CHS6_CRYNH
ID CHS6_CRYNH Reviewed; 944 AA.
AC J9VWT0;
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 6 {ECO:0000303|PubMed:16278457};
DE EC=2.4.1.16 {ECO:0000255|RuleBase:RU366040};
GN Name=CHS6 {ECO:0000303|PubMed:16278457};
GN ORFNames=CNAG_06487 {ECO:0000312|EMBL:AFR98718.2};
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, AND DISRUPTION PHENOTYPE.
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 INDUCTION.
RX PubMed=27611567; DOI=10.1371/journal.ppat.1005873;
RA Park H.S., Chow E.W., Fu C., Soderblom E.J., Moseley M.A., Heitman J.,
RA Cardenas M.E.;
RT "Calcineurin Targets Involved in Stress Survival and Fungal Virulence.";
RL PLoS Pathog. 12:e1005873-e1005873(2016).
RN [4] {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 [5] {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 high temperature (PubMed:27611567). Repressed by
CC the antifungal agent caspofungin (PubMed:31266771).
CC {ECO:0000269|PubMed:27611567, ECO:0000269|PubMed:31266771}.
CC -!- DISRUPTION PHENOTYPE: Abnormal capsular morphology: lower fiber
CC density, abnormal fiber distribution, decreases capsular diameter
CC (PubMed:32743128). Decreases extracellular vesicle secretion
CC (PubMed:32743128). Sensitive to high temperature (PubMed:16278457).
CC {ECO:0000269|PubMed:16278457, ECO:0000269|PubMed:32743128}.
CC -!- SIMILARITY: Belongs to the chitin synthase family. {ECO:0000305}.
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DR EMBL; CP003832; AFR98718.2; -; Genomic_DNA.
DR RefSeq; XP_012053352.1; XM_012197962.1.
DR AlphaFoldDB; J9VWT0; -.
DR EnsemblFungi; AFR98718; AFR98718; CNAG_06487.
DR GeneID; 23889683; -.
DR VEuPathDB; FungiDB:CNAG_06487; -.
DR HOGENOM; CLU_004760_2_1_1; -.
DR Proteomes; UP000010091; Chromosome 13.
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..944
FT /note="Chitin synthase 6"
FT /id="PRO_0000451815"
FT TRANSMEM 690..710
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 726..746
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 761..781
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 791..813
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 827..847
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..916
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 653
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 927
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 944 AA; 104522 MW; 3B6FCB379D894595 CRC64;
MPNISRKPPP RFYSPSHSPS PSLYAPIQSP PAPSYDYHAN PRTLNPFSDA REVGGYAQLQ
GEDQMTGAPL YQPPYAPQLL VAQPTPVSSR LPFFEAALAR ARGIQTPSLP EAPTPAYAQP
LPSYLPPPDP NHPDLSVGLT QANTVRYAIN PRSQLKEGSR SPSPFMDDSF VYNDAAHLYN
VEPDVEKALL GSGLGYESEK RVESSMGFND NDGDLSVPQS FGGRPPSWEP SGILDEKGEM
STTKHFGPAP AGRVGRRAHN AAGYRRIKQS ATLDENGFFA IEMNIPTRLA QFLPIKGVEE
QKTTRYTAIT TDPDDVPAAG FRLRQNMTSP PRQTELFIVI TMYNENAELF CRTLYGVMKN
IAHLCGRKNS RVWGKDGWQK VVVCIVADGR KAVNPRVLDC LAALGVYQEG AMTNTVKDRP
VTAHVFEYTT SFALDGDLHF KYPDKGIVPC QIIFCMKEKN AKKINSHRWF FNAFAPLLSP
NVCILLDVGT QPAPKSIYHL WKAFDVNSNV GGACGEIATF KGKTWRSLLN PLVAAQAFEY
KMSNILDKPL ESLFGYCTVL PGAFSAYRWI ALQNNGDGRT GPLASYFAGE QLNTGKADTF
TGNITWQKIE SCVSKSAKPK ANWVLKFVKA AVGETDCPDT IPEFIAQRRR WLNGSFFAAV
YALMHTNQIW RSDHSFARKS ALMLESVYNF LNLIFSWFAL ANFYIFFVIL TSALEGSAFN
VPHIDVLNTI ARYGYLGALV GCFIFAMGNR PQGSPWKYKA AIYFFALLTT YMLVAAVLCT
VQAIKNINSP IFAKMVVSLI STYGIYVISS FLALDPWHIF TCFIQYVLFS PITDLLLLKL
ISMFHDLSWG TKGSDATQAS DLGAVSGVGK HVEVELVTAQ QDIDIAYQDA LDNIRLRGSK
VDSAESEPKK EQSEQAQKDT YANFRTNVSI AIMLVQKKRD DAKS
