catalytic activity by 87%. 1 Publication
Mutagenesisi999 – 9991S → A: Reduces catalytic activity by 59%. 1 Publication

Chemistry

ChEMBLiCHEMBL5597.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11651165Chitin synthase 3PRO_0000193729Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi82 – 821N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi114 – 1141N-linked (GlcNAc...)PROSITE-ProRule annotation
Cross-linki136 – 136Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Glycosylationi152 – 1521N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi163 – 1631N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi303 – 3031N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi332 – 3321N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi371 – 3711N-linked (GlcNAc...)PROSITE-ProRule annotation
Modified residuei537 – 5371PhosphoserineCombined sources
Modified residuei538 – 5381PhosphothreonineCombined sources

Post-translational modificationi

Glycoslated.1 Publication
Palmitoylated by PFA4; required for proper export from the ER.1 Publication

Keywords - PTMi

Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP29465.

PTM databases

iPTMnetiP29465.
SwissPalmiP29465.

Interactioni

Subunit structurei

Seems to interact with BNI4 and SKT5 which link CHS3 to septins.

Protein-protein interaction databases

BioGridi32726. 175 interactions.
DIPiDIP-2482N.
IntActiP29465. 19 interactions.
MINTiMINT-1363219.

Chemistry

BindingDBiP29465.

Structurei

Secondary structure

1
1165
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 2311Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WJWX-ray2.59P10-27[»]
ProteinModelPortaliP29465.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00530000064569.
HOGENOMiHOG000158449.
InParanoidiP29465.
KOiK00698.
OMAiTELEFEM.
OrthoDBiEOG7V76FQ.

Family and domain databases

InterProiIPR004835. Chitin_synth.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR22914. PTHR22914. 2 hits.
SUPFAMiSSF53448. SSF53448. 3 hits.

Sequencei

Sequence statusi: Complete.

P29465-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGLNGDDPD DYYLNLNQDE ESLLRSRHSV GSGAPHRQGS LVRPERSRLN
60 70 80 90 100
NPDNPHFYYA QKTQEQMNHL DVLPSSTGVN PNATRRSGSL RSKGSVRSKF
110 120 130 140 150
SGRETDSYLL QDMNTTDKKA SVKISDEGVA EDEFDKDGDV DNFEESSTQP
160 170 180 190 200
INKSIKPLRK ETNDTLSFWQ MYCYFITFWA PAPILAFCGM PKKERQMAWR
210 220 230 240 250
EKVALISVIL YIGAIVAFLT FGFTKTVCSS SKLRLKNNEV STEFVVINGK
260 270 280 290 300
AYELDTSSRS GIQDVEVDSD TLYGPWSDAG KDASFLFQNV NGNCHNLITP
310 320 330 340 350
KSNSSIPHDD DNNLAWYFPC KLKNQDGSSK PNFTVENYAG WNCHTSKEDR
360 370 380 390 400
DAFYGLKSKA DVYFTWDGIK NSSRNLIVYN GDVLDLDLLD WLEKDDVDYP
410 420 430 440 450
VVFDDLKTSN LQGYDLSLVL SNGHERKIAR CLSEIIKVGE VDSKTVGCIA
460 470 480 490 500
SDVVLYVSLV FILSVVIIKF IIACYFRWTV ARKQGAYIVD NKTMDKHTND
510 520 530 540 550
IEDWSNNIQT KAPLKEVDPH LRPKKYSKKS LGHKRASTFD LLKKHSSKMF
560 570 580 590 600
QFNESVIDLD TSMSSSLQSS GSYRGMTTMT TQNAWKLSNE NKAVHSRNPS
610 620 630 640 650
TLLPTSSMFW NKATSSPVPG SSLIQSLDST IIHPDIVQQP PLDFMPYGFP
660 670 680 690 700
LIHTICFVTC YSEDEEGLRT TLDSLSTTDY PNSHKLLMVV CDGLIKGSGN
710 720 730 740 750
DKTTPEIALG MMDDFVTPPD EVKPYSYVAV ASGSKRHNMA KIYAGFYKYD
760 770 780 790 800
DSTIPPENQQ RVPIITIVKC GTPAEQGAAK PGNRGKRDSQ IILMSFLEKI
810 820 830 840 850
TFDERMTQLE FQLLKNIWQI TGLMADFYET VLMVDADTKV FPDALTHMVA
860 870 880 890 900
EMVKDPLIMG LCGETKIANK AQSWVTAIQV FEYYISHHQA KAFESVFGSV
910 920 930 940 950
TCLPGCFSMY RIKSPKGSDG YWVPVLANPD IVERYSDNVT NTLHKKNLLL
960 970 980 990 1000
LGEDRFLSSL MLKTFPKRKQ VFVPKAACKT IAPDKFKVLL SQRRRWINST
1010 1020 1030 1040 1050
VHNLFELVLI RDLCGTFCFS MQFVIGIELI GTMVLPLAIC FTIYVIIFAI
1060 1070 1080 1090 1100
VSKPTPVITL VLLAIILGLP GLIVVITATR WSYLWWMCVY ICALPIWNFV
1110 1120 1130 1140 1150
LPSYAYWKFD DFSWGDTRTI AGGNKKAQDE NEGEFDHSKI KMRTWREFER
1160
EDILNRKEES DSFVA
Length:1,165
Mass (Da):131,601
Last modified:October 1, 1994 - v3
Checksum:iEBF9227DC30D3EA4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1163 – 11631F → L in AAA34844 (PubMed:1532231).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76078 Genomic DNA. Translation: CAA53680.1.
M73697 Genomic DNA. Translation: AAA34844.1.
Z35892 Genomic DNA. Translation: CAA84965.1.
X57300 Genomic DNA. Translation: CAA40559.1.
BK006936 Genomic DNA. Translation: DAA07145.1.
PIRiS45879.
RefSeqiNP_009579.1. NM_001178371.1.

