PGA13_CANAL
ID PGA13_CANAL Reviewed; 456 AA.
AC Q5A343; A0A1D8PTT1;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=GPI-anchored protein 13;
DE Flags: Precursor;
GN Name=PGA13; OrderedLocusNames=CAALFM_CR08510WA;
GN ORFNames=CaO19.13778, CaO19.6420;
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=15917516; DOI=10.1128/aac.49.6.2226-2236.2005;
RA Liu T.T., Lee R.E., Barker K.S., Lee R.E., Wei L., Homayouni R.,
RA Rogers P.D.;
RT "Genome-wide expression profiling of the response to azole, polyene,
RT echinocandin, and pyrimidine antifungal agents in Candida albicans.";
RL Antimicrob. Agents Chemother. 49:2226-2236(2005).
RN [6]
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 [7]
RP INDUCTION.
RX PubMed=16102003; DOI=10.1111/j.1365-2958.2005.04771.x;
RA Urban C., Xiong X., Sohn K., Schroppel K., Brunner H., Rupp S.;
RT "The moonlighting protein Tsa1p is implicated in oxidative stress response
RT and in cell wall biogenesis in Candida albicans.";
RL Mol. Microbiol. 57:1318-1341(2005).
RN [8]
RP INDUCTION.
RX PubMed=16455273; DOI=10.1016/j.fgb.2005.12.002;
RA Castillo L., Martinez A.I., Garcera A., Garcia-Martinez J.,
RA Ruiz-Herrera J., Valentin E., Sentandreu R.;
RT "Genomic response programs of Candida albicans following protoplasting and
RT regeneration.";
RL Fungal Genet. Biol. 43:124-134(2006).
RN [9]
RP INDUCTION.
RX PubMed=18434592; DOI=10.1091/mbc.e08-02-0191;
RA Rauceo J.M., Blankenship J.R., Fanning S., Hamaker J.J., Deneault J.S.,
RA Smith F.J., Nantel A., Mitchell A.P.;
RT "Regulation of the Candida albicans cell wall damage response by
RT transcription factor Sko1 and PAS kinase Psk1.";
RL Mol. Biol. Cell 19:2741-2751(2008).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=22343036; DOI=10.1016/j.fgb.2012.01.010;
RA Gelis S., de Groot P.W., Castillo L., Moragues M.D., Sentandreu R.,
RA Gomez M.M., Valentin E.;
RT "Pga13 in Candida albicans is localized in the cell wall and influences
RT cell surface properties, morphogenesis and virulence.";
RL Fungal Genet. Biol. 49:322-331(2012).
RN [11]
RP INDUCTION.
RX PubMed=23731904; DOI=10.1016/j.ijmm.2013.05.003;
RA Yu Q., Ding X., Zhang B., Xu N., Cheng X., Qian K., Zhang B., Xing L.,
RA Li M.;
RT "The P-type ATPase Spf1 is required for endoplasmic reticulum functions and
RT cell wall integrity in Candida albicans.";
RL Int. J. Med. Microbiol. 303:257-266(2013).
RN [12]
RP INDUCTION.
RX PubMed=23613980; DOI=10.1371/journal.pone.0061940;
RA Palige K., Linde J., Martin R., Bottcher B., Citiulo F., Sullivan D.J.,
RA Weber J., Staib C., Rupp S., Hube B., Morschhauser J., Staib P.;
RT "Global transcriptome sequencing identifies chlamydospore specific markers
RT in Candida albicans and Candida dubliniensis.";
RL PLoS ONE 8:E61940-E61940(2013).
CC -!- FUNCTION: Cell wall protein which contributes to cell wall synthesis
CC and is important for acquiring normal surface properties. Required for
CC virulence in a mouse infection model. {ECO:0000269|PubMed:22343036}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:22343036}. Membrane {ECO:0000269|PubMed:22343036};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:22343036}.
CC Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP).
CC -!- INDUCTION: Induced by caspofungin, tunicamycin, during chlamydospore
CC formation and during cell wall regeneration following protoplasting.
CC Repressed by NRG1 and TUP1. Also regulated by TSA1.
CC {ECO:0000269|PubMed:15814841, ECO:0000269|PubMed:15917516,
CC ECO:0000269|PubMed:16102003, ECO:0000269|PubMed:16455273,
CC ECO:0000269|PubMed:18434592, ECO:0000269|PubMed:23613980,
CC ECO:0000269|PubMed:23731904}.
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 -!- DISRUPTION PHENOTYPE: leads to increased sensitivity to Congo red,
CC Calcofluor white, and zymolyase, delayed filamentation, a higher
CC surface hydrophobicity, increased adherence and flocculation; as well
CC as to a diminished ability of protoplasts to recover their cell wall.
CC {ECO:0000269|PubMed:22343036}.
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DR EMBL; CP017630; AOW31531.1; -; Genomic_DNA.
DR RefSeq; XP_716258.1; XM_711165.1.
DR AlphaFoldDB; Q5A343; -.
DR GeneID; 3642138; -.
DR KEGG; cal:CAALFM_CR08510WA; -.
DR CGD; CAL0000178196; PGA13.
DR VEuPathDB; FungiDB:CR_08510W_A; -.
DR HOGENOM; CLU_599905_0_0_1; -.
DR InParanoid; Q5A343; -.
DR OMA; CHPTTIE; -.
DR OrthoDB; 1631039at2759; -.
DR PRO; PR:Q5A343; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR GO; GO:0060257; P:negative regulation of flocculation; IMP:CGD.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Reference proteome; Secreted; Signal; Virulence.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..433
FT /note="GPI-anchored protein 13"
FT /id="PRO_0000424654"
FT PROPEP 434..456
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424655"
FT LIPID 433
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 456 AA; 46501 MW; EE845713A3F54A95 CRC64;
MRSPSLAVAA TTVLGLFSSS ALAYYGNTTT VALTTTEFVT TCPYPTTFTV STCTNDVCQP
TVVTVTEETT ITIPGTVVCP VVSTPSGSAS ASASAGASSE EEGSVVTTQV TVTDFTTYCP
YPTTLTITKC ENNECHPTTI PVETATTVTV TGEVICPTTT STSPKESSSE AASSEVITTQ
VTVTDYTTYC PLPTTIVVST CDEEKCHPTT IEVSTPTTVV VPGTVVCPTT SVATPSQSEV
ATKPTTINSV VTTGVTTTDY TTYCPSPTTI VVSTCDEEKC HPTTIEVSTP TTVVVPGTVV
HPSTSATIIT TTAEQPPASP EVSTIESVVT TPATLTGYTT YCPEPTTIVL TTCSDDQCKP
HTVSATGGET VSIPATIVVP SSHTTQVEIT VSSASVPASE KPTTPVTVAA VSSSPAVSTE
TPSLVTPAIS IAGAAAVNVV PTTAFGLFAI ILASIF
