Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q4P9K9 (CHS8_USTMA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chitin synthase 8

EC=2.4.1.16
Alternative name(s):
Chitin-UDP acetyl-glucosaminyl transferase 8
Myosin chitin synthase 1
Gene names
Name:CHS8
Synonyms:MCS1
ORF Names:UM03204
OrganismUstilago maydis (strain 521 / FGSC 9021) (Smut fungus)
Taxonomic identifier237631 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaUstilaginomycotinaUstilaginomycetesUstilaginalesUstilaginaceaeUstilago

Protein attributes

Sequence length2005 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Plays a major role in cell wall biogenesis. Involved in mating tube and dikaryotic hyphae formation. Required for the formation of invading hyphae during plant infection. Essential for pathogenicity. Ref.3

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. 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. Ref.2 Ref.3

Sequence similarities

Belongs to the chitin synthase family. Class V subfamily.

Contains 2 myosin head-like domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20052005Chitin synthase 8
PRO_0000270624

Regions

Transmembrane929 – 94921Helical; Potential
Transmembrane965 – 98521Helical; Potential
Transmembrane1232 – 125221Helical; Potential
Transmembrane1604 – 162421Helical; Potential
Transmembrane1626 – 164621Helical; Potential
Transmembrane1653 – 167321Helical; Potential
Transmembrane1680 – 170021Helical; Potential
Domain7 – 535529Myosin head-like 1
Domain629 – 69264Myosin head-like 2
Compositional bias614 – 6218Poly-Asp
Compositional bias1917 – 192610Poly-Gln

Amino acid modifications

Glycosylation1641N-linked (GlcNAc...) Potential
Glycosylation3641N-linked (GlcNAc...) Potential
Glycosylation3901N-linked (GlcNAc...) Potential
Glycosylation5461N-linked (GlcNAc...) Potential
Glycosylation10761N-linked (GlcNAc...) Potential
Glycosylation16501N-linked (GlcNAc...) Potential
Glycosylation17701N-linked (GlcNAc...) Potential
Glycosylation17941N-linked (GlcNAc...) Potential
Glycosylation18821N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q4P9K9 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: EAB6EA732428DA10

FASTA2,005222,618
        10         20         30         40         50         60 
MSALDEVAKL SQLTNITPDT IFSVLRDRFY AGLPYTALSD SILVSVNPYA SSGNRNSDDT 

        70         80         90        100        110        120 
LREYTSDYRQ TNKQLRAATL PPHIFAHACN AYFYMRRTGQ DQSLLMAGDT SSGKSEVRRL 

       130        140        150        160        170        180 
ALRALIDLSV APPGKKGSKL GVQIPSAEYI LEALGNSRTL ENSNASRFGK YTELQFSDSG 

       190        200        210        220        230        240 
KLVGAKTLDY YLEKNRVVSA ASSERNFHIF HYMVAGASDE EKQYLGIHDA ASFRYLGQAS 

       250        260        270        280        290        300 
RNMDTQDAAK FDRLKLAFKN VGFSKRNVAS ICQVLAAILH LGNIEFHYDR QRTQDSATIR 

       310        320        330        340        350        360 
NPEVLDKVAE YLGISSKSLE EALTYKTKMI RNEVCTILLD ADGASDHRDD LAKSLYSLLF 

       370        380        390        400        410        420 
AWVNESLNEK LCRDDFDTFI GLLDLPGFQN LSKGNSLDQF CVNFACENLH RFMLRSVFEK 

       430        440        450        460        470        480 
RRDEFADEGI SHLSPEVPYF DNAETLRLMT NQPGGLIHIM DDQARRMPKK TDQTMIEAFG 

       490        500        510        520        530        540 
KRWGNHPSFK VGPADRSGFS SFTISHYNSA VTYTSENLLE KNSEVVSTDF VSLLRGNPQE 

       550        560        570        580        590        600 
SGKLRNDSSQ SSGSTIPFIR GIFNTKVLKT QSHPKNDQTI VAAQQSVKPM RAPSTRRPNR 

       610        620        630        640        650        660 
GNTIKRTNTI KKADDDDSDE DAADAADAST SKKNAVRCVA GDFRGALDLL LETLEDTKTW 

       670        680        690        700        710        720 
FTLCLRPNDN QLPNQFEARV VKQQITTLGL SEMSRKLLNE YSVSMTYEEF CQRYADVPSL 

       730        740        750        760        770        780 
QAVQMRDAVS GEAKQKFSAA RQVMSWSDQE AVSGRVKVFL SHTAFRELED ELRAADAEEV 

       790        800        810        820        830        840 
KNNEKRAQLD ADAAARGESD PFSPVAVLAD DYTRSRSNDF VGAYGDPFKE RSSVALPLVG 

       850        860        870        880        890        900 
RGAAGNEDDL EEVKSQYSGM SGTLARHSFV GGLSGAPSFV ASEAYAPSRN MFADMGKNGL 

       910        920        930        940        950        960 
NEKAGTAAFT EEPLGEVAEE VGVSSTRRKW VALTWAITFW IPSFILSRFR SLKRPDIRMA 

       970        980        990       1000       1010       1020 
WREKLAINLI IWFICACAVF VIVVLGNLIC PKQHVYSPTE FASHKGDSSF TAIRGEVFDL 

