CHS7_CRYNH
ID CHS7_CRYNH Reviewed; 931 AA.
AC J9VMX7;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 2.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Chitin synthase 7 {ECO:0000303|PubMed:16278457};
DE EC=2.4.1.16 {ECO:0000255|RuleBase:RU366040};
GN Name=CHS7 {ECO:0000303|PubMed:16278457};
GN ORFNames=CNAG_02217 {ECO:0000312|EMBL:AFR95603.2};
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 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). Induced by
CC the antifungal agent caspofungin (PubMed:31266771).
CC {ECO:0000269|PubMed:27611567, ECO:0000269|PubMed:31266771}.
CC -!- DISRUPTION PHENOTYPE: Decreases capsular diameter (PubMed:32743128).
CC Decreases 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; CP003825; AFR95603.2; -; Genomic_DNA.
DR RefSeq; XP_012049807.1; XM_012194417.1.
DR AlphaFoldDB; J9VMX7; -.
DR EnsemblFungi; AFR95603; AFR95603; CNAG_02217.
DR GeneID; 23885872; -.
DR VEuPathDB; FungiDB:CNAG_02217; -.
DR HOGENOM; CLU_004760_3_1_1; -.
DR Proteomes; UP000010091; Chromosome 6.
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..931
FT /note="Chitin synthase 7"
FT /id="PRO_0000451816"
FT TRANSMEM 573..593
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 615..635
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 647..667
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 695..715
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 725..745
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 826..846
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 899..919
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 536
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"
FT CARBOHYD 819
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 866
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 874
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 931 AA; 104529 MW; A6720EF34786C7EB CRC64;
MVRHDPFTNS VSEDSSFTPS VNPSTPYPQS GHYRPYYPPQ LTYCQGQQGY QYDHTGDVGY
GGRSRRHGSW ASVNNEDNEE LTPLTTGPAS SSTFLTTDPY LSGGPDLPLS SSSASISSAG
ADFLRRQTVP RRGATIKKIK LTNGNFIADY PVPGPVSSSV EAKWLNDKTS NEFWHMRYTA
ATCDPDDFTP ENGWKLKTTS YNRETELLVA ITSYNEDKIL YARTLHNVML NIRDICNTKA
SKFWRRSAEE GRPGWQKIVV ALVADGLDPM DKQVLDVLQT IGVFQDGILK KEVDGKKTAA
HIFEYTTQLS IDATPQLVQP HPGDPNNLVP VQIIFVLKQE NSKKINSHRW LFNALGRQLQ
PEICVLLDAG TKPGHKAIYH LWEAFYNNQN LGGACGEIHA MIKKGVKLLN PLVAAQNFEY
KMSNILDKPL ESSFGYVSVL PGAFSAYRYK AIQGRPLTQY FHGDATLAAR LGKKGIYGMG
IFTKNMFLAE DRILCFELVA KKGEKWVLQY VKPSKAETDV PEQAAELISQ RRRWLNGSFA
ASVYSVFHFF RLYRSGHGPI RMLFLHIQAI YNIFSLIFSW FALANLWLTF SIIIELLPES
ANINLFGTAD ITHWINLVFA WVYLAFLMLQ LVLALGNRPK AEKGLYILTL WVYAFLSFYL
IVCSIILSVV AFKGALRDGG SIGAKLGNLF NSTNGVLVAA IMSTIGIYLI ASFLYRDPWH
MFSSFPQYML LAPSFTNVLN IYAFCNLHDV SWGTKGSDRA ESLPAISSSK QKDGETAVVE
EQQRSQGELD ESFKQVVRRA VAPYKPEDAD EKPNLDDQNR TFRTRLVVVW LLTNAALAIS
IQTLNGLDTT KPLVEACLPN SYNPENGTVI VSTNGTCITQ ALEHDGDKLQ DKQQIYFQAI
LWTTFALSMV RFIGCVFYWA MRQMGRCWRR N
