CHS4_CRYNH
ID CHS4_CRYNH Reviewed; 1271 AA.
AC J9VF17;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 2.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Chitin synthase 4 {ECO:0000303|PubMed:16278457};
DE EC=2.4.1.16 {ECO:0000250|UniProtKB:P29465};
GN Name=CHS4 {ECO:0000303|PubMed:16278457};
GN ORFNames=CNAG_00546 {ECO:0000312|EMBL:AFR92678.2};
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 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 [4] {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 the antifungal agent caspofungin.
CC {ECO:0000269|PubMed:31266771}.
CC -!- DISRUPTION PHENOTYPE: Decreases cellular chitin level
CC (PubMed:16278457). Decreases capsular diameter (PubMed:32743128).
CC Increases extracellular vesicle secretion (PubMed:32743128).
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; CP003820; AFR92678.2; -; Genomic_DNA.
DR RefSeq; XP_012046345.1; XM_012190955.1.
DR AlphaFoldDB; J9VF17; -.
DR EnsemblFungi; AFR92678; AFR92678; CNAG_00546.
DR GeneID; 23884344; -.
DR VEuPathDB; FungiDB:CNAG_00546; -.
DR HOGENOM; CLU_002572_0_1_1; -.
DR Proteomes; UP000010091; Chromosome 1.
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; IMP:UniProtKB.
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 Gene3D; 3.10.120.10; -; 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; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; PTHR22914; 1.
DR Pfam; PF00173; Cyt-b5; 2.
DR Pfam; PF08766; DEK_C; 1.
DR SMART; SM01117; Cyt-b5; 2.
DR SUPFAM; SSF53448; SSF53448; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR PROSITE; PS51998; DEK_C; 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..1271
FT /note="Chitin synthase 4"
FT /id="PRO_0000451813"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 867..887
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 894..914
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 919..939
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1213..1269
FT /note="DEK-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01342"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 713
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 836
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1055
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1271 AA; 143011 MW; 5AB53D5B4ECC5368 CRC64;
MPPTSSQAPF HRYSHLDQRS APDTQESSPA DGNHDPRRQS TSFDHPNLYA QRDVFAVPNH
PQSTNLNHQP YLHQGRSGSF EEPIYETPQP GHNVGYEDAE PYGHEQHDGT MWSERPSYSA
PYDSDIKAPL DPTPYTPDLE ADGMVVKEKK VHATEVMATT NARRWWIRIT WMMTWWIPSF
LLVHLGRMKR ADVRMAWREK LAIFMMICLA CAVVLFYIIF FGKLLCPDSD KAWNEKELAT
HQGDDDYYAA IAGKVYDFTN FYKAQHSDLS SYTTSSALML EFAGQDLTNY FPMPMTVACP
NLVTSTDLTL MYSNFTPIVQ YAVHTSGPLQ TGTDTKLNDI NWYTDTLNPA LEDYYKGYYV
YDKSSIASGA DSDSKYWAIY NNKVYDLSNY IYTISYYSSS SGTDLPNYSF LNSDITDLFQ
TSAGQDITKD MDEKLSALTA EDAANQMTCL NNAFYLGELD FRKTPRCTVQ NYLLLAFSII
LIATIASKFL AALQLGSKRQ PELLDKFVIC QVPCYTEGEE SLKRTIDSLA ALNYDDKRKL
IFIICDGNIV GSGNNRPTPR IVLDLLGVDD KLEAEPLLFK SIGEGSKQLN YGKVYSGLYE
FEGHVVPYIV VVKVGKPSEI SKPGNRGKRD SQVLLMQYLN RVHFDAPMTP LELEIYHQMR
NVIGIDPAFY EYIFQVDADT SVTPDSLNRL IACTADDQQI IGICGETKLA NENESLTTMI
QVYEYYISHH LTKAFESLFG SVTCLPGCFS VYRIRTAEGG RPVIISSVVI DEYAEPNVDT
LHKKNLFSLG EDRYLTTLMM KNFPTFKMKF TPDAIAHTVA PSKWSVLLSQ RRRWINSTIH
NLVELLFLPE MCGFCFFSMR WVVFLDLLGT IILPATCGYL IYLVIVVSTG KAAIPVISLA
MIGATYGLQA LIFILKREFM LIGWMLVYIL AFPVWSVFLP IYSFWSMDDF SWGNTRKVIG
EGNQKTVVID DDEPFNEGMI PYRTFKEYEW NAWEAASLHS ESPAPSEKSQ RTTRTGQSYR
PHPHSIRSPS FHSSASELPS KADYWRDSSP LGMGNESKRL HQVSSDPSMR GDKSFIRGSK
PQVERVQSMA GMSMWGSGSV YDPYKQAMGG PGFLHPMMTG NSLASQATFY PPQTQYPMSM
YGSPMMMPMG MPMMGLQYAG NASMAGGAAG PRGTMMTMGM GDQSRISSFS MGGPVAESGA
GRLVGLSINE EKEVQDEEVL DKLKTWLSKQ DLMSVTKRQT REAIYTLFPN AGLQNRAGWL
NEQIDKILSE S
