Q4P9K9 · CHS8_USTMA
- ProteinChitin synthase 8
- GeneCHS8
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids2005 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer (Probable). Involved in mating tube and dikaryotic hyphae formation and required for the formation of invading hyphae during plant infection (PubMed:16314447, PubMed:20663961).
Catalytic activity
- [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H+ + UDPThis reaction proceeds in the forward direction.
[(1→4)-N-acetyl-β-D-glucosaminyl](n) RHEA-COMP:9593 + CHEBI:57705 = [(1→4)-N-acetyl-β-D-glucosaminyl](n+1) RHEA-COMP:9595 + CHEBI:15378 + CHEBI:58223
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cell periphery | |
Cellular Component | cell septum | |
Cellular Component | cytoplasmic vesicle membrane | |
Cellular Component | myosin complex | |
Cellular Component | plasma membrane | |
Molecular Function | actin binding | |
Molecular Function | ATP binding | |
Molecular Function | chitin synthase activity | |
Molecular Function | cytoskeletal motor activity | |
Biological Process | cell wall chitin biosynthetic process | |
Biological Process | cell wall organization |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameChitin synthase 8
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Ustilaginomycotina > Ustilaginomycetes > Ustilaginales > Ustilaginaceae > Ustilago
Accessions
- Primary accessionQ4P9K9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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. 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 in a tip-ward gradient at the hyphal apex (PubMed:16314447, PubMed:17042749).
Apical localization depends on F-actin and the motor domain, whereas motility requires microtubules (PubMed:20663961, PubMed:22027862, PubMed:27563844).
Apical localization depends on F-actin and the motor domain, whereas motility requires microtubules (PubMed:20663961, PubMed:22027862, PubMed:27563844).
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 929-949 | Helical | ||||
Sequence: KWVALTWAITFWIPSFILSRF | ||||||
Transmembrane | 965-985 | Helical | ||||
Sequence: LAINLIIWFICACAVFVIVVL | ||||||
Transmembrane | 1232-1252 | Helical | ||||
Sequence: ILLALSLFMVAILGFKFLAAL | ||||||
Transmembrane | 1604-1624 | Helical | ||||
Sequence: LIFTPGLCGFCLFSMRFIVFI | ||||||
Transmembrane | 1626-1646 | Helical | ||||
Sequence: LLSTIIAPVTVCYIVYLIVLV | ||||||
Transmembrane | 1653-1673 | Helical | ||||
Sequence: VPLTAIIMLAAIYGCQAVIFL | ||||||
Transmembrane | 1680-1700 | Helical | ||||
Sequence: MIGWMIVYIIGIPIWSLFLPL |
Keywords
- Cellular component
Phenotypes & Variants
Miscellaneous
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000270624 | 1-2005 | Chitin synthase 8 | |||
