ID CHS1_CRYNH Reviewed; 1236 AA.
AC O13356; J9VPY6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 2.
DT 22-FEB-2023, entry version 104.
DE RecName: Full=Chitin synthase 1;
DE EC=2.4.1.16;
DE AltName: Full=Chitin-UDP acetyl-glucosaminyl transferase 1;
DE AltName: Full=Class-IV chitin synthase 1;
GN Name=CHS1; ORFNames=CNAG_03099;
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;
RN [1]
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1125.
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RA Specht C.A.;
RT "chs1, a class IV chitin synthase of Cryptococcus neoformans.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP FUNCTION, AND 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 [5]
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, ECO:0000305|PubMed:32743128}.
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 -!- INDUCTION: Induced by the antifungal agent caspofungin.
CC {ECO:0000269|PubMed:31266771}.
CC -!- DISRUPTION PHENOTYPE: Abnormal capsular morphology: lower fiber
CC density, decreases capsular diameter. {ECO:0000269|PubMed:32743128}.
CC -!- SIMILARITY: Belongs to the chitin synthase family. Class IV subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB71697.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CP003827; AFR96323.1; -; Genomic_DNA.
DR EMBL; AF021318; AAB71697.1; ALT_SEQ; Genomic_DNA.
DR PIR; T31097; T31097.
DR RefSeq; XP_012051025.1; XM_012195635.1.
DR AlphaFoldDB; O13356; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR GlyCosmos; O13356; 3 sites, No reported glycans.
DR SwissPalm; O13356; -.
DR GeneID; 23886628; -.
DR KEGG; cng:CNAG_03099; -.
DR VEuPathDB; FungiDB:CNAG_03099; -.
DR HOGENOM; CLU_002572_0_0_1; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000010091; Chromosome 8.
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 CDD; cd04190; Chitin_synth_C; 1.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR PANTHER; PTHR22914:SF26; CHITIN SYNTHASE 7; 1.
DR Pfam; PF03142; Chitin_synth_2; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 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..1236
FT /note="Chitin synthase 1"
FT /id="PRO_0000193689"
FT TOPO_DOM 1..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..108
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..823
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 824..844
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 845..860
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 861..881
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 882..884
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 885..905
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 906..1236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1099
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 799
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1236 AA; 136334 MW; 30A463626EFC8272 CRC64;
MSSNQDVPLP FTSSRPLPSR QPTTSRPGGT LKRNKTLTRP ERHVAPAPLV APPTQSFSPT
SPLPQSDGFL NIDWWRLWAY ATTFWAPPVL LRWFGIKEKQ SRQAWREKIA LCWIAVLLGG
VVGFVTMGLQ RALCPADQQN QSMYQRLGDT NMTLSISGWA FNISTSITQS NVDFYSLANQ
MPGQDITDLF TRSVSDYPAC TSSLAYSSGA FCNSTSSSSG TSCVLSSMSQ ETFDSLQIQN
TSLLEGYSWD QVAKLENYMV IDGYVLNMSP YLSFNPTAVE GDEVDSIIRH VLSNQTGSGK
DATRLFFNRQ VPQDAVGCMK ARYVAGRIDK ITPGCFVASF FLYVSLVVIL AVVLARFAMA
CVFNWFLSEK LVKPVTEKEL GRKGINPTIM PEGANVSVNN KLGTAPWAGG GGAAEGKGGG
VGPGKKLVNG KKINPLSPLP SPSHSLPNAP LITLSQIGPE LFTVCLVTCY SEGPSSIRGT
LESIASTNYS DRRKLIWVVC DGMITGQGEK RSTPDVCVGM LDADGRFGNP VPMGYEAVGS
GQKRENRAMV YAGHYVSRNG HRTPTIIVVK CGMPQEATEK KPGNRGKRDS QLILMNFFSR
VTYNDRMTPL DFDLFRKIWT LMGVTPDYFE AVLMVDADTR IYPDSLKHLV NCMHHDNMIM
GVCGETRIAN KRQSWVTAIQ VFEYFISHHH VKAFESVFGG VTCLPGCFSM YRIKARKDGD
NDWVPILVKP EIVNEYSQSE VETLHQKNLL LLGEDRFLST IMLRTFPRRK NIFLPQARCR
TVAPDTFSVL LSQRRRWINS TVHNLMELVR VRDLCGTFCF SMQFVVFMDL VGTVVLPVAI
CLTFALIVNS IITPPKSFEE AIPLMLLAIV LGLPAILILI TTRKVVYVAW MLVYLLALPI
WNFVLPVYSF WHFDDFSWGE TRRVEGEIRS KGHDDSTAVF NGTTIPLRRW EDWEKSRLRK
LRREEKRRKE MERQFGAGFH GDPRLGGDLR GMGMGERPWA RSEYDSDNGS LYSSEEDMWG
GEVGGYNEHN PAFPPPPIAL PPTDDPVSNI NGETLGMDEM AAILDSGFDD DPQSQSTYPP
LSHPRPHAHP PPPPISRTLA NAPSPVRRHQ HEYNAPQPRF NRIDSPSFGS GPNSARSSPH
SADAGRYAAG EYVSIDRQDT NDLDAQMPHS GGSVSSSVES RPHGVGHAKK RSGGGAGIGA
GTGARGGGYG PLGPLADVNE VGRGQTRGYG GSGKDR
//
