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P30601 (CHS2_EXODE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Chitin synthase 2

EC=2.4.1.16
Alternative name(s):
Chitin-UDP acetyl-glucosaminyl transferase 2
Class-I chitin synthase 2
Gene names
Name:CHS2
OrganismExophiala dermatitidis (Wangiella dermatitidis)
Taxonomic identifier5970 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesChaetothyriomycetidaeChaetothyrialesHerpotrichiellaceaemitosporic HerpotrichiellaceaeExophiala

Protein attributes

Sequence length928 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Plays a major role in cell wall biogenesis.

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.

Sequence similarities

Belongs to the chitin synthase family. Class I subfamily.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 928928Chitin synthase 2
PRO_0000193695

Regions

Transmembrane472 – 49221Helical; Potential
Transmembrane570 – 58920Helical; Potential
Transmembrane613 – 63321Helical; Potential
Transmembrane644 – 66421Helical; Potential
Transmembrane678 – 69821Helical; Potential
Transmembrane723 – 74321Helical; Potential
Transmembrane753 – 77321Helical; Potential
Transmembrane854 – 87421Helical; Potential
Transmembrane893 – 91321Helical; Potential

Experimental info

Sequence conflict259 – 2602VV → KL in AAA30335. Ref.2
Sequence conflict4621M → L in AAA30335. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P30601 [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: 001AF053F8873C9B

FASTA928105,713
        10         20         30         40         50         60 
MAYNRLGSPQ RDGPYSPSAQ PQYDSRSPSP GRPLQPYIHP DEAYARQQPL HLQMPTASDD 

        70         80         90        100        110        120 
RLAMQPTYSV ENVHNPQAYG QQYGQHLPDS GDMGYGRNDY IVSPEEHHDA YYTQPYSPHP 

       130        140        150        160        170        180 
QGDYALDPYP SHDEPYRPDT DNVPILQPDS AYGPDPHTQP GMDYDDYQEE PRPTPSPAPI 

       190        200        210        220        230        240 
RRWKTVKEVQ LFNGNLVLDC PVPPKLLANV PHAKPPERDE FTHMRYSAAT CDPSDFHNER 

       250        260        270        280        290        300 
FTLRQRLFAK PRQTELFIVV TMYNEDEFLF ARTMIGVFKN IEFMCNRSSS KTWGKEAWKK 

       310        320        330        340        350        360 
IVVCIVSDGR AKINPRTRAV LAGLGVYQDG IAKQQVNGKD VTAHIYEYTT QVGLELKGTQ 

       370        380        390        400        410        420 
VSLKPRSATP VQLLFCLKEK NQKKINSHRW FFQAFGRVLD PNICVLIDAG TKPGKDSIYQ 

       430        440        450        460        470        480 
LWKAFDLEPM CGGACGEIKV MLDHGKKLLN PLVATQNFEY KMSNILDKPL ESAFGFISVL 

       490        500        510        520        530        540 
PGAFCAYRYV ALQNDKNGVG PLEKYFKGET MHADAGVFTA NMYLAEDRIL CFELVSKRNC 

       550        560        570        580        590        600 
RWILQYVKSA TGETDVPDRI PEFVLQRRRW LNGSFFAAVY AVAHVYQLWR TDHSFLRKLM 

       610        620        630        640        650        660 
FLIEFTYQTI NMLFAWFAIG NFFLVFRLLT ASLGTKETLG TAGTVLGVVF EFVYLGTLLY 

       670        680        690        700        710        720 
CFILSMGNRP QGNPKSYMMM VIFWSVLMVW LTFASIFLTV KSIETEVQQK DFSFSTIFNN 

       730        740        750        760        770        780 
STFFGLIVSL ASTYVLWFVA SFLFFDPWHM FTCFLQYIVL TPTYINVLNI YAFCNTHDIT 

       790        800        810        820        830        840 
WGTKGDDKAE KLPSANVKPG GKVDVLIPQD DGDLNAQYDS ELKKFATKPP KEVKAPNPAD 

       850        860        870        880        890        900 
KQEDYYKSFR SNVVTAWMIT NFILVAAVLN IAGFDRINVH DTQQQNSTIY LAVILWSVAG 

       910        920 
LSLFRFTGAC WFLVVRMVSL EIWSVCKV 

« Hide

References

[1]"Cloning and characterization of WdCHS2, a class I chitin synthase gene, in Wangiella (Exophiala) dermatitidis."
Zheng L., Szaniszlo P.J.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 8656.
[2]"Classification of fungal chitin synthases."
Bowen A.R., Chen-Wu J.L.-P., Momany M., Young R., Szaniszlo P.J., Robbins P.W.
Proc. Natl. Acad. Sci. U.S.A. 89:519-523(1992) [PubMed: 1731323] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 259-462.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF052606 Genomic DNA. Translation: AAC34496.1.
M81906 Genomic DNA. Translation: AAA30335.1.
PIRA45188.

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGT2. Glycosyltransferase Family 2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR004834. Chitin_synth.
IPR013616. Chitin_synth_N.
[Graphical view]
PfamPF01644. Chitin_synth_1. 1 hit.
PF08407. Chitin_synth_1N. 1 hit.
[Graphical view]
ProDomPD002998. Chitin_synth. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Entry information

Entry nameCHS2_EXODE
AccessionPrimary (citable) accession number: P30601
Secondary accession number(s): O74210
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: July 15, 1999
Last modified: May 31, 2011
This is version 65 of the entry and version 2 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