CHS5_CRYNH
ID CHS5_CRYNH Reviewed; 1931 AA.
AC J9VNT4;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Chitin synthase 5 {ECO:0000303|PubMed:16278457};
DE EC=2.4.1.16 {ECO:0000250|UniProtKB:P29465};
GN Name=CHS5 {ECO:0000303|PubMed:16278457};
GN ORFNames=CNAG_05818 {ECO:0000312|EMBL:AFR96137.1};
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 (PubMed:16278457). Produces
CC a large proportion of the chitin that is not deacetylated to chitosan
CC (PubMed:16278457). {ECO:0000269|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 -!- 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: Decreases cellular chitin level
CC (PubMed:16278457). Abnormal capsular morphology: lower fiber density,
CC abnormal fiber distribution, decreases capsular diameter
CC (PubMed:32743128). Increases extracellular vesicle secretion
CC (PubMed:32743128). Sensitive to high temperature (PubMed:16278457).
CC {ECO:0000269|PubMed:16278457, ECO:0000269|PubMed:32743128}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the TRAFAC class CC
CC myosin-kinesin ATPase superfamily. Myosin family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the chitin synthase
CC family. Class V subfamily. {ECO:0000305}.
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DR EMBL; CP003826; AFR96137.1; -; Genomic_DNA.
DR RefSeq; XP_012050554.1; XM_012195164.1.
DR AlphaFoldDB; J9VNT4; -.
DR SMR; J9VNT4; -.
DR EnsemblFungi; AFR96137; AFR96137; CNAG_05818.
DR GeneID; 23889107; -.
DR VEuPathDB; FungiDB:CNAG_05818; -.
DR HOGENOM; CLU_000192_0_2_1; -.
DR Proteomes; UP000010091; Chromosome 7.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004100; F:chitin synthase activity; IMP:UniProtKB.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0034221; P:fungal-type cell wall chitin biosynthetic process; IMP:UniProtKB.
DR CDD; cd14879; MYSc_Myo17; 1.
DR Gene3D; 3.10.120.10; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR014876; DEK_C.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036037; MYSc_Myo17.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR22914; PTHR22914; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF08766; DEK_C; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01117; Cyt-b5; 2.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR PROSITE; PS51998; DEK_C; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; ATP-binding; Cell membrane;
KW Cell wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW Membrane; Motor protein; Myosin; Nucleotide-binding; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1931
FT /note="Chitin synthase 5"
FT /id="PRO_0000451814"
FT TRANSMEM 912..932
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 951..971
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1220..1240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1615..1635
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1641..1661
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1668..1688
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 11..777
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 1875..1930
FT /note="DEK-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01342"
FT REGION 655..677
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 798..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1826..1847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1832..1847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 122..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 842
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1062
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1078
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1931 AA; 218295 MW; 459F76724E81FF5A CRC64;
MAQQPPPSRF LGVTDLSSLA VTEDTVLVTL QERYISHKPY TSLSPAALVF LSPYSHLPID
DEESLLHYVE EYYQCNNEEG GSRNEQGWWK KKMEQPHVFQ LALSAYYNMR RTGQDQVIIA
SGPTGSGKSE LKRLAIEAIT QVSLANPGKK GSKIGLQVSS AEFILKCFGN AHTLSNDEAS
RFGTYTELQF NERGRLEGLK TIVYYFERSR VSQAPINGER NFHAFYYLVS GAPEEERNFL
KLGDVSDYRY LNCRVRRVGV DDRHRYSQLR QAFKLMGISS RLIAQIFQLL ASILHIGNLR
FSPSDGIQEG ASVINVETLD IVAEFLGVHS ESLAEIFSLK TVLVRKEVCT TFLGPEQAEQ
VRDELARTLY SLLFSWINEH INTKLCKDSF GSFIALVDLP GIQRNSGSMG SFNSVDQFCL
NFAAEKMHNW VLHRVHETTR QEAETERLLI SRVPYFDNSE CLGMLSNPRG GLISVIDDLS
QKKRSESNLL ESLGKRFHNH PSMSISPQGN RSSASFTINH YDGPVTYSTS NFLERNANET
STDIIQLLRG DTTSRSQVST TEGHGSSNPF IKGLFGMKNI AMQTHPRSDS TIVAAQQSVR
PVRAPSTRRK KMMSLVPVSE EGGEETSDFQ VGGGNDESYS SKELHCIAGQ HWAAVDSLLK
SFDQTQTWYI FALRPNDSQL PSQFDLRSMK QQVRSFGLVE MAQQLQTSWE VRLSHKEACE
RYNEELLYRG IPEGTGDVER LRDLKRLMSL NDADMGIGLQ RVFLSHDLFR FLEDRLRAKE
PGEQHAYEDL GHRKLQTDPF SPHRYQPTSF DSQDHVYKDP SIRPVDSSAN LPLMEHAQPI
VNSSLEIEDR ESSAAPYVSY GGRSITDIEG YASSRDLLAS SIHKSEKDPL DTEPQAGETT
EVYRESIARR RWVWLCSILT WWIPGFLLSK IAGMKRQDIR QAWREKLAIN MIIWFICGCA
IFVIAILGPV ICPTQHVYST NELASHSYTL DPNNAFVAIR GEVFDLSQFA PTHLTAVSVV
PTKSIMQYGG LDASELLPVQ VSALCGGVSG SISQYVTLDS TNTTDVYSQY HDFRAFTNDS
RPDWYAEMMI MMRHRFRVGF MGYTKKDLKK MAAQGKAVAI YDNLVYDMSN YIRQNGGGLK
APDGVNLTAQ DQADRQFMSD QVVSLFKYNS GKDITTLLDN LGSTIGTDVV DRQKTCLRNL
FILGKLDTRD SAQCQFSTYI LLALSCVMVA VIGFKFLSAL HFGSVRAPES HDKFVICQVP
CYTEGEESLR RTIDSLCKLR YDDKRKLILV ICDGNIKGFG NDKPTPAIVL DILGVDVNSD
PEPLSFQSLG EGAKQHNMGK VYAGLYECAG HVVPYLVVAK VGKPNERQKP GNRGKRDSQM
LVMHFLNKVH FSAPMNPLEL EMYHQIKNVI GVNPSFYEYL FMVDADTTVD EMSLNRLVSA
MRHDKKIIGV CGETSIANAK QSIVTMSQVY EYFISHHLSK AFESLFGSIT CLPGCFSMYR
LRSPDTNKPL FISHGIIQDY SENRVDTLHL KNLLHLGEDR YLTTLVLKHF QDYKTKFVRH
AYAKTVAPDS IKVLLSQRRR WINSTVHNLA ELVFLDQLCG FCCFSMRFVV FIDLLSTIIA
PVTVAYIVYL IYLIVHDGSS IPTLSIIMLA AIYGLQAMIF IFRMRWDMIA WMIFYICAIP
VFSFLLPLYS FWKMDDFSWG STRLVVGDKG KKIVIHDEGK FDPSSIPLRS WEEYENELWD
QESVHSGSYM PPKAEYSYDY PRTRSTYSHG GYAYGQPIHP MQTRSTSPVS SRYQMSQFRQ
SPYQSPYQGP YGGSTADFRS SRMDMAHRPS LDDTSSFHQP YQPAPRPQSS YAFNLPDPSS
DSFTAPAVDY LGAQAITDSQ LERSIRKICA NAELDKLTKK GVRKELEREY GVELTERREA
INRLVEKVLT E
