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P29465 (CHS3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chitin synthase 3

EC=2.4.1.16
Alternative name(s):
Chitin-UDP acetyl-glucosaminyl transferase 3
Class-IV chitin synthase 3
Gene names
Name:CHS3
Synonyms:CAL1, CSD2, DIT101, KIT2
Ordered Locus Names:YBR023C
ORF Names:YBR0305
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1165 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

Subunit structure

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

Subcellular location

Membrane; Multi-pass membrane protein.

Miscellaneous

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

Sequence similarities

Belongs to the chitin synthase family. Class IV subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11651165Chitin synthase 3
PRO_0000193729

Regions

Topological domain1 – 170170Extracellular Potential
Transmembrane171 – 19121Helical; Potential
Topological domain192 – 20211Cytoplasmic Potential
Transmembrane203 – 22321Helical; Potential
Topological domain224 – 452229Extracellular Potential
Transmembrane453 – 47321Helical; Potential
Topological domain474 – 1006533Cytoplasmic Potential
Transmembrane1007 – 102721Helical; Potential
Topological domain1028 – 10292Extracellular Potential
Transmembrane1030 – 105021Helical; Potential
Topological domain1051 – 10555Cytoplasmic Potential
Transmembrane1056 – 107621Helical; Potential
Topological domain1077 – 10804Extracellular Potential
Transmembrane1081 – 110121Helical; Potential
Topological domain1102 – 116564Cytoplasmic Potential

Amino acid modifications

Modified residue5371Phosphoserine Ref.9
Modified residue5381Phosphothreonine Ref.9
Cross-link136Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7

Experimental info

Sequence conflict11631F → L in AAA34844. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P29465 [UniParc].

Last modified October 1, 1994. Version 3.
Checksum: EBF9227DC30D3EA4

FASTA1,165131,601
        10         20         30         40         50         60 
MTGLNGDDPD DYYLNLNQDE ESLLRSRHSV GSGAPHRQGS LVRPERSRLN NPDNPHFYYA 

        70         80         90        100        110        120 
QKTQEQMNHL DVLPSSTGVN PNATRRSGSL RSKGSVRSKF SGRETDSYLL QDMNTTDKKA 

       130        140        150        160        170        180 
SVKISDEGVA EDEFDKDGDV DNFEESSTQP INKSIKPLRK ETNDTLSFWQ MYCYFITFWA 

       190        200        210        220        230        240 
PAPILAFCGM PKKERQMAWR EKVALISVIL YIGAIVAFLT FGFTKTVCSS SKLRLKNNEV 

       250        260        270        280        290        300 
STEFVVINGK AYELDTSSRS GIQDVEVDSD TLYGPWSDAG KDASFLFQNV NGNCHNLITP 

       310        320        330        340        350        360 
KSNSSIPHDD DNNLAWYFPC KLKNQDGSSK PNFTVENYAG WNCHTSKEDR DAFYGLKSKA 

       370        380        390        400        410        420 
DVYFTWDGIK NSSRNLIVYN GDVLDLDLLD WLEKDDVDYP VVFDDLKTSN LQGYDLSLVL 

       430        440        450        460        470        480 
SNGHERKIAR CLSEIIKVGE VDSKTVGCIA SDVVLYVSLV FILSVVIIKF IIACYFRWTV 

       490        500        510        520        530        540 
ARKQGAYIVD NKTMDKHTND IEDWSNNIQT KAPLKEVDPH LRPKKYSKKS LGHKRASTFD 

       550        560        570        580        590        600 
LLKKHSSKMF QFNESVIDLD TSMSSSLQSS GSYRGMTTMT TQNAWKLSNE NKAVHSRNPS 

       610        620        630        640        650        660 
TLLPTSSMFW NKATSSPVPG SSLIQSLDST IIHPDIVQQP PLDFMPYGFP LIHTICFVTC 

       670        680        690        700        710        720 
YSEDEEGLRT TLDSLSTTDY PNSHKLLMVV CDGLIKGSGN DKTTPEIALG MMDDFVTPPD 

       730        740        750        760        770        780 
EVKPYSYVAV ASGSKRHNMA KIYAGFYKYD DSTIPPENQQ RVPIITIVKC GTPAEQGAAK 

       790        800        810        820        830        840 
PGNRGKRDSQ IILMSFLEKI TFDERMTQLE FQLLKNIWQI TGLMADFYET VLMVDADTKV 

       850        860        870        880        890        900 
FPDALTHMVA EMVKDPLIMG LCGETKIANK AQSWVTAIQV FEYYISHHQA KAFESVFGSV 

       910        920        930        940        950        960 
TCLPGCFSMY RIKSPKGSDG YWVPVLANPD IVERYSDNVT NTLHKKNLLL LGEDRFLSSL 

       970        980        990       1000       1010       1020 
MLKTFPKRKQ VFVPKAACKT IAPDKFKVLL SQRRRWINST VHNLFELVLI RDLCGTFCFS 

      1030       1040       1050       1060       1070       1080 
MQFVIGIELI GTMVLPLAIC FTIYVIIFAI VSKPTPVITL VLLAIILGLP GLIVVITATR 

      1090       1100       1110       1120       1130       1140 
WSYLWWMCVY ICALPIWNFV LPSYAYWKFD DFSWGDTRTI AGGNKKAQDE NEGEFDHSKI 

      1150       1160 
KMRTWREFER EDILNRKEES DSFVA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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.
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"A proteomics approach to understanding protein ubiquitination."
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P.
Nat. Biotechnol. 21:921-926(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-136.
Strain: SUB592.
[8]"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.
[9]"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.
[10]"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].
[11]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS45879.
RefSeqNP_009579.1. NM_001178371.1.

3D structure databases

ProteinModelPortalP29465.
SMRP29465. Positions 235-290.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32726. 174 interactions.
DIPDIP-2482N.
IntActP29465. 19 interactions.
MINTMINT-1363219.
STRING4932.YBR023C.

Protein family/group databases

CAZyGT2. Glycosyltransferase Family 2.

Proteomic databases

MaxQBP29465.
PaxDbP29465.
PeptideAtlasP29465.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR023C; YBR023C; YBR023C.
GeneID852311.
KEGGsce:YBR023C.

Organism-specific databases

CYGDYBR023c.
SGDS000000227. CHS3.

Phylogenomic databases

eggNOGCOG1215.
GeneTreeENSGT00530000064569.
HOGENOMHOG000158449.
KOK00698.
OMATELEFEM.
OrthoDBEOG7V76FQ.

Enzyme and pathway databases

BioCycYEAST:YBR023C-MONOMER.
BRENDA2.4.1.16. 984.

Gene expression databases

GenevestigatorP29465.

Family and domain databases

InterProIPR004835. Chitin_synth.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERPTHR22914. PTHR22914. 1 hit.
SUPFAMSSF53448. SSF53448. 3 hits.
ProtoNetSearch...

Other

NextBio970993.

Entry information

Entry nameCHS3_YEAST
AccessionPrimary (citable) accession number: P29465
Secondary accession number(s): D6VQ25
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 1, 1994
Last modified: June 11, 2014
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families