O13394 · CHS5_USTMA
- ProteinChitin synthase 5
- GeneCHS5
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1609 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
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.
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) + UDP + H+This 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:58223 + CHEBI:15378
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 | plasma membrane | |
Molecular Function | chitin synthase activity | |
Biological Process | cell wall organization | |
Biological Process | chitin biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameChitin synthase 5
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Ustilaginomycotina > Ustilaginomycetes > Ustilaginales > Ustilaginaceae > Ustilago
Accessions
- Primary accessionO13394
- 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 (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 in a tip-ward gradient at the hyphal apex
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
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-326 | Cytoplasmic | ||||
Sequence: MNPFESLPDAARPAQGTRPNRSDGPPPLPPLTIPGSTGRPQNPIFSPPPNLHHILPPGYLPQQQQQQQQQQQQQQQRSQQPFFSPPPPDAMSPPLGSHQAYLNSTSSQPTQRLPGISFQEPQRMPVQRSGPSRDSVKSYGDDKRSINDPNSSSTALTQVNSLDPESGFSAHNDTFRRKKSLVRPDRERMDPSHRQWYYRNHAAHMDVMAASGGRVGYMPSTTGHLPQHGAAPHGSGMAGIVGPGGGLSGLGVTGPTNVPPGGLGRAPPLRRGKSLLGRDEDQVETGINVLKRGVSLRRKQSKSGNKPSKEVPRDLGESKTSRIAPG | ||||||
Transmembrane | 327-347 | Helical | ||||
Sequence: PVGGWMIYCYILTICCPGPFL | ||||||
Topological domain | 348-364 | Extracellular | ||||
Sequence: RIFGIRTPEQQRAWREK | ||||||
Transmembrane | 365-385 | Helical | ||||
Sequence: MGLIGIITLIMAAVGFLTFGF | ||||||
Topological domain | 386-624 | Cytoplasmic | ||||
Sequence: TQTVCGQQPDRYTLGTIDVGSMTFNGYDYSFDGFIHPQVGPFGADTIYNRTNPIYSEPWSSGGQDGSLLFQKIGAACTGIISNRAGGAQPERYFDCTLVRQDGKGGYANSTMPMCHTGSIVDQFNDGAQPRNSVLKKRGQVSLQWNNVTDPARNLAVYRGSVLDLNRLNNLTTGLSYPELYDTLKRRNDSWAGRDVTSAVMRQRLEREFQCLEQITRVGFIDSETIGCVASKVELYLSL | ||||||
Transmembrane | 625-645 | Helical | ||||
Sequence: VFIIGVVAIKFFMAVMFGWFI | ||||||
Topological domain | 646-1176 | Extracellular | ||||
