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PGA47_CANAL
ID   PGA47_CANAL             Reviewed;         653 AA.
AC   G1UBC2; A0A1D8PID9; G1UB13;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Cell wall adhesin EAP1;
DE   AltName: Full=Enhanced adherence to polystyrene protein 1;
DE   AltName: Full=GPI-anchored protein 47;
DE   Flags: Precursor;
GN   Name=EAP1; Synonyms=PGA47; OrderedLocusNames=CAALFM_C209530WA;
GN   ORFNames=CaO19.1401, CaO19.8979;
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   FUNCTION, AND INDUCTION.
RX   PubMed=14665461; DOI=10.1128/ec.2.6.1266-1273.2003;
RA   Li F., Palecek S.P.;
RT   "EAP1, a Candida albicans gene involved in binding human epithelial
RT   cells.";
RL   Eukaryot. Cell 2:1266-1273(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=15387822; DOI=10.1111/j.1365-2958.2004.04214.x;
RA   Lan C.Y., Rodarte G., Murillo L.A., Jones T., Davis R.W., Dungan J.,
RA   Newport G., Agabian N.;
RT   "Regulatory networks affected by iron availability in Candida albicans.";
RL   Mol. Microbiol. 53:1451-1469(2004).
RN   [7]
RP   FUNCTION.
RX   PubMed=16321041; DOI=10.1021/bp050236c;
RA   Li F., Palecek S.P.;
RT   "Identification of Candida albicans genes that induce Saccharomyces
RT   cerevisiae cell adhesion and morphogenesis.";
RL   Biotechnol. Prog. 21:1601-1609(2005).
RN   [8]
RP   SUBCELLULAR LOCATION, GPI-ANCHOR, FUNCTION, AND INDUCTION.
RX   PubMed=17416898; DOI=10.1128/ec.00049-07;
RA   Li F., Svarovsky M.J., Karlsson A.J., Wagner J.P., Marchillo K., Oshel P.,
RA   Andes D., Palecek S.P.;
RT   "Eap1p, an adhesin that mediates Candida albicans biofilm formation in
RT   vitro and in vivo.";
RL   Eukaryot. Cell 6:931-939(2007).
RN   [9]
RP   SUBCELLULAR LOCATION, FUNCTION, AND DOMAIN.
RX   PubMed=18375812; DOI=10.1099/mic.0.2007/013789-0;
RA   Li F., Palecek S.P.;
RT   "Distinct domains of the Candida albicans adhesin Eap1p mediate cell-cell
RT   and cell-substrate interactions.";
RL   Microbiology 154:1193-1203(2008).
RN   [10]
RP   INDUCTION.
RX   PubMed=19798425; DOI=10.1371/journal.ppat.1000601;
RA   Sahni N., Yi S., Daniels K.J., Srikantha T., Pujol C., Soll D.R.;
RT   "Genes selectively up-regulated by pheromone in white cells are involved in
RT   biofilm formation in Candida albicans.";
RL   PLoS Pathog. 5:E1000601-E1000601(2009).
RN   [11]
RP   FUNCTION.
RX   PubMed=20709785; DOI=10.1128/ec.00103-10;
RA   Nobbs A.H., Vickerman M.M., Jenkinson H.F.;
RT   "Heterologous expression of Candida albicans cell wall-associated adhesins
RT   in Saccharomyces cerevisiae Reveals differential specificities in adherence
RT   and biofilm formation and in binding oral Streptococcus gordonii.";
RL   Eukaryot. Cell 9:1622-1634(2010).
RN   [12]
RP   INDUCTION.
RX   PubMed=21566087; DOI=10.1099/jmm.0.032037-0;
RA   Kucharikova S., Tournu H., Lagrou K., Van Dijck P., Bujdakova H.;
RT   "Detailed comparison of Candida albicans and Candida glabrata biofilms
RT   under different conditions and their susceptibility to caspofungin and
RT   anidulafungin.";
RL   J. Med. Microbiol. 60:1261-1269(2011).
RN   [13]
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).
RN   [14]
RP   INDUCTION.
RX   PubMed=23948468; DOI=10.1016/j.micpath.2013.07.003;
RA   Tian J., Weng L.X., Zhang Y.Q., Wang L.H.;
RT   "BDSF inhibits Candida albicans adherence to urinary catheters.";
RL   Microb. Pathog. 64:33-38(2013).
RN   [15]
RP   INDUCTION.
RX   PubMed=23704884; DOI=10.1371/journal.pone.0062902;
RA   Samaranayake Y.H., Cheung B.P., Yau J.Y., Yeung S.K., Samaranayake L.P.;
RT   "Human serum promotes Candida albicans biofilm growth and virulence gene
RT   expression on silicone biomaterial.";
RL   PLoS ONE 8:E62902-E62902(2013).
CC   -!- FUNCTION: Cell wall protein which mediates cell-cell and cell-substrate
CC       adhesion. Required for biofilm formation and plays a role in virulence.
CC       {ECO:0000269|PubMed:14665461, ECO:0000269|PubMed:16321041,
CC       ECO:0000269|PubMed:17416898, ECO:0000269|PubMed:18375812,
CC       ECO:0000269|PubMed:20709785}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:17416898,
CC       ECO:0000269|PubMed:18375812}. Membrane {ECO:0000305}; Lipid-anchor,
CC       GPI-anchor {ECO:0000305}.
CC   -!- INDUCTION: Expressed in white cells. Transcription is regulated by the
CC       transcription factor EFG1 and up-regulated by alpha-pheromone, by host
CC       serum, in biofilms, and in high iron conditions. Repressed by BCR1 in
CC       a/a biofilms. {ECO:0000269|PubMed:14665461,
CC       ECO:0000269|PubMed:15387822, ECO:0000269|PubMed:17416898,
CC       ECO:0000269|PubMed:19798425, ECO:0000269|PubMed:21566087,
CC       ECO:0000269|PubMed:23563485, ECO:0000269|PubMed:23704884,
CC       ECO:0000269|PubMed:23948468}.
