CHS2_EXODE
ID CHS2_EXODE Reviewed; 928 AA.
AC P30601; O74210;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Chitin synthase 2;
DE EC=2.4.1.16;
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 2;
DE AltName: Full=Class-I chitin synthase 2;
GN Name=CHS2;
OS Exophiala dermatitidis (Black yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=5970;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=8656;
RA Zheng L., Szaniszlo P.J.;
RT "Cloning and characterization of WdCHS2, a class I chitin synthase gene, in
RT Wangiella (Exophiala) dermatitidis.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 259-462.
RX PubMed=1731323; DOI=10.1073/pnas.89.2.519;
RA Bowen A.R., Chen-Wu J.L.-P., Momany M., Young R., Szaniszlo P.J.,
RA Robbins P.W.;
RT "Classification of fungal chitin synthases.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:519-523(1992).
CC -!- FUNCTION: Polymerizes chitin, a structural polymer of the cell wall and
CC septum, by transferring the sugar moiety of UDP-GlcNAc to the non-
CC reducing end of the growing chitin polymer. {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-
CC D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) +
CC UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9595,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17029, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223; EC=2.4.1.16;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the chitin synthase family. Class I subfamily.
CC {ECO:0000305}.
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DR EMBL; AF052606; AAC34496.1; -; Genomic_DNA.
DR EMBL; M81906; AAA30335.1; -; Genomic_DNA.
DR PIR; A45188; A45188.
DR AlphaFoldDB; P30601; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR VEuPathDB; FungiDB:HMPREF1120_06816; -.
DR PHI-base; PHI:236; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006031; P:chitin biosynthetic process; IEA:InterPro.
DR GO; GO:0048315; P:conidium formation; IEA:UniProt.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR004834; Chitin_synth_fun.
DR InterPro; IPR013616; Chitin_synth_N.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; PTHR22914; 1.
DR Pfam; PF01644; Chitin_synth_1; 1.
DR Pfam; PF08407; Chitin_synth_1N; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cell wall biogenesis/degradation; Glycosyltransferase;
KW Membrane; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..928
FT /note="Chitin synthase 2"
FT /id="PRO_0000193695"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 570..589
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 613..633
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 644..664
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 678..698
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 723..743
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 753..773
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 854..874
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 893..913
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 259..260
FT /note="VV -> KL (in Ref. 2; AAA30335)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="M -> L (in Ref. 2; AAA30335)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 928 AA; 105713 MW; 001AF053F8873C9B CRC64;
MAYNRLGSPQ RDGPYSPSAQ PQYDSRSPSP GRPLQPYIHP DEAYARQQPL HLQMPTASDD
RLAMQPTYSV ENVHNPQAYG QQYGQHLPDS GDMGYGRNDY IVSPEEHHDA YYTQPYSPHP
QGDYALDPYP SHDEPYRPDT DNVPILQPDS AYGPDPHTQP GMDYDDYQEE PRPTPSPAPI
RRWKTVKEVQ LFNGNLVLDC PVPPKLLANV PHAKPPERDE FTHMRYSAAT CDPSDFHNER
FTLRQRLFAK PRQTELFIVV TMYNEDEFLF ARTMIGVFKN IEFMCNRSSS KTWGKEAWKK
IVVCIVSDGR AKINPRTRAV LAGLGVYQDG IAKQQVNGKD VTAHIYEYTT QVGLELKGTQ
VSLKPRSATP VQLLFCLKEK NQKKINSHRW FFQAFGRVLD PNICVLIDAG TKPGKDSIYQ
LWKAFDLEPM CGGACGEIKV MLDHGKKLLN PLVATQNFEY KMSNILDKPL ESAFGFISVL
PGAFCAYRYV ALQNDKNGVG PLEKYFKGET MHADAGVFTA NMYLAEDRIL CFELVSKRNC
RWILQYVKSA TGETDVPDRI PEFVLQRRRW LNGSFFAAVY AVAHVYQLWR TDHSFLRKLM
FLIEFTYQTI NMLFAWFAIG NFFLVFRLLT ASLGTKETLG TAGTVLGVVF EFVYLGTLLY
CFILSMGNRP QGNPKSYMMM VIFWSVLMVW LTFASIFLTV KSIETEVQQK DFSFSTIFNN
STFFGLIVSL ASTYVLWFVA SFLFFDPWHM FTCFLQYIVL TPTYINVLNI YAFCNTHDIT
WGTKGDDKAE KLPSANVKPG GKVDVLIPQD DGDLNAQYDS ELKKFATKPP KEVKAPNPAD
KQEDYYKSFR SNVVTAWMIT NFILVAAVLN IAGFDRINVH DTQQQNSTIY LAVILWSVAG
LSLFRFTGAC WFLVVRMVSL EIWSVCKV
