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PGA31_CANAL
ID   PGA31_CANAL             Reviewed;         293 AA.
AC   Q5A5U9; A0A1D8PM04; Q5A631;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2017, sequence version 2.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Cell wall protein PGA31;
DE   AltName: Full=GPI-anchored protein 31;
DE   AltName: Full=LDG family protein 5;
DE   Flags: Precursor;
GN   Name=PGA31; Synonyms=LDG5; OrderedLocusNames=CAALFM_C404080CA;
GN   ORFNames=CaO19.12761, CaO19.5302;
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=12397174; DOI=10.1073/pnas.232566499;
RA   Lan C.Y., Newport G., Murillo L.A., Jones T., Scherer S., Davis R.W.,
RA   Agabian N.;
RT   "Metabolic specialization associated with phenotypic switching in
RT   Candidaalbicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14907-14912(2002).
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=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   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18765290; DOI=10.1016/j.fgb.2008.08.003;
RA   Plaine A., Walker L., Da Costa G., Mora-Montes H.M., McKinnon A., Gow N.A.,
RA   Gaillardin C., Munro C.A., Richard M.L.;
RT   "Functional analysis of Candida albicans GPI-anchored proteins: roles in
RT   cell wall integrity and caspofungin sensitivity.";
RL   Fungal Genet. Biol. 45:1404-1414(2008).
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   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=22997008; DOI=10.1002/pmic.201200228;
RA   Ene I.V., Heilmann C.J., Sorgo A.G., Walker L.A., de Koster C.G.,
RA   Munro C.A., Klis F.M., Brown A.J.;
RT   "Carbon source-induced reprogramming of the cell wall proteome and
RT   secretome modulates the adherence and drug resistance of the fungal
RT   pathogen Candida albicans.";
RL   Proteomics 12:3164-3179(2012).
RN   [10]
RP   INDUCTION.
RX   PubMed=23208712; DOI=10.1128/aac.02040-12;
RA   Silva L.V., Sanguinetti M., Vandeputte P., Torelli R., Rochat B.,
RA   Sanglard D.;
RT   "Milbemycins: more than efflux inhibitors for fungal pathogens.";
RL   Antimicrob. Agents Chemother. 57:873-886(2013).
RN   [11]
RP   INDUCTION.
RX   PubMed=23563485; DOI=10.1128/ec.00071-13;
RA   Srikantha T., Daniels K.J., Pujol C., Kim E., Soll D.R.;
RT   "Identification of genes upregulated by the transcription factor Bcr1 that
RT   are involved in impermeability, impenetrability, and drug resistance of
RT   Candida albicans a/alpha biofilms.";
RL   Eukaryot. Cell 12:875-888(2013).
CC   -!- FUNCTION: Component of the cell wall involved in virulence which plays
CC       a role in the relationship between C.albicans and the host (By
CC       similarity). Involved in the regulation or assembly of chitin within
CC       the cell wall. {ECO:0000250, ECO:0000269|PubMed:18765290}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Lipid-anchor, GPI-
CC       anchor.
CC   -!- INDUCTION: Expression is regulated upon white-opaque switch, during
CC       cell wall regeneration, and when cells are grown on lactate. Also up-
CC       regulated upon milbemycin A3 oxim derivative (A3Ox) treatment.
CC       Repressed by BCR1. {ECO:0000269|PubMed:12397174,
CC       ECO:0000269|PubMed:16455273, ECO:0000269|PubMed:22997008,
CC       ECO:0000269|PubMed:23208712, ECO:0000269|PubMed:23563485}.
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 hypersensitivity to caspofungin.
CC       {ECO:0000269|PubMed:18765290}.
CC   -!- SIMILARITY: Belongs to the SRP1/TIP1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AOW29157.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP017626; AOW29157.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_717105.1; XM_712012.1.
DR   AlphaFoldDB; Q5A5U9; -.
DR   GeneID; 3641226; -.
DR   KEGG; cal:CAALFM_C404080CA; -.
DR   CGD; CAL0000183944; PGA31.
DR   eggNOG; ENOG502SXWZ; Eukaryota.
DR   HOGENOM; CLU_083354_0_0_1; -.
DR   OrthoDB; 1611342at2759; -.
DR   PRO; PR:Q5A5U9; -.
DR   Proteomes; UP000000559; Chromosome 4.
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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..271
FT                   /note="Cell wall protein PGA31"
FT                   /id="PRO_0000424729"
FT   PROPEP          272..293
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000424730"
FT   REGION          161..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          233..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           271
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        190
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   293 AA;  29735 MW;  F8FD74DCBD1C544A CRC64;
     MKFLTAASLL TLSSSALAAI KDIQLYAQSS NNEVNDFGIS SRHEGAALNY LFLAAPGVAE
     NLKYDDETKT VYTELKAGSS TVRQPLNVGN TVLQLGGSGD GTKVDIAEDG TLSFDGSDSV
     GAAKNINDPY NYSKDSYAVV KGGDGAIPIK LVAKFTGDDK ESASSSSSSA APEPTASSSE
     APKETPVYSN STVTLYTTYC PLSTTITLTV CSDVCTPTVI ETSGSVTVSS VQVPSKTASS
     EAAPPKTTVD SVSKPAPSGK KPTAAVTSFE GAANALTGGS VAIAVAAAIG LVF
 
 
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