PGA4_CANAL
ID PGA4_CANAL Reviewed; 451 AA.
AC Q5AJY5; A0A1D8PP82;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=1,3-beta-glucanosyltransferase PGA4;
DE EC=2.4.1.-;
DE AltName: Full=GPI-anchored protein 4;
DE Flags: Precursor;
GN Name=PGA4; Synonyms=GAS1; OrderedLocusNames=CAALFM_C505390CA;
GN ORFNames=CaO19.11518, CaO19.4035;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP PREDICTION OF GPI-ANCHOR.
RX PubMed=12845604; DOI=10.1002/yea.1007;
RA De Groot P.W., Hellingwerf K.J., Klis F.M.;
RT "Genome-wide identification of fungal GPI proteins.";
RL Yeast 20:781-796(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=15302828; DOI=10.1128/ec.3.4.955-965.2004;
RA de Groot P.W., de Boer A.D., Cunningham J., Dekker H.L., de Jong L.,
RA Hellingwerf K.J., de Koster C., Klis F.M.;
RT "Proteomic analysis of Candida albicans cell walls reveals covalently bound
RT carbohydrate-active enzymes and adhesins.";
RL Eukaryot. Cell 3:955-965(2004).
RN [6]
RP INDUCTION.
RX PubMed=17645752; DOI=10.1111/j.1462-5822.2007.01009.x;
RA Zakikhany K., Naglik J.R., Schmidt-Westhausen A., Holland G., Schaller M.,
RA Hube B.;
RT "In vivo transcript profiling of Candida albicans identifies a gene
RT essential for interepithelial dissemination.";
RL Cell. Microbiol. 9:2938-2954(2007).
RN [7]
RP INDUCTION.
RX PubMed=17257864; DOI=10.1016/j.fgb.2006.12.006;
RA Eckert S.E., Heinz W.J., Zakikhany K., Thewes S., Haynes K., Hube B.,
RA Muhlschlegel F.A.;
RT "PGA4, a GAS homologue from Candida albicans, is up-regulated early in
RT infection processes.";
RL Fungal Genet. Biol. 44:368-377(2007).
RN [8]
RP INDUCTION.
RX PubMed=17238235; DOI=10.1002/yea.1444;
RA Moreno I., Castillo L., Sentandreu R., Valentin E.;
RT "Global transcriptional profiling of Candida albicans cwt1 null mutant.";
RL Yeast 24:357-370(2007).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18765290; DOI=10.1016/j.fgb.2008.08.003;
RA Plaine A., Walker L., Da Costa G., Mora-Montes H.M., McKinnon A., Gow N.A.,
RA Gaillardin C., Munro C.A., Richard M.L.;
RT "Functional analysis of Candida albicans GPI-anchored proteins: roles in
RT cell wall integrity and caspofungin sensitivity.";
RL Fungal Genet. Biol. 45:1404-1414(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=18227255; DOI=10.1099/mic.0.2007/012617-0;
RA Sosinska G.J., de Groot P.W., Teixeira de Mattos M.J., Dekker H.L.,
RA de Koster C.G., Hellingwerf K.J., Klis F.M.;
RT "Hypoxic conditions and iron restriction affect the cell-wall proteome of
RT Candida albicans grown under vagina-simulative conditions.";
RL Microbiology 154:510-520(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=18712765; DOI=10.1002/pmic.200800110;
RA Castillo L., Calvo E., Martinez A.I., Ruiz-Herrera J., Valentin E.,
RA Lopez J.A., Sentandreu R.;
RT "A study of the Candida albicans cell wall proteome.";
RL Proteomics 8:3871-3881(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=20641015; DOI=10.1002/yea.1775;
RA Sorgo A.G., Heilmann C.J., Dekker H.L., Brul S., de Koster C.G., Klis F.M.;
RT "Mass spectrometric analysis of the secretome of Candida albicans.";
RL Yeast 27:661-672(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=20864472; DOI=10.1099/mic.0.044206-0;
RA Sosinska G.J., de Koning L.J., de Groot P.W., Manders E.M., Dekker H.L.,
RA Hellingwerf K.J., de Koster C.G., Klis F.M.;
RT "Mass spectrometric quantification of the adaptations in the wall proteome
RT of Candida albicans in response to ambient pH.";
RL Microbiology 157:136-146(2011).
RN [14]
RP INDUCTION.
RX PubMed=21622905; DOI=10.1128/ec.05011-11;
RA Sorgo A.G., Heilmann C.J., Dekker H.L., Bekker M., Brul S., de Koster C.G.,
RA de Koning L.J., Klis F.M.;
RT "Effects of fluconazole on the secretome, the wall proteome, and wall
RT integrity of the clinical fungus Candida albicans.";
RL Eukaryot. Cell 10:1071-1081(2011).
RN [15]
RP FUNCTION, AND INDUCTION.
RX PubMed=22997008; DOI=10.1002/pmic.201200228;
RA Ene I.V., Heilmann C.J., Sorgo A.G., Walker L.A., de Koster C.G.,
RA Munro C.A., Klis F.M., Brown A.J.;
RT "Carbon source-induced reprogramming of the cell wall proteome and
RT secretome modulates the adherence and drug resistance of the fungal
RT pathogen Candida albicans.";
RL Proteomics 12:3164-3179(2012).
