SKT5_CRYNH
ID SKT5_CRYNH Reviewed; 485 AA.
AC J9VSG5;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Chitin synthase regulator 2 {ECO:0000303|PubMed:16278457};
DE Flags: Precursor;
GN Name=CSR2 {ECO:0000303|PubMed:16278457};
GN ORFNames=CNAG_07636 {ECO:0000312|EMBL:AFR95549.1};
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, SUBCELLULAR LOCATION, 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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=KN99;
RX PubMed=17400891; DOI=10.1128/ec.00399-06;
RA Baker L.G., Specht C.A., Donlin M.J., Lodge J.K.;
RT "Chitosan, the deacetylated form of chitin, is necessary for cell wall
RT integrity in Cryptococcus neoformans.";
RL Eukaryot. Cell 6:855-867(2007).
RN [4] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
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).
RN [5] {ECO:0000305}
RP FUNCTION.
RC STRAIN=KN99;
RX PubMed=32071275; DOI=10.1128/mbio.03373-19;
RA Hole C.R., Lam W.C., Upadhya R., Lodge J.K.;
RT "Cryptococcus neoformans Chitin Synthase 3 Plays a Critical Role in
RT Dampening Host Inflammatory Responses.";
RL MBio 11:0-0(2020).
CC -!- FUNCTION: Activator of the chitin synthase CHS3 which polymerizes
CC chitin, a structural polymer of the fungal cell wall (PubMed:16278457,
CC PubMed:17400891). Chitin produced by CHS3 is deacetylated to chitosan,
CC which helps to maintain cell wall integrity, anchor melanin, and offers
CC an advantage during infection, as chitosan is less readily detected by
CC host immunosurveillance (PubMed:16278457, PubMed:17400891,
CC PubMed:32071275). {ECO:0000269|PubMed:16278457,
CC ECO:0000269|PubMed:17400891, ECO:0000269|PubMed:32071275}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:16278457};
CC Lipid-anchor {ECO:0000250|UniProtKB:P34226}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P34226}. Note=Farnesylation is not required for
CC cellular membrane localization. {ECO:0000250|UniProtKB:P34226}.
CC -!- DISRUPTION PHENOTYPE: Increases cellular chitin level and decreases
CC cellular chitosan level (PubMed:16278457, PubMed:17400891). Swollen
CC cell with abnormal cytokinesis (PubMed:16278457, PubMed:17400891).
CC Melanization of surrounding media (PubMed:16278457, PubMed:17400891).
CC Irregular capsular width (PubMed:17400891). Sensitive to: high
CC temperature, Congo Red (cell wall stressor), caspofungin (cell wall
CC stressor), sodium dodecyl sulfate (cell wall stressor), Calcofluor
CC White (cell wall stressor), caffeine, NaCl (osmotic stressor)
CC (PubMed:16278457, PubMed:17400891, PubMed:31266771).
CC {ECO:0000269|PubMed:16278457, ECO:0000269|PubMed:17400891,
CC ECO:0000269|PubMed:31266771}.
CC -!- SIMILARITY: Belongs to the SKT5 family. {ECO:0000305}.
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DR EMBL; CP003825; AFR95549.1; -; Genomic_DNA.
DR RefSeq; XP_012050245.1; XM_012194855.1.
DR AlphaFoldDB; J9VSG5; -.
DR SMR; J9VSG5; -.
DR EnsemblFungi; AFR95549; AFR95549; CNAG_07636.
DR GeneID; 23890461; -.
DR VEuPathDB; FungiDB:CNAG_07636; -.
DR HOGENOM; CLU_000288_126_3_1; -.
DR Proteomes; UP000010091; Chromosome 6.
DR GO; GO:0005886; C:plasma membrane; IC:UniProtKB.
DR GO; GO:0008047; F:enzyme activator activity; IMP:UniProtKB.
DR GO; GO:0034221; P:fungal-type cell wall chitin biosynthetic process; IMP:UniProtKB.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR006597; Sel1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF08238; Sel1; 7.
DR SMART; SM00671; SEL1; 7.
PE 3: Inferred from homology;
KW Cell membrane; Lipoprotein; Membrane; Methylation; Prenylation; Repeat.
FT CHAIN 1..485
FT /note="Chitin synthase regulator 2"
FT /id="PRO_0000451818"
FT PROPEP 483..485
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P34165"
FT /id="PRO_0000451819"
FT REPEAT 164..202
FT /note="Sel1-like 1"
FT /evidence="ECO:0000255"
FT REPEAT 203..238
FT /note="Sel1-like 2"
FT /evidence="ECO:0000255"
FT REPEAT 239..275
FT /note="Sel1-like 3"
FT /evidence="ECO:0000255"
FT REPEAT 279..316
FT /note="Sel1-like 4"
FT /evidence="ECO:0000255"
FT REPEAT 317..353
FT /note="Sel1-like 5"
FT /evidence="ECO:0000255"
FT REPEAT 354..391
FT /note="Sel1-like 6"
FT /evidence="ECO:0000255"
FT REPEAT 392..427
FT /note="Sel1-like 7"
FT /evidence="ECO:0000255"
FT REGION 460..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 482
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P34165"
FT LIPID 482
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P34165"
SQ SEQUENCE 485 AA; 52855 MW; 4EC4040586D919C7 CRC64;
MATTNAQIYQ QSQMPIPMPT PSLNPNINSA PTPGPNAMSV YEDCQSPLDT SVSGMYPGDR
GSRVVSQPAP LLDQSHLRPG NQANLLSHDR TIELYRENAK KTNDPELIFE FSAFMIDAAK
AMIPPEQEKD TNPSPALIKQ MEKREEIIKE ATSLLKRLAD RGFPDAQYFL ADCYANGIGT
ARGKQDFDRA FPLFILAAKH GHPDACYRAG TCCEHGWGCR RDSAKAVSFY KKAAVGLHPG
AMYRLGTAEL NGALGFPRRP KEGVKWLKRS AEHATEEFPH ALHELALLHE RGIENVVFVD
NDYAAELLAQ SAELGYAPSA FKLGECYEYG KMGCPVDPAL SIHYYNISAQ QDHKDACFAL
TAWYLVGSPG VLPQSDTEAY LWAKKAAELG LAKAQYAVGY FTETGIGIEA NPQAALTWYK
QAAEGGDKRA AKRLATGSRS SALDRRLEME ALKEEKRLGA ANLAQRSGSG SGASGKDGKD
GCLIM
