CHS3_CANAX
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 25-MAY-2022, entry version 100.
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; Saccharomycetes;
OC Saccharomycetales; 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) + 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 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 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: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; IMP:CGD.
DR GO; GO:0006038; P:cell wall chitin biosynthetic process; IMP:CGD.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IMP:CGD.
DR GO; GO:0030448; P:hyphal growth; IMP:CGD.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; PTHR22914; 1.
DR SUPFAM; SSF53448; SSF53448; 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 11..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1213
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
