PGA18_CANAL
ID PGA18_CANAL Reviewed; 753 AA.
AC Q5AEG7; A0A1D8PJK4;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Probable GPI-anchored adhesin-like protein PGA18;
DE AltName: Full=Predicted GPI-anchored protein 18;
DE Flags: Precursor;
GN Name=PGA18; OrderedLocusNames=CAALFM_C303050CA;
GN ORFNames=CaO19.301, CaO19.7933;
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 FUNCTION.
RX PubMed=21496229; DOI=10.1186/1471-2164-12-192;
RA Chaudhuri R., Ansari F.A., Raghunandanan M.V., Ramachandran S.;
RT "FungalRV: adhesin prediction and immunoinformatics portal for human fungal
RT pathogens.";
RL BMC Genomics 12:192-192(2011).
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 (By similarity). {ECO:0000250, ECO:0000269|PubMed:21496229}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}. Membrane
CC {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
CC -!- INDUCTION: Expression in regulated by NRG1 and TUP1.
CC {ECO:0000269|PubMed:15814841}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PGA18 family. {ECO:0000305}.
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DR EMBL; CP017625; AOW28336.1; -; Genomic_DNA.
DR RefSeq; XP_719997.2; XM_714904.2.
DR AlphaFoldDB; Q5AEG7; -.
DR GeneID; 3638394; -.
DR KEGG; cal:CAALFM_C303050CA; -.
DR CGD; CAL0000183589; PGA18.
DR VEuPathDB; FungiDB:C3_03050C_A; -.
DR HOGENOM; CLU_356374_0_0_1; -.
DR InParanoid; Q5AEG7; -.
DR OrthoDB; 1624648at2759; -.
DR PRO; PR:Q5AEG7; -.
DR Proteomes; UP000000559; Chromosome 3.
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; 3.
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..730
FT /note="Probable GPI-anchored adhesin-like protein PGA18"
FT /id="PRO_0000424947"
FT PROPEP 731..753
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424948"
FT REPEAT 253..260
FT /note="1-1"
FT REPEAT 265..272
FT /note="1-2"
FT REPEAT 289..296
FT /note="1-3"
FT REPEAT 373..380
FT /note="1-4"
FT REPEAT 381..389
FT /note="2-1"
FT REPEAT 390..397
FT /note="1-5"
FT REPEAT 398..405
FT /note="1-6"
FT REPEAT 406..413
FT /note="1-7"
FT REPEAT 414..421
FT /note="1-8"
FT REPEAT 422..430
FT /note="2-2"
FT REPEAT 431..438
FT /note="1-9"
FT REPEAT 439..446
FT /note="1-10"
FT REPEAT 447..454
FT /note="1-11"
FT REPEAT 455..462
FT /note="1-12"
FT REPEAT 463..471
FT /note="2-3"
FT REPEAT 472..479
FT /note="1-13"
FT REPEAT 489..496
FT /note="1-14"
FT REPEAT 497..504
FT /note="1-15"
FT REPEAT 505..512
FT /note="1-16"
FT REPEAT 513..521
FT /note="2-4"
FT REPEAT 522..529
FT /note="1-17"
FT REPEAT 539..546
FT /note="1-18"
FT REPEAT 547..554
FT /note="1-19"
FT REPEAT 555..563
FT /note="2-5"
FT REGION 241..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 730
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 719
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 753 AA; 75178 MW; 611068807F778DCA CRC64;
MKLESIAVFA GIVSTALAGV YHKPPPATTY WTTIYAPSTS VVTVTSCSKG GCGTQSYATG
VTKTKTVHEG VTTEYTTYCP LTTSHEVVKS TCSDTLVVWS TRSFSWVWSF SKPDGCGQST
STIKTTAQTD VPTTATATPS VSTTCTTGTK TKWWWVIKTT DCSVYTVSST SSSLISTSQV
TSSSSIASTT ATAPATPSVS TTCTTGTKTK WWWVIKTTDC SVYTVSSTLS SLISTSKATS
SSSVASSTGS TPATTPGSSI ESTPATTPGS STESTPATAT GSSTKSTPAT TPGSSVTTGK
TSTDWITSFT THTAHTTTVI TVTDCDHHSC TSNVVTTGVT VVTVTTTGTV TEYTTYCPLT
STETIVTSKT TSATTPGSSS VESTPGSSSA TTPGSSSATT PGSSSATTPG SSSATTPGLS
SVESTPGSSS ATTPGSSSAT TPGSSSATTP GSSSATTPGT SSVESTPGSS SATTPGSSTI
ESTSGSSSAT TPGSSSATTP GSSSATTPGT SSVESTPGSS SATTPGSSTI ESTSGSSSAT
TPGSSSATTP GTSSVESTPG TSTGSCWVSV STGGYGYETT VTICSDVTSG QSVTTPTTIS
VPSTFCTTVP TAGTDETVIT SYVTSTAHST EVITVTSCAD NGCQTHTTHT GVVVVTVTTT
DVATTYTTYC PLTTTKAVYR VAKLANYKRD QTEFIATETN ENTSNWPAPT LVPYVGISND
SSAAVSTFEG AANSVVPRLG LIAGFLSALL FLF
