AWP3B_CANGA
ID AWP3B_CANGA Reviewed; 1386 AA.
AC B4UN32;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 2.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Adhesin AWP3b {ECO:0000303|PubMed:34962966};
DE Flags: Precursor;
GN Name=AWP3b {ECO:0000303|PubMed:34962966};
GN OrderedLocusNames=CAGL0J11891g {ECO:0000312|EMBL:CAR58048.1};
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] OF 179-1386.
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 70-92 AND 297-309, IDENTIFICATION BY MASS SPECTROMETRY,
RP 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:0007744|PDB:7O9O, ECO:0007744|PDB:7O9P}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 20-344, 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:0000269|PubMed:18806209}. Note=May be GPI-anchored.
CC {ECO:0000303|PubMed:18806209}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAR58048.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR380956; CAR58048.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_002999575.1; XM_002999529.1.
DR PDB; 7O9O; X-ray; 1.55 A; A=20-344.
DR PDB; 7O9P; X-ray; 1.99 A; A=21-338.
DR PDBsum; 7O9O; -.
DR PDBsum; 7O9P; -.
DR STRING; 5478.XP_002999575.1; -.
DR EnsemblFungi; CAR58048; CAR58048; CAGL0J11891g.
DR GeneID; 9488026; -.
DR KEGG; cgr:CAGL0J11891g; -.
DR HOGENOM; CLU_270009_0_0_1; -.
DR OMA; PGHTITG; -.
DR Proteomes; UP000002428; Chromosome J.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:UniProtKB.
DR GO; GO:0098631; F:cell adhesion mediator activity; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell wall; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1386
FT /note="Adhesin AWP3b"
FT /evidence="ECO:0000255"
FT /id="PRO_0000455716"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 651
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 709
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 834
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 898
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1008
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1017
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1096
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 115..145
FT /evidence="ECO:0000269|PubMed:34962966,
FT ECO:0007744|PDB:7O9O, ECO:0007744|PDB:7O9P"
FT DISULFID 144..178
FT /evidence="ECO:0000269|PubMed:34962966,
FT ECO:0007744|PDB:7O9O, ECO:0007744|PDB:7O9P"
FT DISULFID 304..341
FT /evidence="ECO:0000269|PubMed:34962966,
FT ECO:0007744|PDB:7O9O"
SQ SEQUENCE 1386 AA; 143685 MW; 273900CA207B4A4F CRC64;
MISFVTLLAI LGLLSISWAD QTVRSVAGDQ RVTDPVIVGD NSILDYYGGS NYDFSNNFEI
GRGTLYIGKE SYFSSFQSAP TDVPNSFHLL IKNTNNLQNN GQFIIENIKR HANQCSNSSI
QVFPINFQND GEFEIISGGV EGRCCLPTSV IAPQNFLNNG KFYYKVLTDT GSIYSGSCMQ
NVDIGASTTT TVNNNLWEFT GSINAQINGA VSGAAQINLD GSNMFVNANT FSGQVVNLIN
GGSFLQTSDP LSNIVVINGL GTSDTGVTSI AVKGKGKSFT YNPSSGIVKL TTVEGKTYAY
QIGCGYNTKK FITNNDSGAS YESADNFFVL TYSEPYSPQT CQLENSSIFS SNFISTSTSS
SSSSSSASSL PSSMSSSLPS SLSSSLSSSL SSSMSSSMSS LFIIPPPYTT TRSSGSSIID
TEIVSFYSTT DSPGHTITGT TTTTLYGPHT HSSVSTPSSS SESSTTSNSS IESSSLPHTS
VSSTPESSIT PSSNTISSSP TSDFSSVQSS SIMESSSVVA SSSVINSSSI VDSSSSSASS
LPSSMSSSLS SSMSSSLPSS MSSSLSSSLS SSLSSSMSSS MSSLFIIPPP YTTTRSSGSS
IIDTEIVSFY STTDSPGHTI TGTTTTTLYG PHTHSSVSTP SSSSESSTTS NSSIESSSLP
HTSVSSTPES SITPSSNTIS SSPTSDFSSV QSSSIMESSS VVASSSVINS SSIVDSSSSS
ASSLPSSMPS SLPSSMSSSL SSSMSSSLSS SLSSSLSSSM SSSMSSLFII PPPYTTTRSS
GSSIIDTEIV SFYSTTDSPG HTITGTTTTT LYGPHTHSSV STPSSSSESS TTSNSSIESS
SLPHTSVSST PESSITPSSN TISSSPTSDF SSVQSSSIME SSSVVASSSA TQSSSVINSS
SIVDSSSSSA SSLPSSMPSS LPSSLSSSLS SSLSSSMSSS MSSLFIIPPP YTTTRSSGSS
IIDTEIVSFY STTDSPGHTI TGTTTTTLYE SSIYSSSSST IQESELSNTS RTTMTSNSSV
SISSTSSRSS FSNTKSSTIV ISQSASLPDS KTDIILSTSS NIGYSSRSLL SDLGTSISDS
DIHHSVLHST ESYSSNESGT NPFTSIASLS NFIPESSSHT STALGSENSV ISSDILTTMS
HPVATNSGDK PTTPKRSEQV STTMTSSGPT PDTSSFDTDG MSAYSRPEFT TNSLEVNKSS
TSQLGNNKQT FSNLQLESTR PHSENEVDNN TRLLQSIQQS STYGTNNVNP LSPTGSISIP
LTEDGQGDNN NWNSPATNDL CTQISFNLTA TTITVTDRIT ITDSIHDISS EVITSYIYQT
IVDQKTVTQT VDGKSLANKM SSIPKPSSRS LIQPQPPVAI ELQEGAASTS RVSLVSLFIS
IILVLL