ID   PGA50_CANAL             Reviewed;         309 AA.
AC   Q59MD0; A0A1D8PDR6;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Probable cell wall protein PGA50;
DE   AltName: Full=Predicted GPI-anchored protein 50;
DE   Flags: Precursor;
GN   Name=PGA50; OrderedLocusNames=CAALFM_C106260WA;
GN   ORFNames=CaO19.1824, CaO19.9383;
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).
CC   -!- FUNCTION: Probable GPI-anchored cell wall protein that may be involved
CC       in cell wall organization, hyphal growth, as well as in virulence.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}. Membrane
CC       {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
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 IHD1 family. {ECO:0000305}.
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DR   EMBL; CP017623; AOW26287.1; -; Genomic_DNA.
DR   RefSeq; XP_710875.2; XM_705783.2.
DR   AlphaFoldDB; Q59MD0; -.
DR   GeneID; 3647524; -.
DR   KEGG; cal:CAALFM_C106260WA; -.
DR   CGD; CAL0000197770; PGA50.
DR   VEuPathDB; FungiDB:C1_06260W_A; -.
DR   HOGENOM; CLU_900138_0_0_1; -.
DR   PRO; PR:Q59MD0; -.
DR   Proteomes; UP000000559; Chromosome 1.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cell wall; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW   Reference proteome; Secreted; Signal; Virulence.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..286
FT                   /note="Probable cell wall protein PGA50"
FT                   /id="PRO_0000424743"
FT   PROPEP          287..309
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000424744"
FT   REGION          241..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           286
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        267
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        277
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   309 AA;  33997 MW;  497EEBFCC599ACB1 CRC64;
     MKLNLLLLLF IVELVAAVTN YNLGSAPVSR YLSKTGTYSP VAASRVCNDN CYSFYEGELF
     CGKFDSNVSE TDYLNCLCLN KQYRSNFEGC NCKSESEVNF FDWKSSCSDI SSVKNYSLPT
     TQLGTCNSHC SAYQTIPAEC LVYESGKYQE DQVCICQNAE FWYHYENCDC LDFGDVDHEY
     EDICYYATNS FVTSDDYYDS FFATYTEGSF ESILEKGSFL AEQKGSITSG LASKTETSKV
     STTTFSSNGT SSGTTNGDTR AETKSSNSTQ TSSSDKNSSQ INSISSTGVA NFVASFGMGT
     LLLFVLSLC