Sequence: MSALDEVAKLSQLTNITPDTIFSVLRDRFYAGLPYTALSDSILVSVNPYASSGNRNSDDTLREYTSDYRQTNKQLRAATLPPHIFAHACNAYFYMRRTGQDQSLLMAGDTSSGKSEVRRLALRALIDLSVAPPGKKGSKLGVQIPSAEYILEALGNSRTLENSNASRFGKYTELQFSDSGKLVGAKTLDYYLEKNRVVSAASSERNFHIFHYMVAGASDEEKQYLGIHDAASFRYLGQASRNMDTQDAAKFDRLKLAFKNVGFSKRNVASICQVLAAILHLGNIEFHYDRQRTQDSATIRNPEVLDKVAEYLGISSKSLEEALTYKTKMIRNEVCTILLDADGASDHRDDLAKSLYSLLFAWVNESLNEKLCRDDFDTFIGLLDLPGFQNLSKGNSLDQFCVNFACENLHRFMLRSVFEKRRDEFADEGISHLSPEVPYFDNAETLRLMTNQPGGLIHIMDDQARRMPKKTDQTMIEAFGKRWGNHPSFKVGPADRSGFSSFTISHYNSAVTYTSENLLEKNSEVVSTDFVSLLRGNPQESGKLRNDSSQSSGSTIPFIRGIFNTKVLKTQSHPKNDQTIVAAQQSVKPMRAPSTRRPNRGNTIKRTNTIKKADDDDSDEDAADAADASTSKKNAVRCVAGDFRGALDLLLETLEDTKTWFTLCLRPNDNQLPNQFEARVVKQQITTLGLSEMSRKLLNEYSVSMTYEEFCQRYADVPSLQAVQMRDAVSGEAKQKFSAARQVMSWSDQEAVSGRVKVFLSHTAFRELEDELRAADAEEVKNNEKRAQLDADAAARGESDPFSPVAVLADDYTRSRSNDFVGAYGDPFKERSSVALPLVGRGAAGNEDDLEEVKSQYSGMSGTLARHSFVGGLSGAPSFVASEAYAPSRNMFADMGKNGLNEKAGTAAFTEEPLGEVAEEVGVSSTRRKWVALTWAITFWIPSFILSRFRSLKRPDIRMAWREKLAINLIIWFICACAVFVIVVLGNLICPKQHVYSPTEFASHKGDSSFTAIRGEVFDLSNLVASHKTIVPVVPANSILAYAGEDATPIFPVQVNALCNGVDGNVSPWVQLSNENSTDKHAQYHDFRSYHIDDARPDWYYESMWLLRSNYRVGFMGYTTDGIRDILSEGRAVAIYRGDIYDVSDYIKQGNQGVLRAPDGFQAPANTNRKFMSDAIISLIAQNPGKDITKQLDNLPLDPVVLDRQRVCLRNLYFIGKVDHRNSPQCRFAQYILLALSLFMVAILGFKFLAALQFGRARKPEDHDKFVICQVPCYTEGEESMRKTINSLAALKYDDKRKLLFIICDGMIVGSGNDRPTPRIVLDILGADPNLEPEALSFLSLGEGSKQHNMAKIYSGLYEHHGHVVPYIVVVKCGKPSERSRPGNRGKRDSQLVLMRFLNKVHFGLPMNPMELEIYHQIKNVIGVNPSFYEYILQVDADTEVEAMSLNRFISAFIRDKKVIGLCGETALSNAKASIITMLQVYEYYISHYLAKAFESLFGSVTCLPGCFSMFRIRTPDTHRPLFIASQIVEDYAENRVDTLHTKNLLHLGEDRYLTTLVLKHFGKYKTIFVRDCKAWTVAPDDWKVLLSQRRRWINSTVHNLVELIFTPGLCGFCLFSMRFIVFIDLLSTIIAPVTVCYIVYLIVLVATANGTVPLTAIIMLAAIYGCQAVIFLLNRKFEMIGWMIVYIIGIPIWSLFLPLYSFWHMDDFSWGNTRVVMGEKGQKVVLHEEGTFDPSEIPLQTWTDYENELWERNSARSIGSIIEAARAENKSLGSRAGSQYAPSLYGQPMLPHNASFGHSPSPSYGGTPSQFGAFAPGPGSQIGGSQIGAGAGYFPQDAARQSTYSIGGGYGGQAMSMYGLPPSSSFGVPTGGSGFMPQPFNTTASMYGYPQQVAATQSIYGGSQLGFGGGFATAEQQQQQQQQQQAAGLSGSGGSKSPPREAVAGGLPSDSQIKLDIRSLIAESDLTTITKKQLRAKLEQKYATSIESKKAFINSEIENVLSES | ||||||
Glycosylation | 164 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 364 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 390 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 546 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1076 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1650 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1770 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1794 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1882 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Expression
Induction
Expression is slightly lower in the yeast form than in the mycelium and shows a maximal expression in the log phase at about 14-18 h of incubation (PubMed:22538468).
Shows a late increase in transcription at the stationary phase in both yeast and mycelial cells (PubMed:22538468).
