PGA45_CANAL
ID PGA45_CANAL Reviewed; 463 AA.
AC Q5AA33; A0A1D8PDS2; Q5AAC1;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Predicted GPI-anchored protein 45;
DE Flags: Precursor;
GN Name=PGA45; OrderedLocusNames=CAALFM_C105960WA;
GN ORFNames=CaO19.2451, CaO19.9987;
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=15814841; DOI=10.1091/mbc.e05-01-0071;
RA Garcia-Sanchez S., Mavor A.L., Russell C.L., Argimon S., Dennison P.,
RA Enjalbert B., Brown A.J.;
RT "Global roles of Ssn6 in Tup1- and Nrg1-dependent gene regulation in the
RT fungal pathogen, Candida albicans.";
RL Mol. Biol. Cell 16:2913-2925(2005).
RN [6]
RP INDUCTION.
RX PubMed=16339080; DOI=10.1091/mbc.e05-06-0501;
RA Enjalbert B., Smith D.A., Cornell M.J., Alam I., Nicholls S., Brown A.J.P.,
RA Quinn J.;
RT "Role of the Hog1 stress-activated protein kinase in the global
RT transcriptional response to stress in the fungal pathogen Candida
RT albicans.";
RL Mol. Biol. Cell 17:1018-1032(2006).
RN [7]
RP INDUCTION.
RX PubMed=16552442; DOI=10.1371/journal.ppat.0020021;
RA Bruno V.M., Kalachikov S., Subaran R., Nobile C.J., Kyratsous C.,
RA Mitchell A.P.;
RT "Control of the C. albicans cell wall damage response by transcriptional
RT regulator Cas5.";
RL PLoS Pathog. 2:E21-E21(2006).
RN [8]
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 [9]
RP INDUCTION.
RX PubMed=21414038; DOI=10.1111/j.1365-2958.2011.07626.x;
RA Bonhomme J., Chauvel M., Goyard S., Roux P., Rossignol T., d'Enfert C.;
RT "Contribution of the glycolytic flux and hypoxia adaptation to efficient
RT biofilm formation by Candida albicans.";
RL Mol. Microbiol. 80:995-1013(2011).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}. Secreted, cell wall
CC {ECO:0000269|PubMed:18712765}.
CC -!- INDUCTION: Expression is induced by HOG1 and during biofoilm formation,
CC and repressed by caspofungin. Also regulated by SSN6.
CC {ECO:0000269|PubMed:15814841, ECO:0000269|PubMed:16339080,
CC ECO:0000269|PubMed:16552442, ECO:0000269|PubMed:21414038}.
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.
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DR EMBL; CP017623; AOW26260.1; -; Genomic_DNA.
DR RefSeq; XP_718473.2; XM_713380.2.
DR AlphaFoldDB; Q5AA33; -.
DR GeneID; 3639875; -.
DR KEGG; cal:CAALFM_C105960WA; -.
DR CGD; CAL0000189107; PGA45.
DR VEuPathDB; FungiDB:C1_05960W_A; -.
DR eggNOG; ENOG502T3NC; Eukaryota.
DR HOGENOM; CLU_032732_0_0_1; -.
DR OrthoDB; 1490025at2759; -.
DR PRO; PR:Q5AA33; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005576; C:extracellular region; IDA:CGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030445; C:yeast-form cell wall; IDA:CGD.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..441
FT /note="Predicted GPI-anchored protein 45"
FT /id="PRO_0000429948"
FT PROPEP 442..463
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000429949"
FT REGION 397..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 441
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 463 AA; 49049 MW; 27D6747C0523E003 CRC64;
MQFLFTFIFL LIPLVYSLPA ASPKSGTDFD FNQEIETFVE QAFNQDDPSQ AAAAAASFEE
FLVNVFNYDQ ADGQVDGQVL KVFEKRDANT EQTIEGILKA VNNSGVIWTL LDSVADDPSR
IEYIGNLTSS FLKNYNITLN IADLLSESSS LTENLNITGL LSAVENSGLI TSLLDGILLD
ENFRPRLVDL IDRLVLSQKN VLLYIFAGVL SKRDLMADGE LVNVLLKRAT SNDDSYSGSL
GSFLNNAAST VLSSSLVSNA VADVLNALND TGFLVYATKR FLSSDSYINM TVALVNDIVS
SSSVTIDTSG LNITELISGT LGNPKEIAAL VGSLLSGDSS QTSQLSNYLG RYSGALSQIL
QDLEKKGLFA ELNSYIFGDS TTKASATATA TATATSSANG KNVANNNNKD AATSGSATSN
SSTSTNTKSA SNGAGAVIYT GSNTQTTFLK ALTILFGGAL LFL
