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UniProtKB - P30573 (CHS3_CANAX)
Protein
Chitin synthase 3
Gene
CHS3
Organism
Candida albicans (Yeast)
Status
Functioni
Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
CuratedCatalytic activityi
- [(1→4)-N-acetyl-β-D-glucosaminyl](n) + UDP-N-acetyl-α-D-glucosamine = [(1→4)-N-acetyl-β-D-glucosaminyl](n+1) + H+ + UDPEC:2.4.1.16
GO - Molecular functioni
- chitin synthase activity Source: CGD
GO - Biological processi
- cellular response to mechanical stimulus Source: CGD
- cell wall chitin biosynthetic process Source: CGD
- cell wall organization Source: UniProtKB-KW
- hyphal growth Source: CGD
Keywordsi
Molecular function | Glycosyltransferase, Transferase |
Biological process | Cell wall biogenesis/degradation |
Enzyme and pathway databases
BRENDAi | 2.4.1.16, 1096 |
Protein family/group databases
CAZyi | GT2, Glycosyltransferase Family 2 |
Names & Taxonomyi
Protein namesi | Recommended name: Chitin synthase 3 (EC:2.4.1.16)Alternative name(s): Chitin-UDP acetyl-glucosaminyl transferase 3 Class-IV chitin synthase 3 |
Gene namesi | Name:CHS3 |
Organismi | Candida albicans (Yeast) |
Taxonomic identifieri | 5476 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Candida/Lodderomyces clade › Candida |
Organism-specific databases
CGDi | CAL0000195982, CHS3 |
VEuPathDBi | FungiDB:C1_13110C_A FungiDB:CAWG_00138 |
Subcellular locationi
Plasma membrane
- Cell membrane Curated; Multi-pass membrane protein Sequence analysis
Extracellular region or secreted
- extracellular vesicle Source: CGD
Plasma Membrane
- plasma membrane Source: UniProtKB-SubCell
Other locations
- cell septum Source: CGD
- integral component of membrane Source: UniProtKB-KW
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 168 | CytoplasmicCuratedAdd BLAST | 168 | |
Transmembranei | 169 – 189 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 190 – 200 | ExtracellularCuratedAdd BLAST | 11 | |
Transmembranei | 201 – 221 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 222 – 450 | CytoplasmicCuratedAdd BLAST | 229 | |
Transmembranei | 451 – 471 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 472 – 1016 | ExtracellularCuratedAdd BLAST | 545 | |
Transmembranei | 1017 – 1037 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1038 – 1039 | CytoplasmicCurated | 2 | |
Transmembranei | 1040 – 1060 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1061 – 1065 | ExtracellularCurated | 5 | |
Transmembranei | 1066 – 1086 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1087 – 1213 | CytoplasmicCuratedAdd BLAST | 127 |
Keywords - Cellular componenti
Cell membrane, MembranePathology & Biotechi
Miscellaneous databases
PHI-basei | PHI:31 PHI:7234 |
Chemistry databases
ChEMBLi | CHEMBL2366568 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000193688 | 1 – 1213 | Chitin synthase 3Add BLAST | 1213 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 588 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Glycosylationi | 1008 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 |
Keywords - PTMi
GlycoproteinStructurei
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 97 | DisorderedSequence analysisAdd BLAST | 97 | |
Regioni | 1161 – 1213 | DisorderedSequence analysisAdd BLAST | 53 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 11 – 45 | Basic and acidic residuesSequence analysisAdd BLAST | 35 | |
Compositional biasi | 47 – 88 | Polar residuesSequence analysisAdd BLAST | 42 | |
Compositional biasi | 1169 – 1189 | Polar residuesSequence analysisAdd BLAST | 21 | |
Compositional biasi | 1198 – 1213 | Polar residuesSequence analysisAdd BLAST | 16 |
Sequence similaritiesi
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
PhylomeDBi | P30573 |
Family and domain databases
Gene3Di | 3.90.550.10, 1 hit |
InterProi | View protein in InterPro IPR004835, Chitin_synth IPR029044, Nucleotide-diphossugar_trans |
PANTHERi | PTHR22914, PTHR22914, 1 hit |
SUPFAMi | SSF53448, SSF53448, 1 hit |
i Sequence
Sequence statusi: Complete.