Highly expressed during the stage of white tumors of plant infection (PubMed:22538468).
Shows a late increase in transcription at the stationary phase in both yeast and mycelial cells (PubMed:22538468).
Highly expressed during the stage of white tumors of plant infection (PubMed:22538468).
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-773 | Myosin motor | ||||
Sequence: DEVAKLSQLTNITPDTIFSVLRDRFYAGLPYTALSDSILVSVNPYASSGNRNSDDTLREYTSDYRQTNKQLRAATLPPHIFAHACNAYFYMRRTGQDQSLLMAGDTSSGKSEVRRLALRALIDLSVAPPGKKGSKLGVQIPSAEYILEALGNSRTLENSNASRFGKYTELQFSDSGKLVGAKTLDYYLEKNRVVSAASSERNFHIFHYMVAGASDEEKQYLGIHDAASFRYLGQASRNMDTQDAAKFDRLKLAFKNVGFSKRNVASICQVLAAILHLGNIEFHYDRQRTQDSATIRNPEVLDKVAEYLGISSKSLEEALTYKTKMIRNEVCTILLDADGASDHRDDLAKSLYSLLFAWVNESLNEKLCRDDFDTFIGLLDLPGFQNLSKGNSLDQFCVNFACENLHRFMLRSVFEKRRDEFADEGISHLSPEVPYFDNAETLRLMTNQPGGLIHIMDDQARRMPKKTDQTMIEAFGKRWGNHPSFKVGPADRSGFSSFTISHYNSAVTYTSENLLEKNSEVVSTDFVSLLRGNPQESGKLRNDSSQSSGSTIPFIRGIFNTKVLKTQSHPKNDQTIVAAQQSVKPMRAPSTRRPNRGNTIKRTNTIKKADDDDSDEDAADAADASTSKKNAVRCVAGDFRGALDLLLETLEDTKTWFTLCLRPNDNQLPNQFEARVVKQQITTLGLSEMSRKLLNEYSVSMTYEEFCQRYADVPSLQAVQMRDAVSGEAKQKFSAARQVMSWSDQEAVSGRVKVFLSHTAFRELEDELR | ||||||
Compositional bias | 585-606 | Polar residues | ||||
Sequence: QSVKPMRAPSTRRPNRGNTIKR | ||||||
Region | 585-631 | Disordered | ||||
Sequence: QSVKPMRAPSTRRPNRGNTIKRTNTIKKADDDDSDEDAADAADASTS | ||||||
Region | 647-669 | Actin-binding | ||||
Sequence: LDLLLETLEDTKTWFTLCLRPND | ||||||
Region | 1796-1821 | Disordered | ||||
Sequence: SFGHSPSPSYGGTPSQFGAFAPGPGS | ||||||
Compositional bias | 1912-1933 | Polar residues | ||||
Sequence: FATAEQQQQQQQQQQAAGLSGS | ||||||
Region | 1912-1950 | Disordered | ||||
Sequence: FATAEQQQQQQQQQQAAGLSGSGGSKSPPREAVAGGLPS | ||||||
Domain | 1948-2003 | DEK-C | ||||
Sequence: LPSDSQIKLDIRSLIAESDLTTITKKQLRAKLEQKYATSIESKKAFINSEIENVLS |
Domain
The N-terminal myosin motor-like domain (MMD) supports exocytosis but not long-range delivery of transport vesicles.
Sequence similarities
In the N-terminal section; belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.
In the C-terminal section; belongs to the chitin synthase family. Class V subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,005
- Mass (Da)222,618
- Last updated2005-07-19 v1
- ChecksumEAB6EA732428DA10
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 585-606 | Polar residues | ||||
Sequence: QSVKPMRAPSTRRPNRGNTIKR | ||||||
Compositional bias | 1912-1933 | Polar residues | ||||
Sequence: FATAEQQQQQQQQQQAAGLSGS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CM003147 EMBL· GenBank· DDBJ | KIS68630.1 EMBL· GenBank· DDBJ | Genomic DNA |