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Protein

Chitin biosynthesis protein CHS5

Gene

CHS5

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

Component of the CHS5/6 complex which mediates export of specific cargo proteins, including chitin synthase CHS3. Also involved in targeting FUS1 to sites of polarized growth.8 Publications

GO - Biological processi

  • ascospore wall assembly Source: SGD
  • cellular bud site selection Source: SGD
  • cell wall chitin catabolic process Source: SGD
  • conjugation with cellular fusion Source: SGD
  • Golgi to plasma membrane transport Source: SGD
  • protein transport Source: UniProtKB-KW
  • regulation of transcription, DNA-templated Source: SGD
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:YLR330W-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Chitin biosynthesis protein CHS5
Alternative name(s):
Protein CAL3
Gene namesi
Name:CHS5
Synonyms:CAL3
Ordered Locus Names:YLR330W
ORF Names:L8543.18
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR330W.
SGDiS000004322. CHS5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • exomer complex Source: SGD
  • membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 671671Chitin biosynthesis protein CHS5PRO_0000089661Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei305 – 3051PhosphothreonineCombined sources
Modified residuei338 – 3381PhosphoserineCombined sources
Modified residuei362 – 3621PhosphoserineCombined sources
Modified residuei365 – 3651PhosphoserineCombined sources
Modified residuei383 – 3831PhosphoserineCombined sources
Modified residuei384 – 3841PhosphoserineCombined sources
Modified residuei573 – 5731PhosphoserineCombined sources
Modified residuei579 – 5791PhosphoserineCombined sources
Modified residuei590 – 5901PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12114.
PeptideAtlasiQ12114.

PTM databases

iPTMnetiQ12114.

Interactioni

Subunit structurei

Component of the CHS5/6 complex composed of the 4 CHAPS proteins BCH1, BCH2, BUD7, and CHS6 as well as at least CHS5 and GTP-bound ARF1. The complex interacts with the cargo protein CHS3.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARF1P110765EBI-4640,EBI-2816
BCH1Q0502913EBI-4640,EBI-27508
BCH2P361227EBI-4640,EBI-26374
BUD7Q087549EBI-4640,EBI-32770
CHS6P4095516EBI-4640,EBI-4649

Protein-protein interaction databases

BioGridi31594. 253 interactions.
DIPiDIP-8073N.
IntActiQ12114. 41 interactions.
MINTiMINT-1174352.

Structurei

Secondary structure

1
671
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 1310Combined sources
Beta strandi19 – 213Combined sources
Beta strandi27 – 315Combined sources
Turni32 – 343Combined sources
Beta strandi44 – 5310Combined sources
Helixi57 – 7418Combined sources
Beta strandi84 – 896Combined sources
Beta strandi94 – 985Combined sources
Beta strandi108 – 11710Combined sources
Turni126 – 1283Combined sources
Beta strandi131 – 1344Combined sources
Beta strandi142 – 15110Combined sources
Beta strandi154 – 16411Combined sources
Beta strandi176 – 1783Combined sources
Helixi183 – 1853Combined sources
Helixi189 – 19810Combined sources
Beta strandi205 – 2073Combined sources
Beta strandi214 – 2163Combined sources
Helixi227 – 2348Combined sources
Helixi243 – 2508Combined sources
Helixi258 – 2603Combined sources
Helixi266 – 2727Combined sources
Helixi279 – 2846Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IN3X-ray2.94A/C1-77[»]
4WJWX-ray2.59A1-77[»]
4YG8X-ray2.75A50-299[»]
ProteinModelPortaliQ12114.
SMRiQ12114. Positions 1-276.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini78 – 16891Fibronectin type-IIIPROSITE-ProRule annotationAdd
BLAST
Domaini166 – 26297BRCTPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi279 – 635357Glu-richAdd
BLAST
Compositional biasi645 – 67127Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the CHS5 family.Curated
Contains 1 BRCT domain.PROSITE-ProRule annotation
Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00730000113735.
HOGENOMiHOG000093664.
InParanoidiQ12114.
KOiK19877.
OMAiINGQQER.
OrthoDBiEOG7MH16T.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.40.50.10190. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR031673. Chs5_N.
IPR031669. Fn3_2.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00533. BRCT. 1 hit.
PF16892. CHS5_N. 1 hit.
PF16893. fn3_2. 1 hit.
[Graphical view]
SMARTiSM00292. BRCT. 1 hit.
SM00060. FN3. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
PS50853. FN3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12114-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSVDVLLTV GKLDASLALL TTQDHHVIEF PTVLLPENVK AGSIIKMQVS
60 70 80 90 100
QNLEEEKKQR NHFKSIQAKI LEKYGTHKPE SPVLKIVNVT QTSCVLAWDP
110 120 130 140 150
LKLGSAKLKS LILYRKGIRS MVIPNPFKVT TTKISGLSVD TPYEFQLKLI
160 170 180 190 200
TTSGTLWSEK VILRTHKMTD MSGITVCLGP LDPLKEISDL QISQCLSHIG
210 220 230 240 250
ARPLQRHVAI DTTHFVCNDL DNEESNEELI RAKHNNIPIV RPEWVRACEV
260 270 280 290 300
EKRIVGVRGF YLDADQSILK NYTFPPVNEE ELSYSKENEP VAEVADENKM
310 320 330 340 350
PEDTTDVEQV ASPNDNESNP SEAKEQGEKS GHETAPVSPV EDPLHASTAL
360 370 380 390 400
ENETTIETVN PSVRSLKSEP VGTPNIEENK ADSSAEAVVE EPNEAVAESS
410 420 430 440 450
PNEEATGQKS EDTDTHSNEQ ADNGFVQTEE VAENNITTES AGENNEPADD
460 470 480 490 500
AAMEFGRPEA EIETPEVNES IEDANEPAED SNEPVEDSNK PVKDSNKPVE
510 520 530 540 550
DSNKPVEDSN KPVEDSNKPV EDANEPVEDT SEPVEDAGEP VQETNEFTTD
560 570 580 590 600
IASPRHQEED IELEAEPKDA TESVAVEPSN EDVKPEEKGS EAEDDINNVS
610 620 630 640 650
KEAASGESTT HQKTEASASL ESSAVTEEQE TTEAEVNTDD VLSTKEAKKN
660 670
TGNSNSNKKK NKKNKKKGKK K
Length:671
Mass (Da):73,639
Last modified:November 1, 1997 - v1
Checksum:iFA92741B862814C2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49198 Genomic DNA. Translation: CAA89059.1.
U20618 Genomic DNA. Translation: AAB64526.1.
BK006945 Genomic DNA. Translation: DAA09638.1.
PIRiS53407.
RefSeqiNP_013434.1. NM_001182219.1.