Sequence: SWRLGNYANETYEQRMKRAAEIEQWSDDIYRPAPAGYRPNARKHKSFLPAKSRFSVADPLSLKSGSRAPMPLSEKRMTRASRLGVASPLGGSPPGSPSVAGGRSSASLAPAHSRRSSFSGSPAEGAMGVCPFPLHNTIPQPGPDYRPFGFQLAHSICLVTAYSESFEGLRTTLDSLATTDYPNSHKLLLVIADGIVKGAGSDISTPDICLSMMKDLVIPAEEVEGNSYVAIADGYKRHNMCKIYAGFYDYDDETVERSKQQRVPMILVAKCGTPLEADSAKPGNRGKRDSQVLLMAFMQKVMFDERMTAFEYEFFNSIWRVTGVSPDNYEIVLCVDADTKVFPDSLSRMVACMVEDPEIMGLCGETKIANKSETWVTMIQVFEYYISHHQTKAFEACFGGVTCLPGCFSAYRIKAPKGPHGYWVPILANPDIVEHYSENVVDTLHKKNLLLLGEDRYLTTLMLKTFPKRKMMFVPQAVCKTIVPDTFRILLSQRRRWINSTVHNLFELVMVNDLCGTFCFSMRFVVFMELT | ||||||
Transmembrane | 1177-1197 | Helical | ||||
Sequence: GTLVLPAAIAFTLYVVVQAFL | ||||||
Topological domain | 1198-1202 | Cytoplasmic | ||||
Sequence: PNVPT | ||||||
Transmembrane | 1203-1223 | Helical | ||||
Sequence: PTIPLILLALILGLPGILIVV | ||||||
Topological domain | 1224-1227 | Extracellular | ||||
Sequence: TSRK | ||||||
Transmembrane | 1228-1248 | Helical | ||||
Sequence: IAYVGWMLIYLLSLPIWNFVL | ||||||
Topological domain | 1249-1609 | Cytoplasmic | ||||
Sequence: PLYAYWHMDDFSWGATRVVQGENKKDNHGDADGKFDPSHIVMKRWAEFERERRWKSGTHSRDSTYDVVQRTGSPERAGSTRYSVVSSDTFHSSPFGQHDQFGRALPNAMSSSSASQFGPDVSEVSHSKSPSGARARLDAVPLLELPAPLATDAKHRSGASPTGTVVVPRPRATSPAPLPHNSGHPALGSVSAFSPTQHSAGRLPTLPGAATYEAYPHTDAADEERRPMIGSTSSSPDPEPRRYIGPDAGVRHGNVSTEQRYPTVSESAYPMQAYTAEPETDGSASPTPAQQGFNAANSNQQTRPLTRGFSLVDDGPVASAQGVRQVQRGARRSQMPNSAASPPPANRTGNLPPGAAPPSFD |
Keywords
- Cellular component
Phenotypes & Variants
Miscellaneous
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000193723 | 1-1609 | Chitin synthase 5 | |||
Sequence: MNPFESLPDAARPAQGTRPNRSDGPPPLPPLTIPGSTGRPQNPIFSPPPNLHHILPPGYLPQQQQQQQQQQQQQQQRSQQPFFSPPPPDAMSPPLGSHQAYLNSTSSQPTQRLPGISFQEPQRMPVQRSGPSRDSVKSYGDDKRSINDPNSSSTALTQVNSLDPESGFSAHNDTFRRKKSLVRPDRERMDPSHRQWYYRNHAAHMDVMAASGGRVGYMPSTTGHLPQHGAAPHGSGMAGIVGPGGGLSGLGVTGPTNVPPGGLGRAPPLRRGKSLLGRDEDQVETGINVLKRGVSLRRKQSKSGNKPSKEVPRDLGESKTSRIAPGPVGGWMIYCYILTICCPGPFLRIFGIRTPEQQRAWREKMGLIGIITLIMAAVGFLTFGFTQTVCGQQPDRYTLGTIDVGSMTFNGYDYSFDGFIHPQVGPFGADTIYNRTNPIYSEPWSSGGQDGSLLFQKIGAACTGIISNRAGGAQPERYFDCTLVRQDGKGGYANSTMPMCHTGSIVDQFNDGAQPRNSVLKKRGQVSLQWNNVTDPARNLAVYRGSVLDLNRLNNLTTGLSYPELYDTLKRRNDSWAGRDVTSAVMRQRLEREFQCLEQITRVGFIDSETIGCVASKVELYLSLVFIIGVVAIKFFMAVMFGWFISWRLGNYANETYEQRMKRAAEIEQWSDDIYRPAPAGYRPNARKHKSFLPAKSRFSVADPLSLKSGSRAPMPLSEKRMTRASRLGVASPLGGSPPGSPSVAGGRSSASLAPAHSRRSSFSGSPAEGAMGVCPFPLHNTIPQPGPDYRPFGFQLAHSICLVTAYSESFEGLRTTLDSLATTDYPNSHKLLLVIADGIVKGAGSDISTPDICLSMMKDLVIPAEEVEGNSYVAIADGYKRHNMCKIYAGFYDYDDETVERSKQQRVPMILVAKCGTPLEADSAKPGNRGKRDSQVLLMAFMQKVMFDERMTAFEYEFFNSIWRVTGVSPDNYEIVLCVDADTKVFPDSLSRMVACMVEDPEIMGLCGETKIANKSETWVTMIQVFEYYISHHQTKAFEACFGGVTCLPGCFSAYRIKAPKGPHGYWVPILANPDIVEHYSENVVDTLHKKNLLLLGEDRYLTTLMLKTFPKRKMMFVPQAVCKTIVPDTFRILLSQRRRWINSTVHNLFELVMVNDLCGTFCFSMRFVVFMELTGTLVLPAAIAFTLYVVVQAFLPNVPTPTIPLILLALILGLPGILIVVTSRKIAYVGWMLIYLLSLPIWNFVLPLYAYWHMDDFSWGATRVVQGENKKDNHGDADGKFDPSHIVMKRWAEFERERRWKSGTHSRDSTYDVVQRTGSPERAGSTRYSVVSSDTFHSSPFGQHDQFGRALPNAMSSSSASQFGPDVSEVSHSKSPSGARARLDAVPLLELPAPLATDAKHRSGASPTGTVVVPRPRATSPAPLPHNSGHPALGSVSAFSPTQHSAGRLPTLPGAATYEAYPHTDAADEERRPMIGSTSSSPDPEPRRYIGPDAGVRHGNVSTEQRYPTVSESAYPMQAYTAEPETDGSASPTPAQQGFNAANSNQQTRPLTRGFSLVDDGPVASAQGVRQVQRGARRSQMPNSAASPPPANRTGNLPPGAAPPSFD | ||||||
Glycosylation | 654 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1015 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1144 | 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.
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-188 | Disordered | ||||
Sequence: MNPFESLPDAARPAQGTRPNRSDGPPPLPPLTIPGSTGRPQNPIFSPPPNLHHILPPGYLPQQQQQQQQQQQQQQQRSQQPFFSPPPPDAMSPPLGSHQAYLNSTSSQPTQRLPGISFQEPQRMPVQRSGPSRDSVKSYGDDKRSINDPNSSSTALTQVNSLDPESGFSAHNDTFRRKKSLVRPDRER | ||||||
Compositional bias | 20-55 | Pro residues | ||||
Sequence: NRSDGPPPLPPLTIPGSTGRPQNPIFSPPPNLHHIL | ||||||
Compositional bias | 59-80 | Polar residues | ||||
Sequence: YLPQQQQQQQQQQQQQQQRSQQ | ||||||
Compositional bias | 97-134 | Polar residues | ||||
Sequence: SHQAYLNSTSSQPTQRLPGISFQEPQRMPVQRSGPSRD | ||||||
Compositional bias | 145-168 | Polar residues | ||||
Sequence: SINDPNSSSTALTQVNSLDPESGF | ||||||
Compositional bias | 170-188 | Basic and acidic residues | ||||
Sequence: AHNDTFRRKKSLVRPDRER | ||||||
Region | 248-280 | Disordered | ||||
Sequence: SGLGVTGPTNVPPGGLGRAPPLRRGKSLLGRDE | ||||||
Region | 294-320 | Disordered | ||||
Sequence: VSLRRKQSKSGNKPSKEVPRDLGESKT | ||||||
Compositional bias | 303-317 | Basic and acidic residues | ||||
Sequence: SGNKPSKEVPRDLGE | ||||||
Region | 729-767 | Disordered | ||||
Sequence: GVASPLGGSPPGSPSVAGGRSSASLAPAHSRRSSFSGSP | ||||||
Compositional bias | 743-765 | Polar residues | ||||
Sequence: SVAGGRSSASLAPAHSRRSSFSG | ||||||
Compositional bias | 1354-1377 | Polar residues | ||||
Sequence: PNAMSSSSASQFGPDVSEVSHSKS | ||||||
Region | 1354-1381 | Disordered | ||||
Sequence: PNAMSSSSASQFGPDVSEVSHSKSPSGA | ||||||
Region | 1399-1609 | Disordered | ||||
Sequence: TDAKHRSGASPTGTVVVPRPRATSPAPLPHNSGHPALGSVSAFSPTQHSAGRLPTLPGAATYEAYPHTDAADEERRPMIGSTSSSPDPEPRRYIGPDAGVRHGNVSTEQRYPTVSESAYPMQAYTAEPETDGSASPTPAQQGFNAANSNQQTRPLTRGFSLVDDGPVASAQGVRQVQRGARRSQMPNSAASPPPANRTGNLPPGAAPPSFD | ||||||
