AWP1_CANGA
ID AWP1_CANGA Reviewed; 870 AA.
AC Q6FPN0;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Adhesin AWP1 {ECO:0000303|PubMed:34962966};
DE Flags: Precursor;
GN Name=AWP1 {ECO:0000312|CGD:CAL0133080};
GN OrderedLocusNames=CAGL0J02508g {ECO:0000312|CGD:CAL0133080};
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 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 [3] {ECO:0007744|PDB:7O9Q}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 18-324, AND DISULFIDE BOND.
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: May play a role in cell adhesion.
CC {ECO:0000250|UniProtKB:Q6FNG1}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000250|UniProtKB:Q6FNG1}. Note=May be GPI-anchored.
CC {ECO:0000250|UniProtKB:Q6FNG1}.
CC -!- INDUCTION: Induced during biofilm formation.
CC {ECO:0000269|PubMed:21769633}.
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DR EMBL; CR380956; CAG60763.1; -; Genomic_DNA.
DR RefSeq; XP_447814.1; XM_447814.1.
DR PDB; 7O9Q; X-ray; 1.85 A; A=18-324.
DR PDBsum; 7O9Q; -.
DR SMR; Q6FPN0; -.
DR STRING; 5478.XP_447814.1; -.
DR EnsemblFungi; CAG60763; CAG60763; CAGL0J02508g.
DR GeneID; 2889767; -.
DR KEGG; cgr:CAGL0J02508g; -.
DR CGD; CAL0133080; AWP1.
DR VEuPathDB; FungiDB:CAGL0J02508g; -.
DR eggNOG; KOG3544; Eukaryota.
DR HOGENOM; CLU_369178_0_0_1; -.
DR OMA; NANSGGW; -.
DR Proteomes; UP000002428; Chromosome J.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0098631; F:cell adhesion mediator activity; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR SUPFAM; SSF51161; SSF51161; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell wall; Disulfide bond; Glycoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..870
FT /note="Adhesin AWP1"
FT /evidence="ECO:0000255"
FT /id="PRO_5004274134"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 284..322
FT /evidence="ECO:0000269|PubMed:34962966,
FT ECO:0007744|PDB:7O9Q"
SQ SEQUENCE 870 AA; 84312 MW; 6BC9C0FC36C0EB4E CRC64;
MSLITIFAFF IKATLVLSLD ILTPTTLTGD QTFNEDVSVV SSLTLNDGSQ YLFNNLLQIA
PSSASVTANA LAAVSVFTFS LPPSSSLSNS GTLIISNSNT GPSTEQHIVI TPNVMANTGT
ITLSLAHTNT DSSSTLIIDP VTFYNTGTIN YESIGSETND PSLTGNILSI GSSGRTLQNL
GTINLNAANS YYLLGTITEN SGSINVQKGF LYVNALDFIG NTINLSTTTA LAFISPVSQV
VRVRGVFFGN IIASVGSSGT FSYNTQTGIL TVTTNGVYSY DIGCGYNPAL MSGQQETLSF
QGNLYDTFLV LVNQPIPSDL TCAAVSSSIT PSSSVEPSSS VEPSSSVEPS SSVEPSSSVE
PSSSVEPSSS VEPSSSVEPS SSVEPSSSVE PSSSVEPSSS VEPSSSVEPS SSVEPSSSVE
PSSSVEPSSS VEPSSSVEPS SSVEPSSSVE PSSPAVPSSS AEPSSSVVPP ITPIPSSSVV
SASVFDTSST LPSSPTVPTS SVSPSSPTVP TSSVSPSSPT VPTSSESPST LSTPSSSAAP
SSFCPTCVSS GTPPAPSSSA VVPTSSAGGG NGGDNGQPGA DGQPGAAGQP GAAGQPGAAG
QPGAAGQPGA AGQPGAAGQP GAAGQPGAAG QPGAAGQPGA AGQPGAGSGG GSEQPTPGAG
AGSGSADGNQ SGTSSGTGNG QAGSGQAGSG QVGSGQAGAG QAGSGQAGAG QAGSGQAGAG
QAGLDNTASG QSEGGQASAM DGDQSGRGGQ SNSGSLLQPN AQQGTGSGTG SDTGADQASG
ESPGQIGDAQ PGSGTDQSSG RHSLAAEART SQSHSLAADA RTRSTTRQTS VIAPGTAPGT
AVVTTFHGCG TVNHKGMINI LLALALLVLL
