ECM33_CANAL
ID ECM33_CANAL Reviewed; 413 AA.
AC Q5AGC4; A0A1D8PNF1;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Cell surface GPI-anchored protein ECM33;
DE Flags: Precursor;
GN Name=ECM331; Synonyms=ECM33, PST1; OrderedLocusNames=CAALFM_C502460CA;
GN ORFNames=CaO19.11730, CaO19.4255;
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 INDUCTION.
RX PubMed=12912891; DOI=10.1128/ec.2.4.718-728.2003;
RA Ramon A.M., Fonzi W.A.;
RT "Diverged binding specificity of Rim101p, the Candida albicans ortholog of
RT PacC.";
RL Eukaryot. Cell 2:718-728(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 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 [7]
RP INDUCTION.
RX PubMed=15964282; DOI=10.1016/j.cub.2005.05.047;
RA Nobile C.J., Mitchell A.P.;
RT "Regulation of cell-surface genes and biofilm formation by the C. albicans
RT transcription factor Bcr1p.";
RL Curr. Biol. 15:1150-1155(2005).
RN [8]
RP INDUCTION.
RX PubMed=16207920; DOI=10.1099/mic.0.28353-0;
RA Kunze D., Melzer I., Bennett D., Sanglard D., MacCallum D., Norskau J.,
RA Coleman D.C., Odds F.C., Schafer W., Hube B.;
RT "Functional analysis of the phospholipase C gene CaPLC1 and two unusual
RT phospholipase C genes, CaPLC2 and CaPLC3, of Candida albicans.";
RL Microbiology 151:3381-3394(2005).
RN [9]
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 [10]
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 [11]
RP GPI-ANCHOR AT GLY-390, AND SUBCELLULAR LOCATION.
RX PubMed=18723603; DOI=10.1128/ec.00148-08;
RA Mao Y., Zhang Z., Gast C., Wong B.;
RT "C-terminal signals regulate targeting of glycosylphosphatidylinositol-
RT anchored proteins to the cell wall or plasma membrane in Candida
RT albicans.";
RL Eukaryot. Cell 7:1906-1915(2008).
RN [12]
RP INDUCTION.
RX PubMed=18799621; DOI=10.1091/mbc.e08-05-0479;
RA Alvarez F.J., Douglas L.M., Rosebrock A., Konopka J.B.;
RT "The Sur7 protein regulates plasma membrane organization and prevents
RT intracellular cell wall growth in Candida albicans.";
RL Mol. Biol. Cell 19:5214-5225(2008).
RN [13]
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).
CC -!- FUNCTION: Cell surface protein required for proper cell wall integrity
CC and for the correct assembly of the mannoprotein outer layer of the
CC cell wall. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18723603};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:18723603}. Secreted, cell
CC wall {ECO:0000269|PubMed:18723603}. Note=Mostly targeted to the plasma
CC membrane.
CC -!- INDUCTION: Expression is induced by growth in hypoxic conditions and by
CC caspofungin and ketoconazole. Expression is negatively regulated by
CC BCR1, HOG1, PLC1, RIM101, SSN6, and SUR7. {ECO:0000269|PubMed:12912891,
CC ECO:0000269|PubMed:15814841, ECO:0000269|PubMed:15917516,
CC ECO:0000269|PubMed:15964282, ECO:0000269|PubMed:16207920,
CC ECO:0000269|PubMed:16339080, ECO:0000269|PubMed:18799621,
CC ECO:0000269|PubMed:20870877}.
CC -!- SIMILARITY: Belongs to the SPS2 family. {ECO:0000305}.
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; CP017627; AOW29671.1; -; Genomic_DNA.
DR RefSeq; XP_720564.2; XM_715471.2.
DR AlphaFoldDB; Q5AGC4; -.
DR SMR; Q5AGC4; -.
DR STRING; 237561.Q5AGC4; -.
DR GeneID; 3637731; -.
DR KEGG; cal:CAALFM_C502460CA; -.
DR CGD; CAL0000191729; ECM331.
DR VEuPathDB; FungiDB:C5_02460C_A; -.
DR eggNOG; ENOG502QUZC; Eukaryota.
DR HOGENOM; CLU_035846_0_0_1; -.
DR InParanoid; Q5AGC4; -.
DR OrthoDB; 1342410at2759; -.
DR PHI-base; PHI:6079; -.
DR PRO; PR:Q5AGC4; -.
DR Proteomes; UP000000559; Chromosome 5.
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; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR Gene3D; 3.80.20.20; -; 2.
DR InterPro; IPR036941; Rcpt_L-dom_sf.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall; Cell wall biogenesis/degradation; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..390
FT /note="Cell surface GPI-anchored protein ECM33"
FT /id="PRO_0000424915"
FT PROPEP 391..413
FT /note="Removed in mature form"
FT /id="PRO_0000424916"
FT REGION 347..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 390
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000269|PubMed:18723603"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 413 AA; 43683 MW; 79980741DB53C33C CRC64;
MQIKSFLLPI VAALLTSVSA ADSSNKCSFS KTSITEATAI TQLNACSTLD GEITVSGSGI
GSIDLSSVKV LKAKLSILNS PSIVSLNFNQ LQNITGALVI NNATQLNSID LTQLTNVETL
QLVSLPSFAI LNLNQGVQKA GTIVLSDTAL TNLNGLASFN TIDSININNN KNISKIEFND
LQTVTDSLIL SFNNDDAEVK LDSLKWAGNL TIQDVSSIQA SNLTSVNGSL LISYNTFDEL
EFPNLKSVGN SMQIFAHDEL TKISFPKLSE LDGELEMFNN TQLEEIDFGN LTTIKGAVTI
SGPFDNLTME NLKLVSGDFQ VNSTSDKFDC SAFDKLHEKG KIEGHNYVCT HPANPSSSSK
SGSSTQTGKS DSKSSDGSSS SNSSSSSKKG ASNVLVVPGM VLTTALGVLL ALI
