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   25-MAY-2022, entry version 101.
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   SwissPalm; O13356; -.
DR   PRIDE; O13356; -.
DR   EnsemblFungi; AFR96323; AFR96323; CNAG_03099.
DR   GeneID; 23886628; -.
DR   VEuPathDB; FungiDB:CNAG_03099; -.
DR   HOGENOM; CLU_002572_0_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; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR22914; PTHR22914; 1.
DR   SMART; SM01117; Cyt-b5; 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..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