Compositional bias | 1435-1449 | Polar residues | ||||
Sequence: LGSVSAFSPTQHSAG | ||||||
Compositional bias | 1504-1518 | Polar residues | ||||
Sequence: STEQRYPTVSESAYP | ||||||
Compositional bias | 1526-1555 | Polar residues | ||||
Sequence: PETDGSASPTPAQQGFNAANSNQQTRPLTR | ||||||
Compositional bias | 1574-1593 | Polar residues | ||||
Sequence: VQRGARRSQMPNSAASPPPA | ||||||
Compositional bias | 1594-1609 | Pro residues | ||||
Sequence: NRTGNLPPGAAPPSFD |
Sequence similarities
Belongs to the chitin synthase family. Class IV subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,609
- Mass (Da)176,298
- Last updated2015-09-16 v3
- ChecksumD37C3155BB515528
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 20-55 | Pro residues | ||||
Sequence: NRSDGPPPLPPLTIPGSTGRPQNPIFSPPPNLHHIL | ||||||
Sequence conflict | 54 | in Ref. 1; AAB84284 | ||||
Sequence: I → S | ||||||
Compositional bias | 59-80 | Polar residues | ||||
Sequence: YLPQQQQQQQQQQQQQQQRSQQ | ||||||
Sequence conflict | 75-76 | in Ref. 1; AAB84284 | ||||
Sequence: Missing | ||||||
Compositional bias | 97-134 | Polar residues | ||||
Sequence: SHQAYLNSTSSQPTQRLPGISFQEPQRMPVQRSGPSRD | ||||||
Compositional bias | 145-168 | Polar residues | ||||
Sequence: SINDPNSSSTALTQVNSLDPESGF | ||||||
Compositional bias | 170-188 | Basic and acidic residues | ||||
Sequence: AHNDTFRRKKSLVRPDRER | ||||||
Compositional bias | 303-317 | Basic and acidic residues | ||||
Sequence: SGNKPSKEVPRDLGE | ||||||
Compositional bias | 743-765 | Polar residues | ||||
Sequence: SVAGGRSSASLAPAHSRRSSFSG | ||||||
Compositional bias | 1354-1377 | Polar residues | ||||
Sequence: PNAMSSSSASQFGPDVSEVSHSKS | ||||||
Compositional bias | 1435-1449 | Polar residues | ||||
Sequence: LGSVSAFSPTQHSAG | ||||||
Compositional bias | 1504-1518 | Polar residues | ||||
Sequence: STEQRYPTVSESAYP | ||||||
Compositional bias | 1526-1555 | Polar residues | ||||
Sequence: PETDGSASPTPAQQGFNAANSNQQTRPLTR | ||||||
Compositional bias | 1574-1593 | Polar residues | ||||
Sequence: VQRGARRSQMPNSAASPPPA | ||||||
Compositional bias | 1594-1609 | Pro residues | ||||
Sequence: NRTGNLPPGAAPPSFD |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF030553 EMBL· GenBank· DDBJ | AAB84284.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CM003145 EMBL· GenBank· DDBJ | KIS69221.1 EMBL· GenBank· DDBJ | Genomic DNA |