Genome annotation databases

EnsemblFungiiYBR023C; YBR023C; YBR023C.
GeneIDi852311.
KEGGisce:YBR023C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76078 Genomic DNA. Translation: CAA53680.1.
M73697 Genomic DNA. Translation: AAA34844.1.
Z35892 Genomic DNA. Translation: CAA84965.1.
X57300 Genomic DNA. Translation: CAA40559.1.
BK006936 Genomic DNA. Translation: DAA07145.1.
PIRiS45879.
RefSeqiNP_009579.1. NM_001178371.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WJWX-ray2.59P10-27[»]
ProteinModelPortaliP29465.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32726. 175 interactions.
DIPiDIP-2482N.
IntActiP29465. 19 interactions.
MINTiMINT-1363219.

Chemistry

BindingDBiP29465.
ChEMBLiCHEMBL5597.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.

PTM databases

iPTMnetiP29465.
SwissPalmiP29465.

Proteomic databases

MaxQBiP29465.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR023C; YBR023C; YBR023C.
GeneIDi852311.
KEGGisce:YBR023C.

Organism-specific databases

EuPathDBiFungiDB:YBR023C.
SGDiS000000227. CHS3.

Phylogenomic databases

GeneTreeiENSGT00530000064569.
HOGENOMiHOG000158449.
InParanoidiP29465.
KOiK00698.
OMAiTELEFEM.
OrthoDBiEOG7V76FQ.

Enzyme and pathway databases

BioCyciYEAST:YBR023C-MONOMER.
BRENDAi2.4.1.16. 984.

Miscellaneous databases

PROiP29465.

Family and domain databases

InterProiIPR004835. Chitin_synth.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR22914. PTHR22914. 2 hits.
SUPFAMiSSF53448. SSF53448. 3 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "CSD2, CSD3, and CSD4, genes required for chitin synthesis in Saccharomyces cerevisiae: the CSD2 gene product is related to chitin synthases and to developmentally regulated proteins in Rhizobium species and Xenopus laevis."
    Bulawa C.E.
    Mol. Cell. Biol. 12:1764-1776(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete sequence of a 33 kb fragment on the right arm of chromosome II from Saccharomyces cerevisiae reveals 16 open reading frames, including ten new open reading frames, five previously identified genes and a homologue of the SCO1 gene."
    Smits P.H.M., de Haan M., Maat C., Grivell L.A.
    Yeast 10:S75-S80(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "CAL1, a gene required for activity of chitin synthase 3 in Saccharomyces cerevisiae."
    Valdivieso M.H., Mol P.C., Shaw J.A., Cabib E., Duran A.
    J. Cell Biol. 114:101-109(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 67-1165, FUNCTION.
  6. "The function of chitin synthases 2 and 3 in the Saccharomyces cerevisiae cell cycle."
    Shaw J.A., Mol P.C., Bowers B., Silverman S.J., Valdivieso M.H., Duran A., Cabib E.
    J. Cell Biol. 114:111-123(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "DIT101 (CSD2, CAL1), a cell cycle-regulated yeast gene required for synthesis of chitin in cell walls and chitosan in spore walls."
    Pammer M., Briza P., Ellinger A., Schuster T., Stucka R., Feldmann H., Breitenbach M.
    Yeast 8:1089-1099(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Differential trafficking and timed localization of two chitin synthase proteins, Chs2p and Chs3p."
    Chuang J.S., Schekman R.W.
    J. Cell Biol. 135:597-610(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "Chs1p and Chs3p, two proteins involved in chitin synthesis, populate a compartment of the Saccharomyces cerevisiae endocytic pathway."
    Ziman M., Chuang J.S., Schekman R.W.
    Mol. Biol. Cell 7:1909-1919(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "Molecular analysis of Chs3p participation in chitin synthase III activity."
    Cos T., Ford R.A., Trilla J.A., Duran A., Cabib E., Roncero C.
    Eur. J. Biochem. 256:419-426(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, GLYCOSYLATION, MUTAGENESIS OF SER-991; ARG-993; ARG-994; ARG-995 AND SER-999.
  11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  12. Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-136.
    Strain: SUB592.
  13. "The yeasts Rho1p and Pkc1p regulate the transport of chitin synthase III (Chs3p) from internal stores to the plasma membrane."
    Valdivia R.H., Schekman R.
    Proc. Natl. Acad. Sci. U.S.A. 100:10287-10292(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  14. "Palmitoylation by the DHHC protein Pfa4 regulates the ER exit of Chs3."
    Lam K.K.Y., Davey M., Sun B., Roth A.F., Davis N.G., Conibear E.
    J. Cell Biol. 174:19-25(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  15. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  16. "Chitin synthase III requires Chs4p-dependent translocation of Chs3p into the plasma membrane."
    Reyes A., Sanz M., Duran A., Roncero C.
    J. Cell Sci. 120:1998-2009(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  17. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537 AND THR-538, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  18. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCHS3_YEAST
AccessioniPrimary (citable) accession number: P29465
Secondary accession number(s): D6VQ25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 1, 1994
Last modified: July 6, 2016
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1510 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.