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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};
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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
 
 
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