CHS2_CRYNH
ID CHS2_CRYNH Reviewed; 942 AA.
AC J9VQ06;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 2.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Chitin synthase 2 {ECO:0000303|PubMed:16278457};
DE EC=2.4.1.16 {ECO:0000255|RuleBase:RU366040};
GN Name=CHS2 {ECO:0000303|PubMed:16278457};
GN ORFNames=CNAG_03326 {ECO:0000312|EMBL:AFR96547.2};
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443 {ECO:0000312|Proteomes:UP000010091};
RN [1] {ECO:0000312|Proteomes:UP000010091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
RN [2] {ECO:0000305}
RP FUNCTION.
RX PubMed=16278457; DOI=10.1128/ec.4.11.1902-1912.2005;
RA Banks I.R., Specht C.A., Donlin M.J., Gerik K.J., Levitz S.M., Lodge J.K.;
RT "A chitin synthase and its regulator protein are critical for chitosan
RT production and growth of the fungal pathogen Cryptococcus neoformans.";
RL Eukaryot. Cell 4:1902-1912(2005).
RN [3] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=32743128; DOI=10.1016/j.tcsw.2018.05.002;
RA Rodrigues J., Ramos C.L., Frases S., Godinho R.M.D.C., Fonseca F.L.,
RA Rodrigues M.L.;
RT "Lack of chitin synthase genes impacts capsular architecture and cellular
RT physiology in Cryptococcus neoformans.";
RL Cell Surf. 2:14-23(2018).
RN [4] {ECO:0000305}
RP INDUCTION.
RX PubMed=31266771; DOI=10.1534/genetics.119.302290;
RA Pianalto K.M., Billmyre R.B., Telzrow C.L., Alspaugh J.A.;
RT "Roles for Stress Response and Cell Wall Biosynthesis Pathways in
RT Caspofungin Tolerance in Cryptococcus neoformans.";
RL Genetics 213:213-227(2019).
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.
CC {ECO:0000305|PubMed:16278457}.
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:0000255|RuleBase:RU366040};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255|RuleBase:RU366040}.
CC -!- INDUCTION: Induced by the antifungal agent caspofungin.
CC {ECO:0000269|PubMed:31266771}.
CC -!- DISRUPTION PHENOTYPE: Abnormal capsular morphology: abnormal fiber
CC distribution, decreases capsular diameter (PubMed:32743128). Decreases
CC extracellular vesicle secretion (PubMed:32743128).
CC {ECO:0000269|PubMed:32743128}.
CC -!- SIMILARITY: Belongs to the chitin synthase family. Class III subfamily.
CC {ECO:0000305}.
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DR EMBL; CP003827; AFR96547.2; -; Genomic_DNA.
DR RefSeq; XP_012050916.1; XM_012195526.1.
DR AlphaFoldDB; J9VQ06; -.
DR EnsemblFungi; AFR96547; AFR96547; CNAG_03326.
DR GeneID; 23886838; -.
DR VEuPathDB; FungiDB:CNAG_03326; -.
DR HOGENOM; CLU_004760_3_0_1; -.
DR Proteomes; UP000010091; Chromosome 8.
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; ISS:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0034221; P:fungal-type cell wall chitin biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR004834; Chitin_synth_fun.
DR InterPro; IPR013616; Chitin_synth_N.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; PTHR22914; 1.
DR Pfam; PF01644; Chitin_synth_1; 1.
DR Pfam; PF08407; Chitin_synth_1N; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosyltransferase; Membrane; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..942
FT /note="Chitin synthase 2"
FT /id="PRO_0000451812"
FT TRANSMEM 590..610
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 625..645
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 663..683
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 696..716
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 739..759
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 770..790
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 873..893
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 916..936
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 587
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 736
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 803
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 942 AA; 105826 MW; 13A509E673D220E4 CRC64;
MAYHYSHDSD RRQPHGGYNY PSNYSNPSQY SIPDSVYSGH STNTPRVPSP GGYHQQPSPT
TRAVNPAYYQ PQPTASSMTS HDLMYGRPSP GPNQYGAAPA DVVRGPGATT VPLSQQAPYQ
PYPSHTDYSD EDKSFASTTH LVSPQKEWGV GSVVPVTTIP PVNQLPYQPY QAYPPRPSPS
PITHRGGTSH WHAMRKQLLE RRVIKQIPLH NGNLVMDVPV PKGVIPSTKG LGVMDGEMDS
MRYSAATCDP DDFMGSKFSL RQYLYGRKTE LFIVMTMYNE NSELLLRTLN AVIKNIAHLT
TRTRSKTWGP DSWKKVVVCI VADGRKVVDP RVLKVLQLMG VYAEGVMKDH VVDKETQAHI
FEYTSQVVVS ETGEVGFGST PIQLLFCLKE QNKKKLNSHR WFFNAFGPLI KPNVCVLLDV
GTKPSGHSIY ELYKCFEKHP TVGGACGEIF ADTGKWGKYL WNPLVAGQNF EYKMSNILDK
PFESVFGLIS VLPGAFSAYR YDAVANHADG TGPLAAYFRG ELMNQPGATA TIFDRNKFLA
EDRILAFEIV VKKNARWRLQ YVKAAKAGTD VPATVPEFIS QRRRWLNGSI FAATYAMVCF
WRIWTSGHGI FRKFTLTFLT IYNLFNLLFN WLSVSSFYLA FFFLISSSIS GSSDPFNGAG
DEIFQVFNKV YIALIFVVLV CSLGNRPQGS NYMYTFCIFM FAVCQGILLY CAGWTVYQTV
PHTSEGWEDV SGLFENRTFV QLALSLMATY GLYLISSLLY FEPWHMLTSF VQYLLLLPSY
VNILLIYAMC NLHDVSWGTK GDNGSSKDLG AAKKVEKDGK EMAEVALPTK QEDVEALWQQ
ARQELRVPVK EKAEKRSPET KRADEDRNFR TNVVLLFLGS NMLIILLFTS STFTNWVNSH
FVDATSSTFN PYLTVIFYAV LGLSALRFAG CLLYLIFRMF GY
