ID   CHS3_CANAX              Reviewed;        1213 AA.
AC   P30573;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   02-SEP-2026, entry version 110.
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-IV chitin synthase 3;
GN   Name=CHS3;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC   Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8246889; DOI=10.1007/bf00284688;
RA   Sudoh M., Nagahashi S., Arisawa M., Takagi M.;
RT   "Cloning of the chitin synthase 3 gene from Candida albicans and its
RT   expression during yeast-hyphal transition.";
RL   Mol. Gen. Genet. 241:351-358(1993).
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) + UDP +
CC         H(+); 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 IV subfamily.
CC       {ECO:0000305}.
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DR   EMBL; D13454; BAA02707.1; -; Genomic_DNA.
DR   PIR; S39951; S39951.
DR   AlphaFoldDB; P30573; -.
DR   BindingDB; P30573; -.
DR   ChEMBL; CHEMBL2366568; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   GlyCosmos; P30573; 2 sites, No reported glycans.
DR   EnsemblFungi; C1_13110C_A-T; C1_13110C_A-T-p1; C1_13110C_A.
DR   CGD; CAL0000195982; CHS3.
DR   VEuPathDB; FungiDB:C1_13110C_A; -.
DR   VEuPathDB; FungiDB:CAWG_00138; -.
DR   PhylomeDB; P30573; -.
DR   BRENDA; 2.4.1.16; 1096.
DR   PHI-base; PHI:31; -.
DR   PHI-base; PHI:7234; -.
DR   GO; GO:0030428; C:cell septum; IDA:CGD.
DR   GO; GO:1903561; C:extracellular vesicle; IDA:CGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004100; F:chitin synthase activity; IMP:CGD.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; IMP:CGD.
DR   GO; GO:0006031; P:chitin biosynthetic process; IMP:CGD.
DR   GO; GO:0030448; P:hyphal growth; IMP:CGD.
DR   CDD; cd04190; Chitin_synth_C; 1.
DR   Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 1.
DR   InterPro; IPR004835; Chitin_synth.
DR   InterPro; IPR054295; CHS4-like_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR   PANTHER; PTHR22914:SF16; CHITIN SYNTHASE 3; 1.
DR   Pfam; PF03142; Chitin_synth_2; 1.
DR   Pfam; PF22997; CHS4; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cell wall biogenesis/degradation; Glycoprotein;
KW   Glycosyltransferase; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..1213
FT                   /note="Chitin synthase 3"
FT                   /id="PRO_0000193688"
FT   TOPO_DOM        1..168
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        190..200
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        222..450
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        451..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        472..1016
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1017..1037
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1038..1039
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1040..1060
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1061..1065
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1066..1086
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1087..1213
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          1..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1161..1213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        588
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        1008
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   1213 AA;  136208 MW;  E6D313EEACD10BC6 CRC64;
     MSNFRDSSSP RRGYSEFDPE SGEGLGRKKS LIRPERSRMD ESHPRFHYTQ VANQESNHIK
     VQPSSTGVDP RKSNELSTSR SHLSNYATPP HQEEEEDEGI PLMDIHNASP NVSSDQNNDL
     KGGREVYGLN DEINDYGSSP KKNQVISSSR PMNNEKPAKP KHDIYFWKVY CYAITFWAPA
     PLLKLFGLPT KDRQFAWREK IGLISCILYV GAFVAYLTFG FTKTVCSSQV VRTQINHVNG
     GYLIINGRAY DLTSSQHPKA AGIQAGSNVL YPPMNAGGKD ASFLFQNVNG NCKGLIKPRD
     NCSIPYDGDE LAWYMPCRLF NQDGSTKPNN TFAYYKGWAC HTSETARDAY YKLKVNGDVY
     FTWDDVKNSS RNLVVYSGNV LDLDLINWIE TDDVTYPELF DKLRDDETYR GLDISLVLTN
     SEERQAARCL TEIIKVGSID TDTIGCIASK VVLYMSLVFI LSVVVVKFIM ACWFKWVTSR
     KQGATMYDSK AWAKRNREIE DWVDHDHGIG AEVKTVPVKA RANYKAAKTN RQSVFHRAQK
     LSLGPNADLS QYYDNPNALS KTFKYTTMST QAALLGRNGY GKRGNNANKS VSGGFNGRQS
     NLYLTDQGSS TDLLNRPVSS YNPFDSMGDD SIVINGLSPD IIHPDVVPQP PVEYQPFGYP
     LAHTINLVTC YSEDEEGIRI TLDSIATTDY PNSHKLILVI CDGIIKGSGN DETTPDIVLD
     MMSDLTVPRD EVEAYSYVAV AQGSKRHNMA KVYAGFYKYN DETVPPEKQQ RIPMITIVKC
     GTPEEASAPK PGNRGKRDSQ IILMSFLQKV VFDERMTSLE YEMLQSIWRI TGLMAEFYEI
     VLMVDADTKV FPDSLTHMVA EMVKDPTIMG LCGETKISNK AQTWVTAIQV FEYYISHHQA
     KAFESIFGGV TCLPGCFCMY RIKAPKGSDG YWVPILANPD IVERYSDNVV DTLHRKNLLL
     LGEDRYLSSL MLRTFPTRKQ VFVPKAACKT VVPDKFKVLL SQRRRWINST VHNLFELVLV
     KDLCGTFCFS MQFVIFIELI GTLVLPAAIT FTIYVIIVAI VSKPTPVMSL VLLAVIFGLP
     GCLIVITVSS LSYLVYFVIY LFALPIWNFV LPSYAYWKFD DFSWGETRTV AGGDKGDHSA
     VEGKFDSSKI AMKRWREWER ERRSTENRKQ QQQQQLTNNS SNNLAVPGAA WDPSNTGGNL
     IDDLSQGSSS GSS
//