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Reviewed, UniProtKB/Swiss-Prot Q4P333 (CHS7_USTMA)

Last modified November 3, 2009. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Chitin synthase 7
    EC=2.4.1.16
Alternative name(s):
    Chitin-UDP acetyl-glucosaminyl transferase 7
Gene names
Name: CHS7
ORF Names: UM05480
OrganismUstilago maydis (Smut fungus) [Complete proteome]
Taxonomic identifier5270 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaUstilaginomycotinaUstilaginomycetesUstilaginalesUstilaginaceaeUstilago

Protein attributes

Sequence length1273 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred 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 processCell wall biogenesis/degradation
   Cellular componentCell membrane
Cytoplasmic vesicle
Membrane
   DomainTransmembrane
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcell wall organization

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasmic vesicle

Inferred from electronic annotation. Source: UniProtKB-KW

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionchitin synthase activity

Inferred from electronic annotation. Source: EC

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12731273Chitin synthase 7
PRO_0000270623

Regions

Transmembrane80 – 10021 Potential
Transmembrane118 – 13821 Potential
Transmembrane361 – 38121 Potential
Transmembrane821 – 84121 Potential
Transmembrane858 – 87821 Potential
Transmembrane882 – 90221 Potential
Compositional bias1213 – 124331Pro-rich

Amino acid modifications

Glycosylation221N-linked (GlcNAc...) Potential
Glycosylation2291N-linked (GlcNAc...) Potential
Glycosylation2531N-linked (GlcNAc...) Potential
Glycosylation2691N-linked (GlcNAc...) Potential
Glycosylation9801N-linked (GlcNAc...) Potential
Glycosylation10701N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q4P333-1 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: 4CB36E1DB66DC706

FASTA1,273140,139
        10         20         30         40         50         60 
MPAVERNAPF TKTFIRKPGQ RNDTSIPLHT EAPPPLRQPT RIARAKTLTR PERSQPQVPL 

        70         80         90        100        110        120 
INPSSGGPGF SAASRSKHRF SWWTAFSLFV TFWAPSPLLS SCCGLKDKQS RQAWREKVSL 

       130        140        150        160        170        180 
VFIAILLGGF IGFITMGLNA ALCPSASSHS PNTYSRIGTG GAILGVHGWA FDIAQAHHLP 

       190        200        210        220        230        240 
EAPALFSLST SRPGSDISSL FARSTSDQSP ACRGTTAAYA ADASCVALNG TLLKDCPLGP 

       250        260        270        280        290        300 
LSPATFAQYG MYNQTRKIGY GWEDVESANF SNFLVLDGVV LNMSPYLKAN PSPIAADVVD 

       310        320        330        340        350        360 
LAIRQQLATS PHRGRDATIT FYTNPTTRNA IKCLTQKYVA GYIDKITPGC FISNLVLYCS 

       370        380        390        400        410        420 
LVVILAIVLI RFFMAVWFAW FMAGRMSSPP RPSRRRRLAP NVLPEGAMIS LNSSGAAPWA 

       430        440        450        460        470        480 
NKQRPPPSQP ARRRRDSAQS ATPSVPDSLS VHHIGDEPYV VCLVTAYSEN EEGISTTLTS 

       490        500        510        520        530        540 
LSETHYSDQR KLLFVVADGM VTGSGESMST PDVCVSLLEA DPRFGTPIPM SFVSIASGKK 

       550        560        570        580        590        600 
EHNMAMVYAG HYTRATGRRT PMVVVVKCGA PEEAADSKPG NRGKRDSQMI LMNFFQRVTY 

       610        620        630        640        650        660 
NDRMTPLDYD LFRKVHTLMG VTPDFFELCL MVDADTMVYP KSMKTLTNCM MRDPMIMGAC 

       670        680        690        700        710        720 
GETRIANKTQ SWVTMIQVYE YFISHHQAKA FESVFGGVTC LPGCFSMYRI KARKQTDDDW 

       730        740        750        760        770        780 
VPIIVKPEVT REYSQSVVTT LHQKNLLLLG EDRFLTTTLL RTFPNRKMVF CPEARCKTEV 

       790        800        810        820        830        840 
PHTFKMLLSQ RRRWINSTIH NLMELVLVRD LCGTFCFSMQ FVVFMDLLGT AVLPISIALT 

       850        860        870        880        890        900 
YTLVVTYCLN PPHSFTEAIP LMLLVAVIGM PALLILLATR KVVYVLWMLI YLLALPVWNF 

       910        920        930        940        950        960 
VLPVYSFWHF DDFSWGETRK VEGEAKQTGH GDEGGSATGN AVPLRRWEDW ERSRLRKKKR 

       970        980        990       1000       1010       1020 
EEKRRRELER QFGSGFHNDN ASDGDPDRKE AGMPLSRPGS DSFSDSVTVS DFDDDKWGNQ 

      1030       1040       1050       1060       1070       1080 
IGGYDETLPP PVQIVRHSVW IGDQEVIIDT EDMEKMLETG WDDKAFRARN LSSASSTNAL 

      1090       1100       1110       1120       1130       1140 
LQAQQPQYPS AVNRNRLSQM GAFATKRDAP AVPEIPARYS MYVQNNGGGR PANGHGNSNG 

      1150       1160       1170       1180       1190       1200 
HYEPGSYEME RTPSPGEYAS LIRGGAPSPC SPGFGPAQPY GHSSAVSGGA GQYSTGSHAR 

      1210       1220       1230       1240       1250       1260 
QRSGGANAAY NQPHQHPPQP SQPPQPPQPA QPTRPGGAPA APPRGAGSQG SGFAGARPSN 

      1270 
PTGRGRSYHD RFS 

« Hide

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. expand/collapse author list , Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L., Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., 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.
RefSeqXP_761627.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ4P333.

Genome annotation databases

GeneID3633595.
KEGGuma:UM05480.1.

Phylogenomic databases

OMAETRIANK.

Enzyme and pathway databases

BRENDA2.4.1.16. 2320.

Family and domain databases

InterProIPR004835. Chitin_synth_fng.
IPR001199. Cyt_B5.
[Graphical view]
PfamPF03142. Chitin_synth_2. 1 hit.
PF00173. Cyt-b5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHS7_USTMA
AccessionPrimary (citable) accession number: Q4P333
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: July 19, 2005
Last modified: November 3, 2009
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents