ID A0A1D8PFK5_CANAL Unreviewed; 1213 AA.
AC A0A1D8PFK5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN Name=CHS3 {ECO:0000313|EMBL:AOW26920.1};
GN OrderedLocusNames=CAALFM_C113110CA {ECO:0000313|EMBL:AOW26920.1};
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561 {ECO:0000313|EMBL:AOW26920.1, ECO:0000313|Proteomes:UP000000559};
RN [1] {ECO:0000313|EMBL:AOW26920.1, ECO:0000313|Proteomes:UP000000559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2] {ECO:0000313|EMBL:AOW26920.1, ECO:0000313|Proteomes:UP000000559}
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=17419877; DOI=.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3] {ECO:0000313|EMBL:AOW26920.1, ECO:0000313|Proteomes:UP000000559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=24025428; DOI=.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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 Evidence={ECO:0000256|ARBA:ARBA00000319};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP017623; AOW26920.1; -; Genomic_DNA.
DR RefSeq; XP_722148.2; XM_717055.2.
DR AlphaFoldDB; A0A1D8PFK5; -.
DR STRING; 237561.A0A1D8PFK5; -.
DR EnsemblFungi; C1_13110C_A-T; C1_13110C_A-T-p1; C1_13110C_A.
DR GeneID; 3636199; -.
DR KEGG; cal:CAALFM_C113110CA; -.
DR VEuPathDB; FungiDB:C1_13110C_A; -.
DR eggNOG; KOG2571; Eukaryota.
DR InParanoid; A0A1D8PFK5; -.
DR OMA; VEAYSYV; -.
DR OrthoDB; 1331060at2759; -.
DR BRENDA; 2.4.1.16; 1096.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0071944; C:cell periphery; IBA:GO_Central.
DR GO; GO:0030428; C:cell septum; IBA:GO_Central.
DR GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR GO; GO:0045009; C:chitosome; IEA:EnsemblFungi.
DR GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
DR GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
DR GO; GO:0005628; C:prospore membrane; IEA:EnsemblFungi.
DR GO; GO:0004100; F:chitin synthase activity; IBA:GO_Central.
DR GO; GO:0030476; P:ascospore wall assembly; IEA:EnsemblFungi.
DR GO; GO:0006038; P:cell wall chitin biosynthetic process; IBA:GO_Central.
DR GO; GO:0034221; P:fungal-type cell wall chitin biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0097271; P:protein localization to bud neck; IEA:EnsemblFungi.
DR CDD; cd04190; Chitin_synth_C; 1.
DR InterPro; IPR004835; Chitin_synth.
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 SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000559};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 201..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 451..474
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1043..1061
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1068..1088
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1094..1117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
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"
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
//