CHS8_CRYNH
ID CHS8_CRYNH Reviewed; 1032 AA.
AC J9VGT6;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 2.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Chitin synthase 8 {ECO:0000303|PubMed:16278457};
DE EC=2.4.1.16 {ECO:0000250|UniProtKB:P29465};
GN Name=CHS8 {ECO:0000303|PubMed:16278457};
GN ORFNames=CNAG_07499 {ECO:0000312|EMBL:AFR93607.2};
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).
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:0000250|UniProtKB:P29465};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
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. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003822; AFR93607.2; -; Genomic_DNA.
DR RefSeq; XP_012047775.1; XM_012192385.1.
DR AlphaFoldDB; J9VGT6; -.
DR EnsemblFungi; AFR93607; AFR93607; CNAG_07499.
DR GeneID; 23890341; -.
DR VEuPathDB; FungiDB:CNAG_07499; -.
DR HOGENOM; CLU_004760_3_1_1; -.
DR Proteomes; UP000010091; Chromosome 3.
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 3: Inferred from homology;
KW Cell membrane; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosyltransferase; Membrane; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1032
FT /note="Chitin synthase 8"
FT /id="PRO_0000451817"
FT TRANSMEM 728..748
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 762..782
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 796..816
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 842..862
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 870..890
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 972..992
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 995..1015
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..43
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 691
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1032 AA; 114051 MW; 9F594E738CEEBDCA CRC64;
MRPGDIYPPP QGYNAYGSPT RQNQRPPQPQ PYPPQPYPPQ QPAVQYGDPF SASSQGPPTA
PLHNMSPTPQ EPQGSRYNAS HPLQPISPSG PQGPRYSLPT QSLSPFNGSP ASAPAPAPYT
MGSPSHSNAR MHASPPQHIR FDTNPSHLPP QQQLTPSYSY PSGLDDRLTS PPPLLPHHSS
QSSVSSIPAP VPDNINYNPS YPPQGYGNAA DDDMNDSHPL LAHAAPDARF GIPQSTSAMS
MSAPAARYQL SDTGAGDMGV SMYTGNGNAE GQNGFGTGDG VGANGEDEVN MHYGPIPARM
VRRNRTQKRV QLFQGHLVLD IEVPTMLLDQ CPIRQGNEFT KMRYTAVTCD PNDFVEDRYT
LRQRLYDPPR QTELFIVITM YNEDDVLFCR TMRGVMQNIA HLCTRSKSKT WGENGWKKVV
VCIVADGRKK INPRTRSVLA ALGVYQEGVG KNIINGKPVT AHVYEYTTQL SINSSGKIGP
GGSNTVPIQM LFCLKEKNQK KINSHRWFFN AFGACLRPNV CVLLDVGTQP GPDSIYHLWK
AFDINSSVGG ACGEIVALKG MFWKNLLNPL VAAQNFEYKM SNILDKPLES VFGYITVLPG
AFSAYRYIAL LNDEKGNGPL KQYFVGERMH GSGAGIFSSN MYLAEDRILC WELVSKRECK
WKLHYVKSAY AITDVPDTVP ELVSQRRRWL NGSFFAAIHS IVHFGYLYRS SHTFTRKFIL
HVELVYQTLN MVFAWFALGN YYIAFFVLTQ SLNSLGSAWK YVNIPLHYIY IALLLWCFLL
SLGNRPAGSK IGYTSSMVGF ALITIYMLFA AIFLAVKGIE DVQAEGEITA SAVFGNKIFR
NIVISLLATY GLYIISSLMA LEPWHMITSF FQYLLIAPSY INVLNVYAFC NVHDVSWGTK
GSDKVSDDLG AVKSSADNKD EVTVDLPIEQ KDINAVYAAE LQILGNKAPK EVRVVSDDQK
QEDYYKNVRT NVLLVWTMTN GALVAVILQA SGGDNSLATT YMGVLLYTVA GLAFFRFLGS
STYLVVRLFA GE