CC   -!- DOMAIN: The N-terminal domain mediates haploid invasive growth and
CC       yeast cell-cell adhesion. {ECO:0000269|PubMed:18375812}.
CC   -!- DOMAIN: The regions containing tandem repeats are required to project
CC       the N-terminal region into the extracellular environment and to mediate
CC       adhesion to polystyrene and to host cells. In allele CaO19.8979, the N-
CC       terminal tandem repeat region is expended and contains up to 90 repeats
CC       and the C-terminal tandem repeat region has one more repeat.
CC       {ECO:0000269|PubMed:18375812}.
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   -!- SIMILARITY: Belongs to the PGA18 family. {ECO:0000305}.
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DR   EMBL; CP017624; AOW27933.1; -; Genomic_DNA.
DR   RefSeq; XP_714572.2; XM_709479.2.
DR   AlphaFoldDB; G1UBC2; -.
DR   BioGRID; 1226778; 11.
DR   GeneID; 3643814; -.
DR   KEGG; cal:CAALFM_C209530WA; -.
DR   CGD; CAL0000175727; EAP1.
DR   VEuPathDB; FungiDB:C2_09530W_A; -.
DR   HOGENOM; CLU_280330_0_0_1; -.
DR   OrthoDB; 1844974at2759; -.
DR   PHI-base; PHI:517; -.
DR   PRO; PR:G1UBC2; -.
DR   Proteomes; UP000000559; Chromosome 2.
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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   InterPro; IPR025928; Flocculin_t3_rpt.
DR   Pfam; PF13928; Flocculin_t3; 2.
PE   1: Evidence at protein level;
KW   Cell adhesion; Cell wall; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW   Reference proteome; Repeat; Secreted; Signal; Virulence.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..632
FT                   /note="Cell wall adhesin EAP1"
FT                   /id="PRO_0000424809"
FT   PROPEP          633..653
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000424810"
FT   REPEAT          147..152
FT                   /note="1-1"
FT   REPEAT          153..158
FT                   /note="1-2"
FT   REPEAT          159..164
FT                   /note="1-3"
FT   REPEAT          165..170
FT                   /note="1-4"
FT   REPEAT          171..176
FT                   /note="1-5"
FT   REPEAT          177..182
FT                   /note="1-6"
FT   REPEAT          192..197
FT                   /note="1-7"
FT   REPEAT          198..203
FT                   /note="1-8"
FT   REPEAT          204..209
FT                   /note="1-9"
FT   REPEAT          210..215
FT                   /note="1-10"
FT   REPEAT          216..221
FT                   /note="1-11"
FT   REPEAT          222..227
FT                   /note="1-12"
FT   REPEAT          228..233
FT                   /note="1-13"
FT   REPEAT          234..248
FT                   /note="1-14"
FT   REPEAT          249..254
FT                   /note="1-15"
FT   REPEAT          326..345
FT                   /note="2-1"
FT   REPEAT          346..365
FT                   /note="2-2"
FT   REPEAT          366..389
FT                   /note="2-3"
FT   REPEAT          390..413
FT                   /note="2-4"
FT   REPEAT          414..433
FT                   /note="2-5"
FT   REPEAT          434..457
FT                   /note="2-6"
FT   REPEAT          458..477
FT                   /note="2-7"
FT   REPEAT          478..501
FT                   /note="2-8"
FT   REPEAT          502..521
FT                   /note="2-9"
FT   REPEAT          522..541
FT                   /note="2-10"
FT   REGION          19..146
FT                   /note="N-terminal cell-cell adhesion domain"
FT   REGION          144..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          147..254
FT                   /note="15 X 6 AA tandem repeats, Ser/Thr-rich"
FT   REGION          324..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          326..541
FT                   /note="10 X 20 AA approximate tandem repeats"
FT   REGION          572..595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        324..343
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..411
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        514..540
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..595
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           632
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        323
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   653 AA;  65265 MW;  62847FE0F3135DC1 CRC64;
     MKVSQILPLA GAISVASGFW IPDFSNKQNS NSYPGQYKGK GGYQDDCGDD YKKGYKSKTY
     SKVKPITSTD CTTPIQPTGT TTGYTKDVVE STSYTTDTAY TTTVITVTKC DGGSCSHTAV
     TTGVTIITVT TNDVITEYTT YCPLTSTPAT ESTPATESTP ATESTPATES TPATESTPAT
     ESTPCTTSTE TTPATESTPA TESTPATEST PATESTPATE STPATESTPA TESTPATEST
     PCTTSTETTP ATESTASTET ASSTPVESTV IVPSTTVITV SSCYEDKCSV SSVTTGVVTI
     SSEETIYTTY CPITSSITIP VPNTSTPAAP GTPVESQPVI PGTETTPAAP GTPVESQPVI
     PGTETTPAAP GTPVESQPAT TPVAPGTETT PAAPGTPVES QPATTPVAPG TETTPAAPGT
     PVESQPVIPG TETTPAAPGT PVESQPATTP VAPGTETTPA APGTPVESQP VIPGTETTPA
     APGTPVESQP ATTPVAPGTE TTPAAPGTPV ESQPVIPGTE TTPAAPGTPG TEATPVTTQP
     VSVLSTSQVV TASGEFSTVT AHSTSIVASC PEGGCVPEGQ QTETSPSVPT NGPEVEASSS
     VLSIPVSSVT TSTIASSSET SVPPAQVSTF EGSGSALKKP YYGLAVAALV YFM
 
 
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