PGA28_CANAL
ID PGA28_CANAL Reviewed; 226 AA.
AC Q5A5K7; A0A1D8PRA9; Q3MP45; Q5A5D8;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Probable GPI-anchored adhesin-like protein PGA28;
DE AltName: Full=Predicted GPI-anchored protein 28;
DE Flags: Precursor;
GN Name=PGA28; OrderedLocusNames=CAALFM_C703110WA;
GN ORFNames=CaO19.12609, CaO19.5144;
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 PREDICTION AS A CLEAVAGE SUBSTRATE FOR KEX2.
RX PubMed=18625069; DOI=10.1186/1471-2180-8-116;
RA Bader O., Krauke Y., Hube B.;
RT "Processing of predicted substrates of fungal Kex2 proteinases from Candida
RT albicans, C. glabrata, Saccharomyces cerevisiae and Pichia pastoris.";
RL BMC Microbiol. 8:116-116(2008).
RN [6]
RP 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=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).
RN [8]
RP FUNCTION.
RX PubMed=23951271; DOI=10.1371/journal.pone.0071939;
RA Fox S.J., Shelton B.T., Kruppa M.D.;
RT "Characterization of genetic determinants that modulate Candida albicans
RT filamentation in the presence of bacteria.";
RL PLoS ONE 8:E71939-E71939(2013).
CC -!- FUNCTION: Putative adhesin which is involved in cell adhesion and
CC virulence (By similarity). Plays a role in Candida-bacterial
CC interactions and subsequent regulation of filamentation. {ECO:0000250,
CC ECO:0000269|PubMed:21496229, ECO:0000269|PubMed:23951271}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- INDUCTION: Up-regulated upon milbemycins A3 oxim derivative (A3Ox)
CC treatment. {ECO:0000269|PubMed:23208712}.
CC -!- PTM: Predicted to be a cleavage substrate for KEX2.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP017629; AOW30656.1; -; Genomic_DNA.
DR RefSeq; XP_716967.1; XM_711874.1.
DR AlphaFoldDB; Q5A5K7; -.
DR STRING; 237561.Q5A5K7; -.
DR GeneID; 3641350; -.
DR KEGG; cal:CAALFM_C703110WA; -.
DR CGD; CAL0000177517; PGA28.
DR VEuPathDB; FungiDB:C7_03110W_A; -.
DR HOGENOM; CLU_1219555_0_0_1; -.
DR OrthoDB; 1649312at2759; -.
DR Proteomes; UP000000559; Chromosome 7.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Reference proteome; Signal; Virulence.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..197
FT /note="Probable GPI-anchored adhesin-like protein PGA28"
FT /id="PRO_0000424931"
FT PROPEP 198..226
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424932"
FT REGION 119..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 197
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 226 AA; 23267 MW; 1FD0292CF2D6E80E CRC64;
MKFFAYFAVI ALSSASLINL FKRATANGCE VESCYKAHQT LINSCNGAFD FNCLCNLPQS
YFQNLYDCSK SCDTLQESDI HSPSDIRSIY CEAASNSIYT FSIDSISLDM IGYSDFETDT
EATTGSDTRT KAATGATTSA GTGVTKTSET GGVSSTANSE AKSGSVTTSK SGSTSISESK
TTSGSSSSGK SSSSTSSASS QQTSSHAGGA SGAFVSLLGL FAALLI