Genome annotation databases

EnsemblFungiiYLR330W; YLR330W; YLR330W.
GeneIDi851041.
KEGGisce:YLR330W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49198 Genomic DNA. Translation: CAA89059.1.
U20618 Genomic DNA. Translation: AAB64526.1.
BK006945 Genomic DNA. Translation: DAA09638.1.
PIRiS53407.
RefSeqiNP_013434.1. NM_001182219.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IN3X-ray2.94A/C1-77[»]
4WJWX-ray2.59A1-77[»]
4YG8X-ray2.75A50-299[»]
ProteinModelPortaliQ12114.
SMRiQ12114. Positions 1-276.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31594. 253 interactions.
DIPiDIP-8073N.
IntActiQ12114. 41 interactions.
MINTiMINT-1174352.

PTM databases

iPTMnetiQ12114.

Proteomic databases

MaxQBiQ12114.
PeptideAtlasiQ12114.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR330W; YLR330W; YLR330W.
GeneIDi851041.
KEGGisce:YLR330W.

Organism-specific databases

EuPathDBiFungiDB:YLR330W.
SGDiS000004322. CHS5.

Phylogenomic databases

GeneTreeiENSGT00730000113735.
HOGENOMiHOG000093664.
InParanoidiQ12114.
KOiK19877.
OMAiINGQQER.
OrthoDBiEOG7MH16T.

Enzyme and pathway databases

BioCyciYEAST:YLR330W-MONOMER.

Miscellaneous databases

PROiQ12114.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.40.50.10190. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR031673. Chs5_N.
IPR031669. Fn3_2.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00533. BRCT. 1 hit.
PF16892. CHS5_N. 1 hit.
PF16893. fn3_2. 1 hit.
[Graphical view]
SMARTiSM00292. BRCT. 1 hit.
SM00060. FN3. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
PS50853. FN3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "CHS5, a gene involved in chitin synthesis and mating in Saccharomyces cerevisiae."
    Santos B., Duran A., Valdivieso M.H.
    Mol. Cell. Biol. 17:2485-2496(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: S288c / GRF88.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Chitin synthase 3 from yeast has zymogenic properties that depend on both the CAL1 and the CAL3 genes."
    Choi W.-J., Sburlati A., Cabib E.
    Proc. Natl. Acad. Sci. U.S.A. 91:4727-4730(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Fibronectin type III domains in yeast detected by a hidden Markov model."
    Bateman A., Chothia C.
    Curr. Biol. 6:1544-1546(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN FIBRONECTIN TYPE-III.
  6. "Targeting of chitin synthase 3 to polarized growth sites in yeast requires Chs5p and Myo2p."
    Santos B., Snyder M.
    J. Cell Biol. 136:95-110(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "Specific protein targeting during cell differentiation: polarized localization of Fus1p during mating depends on Chs5p in Saccharomyces cerevisiae."
    Santos B., Snyder M.
    Eukaryot. Cell 2:821-825(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "An interactional network of genes involved in chitin synthesis in Saccharomyces cerevisiae."
    Lesage G., Shapiro J., Specht C.A., Sdicu A.-M., Menard P., Hussein S., Tong A.H.Y., Boone C., Bussey H.
    BMC Genet. 6:8-8(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Arf1p, Chs5p and the ChAPs are required for export of specialized cargo from the Golgi."
    Trautwein M., Schindler C., Gauss R., Dengjel J., Hartmann E., Spang A.
    EMBO J. 25:943-954(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARF1; BCH1; BCH2; BUD7; CHS3 AND CHS6, DOMAIN.
  12. "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: FUNCTION.
  13. "Exomer: a coat complex for transport of select membrane proteins from the trans-Golgi network to the plasma membrane in yeast."
    Wang C.-W., Hamamoto S., Orci L., Schekman R.
    J. Cell Biol. 174:973-983(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE CHS5/6 COMPLEX, INTERACTION WITH ARF1, SUBCELLULAR LOCATION.
  14. "Chs5/6 complex: a multiprotein complex that interacts with and conveys chitin synthase III from the trans-Golgi network to the cell surface."
    Sanchatjate S., Schekman R.
    Mol. Biol. Cell 17:4157-4166(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE CHS5/6 COMPLEX, INTERACTION WITH CHS3.
  15. "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-590, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  16. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-362; SER-573 AND SER-590, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-305; SER-338; SER-365; SER-383; SER-384; SER-579 AND SER-590, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCHS5_YEAST
AccessioniPrimary (citable) accession number: Q12114
Secondary accession number(s): D6VYX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 8, 2016
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 172 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: 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.