ID   CHS2_CANAX              Reviewed;        1009 AA.
AC   P30572;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Chitin synthase 2;
DE            EC=2.4.1.16;
DE   AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 2;
GN   Name=CHS2;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1560778; DOI=10.1111/j.1365-2958.1992.tb01494.x;
RA   Chen-Wu J.L.-P., Zwicker J., Bowen A.R., Robbins P.W.;
RT   "Expression of chitin synthase genes during yeast and hyphal growth phases
RT   of Candida albicans.";
RL   Mol. Microbiol. 6:497-502(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   -!- DEVELOPMENTAL STAGE: Very high levels of CHS2 in cells undergoing
CC       hyphal outgrowth.
CC   -!- SIMILARITY: Belongs to the chitin synthase family. {ECO:0000305}.
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DR   EMBL; M82937; AAB59308.2; -; Genomic_DNA.
DR   PIR; S20538; S20538.
DR   AlphaFoldDB; P30572; -.
DR   BindingDB; P30572; -.
DR   ChEMBL; CHEMBL1961; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   VEuPathDB; FungiDB:CAWG_02178; -.
DR   VEuPathDB; FungiDB:CR_09020C_A; -.
DR   BRENDA; 2.4.1.16; 1096.
DR   PHI-base; PHI:7233; -.
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   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   2: Evidence at transcript level;
KW   Cell membrane; Cell wall biogenesis/degradation; Glycosyltransferase;
KW   Membrane; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1009
FT                   /note="Chitin synthase 2"
FT                   /id="PRO_0000193687"
FT   TRANSMEM        647..667
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        682..702
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        722..742
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        757..777
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        804..823
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        930..950
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        967..987
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          175..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..32
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1009 AA;  115586 MW;  182B660678549EF9 CRC64;
     MSYNNPNNSN SHLRPHAYNN SRRDDSDGDE SSIEFLNQRS NTPLTQGTYN YHNTSTNSLN
     FQQPEPIYRN QTRTSLSDSY YDHPIFDTSQ TQIQPPHDNP FTESYEMTDT SYQGNDHHYR
     TGQPNHLMNP TYNQAFIPHV YDEEDNDEQE YDQRIQYNQF QGDHFDLAAI SYADDESQSQ
     LDYVPTERVI PEGEEEEEEG ETSFEKEPGS ETISGPFGEE RSFEEPPPQQ EVRSKKLTRA
     TGLNGHLVLD CPVADELLSK FPDYNPAEKS GGLSREFAFM RYTAVTCGPS NFYRDAYILR
     PVHYPIPRQT ELMIVITMYN EDDILLGRTL KGVFKNIKYL ESKARSSTWG KDSWKKIVVC
     IVSDGRTKIN ERAQALLAGL GVYQEGLAKS RVDDKKVQAH MFEYTTRVGI SKVTDDVVKL
     TTEKVVPVQM LFCLKETNAK KINSHRWCFQ AIGQVLDPKI VVLLDCGTQP SGRSLYELWK
     EFDRDHRVAG ACGEITTSLK KRQMITNPLV YGQNFEYKIS NILDKPTESS FGFISVLPGA
     FSAYRFIALQ NDINGIGPLE KYFKGEFLHS SGELDPNDDE FQMKHLMLKE EAGIFTSNMY
     LAEDRILCFE LVAKRGCNWL LRYCKSARAE TDVPEGLAEF ILQRRRWLNG SFFAAIYSLV
     HFYKVWTSSH SFGRKIFLHI EFFYQLINLI VSWFSIGSYF LVFRILTTSL GDKALGFAPG
     KILSVIFLWL YLASIVTTFV LSFGNKPKGT EKFYVTIVIF FAILMAYMIF AAIFMAVHSI
     QDIYRSGTRI TVSLFFQNSE FRDLVVATSS TYALYFLASF LYFEPWHMFT SFVQYILLSP
     SYVNVLNIYA FCNIDDISWG TKGEVGGKSL GEAKLREDGT FDVSVPISKE QINQSYLDQL
     EKIRDPAPPE EKVLVTNTED YYAFIRSMTV LVWMFTNFVV IALVLETGGF NQFVEATDLA
     NLKSNRAAVF LTVILWTVAF MALFRFIGCI YYLITRLGRE IKASEHATK