PGA10_CANAL
ID PGA10_CANAL Reviewed; 250 AA.
AC Q59UP6; A0A1D8PL58;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=GPI-anchored hemophore PGA10 {ECO:0000305};
DE AltName: Full=GPI-anchored protein 10 {ECO:0000303|PubMed:12845604};
DE AltName: Full=Repressed by TUP1 protein 51 {ECO:0000303|PubMed:15306022};
DE AltName: Full=Repressed by TUP1 protein 8;
DE Flags: Precursor;
GN Name=PGA10 {ECO:0000303|PubMed:12845604};
GN Synonyms=CRW2, RBT51 {ECO:0000303|PubMed:15306022}, RBT8;
GN OrderedLocusNames=CAALFM_C400450CA; ORFNames=CaO19.13119, CaO19.5674;
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 DOMAIN.
RX PubMed=12633989; DOI=10.1016/s0968-0004(03)00025-2;
RA Kulkarni R.D., Kelkar H.S., Dean R.A.;
RT "An eight-cysteine-containing CFEM domain unique to a group of fungal
RT membrane proteins.";
RL Trends Biochem. Sci. 28:118-121(2003).
RN [5]
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 [6]
RP FUNCTION, HEME-BINDING, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=15306022; DOI=10.1111/j.1365-2958.2004.04199.x;
RA Weissman Z., Kornitzer D.;
RT "A family of Candida cell surface haem-binding proteins involved in haemin
RT and haemoglobin-iron utilization.";
RL Mol. Microbiol. 53:1209-1220(2004).
RN [7]
RP FUNCTION.
RX PubMed=17042757; DOI=10.1111/j.1567-1364.2006.00131.x;
RA Perez A., Pedros B., Murgui A., Casanova M., Lopez-Ribot J.L.,
RA Martinez J.P.;
RT "Biofilm formation by Candida albicans mutants for genes coding fungal
RT proteins exhibiting the eight-cysteine-containing CFEM domain.";
RL FEMS Yeast Res. 6:1074-1084(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
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 [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18466294; DOI=10.1111/j.1365-2958.2008.06277.x;
RA Weissman Z., Shemer R., Conibear E., Kornitzer D.;
RT "An endocytic mechanism for haemoglobin-iron acquisition in Candida
RT albicans.";
RL Mol. Microbiol. 69:201-217(2008).
RN [10]
RP INDUCTION.
RX PubMed=20870877; DOI=10.1128/ec.00159-10;
RA Synnott J.M., Guida A., Mulhern-Haughey S., Higgins D.G., Butler G.;
RT "Regulation of the hypoxic response in Candida albicans.";
RL Eukaryot. Cell 9:1734-1746(2010).
RN [11]
RP INDUCTION, AND FUNCTION.
RX PubMed=21205162; DOI=10.1111/j.1567-1364.2010.00714.x;
RA Perez A., Ramage G., Blanes R., Murgui A., Casanova M., Martinez J.P.;
RT "Some biological features of Candida albicans mutants for genes coding
RT fungal proteins containing the CFEM domain.";
RL FEMS Yeast Res. 11:273-284(2011).
CC -!- FUNCTION: Heme-binding protein involved in heme-iron utilization. The
CC ability to acquire iron from host tissues is a major virulence factor
CC of pathogenic microorganisms. Involved in biofilm formation.
CC {ECO:0000269|PubMed:15306022, ECO:0000269|PubMed:17042757,
CC ECO:0000269|PubMed:18466294, ECO:0000269|PubMed:21205162}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:18227255}. Cell membrane
CC {ECO:0000269|PubMed:15306022, ECO:0000269|PubMed:18466294}; Lipid-
CC anchor, GPI-anchor {ECO:0000303|PubMed:12845604}. Note=Found anchored
CC in the cell membrane as well as a covalently-linked GPI-modified cell
CC wall protein (GPI-CWP). {ECO:0000269|PubMed:18466294}.
CC -!- INDUCTION: Induced by RIM101 at pH8, hypoxia, ketoconazole, ciclopirox,
CC and during hyphal growth. Regulated by UPC2 and BCR1.
CC {ECO:0000269|PubMed:18227255, ECO:0000269|PubMed:20870877,
CC ECO:0000269|PubMed:21205162}.
CC -!- DOMAIN: The CFEM domain is involved in heme-binding and contains 8
CC cysteines and is found in proteins from several pathogenic fungi,
CC including both human and plant pathogens (PubMed:12633989). The CFEM
CC domain adopts a novel helical-basket fold that consists of six alpha-
CC helices, and is uniquely stabilized by four disulfide bonds formed by
CC its 8 signature cysteines (By similarity).
CC {ECO:0000250|UniProtKB:Q5A0X8, ECO:0000269|PubMed:12633989}.
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 {ECO:0000305}.
CC -!- PTM: Mannosylated. {ECO:0000269|PubMed:15306022}.
CC -!- SIMILARITY: Belongs to the RBT5 family. {ECO:0000305}.
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DR EMBL; CP017626; AOW28838.1; -; Genomic_DNA.
DR RefSeq; XP_713355.2; XM_708262.2.
DR AlphaFoldDB; Q59UP6; -.
DR SMR; Q59UP6; -.
DR STRING; 237561.Q59UP6; -.
DR GeneID; 3645009; -.
DR KEGG; cal:CAALFM_C400450CA; -.
DR CGD; CAL0000193946; PGA10.
DR VEuPathDB; FungiDB:C4_00450C_A; -.
DR eggNOG; ENOG502SFDE; Eukaryota.
DR HOGENOM; CLU_079397_0_0_1; -.
DR InParanoid; Q59UP6; -.
DR OrthoDB; 1627841at2759; -.
DR PRO; PR:Q59UP6; -.
DR Proteomes; UP000000559; Chromosome 4.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR InterPro; IPR008427; Extracellular_membr_CFEM_dom.
DR Pfam; PF05730; CFEM; 1.
DR SMART; SM00747; CFEM; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall; Disulfide bond; Glycoprotein; GPI-anchor; Heme;
KW Iron; Lipoprotein; Membrane; Metal-binding; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..230
FT /note="GPI-anchored hemophore PGA10"
FT /id="PRO_0000424648"
FT PROPEP 231..250
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424649"
FT REGION 48..111
FT /note="CFEM"
FT /evidence="ECO:0000303|PubMed:12633989"
FT REGION 165..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 72
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
FT LIPID 230
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..94
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
FT DISULFID 58..89
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
FT DISULFID 68..75
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
FT DISULFID 77..110
FT /evidence="ECO:0000250|UniProtKB:Q5A0X8"
SQ SEQUENCE 250 AA; 25163 MW; C6227CD31F011DD8 CRC64;
MMSFSLLSIV SIALAATVSA TSDGTNAYTA YPSVAKTASI NGFADKIYDQ LPECAKECVK
QSTSNTPCPY WDTGCLCVMP QFGGAIGDCV AKNCKGKEVD SVESLATSIC SSAGVGEPYW
MIPSSVSDAL AKAANAASAT TSVETATKSA AAELATTSDT TIVASTSHES KVAETSVAQQ
TASTEKSSAA ETSRAKETSK AEESSKAEET SVAQSSSSAN VASVSAETAN AGNMPVIAIG
GVIAAFAALI
