PIR32_CANAL
ID PIR32_CANAL Reviewed; 422 AA.
AC Q59PW0; A0A1D8PE52;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Probable cell wall mannoprotein PIR32;
DE Flags: Precursor;
GN Name=PIR32; Synonyms=PIR3; OrderedLocusNames=CAALFM_C107620CA;
GN ORFNames=CaO19.10299, CaO19.2783;
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 INDUCTION.
RX PubMed=17164403; DOI=10.1074/mcp.m600210-mcp200;
RA Fernandez-Arenas E., Cabezon V., Bermejo C., Arroyo J., Nombela C.,
RA Diez-Orejas R., Gil C.;
RT "Integrated proteomics and genomics strategies bring new insight into
RT Candida albicans response upon macrophage interaction.";
RL Mol. Cell. Proteomics 6:460-478(2007).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22391823; DOI=10.1007/s11046-012-9533-z;
RA Bahnan W., Koussa J., Younes S., Abi Rizk M., Khalil B., El Sitt S.,
RA Hanna S., El-Sibai M., Khalaf R.A.;
RT "Deletion of the Candida albicans PIR32 results in increased virulence,
RT stress response, and upregulation of cell wall chitin deposition.";
RL Mycopathologia 174:107-119(2012).
CC -!- FUNCTION: Probable structural component of the cell wall involved in
CC cell wall integrity and virulence. {ECO:0000269|PubMed:22391823}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}.
CC -!- INDUCTION: Expression is induced by host macrophages.
CC {ECO:0000269|PubMed:17164403}.
CC -!- PTM: O-glycosylated. Extensively O-mannosylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Leads to increased chitin content in the cell
CC wall, hyperfilamentation, and resistance to sodium dodecyl sulfate,
CC hydrogen peroxide, and sodium chloride. Shows also an increased
CC virulence in a mouse model. {ECO:0000269|PubMed:22391823}.
CC -!- SIMILARITY: Belongs to the PIR protein family. {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; CP017623; AOW26409.1; -; Genomic_DNA.
DR RefSeq; XP_711725.2; XM_706633.2.
DR AlphaFoldDB; Q59PW0; -.
DR STRING; 237561.Q59PW0; -.
DR GeneID; 3646670; -.
DR KEGG; cal:CAALFM_C107620CA; -.
DR CGD; CAL0000195669; PIR32.
DR VEuPathDB; FungiDB:C1_07620C_A; -.
DR eggNOG; ENOG502QQD8; Eukaryota.
DR HOGENOM; CLU_689094_0_0_1; -.
DR InParanoid; Q59PW0; -.
DR OrthoDB; 1472005at2759; -.
DR PHI-base; PHI:2597; -.
DR PRO; PR:Q59PW0; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0005199; F:structural constituent of cell wall; IBA:GO_Central.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
PE 2: Evidence at transcript level;
KW Cell wall; Coiled coil; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..422
FT /note="Probable cell wall mannoprotein PIR32"
FT /id="PRO_0000428630"
FT REGION 116..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 179..214
FT /evidence="ECO:0000255"
FT COMPBIAS 118..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 422 AA; 48491 MW; 63AB5988856481DC CRC64;
MIHYLIFPIL LIFFQIIKSS GYYVPANGDD WTILKPPSCK NKLPGQYIDS LPFTFGIVVN
PYILNEDGDY EKPIVSKIKP SLTTTTFVTS IITTSTATAP GSKPTKTKDI IVQIHDGQVQ
KMKHKHDYSS GGGDDDDDDE DCFDEKNIDM AAKRDYQDMN TQEQANEDSG QVLAESDSHQ
QVVDQNQQIN EEEEETQEQQ MQEENNNTNE IEDNKVQEFE TIEEIYDDID NNESRPNNSK
KYHKKRPHNN YENKHGHKDY HEDHHHNHRY KDHENGHEED DHKWNKPKPM PEQEEQEQEQ
EQKPKHEKSE GYESEFVSPV YSVACYTNST LKMTLTDGIL RDSDDRIGCI VSGHQFQFDG
PTPQHGAIYA AGWSVTKQGQ LALGDSTKFY QCASGDFYNL YDEPIAFQCH PVTLDVVELI
EC
