PGA25_CANAL
ID PGA25_CANAL Reviewed; 872 AA.
AC Q59L86; A0A1D8PP85;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Probable GPI-anchored adhesin-like protein PGA25;
DE AltName: Full=Predicted GPI-anchored protein 25;
DE Flags: Precursor;
GN Name=PGA25; OrderedLocusNames=CAALFM_C600070CA; ORFNames=CaO19.6336;
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 INDUCTION.
RX PubMed=15820985; DOI=10.1093/jac/dki088;
RA Copping V.M.S., Barelle C.J., Hube B., Gow N.A.R., Brown A.J.P., Odds F.C.;
RT "Exposure of Candida albicans to antifungal agents affects expression of
RT SAP2 and SAP9 secreted proteinase genes.";
RL J. Antimicrob. Chemother. 55:645-654(2005).
RN [6]
RP PREDICTION OF FUNCTION.
RX PubMed=21496229; DOI=10.1186/1471-2164-12-192;
RA Chaudhuri R., Ansari F.A., Raghunandanan M.V., Ramachandran S.;
RT "FungalRV: adhesin prediction and immunoinformatics portal for human fungal
RT pathogens.";
RL BMC Genomics 12:192-192(2011).
RN [7]
RP INDUCTION.
RX PubMed=22544909; DOI=10.1128/ec.00103-12;
RA Fanning S., Xu W., Solis N., Woolford C.A., Filler S.G., Mitchell A.P.;
RT "Divergent targets of Candida albicans biofilm regulator Bcr1 in vitro and
RT in vivo.";
RL Eukaryot. Cell 11:896-904(2012).
RN [8]
RP INDUCTION.
RX PubMed=23208712; DOI=10.1128/aac.02040-12;
RA Silva L.V., Sanguinetti M., Vandeputte P., Torelli R., Rochat B.,
RA Sanglard D.;
RT "Milbemycins: more than efflux inhibitors for fungal pathogens.";
RL Antimicrob. Agents Chemother. 57:873-886(2013).
CC -!- FUNCTION: Probable GPI-anchored cell wall protein involved in cell wall
CC organization, hyphal growth, as well as in host-fungal interaction and
CC virulence. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}. Membrane
CC {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
CC -!- INDUCTION: Up-regulated in biofilm, in oralpharyngeal candidasis, and
CC upon milbemycins A3 oxim derivative (A3Ox). Down-regulated by
CC fluconazole. {ECO:0000269|PubMed:15820985, ECO:0000269|PubMed:22544909,
CC ECO:0000269|PubMed:23208712}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HYR1/IFF family. {ECO:0000305}.
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DR EMBL; CP017628; AOW29957.1; -; Genomic_DNA.
DR RefSeq; XP_710504.1; XM_705412.1.
DR AlphaFoldDB; Q59L86; -.
DR GeneID; 3647890; -.
DR KEGG; cal:CAALFM_C600070CA; -.
DR CGD; CAL0000186851; PGA25.
DR VEuPathDB; FungiDB:C6_00070C_A; -.
DR HOGENOM; CLU_016383_0_0_1; -.
DR InParanoid; Q59L86; -.
DR OrthoDB; 1842996at2759; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR InterPro; IPR021642; DUF3246.
DR Pfam; PF11596; DUF3246; 2.
PE 1: Evidence at protein level;
KW Cell wall; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Reference proteome; Secreted; Signal; Virulence.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..845
FT /note="Probable GPI-anchored adhesin-like protein PGA25"
FT /id="PRO_0000424953"
FT PROPEP 846..872
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424954"
FT REGION 43..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..809
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 845
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 872 AA; 87571 MW; 35C39BDEC17CDBC3 CRC64;
MKVTAVSSVL LTVAALTNAN EIDKRSFFGD LFSGLTGSKA AAPAAAPAAQ PAAQPTTQSP
ADQPTVQSPV SSDQPSTAQP VAQNNLLLDS SNSTLVVPSS SKSSTTTRST AGLLDNLLGG
SGATSSEASS SEAPSSEAPS SEAPSSEAPS SEAPSSEAPS SSSSEALSSS STTKRPTAAA
KGFFGDLFGT QSSASETDDE DCVEETESPT SAPASAPTTS KVATTTGGGL PNILSDLFPG
KSSAPISSAE SSPTVASSTT GFPNILSDLF PGKSSVPSSS AETSTTVASN TTTSGGGFPN
ILSDLFPGKS SVPSSSAEED DEECEDPTES VTSNSSPTGG ISIPTFPITS QSKTSVSSVV
SKSTSEDDDD ETECETDIPT IIPSGSVLPT TSVLPTIIPT GSGSITILPT KSATSDDDDD
ETDCETDIPT IVPTESATII PTGSGSVTII PTGSGSITVL PTKSATSDDD DDETDCETDI
PTIIPTGTAT IKPTGSGSIT VLPTKSTTTD DDDDETDCET EIPTIHPTVS TTRTFTSDGV
PTTQTLTTKL PPTTNQHTET EVVSITYTGG GQTFTTYLTQ SGEICDETVT LTITTTCPST
TVAPGGQIYT TTVTVITTHT VYPDDWEDDG YEGEDNAGGS ASGSSDDGEW EWYEEDDGEC
VPTGGSSSGS GTGSWWGSGA GSSGGTTSGS GSGSSSNSGA SSGGTWGGSG NDYVCPGEEG
YDDEEPDNGG SWWGGSGSGS SSGSSSGVSS GDSGSSSVTG GSSGSWWGGS GNDYVCPGED
GYDDEDDQTP EPECDDEDDS WDDDEECDTQ AAKEVVNSVT VAAESVYPST TAASLTTSWI
STQTAQSVTQ IENIGGKVSA SGLFVVLGLL LI