      1030       1040       1050       1060       1070       1080 
SNLVASHKTI VPVVPANSIL AYAGEDATPI FPVQVNALCN GVDGNVSPWV QLSNENSTDK 

      1090       1100       1110       1120       1130       1140 
HAQYHDFRSY HIDDARPDWY YESMWLLRSN YRVGFMGYTT DGIRDILSEG RAVAIYRGDI 

      1150       1160       1170       1180       1190       1200 
YDVSDYIKQG NQGVLRAPDG FQAPANTNRK FMSDAIISLI AQNPGKDITK QLDNLPLDPV 

      1210       1220       1230       1240       1250       1260 
VLDRQRVCLR NLYFIGKVDH RNSPQCRFAQ YILLALSLFM VAILGFKFLA ALQFGRARKP 

      1270       1280       1290       1300       1310       1320 
EDHDKFVICQ VPCYTEGEES MRKTINSLAA LKYDDKRKLL FIICDGMIVG SGNDRPTPRI 

      1330       1340       1350       1360       1370       1380 
VLDILGADPN LEPEALSFLS LGEGSKQHNM AKIYSGLYEH HGHVVPYIVV VKCGKPSERS 

      1390       1400       1410       1420       1430       1440 
RPGNRGKRDS QLVLMRFLNK VHFGLPMNPM ELEIYHQIKN VIGVNPSFYE YILQVDADTE 

      1450       1460       1470       1480       1490       1500 
VEAMSLNRFI SAFIRDKKVI GLCGETALSN AKASIITMLQ VYEYYISHYL AKAFESLFGS 

      1510       1520       1530       1540       1550       1560 
VTCLPGCFSM FRIRTPDTHR PLFIASQIVE DYAENRVDTL HTKNLLHLGE DRYLTTLVLK 

      1570       1580       1590       1600       1610       1620 
HFGKYKTIFV RDCKAWTVAP DDWKVLLSQR RRWINSTVHN LVELIFTPGL CGFCLFSMRF 

      1630       1640       1650       1660       1670       1680 
IVFIDLLSTI IAPVTVCYIV YLIVLVATAN GTVPLTAIIM LAAIYGCQAV IFLLNRKFEM 

      1690       1700       1710       1720       1730       1740 
IGWMIVYIIG IPIWSLFLPL YSFWHMDDFS WGNTRVVMGE KGQKVVLHEE GTFDPSEIPL 

      1750       1760       1770       1780       1790       1800 
QTWTDYENEL WERNSARSIG SIIEAARAEN KSLGSRAGSQ YAPSLYGQPM LPHNASFGHS 

      1810       1820       1830       1840       1850       1860 
PSPSYGGTPS QFGAFAPGPG SQIGGSQIGA GAGYFPQDAA RQSTYSIGGG YGGQAMSMYG 

      1870       1880       1890       1900       1910       1920 
LPPSSSFGVP TGGSGFMPQP FNTTASMYGY PQQVAATQSI YGGSQLGFGG GFATAEQQQQ 

      1930       1940       1950       1960       1970       1980 
QQQQQQAAGL SGSGGSKSPP REAVAGGLPS DSQIKLDIRS LIAESDLTTI TKKQLRAKLE 

      1990       2000 
QKYATSIESK KAFINSEIEN VLSES 

« 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 / FGSC 9021.
[2]"Immunolocalization of chitin synthases in the phytopathogenic dimorphic fungus Ustilago maydis."
Ruiz-Herrera J., Xoconostle-Cazares B., Reynaga-Pena C.G., Leon-Ramirez C., Carabez-Trejo A.
FEMS Yeast Res. 6:999-1009(2006) [PubMed: 17042749] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[3]"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

EMBL
GenBank
DDBJ
AACP01000108 Genomic DNA. Translation: EAK84434.1.
RefSeqXP_759351.1. XM_754258.1.

3D structure databases

HSSPHSSP built from PDB template 1MND based on UniProtKB P08799.
ProteinModelPortalQ4P9K9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ4P9K9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiUM03204T0; UM03204P0; UM03204.
GeneID3631285.
KEGGuma:UM03204.1.

Phylogenomic databases

eggNOGfuNOG06262.
HOGENOMHBG739106.
OMAFESLGEG.
OrthoDBEOG4KM2B4.

Family and domain databases

InterProIPR004835. Chitin_synth_fng.
IPR001199. Cyt_B5.
IPR014876. DEK_C.
IPR001609. Myosin_head_motor_dom.
[Graphical view]
Gene3DG3DSA:3.10.120.10. Cyt_B5. 1 hit.
KOK00698.
PfamPF03142. Chitin_synth_2. 1 hit.
PF00173. Cyt-b5. 1 hit.
PF08766. DEK_C. 1 hit.
PF00063. Myosin_head. 1 hit.
[Graphical view]
PRINTSPR00193. MYOSINHEAVY.
SMARTSM00242. MYSc. 1 hit.
[Graphical view]
SUPFAMSSF55856. Cyt_B5. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCHS8_USTMA
AccessionPrimary (citable) accession number: Q4P9K9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: July 19, 2005
Last modified: December 14, 2011
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families