P30573-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSNFRDSSSP RRGYSEFDPE SGEGLGRKKS LIRPERSRMD ESHPRFHYTQ
60 70 80 90 100
VANQESNHIK VQPSSTGVDP RKSNELSTSR SHLSNYATPP HQEEEEDEGI
110 120 130 140 150
PLMDIHNASP NVSSDQNNDL KGGREVYGLN DEINDYGSSP KKNQVISSSR
160 170 180 190 200
PMNNEKPAKP KHDIYFWKVY CYAITFWAPA PLLKLFGLPT KDRQFAWREK
210 220 230 240 250
IGLISCILYV GAFVAYLTFG FTKTVCSSQV VRTQINHVNG GYLIINGRAY
260 270 280 290 300
DLTSSQHPKA AGIQAGSNVL YPPMNAGGKD ASFLFQNVNG NCKGLIKPRD
310 320 330 340 350
NCSIPYDGDE LAWYMPCRLF NQDGSTKPNN TFAYYKGWAC HTSETARDAY
360 370 380 390 400
YKLKVNGDVY FTWDDVKNSS RNLVVYSGNV LDLDLINWIE TDDVTYPELF
410 420 430 440 450
DKLRDDETYR GLDISLVLTN SEERQAARCL TEIIKVGSID TDTIGCIASK
460 470 480 490 500
VVLYMSLVFI LSVVVVKFIM ACWFKWVTSR KQGATMYDSK AWAKRNREIE
510 520 530 540 550
DWVDHDHGIG AEVKTVPVKA RANYKAAKTN RQSVFHRAQK LSLGPNADLS
560 570 580 590 600
QYYDNPNALS KTFKYTTMST QAALLGRNGY GKRGNNANKS VSGGFNGRQS
610 620 630 640 650
NLYLTDQGSS TDLLNRPVSS YNPFDSMGDD SIVINGLSPD IIHPDVVPQP
660 670 680 690 700
PVEYQPFGYP LAHTINLVTC YSEDEEGIRI TLDSIATTDY PNSHKLILVI
710 720 730 740 750
CDGIIKGSGN DETTPDIVLD MMSDLTVPRD EVEAYSYVAV AQGSKRHNMA
760 770 780 790 800
KVYAGFYKYN DETVPPEKQQ RIPMITIVKC GTPEEASAPK PGNRGKRDSQ
810 820 830 840 850
IILMSFLQKV VFDERMTSLE YEMLQSIWRI TGLMAEFYEI VLMVDADTKV
860 870 880 890 900
FPDSLTHMVA EMVKDPTIMG LCGETKISNK AQTWVTAIQV FEYYISHHQA
910 920 930 940 950
KAFESIFGGV TCLPGCFCMY RIKAPKGSDG YWVPILANPD IVERYSDNVV
960 970 980 990 1000
DTLHRKNLLL LGEDRYLSSL MLRTFPTRKQ VFVPKAACKT VVPDKFKVLL
1010 1020 1030 1040 1050
SQRRRWINST VHNLFELVLV KDLCGTFCFS MQFVIFIELI GTLVLPAAIT
1060 1070 1080 1090 1100
FTIYVIIVAI VSKPTPVMSL VLLAVIFGLP GCLIVITVSS LSYLVYFVIY
1110 1120 1130 1140 1150
LFALPIWNFV LPSYAYWKFD DFSWGETRTV AGGDKGDHSA VEGKFDSSKI
1160 1170 1180 1190 1200
AMKRWREWER ERRSTENRKQ QQQQQLTNNS SNNLAVPGAA WDPSNTGGNL
1210
IDDLSQGSSS GSS
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D13454 Genomic DNA Translation: BAA02707.1 |
PIRi | S39951 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D13454 Genomic DNA Translation: BAA02707.1 |
PIRi | S39951 |
3D structure databases
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Chemistry databases
BindingDBi | P30573 |
ChEMBLi | CHEMBL2366568 |
Protein family/group databases
CAZyi | GT2, Glycosyltransferase Family 2 |
Organism-specific databases
CGDi | CAL0000195982, CHS3 |
VEuPathDBi | FungiDB:C1_13110C_A FungiDB:CAWG_00138 |
Phylogenomic databases
PhylomeDBi | P30573 |
Enzyme and pathway databases
BRENDAi | 2.4.1.16, 1096 |
Miscellaneous databases
PHI-basei | PHI:31 PHI:7234 |
Family and domain databases
Gene3Di | 3.90.550.10, 1 hit |
InterProi | View protein in InterPro IPR004835, Chitin_synth IPR029044, Nucleotide-diphossugar_trans |
PANTHERi | PTHR22914, PTHR22914, 1 hit |
SUPFAMi | SSF53448, SSF53448, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CHS3_CANAX | |
Accessioni | P30573Primary (citable) accession number: P30573 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1993 |
Last sequence update: | April 1, 1993 | |
Last modified: | September 29, 2021 | |
This is version 99 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |