AWP2_CANGA
ID AWP2_CANGA Reviewed; 832 AA.
AC Q6FNG1;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Adhesin AWP2 {ECO:0000303|PubMed:34962966};
DE Flags: Precursor;
GN Name=AWP2 {ECO:0000303|PubMed:18806209};
GN OrderedLocusNames=CAGL0K00110g {ECO:0000312|CGD:CAL0134003};
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593 {ECO:0000312|Proteomes:UP000002428};
RN [1] {ECO:0000312|Proteomes:UP000002428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 71-84; 160-168; 259-280 AND 302-314, IDENTIFICATION BY
RP MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=18806209; DOI=10.1128/ec.00284-08;
RA de Groot P.W., Kraneveld E.A., Yin Q.Y., Dekker H.L., Gross U.,
RA Crielaard W., de Koster C.G., Bader O., Klis F.M., Weig M.;
RT "The cell wall of the human pathogen Candida glabrata: differential
RT incorporation of novel adhesin-like wall proteins.";
RL Eukaryot. Cell 7:1951-1964(2008).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 71-123 AND 160-168, IDENTIFICATION BY MASS
RP SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=21769633; DOI=10.1007/s11046-011-9446-2;
RA Kraneveld E.A., de Soet J.J., Deng D.M., Dekker H.L., de Koster C.G.,
RA Klis F.M., Crielaard W., de Groot P.W.;
RT "Identification and differential gene expression of adhesin-like wall
RT proteins in Candida glabrata biofilms.";
RL Mycopathologia 172:415-427(2011).
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 74-84; 100-112; 114-123; 160-168 AND 302-314,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=26546455; DOI=10.1093/femsyr/fov098;
RA Gomez-Molero E., de Boer A.D., Dekker H.L., Moreno-Martinez A.,
RA Kraneveld E.A., Ichsan I., Chauhan N., Weig M., de Soet J.J.,
RA de Koster C.G., Bader O., de Groot P.W.;
RT "Proteomic analysis of hyperadhesive Candida glabrata clinical isolates
RT reveals a core wall proteome and differential incorporation of adhesins.";
RL FEMS Yeast Res. 15:0-0(2015).
RN [5] {ECO:0000305}
RP INDUCTION.
RX PubMed=25406296; DOI=10.1093/jac/dku447;
RA Kucharikova S., Neirinck B., Sharma N., Vleugels J., Lagrou K.,
RA Van Dijck P.;
RT "In vivo Candida glabrata biofilm development on foreign bodies in a rat
RT subcutaneous model.";
RL J. Antimicrob. Chemother. 70:846-856(2015).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=34962966; DOI=10.1371/journal.ppat.1009980;
RA Reithofer V., Fernandez-Pereira J., Alvarado M., de Groot P., Essen L.O.;
RT "A novel class of Candida glabrata cell wall proteins with beta-helix fold
RT mediates adhesion in clinical isolates.";
RL PLoS Pathog. 17:e1009980-e1009980(2021).
CC -!- FUNCTION: Mediates cell-substrate adhesion and promotes biofilm
CC formation. {ECO:0000269|PubMed:34962966}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:18806209,
CC ECO:0000269|PubMed:21769633, ECO:0000269|PubMed:26546455}. Note=May be
CC GPI-anchored. {ECO:0000303|PubMed:18806209,
CC ECO:0000303|PubMed:21769633, ECO:0000303|PubMed:26546455}.
CC -!- INDUCTION: Induced during biofilm formation on catheters inside the
CC host (PubMed:25406296). May be repressed during biofilm formation ex
CC vivo (PubMed:21769633). {ECO:0000269|PubMed:21769633,
CC ECO:0000269|PubMed:25406296}.
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DR EMBL; CR380957; CAG61192.1; -; Genomic_DNA.
DR RefSeq; XP_448233.1; XM_448233.1.
DR STRING; 5478.XP_448233.1; -.
DR EnsemblFungi; CAG61192; CAG61192; CAGL0K00110g.
DR GeneID; 2889957; -.
DR KEGG; cgr:CAGL0K00110g; -.
DR CGD; CAL0134003; AWP2.
DR VEuPathDB; FungiDB:CAGL0K00110g; -.
DR eggNOG; KOG1216; Eukaryota.
DR HOGENOM; CLU_340973_0_0_1; -.
DR InParanoid; Q6FNG1; -.
DR OMA; NIWINTG; -.
DR Proteomes; UP000002428; Chromosome K.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:UniProtKB.
DR GO; GO:0098631; F:cell adhesion mediator activity; IMP:UniProtKB.
DR GO; GO:0043708; P:cell adhesion involved in biofilm formation; IMP:UniProtKB.
DR InterPro; IPR021031; Hyphal-reg_cell_wall_N.
DR Pfam; PF11765; Hyphal_reg_CWP; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell wall; Direct protein sequencing; Glycoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..832
FT /note="Adhesin AWP2"
FT /evidence="ECO:0000255"
FT /id="PRO_5004273371"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 579
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 695
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 721
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 832 AA; 89380 MW; E9850F5B3EB0F04A CRC64;
MRKLPLFMAW KFWLICLYII KVASTQIVIK SNTIVGGNNP SGFQNGYIVS GDAFLAFQDM
NTVPMYQTVR IDKGGALYYI NNDKQGFSIL SDHNYNHPFV FLNEGTVVVD DRRSISPGSW
TIKDGSFTNN GNIMFTSSQG DIFSIGSNYI TNTGFIFSKG TSFEKPQRLQ IGNGNIWINT
GTVCMANTTY ILENAIQGGG CISVGENSVF NIYSFDMQQQ TVYLSHPSSV LILNGGHEVP
VYGLGNGNGI LYPDAPIRDI YYDSSTGIMD VTAGTNGIYK FTVYIGAGYN ESNFEIVSSI
KIHGISYDNY NFVRYRGPPP NLAPSVCQPC VEIPLYSFQV PDPYTTTNEL GFSETVSFYS
TYNENDIPVI GNTTIYVPPA IYTLTKVNEN TTETDIISRV TGMGYNGLPF TYYTTITVGE
METGVVTKTI TITENKSRST KTTLMSRNYT FSFSNYSPIS SSGTYSVSTV DNITTLTDTV
ANVSSSGPNS IVTATMTTYQ NNHEFNNASV INVTNSSNIM VPITSTFYSS VDSNLTTPIT
SLTRTSQSQI VSHITKLASS INETTIANTF PSPAASGTNY TTVVTNAEGS VQTDIVSHIT
TTDSDGKPTT IVSHITTTDS DGKPTTIVTT FPAPAASGAD YTTVVTNADG SVETDIVSHI
TTKDSIGKPT TVVTTVPYTL CASNADYTTV VTKSNVSVET EVVSHITTTA PCSDLESHVE
NQTTSPSMHT TSLVGSENGV SAKTVNDKPN PTIFTEVAVS EGTTSNAGYV TDQGSSLEMF
APTGASAVES GNKVSQTQTA SIFHGAGSTF KIKFNTILLS TSLTILILLG MA
