Q4P9K9 · CHS8_USTMA

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

Features

Showing features for binding site.

120052004006008001,0001,2001,4001,6001,8002,000
TypeIDPosition(s)Description
Binding site108-115ATP (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcell periphery
Cellular Componentcell septum
Cellular Componentcytoplasmic vesicle membrane
Cellular Componentmyosin complex
Cellular Componentplasma membrane
Molecular Functionactin binding
Molecular FunctionATP binding
Molecular Functionchitin synthase activity
Molecular Functioncytoskeletal motor activity
Biological Processcell wall chitin biosynthetic process
Biological Processcell wall organization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Chitin synthase 8
  • EC number
  • Alternative names
    • Chitin-UDP acetyl-glucosaminyl transferase 8
    • Class-V chitin synthase
    • Myosin chitin synthase 1

Gene names

    • Name
      CHS8
    • Synonyms
      ChsV
      , MCS1
    • ORF names
      UMAG_03204

Organism names

Accessions

  • Primary accession
    Q4P9K9
  • Secondary accessions
    • A0A0D1E236

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Multi-pass membrane protein
Cytoplasmic vesicle membrane
; Multi-pass membrane protein
Cell tip
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).

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane929-949Helical
Transmembrane965-985Helical
Transmembrane1232-1252Helical
Transmembrane1604-1624Helical
Transmembrane1626-1646Helical
Transmembrane1653-1673Helical
Transmembrane1680-1700Helical

Keywords

Phenotypes & Variants

PTM/Processing

Features

Showing features for chain, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00002706241-2005Chitin synthase 8
Glycosylation164N-linked (GlcNAc...) asparagine
Glycosylation364N-linked (GlcNAc...) asparagine
Glycosylation390N-linked (GlcNAc...) asparagine
Glycosylation546N-linked (GlcNAc...) asparagine
Glycosylation1076N-linked (GlcNAc...) asparagine
Glycosylation1650N-linked (GlcNAc...) asparagine
Glycosylation1770N-linked (GlcNAc...) asparagine
Glycosylation1794N-linked (GlcNAc...) asparagine
Glycosylation1882N-linked (GlcNAc...) asparagine

Keywords

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).

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, compositional bias, region.

TypeIDPosition(s)Description
Domain5-773Myosin motor
Compositional bias585-606Polar residues
Region585-631Disordered
Region647-669Actin-binding
Region1796-1821Disordered
Compositional bias1912-1933Polar residues
Region1912-1950Disordered
Domain1948-2003DEK-C

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    2,005
  • Mass (Da)
    222,618
  • Last updated
    2005-07-19 v1
  • Checksum
    EAB6EA732428DA10
MSALDEVAKLSQLTNITPDTIFSVLRDRFYAGLPYTALSDSILVSVNPYASSGNRNSDDTLREYTSDYRQTNKQLRAATLPPHIFAHACNAYFYMRRTGQDQSLLMAGDTSSGKSEVRRLALRALIDLSVAPPGKKGSKLGVQIPSAEYILEALGNSRTLENSNASRFGKYTELQFSDSGKLVGAKTLDYYLEKNRVVSAASSERNFHIFHYMVAGASDEEKQYLGIHDAASFRYLGQASRNMDTQDAAKFDRLKLAFKNVGFSKRNVASICQVLAAILHLGNIEFHYDRQRTQDSATIRNPEVLDKVAEYLGISSKSLEEALTYKTKMIRNEVCTILLDADGASDHRDDLAKSLYSLLFAWVNESLNEKLCRDDFDTFIGLLDLPGFQNLSKGNSLDQFCVNFACENLHRFMLRSVFEKRRDEFADEGISHLSPEVPYFDNAETLRLMTNQPGGLIHIMDDQARRMPKKTDQTMIEAFGKRWGNHPSFKVGPADRSGFSSFTISHYNSAVTYTSENLLEKNSEVVSTDFVSLLRGNPQESGKLRNDSSQSSGSTIPFIRGIFNTKVLKTQSHPKNDQTIVAAQQSVKPMRAPSTRRPNRGNTIKRTNTIKKADDDDSDEDAADAADASTSKKNAVRCVAGDFRGALDLLLETLEDTKTWFTLCLRPNDNQLPNQFEARVVKQQITTLGLSEMSRKLLNEYSVSMTYEEFCQRYADVPSLQAVQMRDAVSGEAKQKFSAARQVMSWSDQEAVSGRVKVFLSHTAFRELEDELRAADAEEVKNNEKRAQLDADAAARGESDPFSPVAVLADDYTRSRSNDFVGAYGDPFKERSSVALPLVGRGAAGNEDDLEEVKSQYSGMSGTLARHSFVGGLSGAPSFVASEAYAPSRNMFADMGKNGLNEKAGTAAFTEEPLGEVAEEVGVSSTRRKWVALTWAITFWIPSFILSRFRSLKRPDIRMAWREKLAINLIIWFICACAVFVIVVLGNLICPKQHVYSPTEFASHKGDSSFTAIRGEVFDLSNLVASHKTIVPVVPANSILAYAGEDATPIFPVQVNALCNGVDGNVSPWVQLSNENSTDKHAQYHDFRSYHIDDARPDWYYESMWLLRSNYRVGFMGYTTDGIRDILSEGRAVAIYRGDIYDVSDYIKQGNQGVLRAPDGFQAPANTNRKFMSDAIISLIAQNPGKDITKQLDNLPLDPVVLDRQRVCLRNLYFIGKVDHRNSPQCRFAQYILLALSLFMVAILGFKFLAALQFGRARKPEDHDKFVICQVPCYTEGEESMRKTINSLAALKYDDKRKLLFIICDGMIVGSGNDRPTPRIVLDILGADPNLEPEALSFLSLGEGSKQHNMAKIYSGLYEHHGHVVPYIVVVKCGKPSERSRPGNRGKRDSQLVLMRFLNKVHFGLPMNPMELEIYHQIKNVIGVNPSFYEYILQVDADTEVEAMSLNRFISAFIRDKKVIGLCGETALSNAKASIITMLQVYEYYISHYLAKAFESLFGSVTCLPGCFSMFRIRTPDTHRPLFIASQIVEDYAENRVDTLHTKNLLHLGEDRYLTTLVLKHFGKYKTIFVRDCKAWTVAPDDWKVLLSQRRRWINSTVHNLVELIFTPGLCGFCLFSMRFIVFIDLLSTIIAPVTVCYIVYLIVLVATANGTVPLTAIIMLAAIYGCQAVIFLLNRKFEMIGWMIVYIIGIPIWSLFLPLYSFWHMDDFSWGNTRVVMGEKGQKVVLHEEGTFDPSEIPLQTWTDYENELWERNSARSIGSIIEAARAENKSLGSRAGSQYAPSLYGQPMLPHNASFGHSPSPSYGGTPSQFGAFAPGPGSQIGGSQIGAGAGYFPQDAARQSTYSIGGGYGGQAMSMYGLPPSSSFGVPTGGSGFMPQPFNTTASMYGYPQQVAATQSIYGGSQLGFGGGFATAEQQQQQQQQQQAAGLSGSGGSKSPPREAVAGGLPSDSQIKLDIRSLIAESDLTTITKKQLRAKLEQKYATSIESKKAFINSEIENVLSES

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias585-606Polar residues
Compositional bias1912-1933Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM003147
EMBL· GenBank· DDBJ
KIS68630.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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