Reviewed,
UniProtKB/Swiss-Prot Q4P333 (CHS7_USTMA)
Last modified
November 3, 2009.
Version 31.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Chitin synthase 7 EC=2.4.1.16 Alternative name(s): Chitin-UDP acetyl-glucosaminyl transferase 7 | ||||
| Gene names |
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| Organism | Ustilago maydis (Smut fungus) [Complete proteome] | ||||
| Taxonomic identifier | 5270 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Basidiomycota › Ustilaginomycotina › Ustilaginomycetes › Ustilaginales › Ustilaginaceae › Ustilago |
Protein attributes
| Sequence length | 1273 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Plays a major role in cell wall biogenesis. Required for the proper morphology of yeast-like cells. Involved in mating tube and dikaryotic hyphae formation. Essential for pathogenicity. Ref.2 |
| Catalytic activity | UDP-N-acetyl-D-glucosamine + (1,4-(N-acetyl-beta-D-glucosaminyl))(n) = UDP + (1,4-(N-acetyl-beta-D-glucosaminyl))(n+1). |
| Subcellular location | Cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane; Multi-pass membrane protein. Note: A constitutive cytoplasmic pool is present that localizes to intracellular microvesicles termed chitosomes. Chitosomes constitute a separate secretory route distinct from the typical secretory pathway and serve as a vehicle for delivering the enzyme to the sites on the cell surface where polysaccharide sythesis takes place By similarity. Localizes to septa of yeast-like cells and to the basal septum separating the living tip cell from the vacuolated part in hyphae. Also localizes to the growing bud tip in yeast-like cells and to the tip of the hyphae. |
| Sequence similarities | Belongs to the chitin synthase family. Class IV subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell wall biogenesis/degradation |
| Cellular component | Cell membrane Cytoplasmic vesicle Membrane |
| Domain | Transmembrane |
| Molecular function | Glycosyltransferase Transferase |
| PTM | Glycoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasmic vesicle Inferred from electronic annotation. Source: UniProtKB-KW integral to membraneInferred from electronic annotation. Source: UniProtKB-SubCell plasma membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | chitin synthase activity Inferred from electronic annotation. Source: EC heme bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1273 | 1273 | Chitin synthase 7 | PRO_0000270623 | |||||
Regions | |||||||||
| Transmembrane | 80 – 100 | 21 | Potential | ||||||
| Transmembrane | 118 – 138 | 21 | Potential | ||||||
| Transmembrane | 361 – 381 | 21 | Potential | ||||||
| Transmembrane | 821 – 841 | 21 | Potential | ||||||
| Transmembrane | 858 – 878 | 21 | Potential | ||||||
| Transmembrane | 882 – 902 | 21 | Potential | ||||||
| Compositional bias | 1213 – 1243 | 31 | Pro-rich | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 22 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 229 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 253 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 269 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 980 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1070 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis." Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J. Birren B.W.Nature 444:97-101(2006) [PubMed: 17080091] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 521. |
| [2] | "Polar localizing class V myosin chitin synthases are essential during early plant infection in the plant pathogenic fungus Ustilago maydis." Weber I., Assmann D., Thines E., Steinberg G. Plant Cell 18:225-242(2006) [PubMed: 16314447] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION. |
Cross-references
Sequence databases | |
|---|---|
| AACP01000197 Genomic DNA. Translation: EAK86413.1. | |
| RefSeq | XP_761627.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q4P333. |
Genome annotation databases | |
| GeneID | 3633595. |
| KEGG | uma:UM05480.1. |
Phylogenomic databases | |
| OMA | ETRIANK. |
Enzyme and pathway databases | |
| BRENDA | 2.4.1.16. 2320. |
Family and domain databases | |
| InterPro | IPR004835. Chitin_synth_fng. IPR001199. Cyt_B5. [Graphical view] |
| Pfam | PF03142. Chitin_synth_2. 1 hit. PF00173. Cyt-b5. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CHS7_USTMA | ||||||||
| Accession | Primary (citable) accession number: Q4P333 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

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