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UniProtKB - J9VXM5 (CHS3_CRYNH)
Protein
Chitin synthase 3
Gene
CHS3
Organism
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
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 (PubMed:16278457).
Activated by CSR2, it produces chitin that is deacetyled to chitosan, which is required to maintain cell wall integrity (PubMed:16278457, PubMed:16102007, PubMed:17400891, PubMed:32743128).
Conversion of chitin to chitosan offers an advantage during infection, as chitosan is less readily detected by host immunosurveillance mechanisms (PubMed:32071275).
5 PublicationsCatalytic 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+ + UDPBy similarityEC:2.4.1.16By similarity
GO - Molecular functioni
- chitin synthase activity Source: UniProtKB
GO - Biological processi
- cell wall organization Source: UniProtKB-KW
- fungal-type cell wall chitin biosynthetic process Source: UniProtKB
- protein localization to bud neck Source: EnsemblFungi
Keywordsi
Molecular function | Glycosyltransferase, Transferase |
Biological process | Cell wall biogenesis/degradation |
Names & Taxonomyi
Protein namesi | Recommended name: Chitin synthase 3By similarity (EC:2.4.1.16By similarity)Alternative name(s): Chitin-UDP acetyl-glucosaminyl transferase 3 Class-IV chitin synthase 3 |
Gene namesi | Name:CHS31 Publication ORF Names:CNAG_05581 |
Organismi | Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) |
Taxonomic identifieri | 235443 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Tremellomycetes › Tremellales › Cryptococcaceae › Cryptococcus › Cryptococcus neoformans species complex › |
Proteomesi |
|
Organism-specific databases
VEuPathDBi | FungiDB:CNAG_05581 |
Subcellular locationi
Plasma membrane
- Cell membrane 1 Publication; Multi-pass membrane protein Sequence analysis
Plasma Membrane
- plasma membrane Source: UniProtKB-SubCell
Other locations
- cellular bud neck Source: EnsemblFungi
- chitosome Source: EnsemblFungi
- incipient cellular bud site Source: EnsemblFungi
- integral component of membrane Source: UniProtKB-KW
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 212 | CytoplasmicCuratedAdd BLAST | 212 | |
Transmembranei | 213 – 233 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 234 – 247 | ExtracellularCuratedAdd BLAST | 14 | |
Transmembranei | 248 – 268 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 269 – 505 | CytoplasmicCuratedAdd BLAST | 237 | |
Transmembranei | 506 – 526 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 527 – 1067 | ExtracellularCuratedAdd BLAST | 541 | |
Transmembranei | 1068 – 1088 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1089 – 1097 | CytoplasmicCurated | 9 | |
Transmembranei | 1098 – 1118 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1119 – 1122 | ExtracellularCurated | 4 | |
Transmembranei | 1123 – 1143 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1144 – 1421 | CytoplasmicCuratedAdd BLAST | 278 |
Keywords - Cellular componenti
Cell membrane, MembranePathology & Biotechi
Disruption phenotypei
Increases cellular chitin level and decreases cellular chitosan level (PubMed:16278457, PubMed:17400891, PubMed:32071275). Swollen cell with abnormal cytokinesis (PubMed:16278457, PubMed:17400891, PubMed:32743128, PubMed:32071275). Abnormal capsular morphology: lower fiber density, short fibers, decreases capsular diameter (PubMed:32743128). Decreases extracellular vesicle secretion (PubMed:32743128). Melanization of surrounding media (PubMed:16278457, PubMed:17400891). Increases CHS5 and CHS7 RNA level (PubMed:16278457). Sensitive to: caspofungin (cell wall stress inducer), sodium dodecyl sulfate (cell wall stress inducer), Congo Red (cell wall stress inducer), Calcofluor White (cell wall stressor), caffeine, NaCl (osmotic stressor), high temperature (PubMed:16278457, PubMed:17400891, PubMed:31266771, PubMed:32071275). Intranasal inoculation with high inoculum causes rapid mortality in mouse; mortality is not due to fungal burden but to a strong hyperinflammatory response in the host driven by host neutrophils (PubMed:32071275).5 Publications
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000435135 | 1 – 1421 | Chitin synthase 3Add BLAST | 1421 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 551 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Glycosylationi | 567 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Glycosylationi | 906 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 | |
Glycosylationi | 1035 | N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation | 1 |
Post-translational modificationi
Palmitoylated by PFA4; required for proper subcellular localization.1 Publication
Keywords - PTMi
GlycoproteinProteomic databases
PRIDEi | J9VXM5 |
PTM databases
SwissPalmi | J9VXM5 |
Structurei
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 56 | DisorderedSequence analysisAdd BLAST | 56 | |
Regioni | 112 – 137 | DisorderedSequence analysisAdd BLAST | 26 | |
Regioni | 170 – 189 | DisorderedSequence analysisAdd BLAST | 20 | |
Regioni | 592 – 658 | DisorderedSequence analysisAdd BLAST | 67 | |
Regioni | 1256 – 1319 | DisorderedSequence analysisAdd BLAST | 64 | |
Regioni | 1338 – 1421 | DisorderedSequence analysisAdd BLAST | 84 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 1 – 16 | Polar residuesSequence analysisAdd BLAST | 16 | |
Compositional biasi | 18 – 32 | Basic and acidic residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 36 – 56 | Polar residuesSequence analysisAdd BLAST | 21 | |
Compositional biasi | 115 – 137 | Polar residuesSequence analysisAdd BLAST | 23 | |
Compositional biasi | 592 – 617 | Polar residuesSequence analysisAdd BLAST | 26 | |
Compositional biasi | 1256 – 1271 | Polar residuesSequence analysisAdd BLAST | 16 | |
Compositional biasi | 1287 – 1319 | Polar residuesSequence analysisAdd BLAST | 33 | |
Compositional biasi | 1338 – 1367 | Polar residuesSequence analysisAdd BLAST | 30 | |
Compositional biasi | 1393 – 1408 | Polar residuesSequence analysisAdd BLAST | 16 |
Sequence similaritiesi
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
HOGENOMi | CLU_002572_1_0_1 |
Family and domain databases
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.
