ID   CHS3_EXODE              Reviewed;         885 AA.
AC   P30602; O74678;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Chitin synthase 3;
DE            EC=2.4.1.16;
DE   AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 3;
DE   AltName: Full=Class-III chitin synthase 3;
GN   Name=CHS3;
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   Wang Z., Graybill J.R., Szaniszlo P.J.;
RT   "Characterization and expression studies of WdCHS3, a gene that encodes a
RT   class III chitin synthase and contributes to virulence in Wangiella
RT   (Exophiala) dermatitidis.";
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 214-410.
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 III subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF053314; AAC35278.1; -; Genomic_DNA.
DR   EMBL; M81907; AAA30336.1; -; Genomic_DNA.
DR   AlphaFoldDB; P30602; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   PRIDE; P30602; -.
DR   VEuPathDB; FungiDB:HMPREF1120_06479; -.
DR   PHI-base; PHI:237; -.
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; IPR001173; Glyco_trans_2-like.
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   Pfam; PF13632; Glyco_trans_2_3; 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..885
FT                   /note="Chitin synthase 3"
FT                   /id="PRO_0000193696"
FT   TRANSMEM        565..585
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        620..640
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        650..670
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        707..727
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        735..755
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        837..857
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        215
FT                   /note="Y -> M (in Ref. 2; AAA30336)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        340
FT                   /note="R -> S (in Ref. 2; AAA30336)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   885 AA;  99423 MW;  48D00BEE408398F0 CRC64;
     MASQYPGHQL DDIPSTNVYR PPPRHEDDEA EHALLHQNSA YQSQYDDPHS RPLTPGQESV
     YTLNESYVGG DPSKVPVTSY NPQYTQPYGQ GYGMNNSRPG FPTPGPPDPI DRTDSTEAWR
     ERQAPGFGTI KRYATRKVKL VQGSVLSIDY PVPSAIQNAI QAKYRNDLEG GSEEFTHMRY
     TAATCDPDDF TLKNGYNLRP AMYNRHTELL IAITYYNEDK VLTARTLHGV MQNIRDIVNL
     KKSEFWNKGG PAWQKIVVCL VFDGIDPCDK NTLDVLATIG VYQDGVMKKD VDGKETVAHI
     FEYTTQLSVT ANQQLIRPND NDATSLPPAQ MIFCLKQKNR KKINSHRWLF NAFGRILNPE
     VCILLDAGTK PGSKSLMALW QAFYNDKDLG GACGEIHAML GPGGVFGRKL LNPLVAAQNF
     EYKISNILDK PLESSFGYVS VLPGAFSAYR FRAIMGRPLE QYFHGDHTLS KTLGKKGIEG
     MNIFKKNMFL AEDRILCFEL VAKAGSKWHL SYVKASKAET DVPEGPPEFI GQRRRWLNGS
     FAASMYCLMH FSRMYKSGHN LIRMFFLHIQ MIYNIVSVLL SWFSLASFWL TTKVLMDLVG
     QPSTSNDNAA FPFGNTATPI INTILQYLYL AFLLLQFILA LGNRPKGSKV AYIISFCLFG
     LIQLYVIVLS MYLVVRAFTT KNGTDIVTNE GANEFVKSFF ASTGPGIVII ALAATFGLYF
     VASFLYMDPW HMFTSFAQYL LLMPSFINIL MIYAFSNWHD VSWGTKGSDK ADVLPSAQTK
     KDEKSKTAVV EEVDKPQADI DSQFEATVRR ALAPYKPPEE KEEKTLEDSY KNFRTRLVAT
     WIFSNALLAV AITSDSLDRF GFTSEPLRGP AISSRRFCGL LRPCL