CC -!- FUNCTION: Splits internally a 1,3-beta-glucan molecule and transfers
CC the newly generated reducing end (the donor) to the non-reducing end of
CC another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta
CC linkage, resulting in the elongation of 1,3-beta-glucan chains in the
CC cell wall. Involved in cell wall biosynthesis and morphogenesis. Plays
CC a key role in virulence. {ECO:0000269|PubMed:18765290,
CC ECO:0000269|PubMed:22997008}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:18227255,
CC ECO:0000269|PubMed:18712765, ECO:0000269|PubMed:20641015,
CC ECO:0000269|PubMed:20864472}. Membrane {ECO:0000305}; Lipid-anchor,
CC GPI-anchor {ECO:0000305}. Note=Covalently-linked GPI-modified cell wall
CC protein (GPI-CWP).
CC -!- INDUCTION: Transcript levels are elevated during host infection, and
CC transiently increased after induction of hyphal formation with serum.
CC Expression is controlled by CWT1 and induced by fluconazole.
CC {ECO:0000269|PubMed:17238235, ECO:0000269|PubMed:17257864,
CC ECO:0000269|PubMed:17645752, ECO:0000269|PubMed:21622905,
CC ECO:0000269|PubMed:22997008}.
CC -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC reticulum and serves to target the protein to the cell surface. There,
CC the glucosamine-inositol phospholipid moiety is cleaved off and the
CC GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
CC -!- DISRUPTION PHENOTYPE: Leads to decreased caspofungin sensitivity.
CC {ECO:0000269|PubMed:18765290}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family. {ECO:0000305}.
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DR EMBL; CP017627; AOW29943.1; -; Genomic_DNA.
DR RefSeq; XP_721943.1; XM_716850.2.
DR AlphaFoldDB; Q5AJY5; -.
DR SMR; Q5AJY5; -.
DR STRING; 237561.Q5AJY5; -.
DR GeneID; 3636406; -.
DR KEGG; cal:CAALFM_C505390CA; -.
DR CGD; CAL0000186924; PGA4.
DR VEuPathDB; FungiDB:C5_05390C_A; -.
DR eggNOG; ENOG502QRZZ; Eukaryota.
DR HOGENOM; CLU_021855_1_0_1; -.
DR InParanoid; Q5AJY5; -.
DR OMA; MFAKYDN; -.
DR OrthoDB; 728071at2759; -.
DR PRO; PR:Q5AJY5; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:CGD.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IDA:CGD.
DR GO; GO:1903561; C:extracellular vesicle; IDA:CGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0030445; C:yeast-form cell wall; IDA:CGD.
DR GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; ISA:CGD.
DR GO; GO:0034411; P:cell wall (1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR GO; GO:0071970; P:fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR InterPro; IPR004886; Glucanosyltransferase.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31468; PTHR31468; 1.
DR Pfam; PF03198; Glyco_hydro_72; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Reference proteome; Secreted; Signal; Transferase;
KW Virulence.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..430
FT /note="1,3-beta-glucanosyltransferase PGA4"
FT /id="PRO_0000424640"
FT PROPEP 431..451
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424641"
FT REGION 316..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 152
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 254
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="1"
FT /ligand_note="donor substrate"
FT /evidence="ECO:0000250"
FT BINDING 108..116
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="1"
FT /ligand_note="donor substrate"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="1"
FT /ligand_note="donor substrate"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="2"
FT /ligand_note="acceptor substrate"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="2"
FT /ligand_note="acceptor substrate"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="(1,3-beta-D-glucosyl)n"
FT /ligand_id="ChEBI:CHEBI:37671"
FT /ligand_label="1"
FT /ligand_note="donor substrate"
FT /evidence="ECO:0000250"
FT LIPID 430
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 451 AA; 48996 MW; 98E90849E77A8D79 CRC64;
MLFRSLVTYL SLVSSVLSIA SIKVEGNAFW DSESGDRFYI RGVDYQPGGS SELEDPLADT
NVCERDVKYF QELGINTIRV YSIDNTKNHT ECMDTLAKAG IYVILDVNTP HSSITRSDAA
CSYNTDYLQE VFASIVEFAQ FDNTLGFFAG NEVINDGPSL EAAPYVKAVV RDMKTFIKNR
GFRTIPVGYS AASVDEYRLP SGLYFNCGDD DMARIDMYGI NDYSWCGDAS MTTSQYSQQM
KDFANYTVPL FFSEFGCNAK RPRPFSEIEA IYSTEMSSVF SGGLVYEYSE EASNYGLVEL
KGDSVTTNDD FDNLKSQFEK TKNPSGDGGY LKSTGGNKCP PKSNIWNVTE EIPDTPKGAL
KYLKGLAEPT GHGFDAYVQG NCNAKGNNVD DTGNYTSSIT ASSRASPSQT SQVSSSSATS
ANSTSSKKND AAVEGAGFLS VIALAAGIAL L