J9VXM5-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSRPHLQQNV SFQDTKPPSR RAGRDDIPPR PPTKSDPSKA SLTTTTTVQS
60 70 80 90 100
VGGYNNHQLD FDDNAYVDAG SSNPQGFSDY NGVRRKKSMV RPERERIDPN
110 120 130 140 150
HRLWHYREHA AEDQVDIQPS STGNQPYNQY NNQRPGANLR RGKSLLARET
160 170 180 190 200
DDVDDSSGLN IFKRGATIRR KASRATPRQA PTGAQSNRVS AGQKEDEECC
210 220 230 240 250
CLGNFAPGPK NCWMIYCYLL TICIPGFVIA KVFGKKTPDA QRAWREKIGI
260 270 280 290 300
VSIVLYLMGA VGFITFGFTQ TVCGDTQLRL PGGSANTGSL VINGYDYDFS
310 320 330 340 350
TWRHPVAGDT FNGTTSPLYM DQYMAGGMDA SFLFQNVNQN CLGLITPASG
360 370 380 390 400
TGIDHDGDQM GWYFPCNLHD QNGTSAANLT GITDRTNCHV SSYARSNFSA
410 420 430 440 450
VVPTAEIYYT WDRVKDESRN LAVYKSAVID MNLLQWLDDT QVSYPEFFNT
460 470 480 490 500
IKNRNDSYAG KDITALIERA GLSQYARCLT DVIQIGFVDT ITIGCIMSEL
510 520 530 540 550
VLYVSLVFIL GAVFIKFGMA VVFGWFLSWR MGNFKGESYQ ERMKRAAEIE
560 570 580 590 600
NWTDDIYRPA PGYLRPNATG TARTGVKKNF LPTTSRFSRA EPMLVSSSRP
610 620 630 640 650
STSYGMVGET RRQGSSIYGN KLGPPAHTTP PGSPLLRNSR SSTSLPFRDD
660 670 680 690 700
SRHSISDRSV NNNVPCPFPL GNVVPQPAPD FEPFGYPLIH SICLVTAYSE
710 720 730 740 750
SIEGLRTTLD SLATTDYPNS HKLILVICDG MVRGSGSKQY TPEIVLGMMK
760 770 780 790 800
ELVTPAEEVE AHSYVAIADG HKRHNMAKVY AGFYAYDSET VEASKQQRVP
810 820 830 840 850
MVLVSKVGNP LEVNDAKPGN RGKRDSQIVL MSFLQKVMFD ERMTTLEYEF
860 870 880 890 900
FNAVWRCTGI PPDRYETVLC VDADTKVFPD SLTRMNACMV NDHEIMGLCG
910 920 930 940 950
ETKIANKSET WVTMIQVFEY YISHHNTKAF ESVFGGVTCL PGCFSMYRIK
960 970 980 990 1000
APKGERGFWV PILANPDICE HYAENVVDTL HKKNLLLLGE DRYLSTLMLK
1010 1020 1030 1040 1050
TFPKRKMVFC PQAVCKTIVP DTFRVLLSQR RRWINSTVHN LCELILVRDL
1060 1070 1080 1090 1100
CGTFCFSMQF VVFMDLVGTL VLPAAISFTL YIIMISIIPQ SVTGMPRPYV
1110 1120 1130 1140 1150
SLVLLAFILG LPGVLIVITS RKIAYVGWML VYLISLPVWN LILPAYSYWH
1160 1170 1180 1190 1200
MDDFTWGETR KIAGEVKEEA HGGKEGTFDS SHIVMKKWAE FERERRWRTG
1210 1220 1230 1240 1250
TASRDSQYFD VVQRANSPRS GIPSNRYSIV STSETFNSGL GTAESNHLFR
1260 1270 1280 1290 1300
QSQSFASMSQ VAPSPETNYG NVPQLALPPP RGASIGREHS PSSTESGTSN
1310 1320 1330 1340 1350
NYAYGSTEEP TASNVDPYYQ PFTNEVYQDE AEQPILPSEY TTTSPEPVYQ
1360 1370 1380 1390 1400
TAPARVRQPS QRGVSLVDTG PVRSAQAAPH DAVRRVSRHQ RRSSSKNQLV
1410 1420
SPISSGGHTG SLPPGAAPPQ Y
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP003833 Genomic DNA Translation: AFR99008.1 |
RefSeqi | XP_012053858.1, XM_012198468.1 |
Genome annotation databases
EnsemblFungii | AFR99008; AFR99008; CNAG_05581 |
GeneIDi | 23888883 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP003833 Genomic DNA Translation: AFR99008.1 |
RefSeqi | XP_012053858.1, XM_012198468.1 |
3D structure databases
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
PTM databases
SwissPalmi | J9VXM5 |
Proteomic databases
PRIDEi | J9VXM5 |
Genome annotation databases
EnsemblFungii | AFR99008; AFR99008; CNAG_05581 |
GeneIDi | 23888883 |
Organism-specific databases
VEuPathDBi | FungiDB:CNAG_05581 |
Phylogenomic databases
HOGENOMi | CLU_002572_1_0_1 |
Family and domain databases
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_CRYNH | |
Accessioni | J9VXM5Primary (citable) accession number: J9VXM5 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 9, 2015 |
Last sequence update: | November 28, 2012 | |
Last modified: | February 23, 2022 | |
This is version 45 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |