PIR1_CANAL
ID PIR1_CANAL Reviewed; 385 AA.
AC Q59SF7; A0A1D8PIA7; Q59SC4;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Cell wall mannoprotein PIR1;
DE AltName: Full=Protein with internal repeats 1;
DE Flags: Precursor;
GN Name=PIR1; Synonyms=PIR2; OrderedLocusNames=CAALFM_C208870CA;
GN ORFNames=CaO19.220, CaO19.7851;
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 IDENTIFICATION, AND SUBCELLULAR LOCATION.
RX PubMed=10802178; DOI=10.1111/j.1574-6968.2000.tb09111.x;
RA Kandasamy R., Vediyappan G., Chaffin W.L.;
RT "Evidence for the presence of pir-like proteins in Candida albicans.";
RL FEMS Microbiol. Lett. 186:239-243(2000).
RN [5]
RP IDENTIFICATION, AND SUBCELLULAR LOCATION.
RX PubMed=10672182; DOI=10.1046/j.1365-2958.2000.01729.x;
RA Kapteyn J.C., Hoyer L.L., Hecht J.E., Muller W.H., Andel A., Verkleij A.J.,
RA Makarow M., Van Den Ende H., Klis F.M.;
RT "The cell wall architecture of Candida albicans wild-type cells and cell
RT wall-defective mutants.";
RL Mol. Microbiol. 35:601-611(2000).
RN [6]
RP INDUCTION.
RX PubMed=12492856; DOI=10.1046/j.1365-2958.2003.03300.x;
RA Sohn K., Urban C., Brunner H., Rupp S.;
RT "EFG1 is a major regulator of cell wall dynamics in Candida albicans as
RT revealed by DNA microarrays.";
RL Mol. Microbiol. 47:89-102(2003).
RN [7]
RP INDUCTION.
RX PubMed=15189998; DOI=10.1128/ec.3.3.776-784.2004;
RA Lotz H., Sohn K., Brunner H., Muhlschlegel F.A., Rupp S.;
RT "RBR1, a novel pH-regulated cell wall gene of Candida albicans, is
RT repressed by RIM101 and activated by NRG1.";
RL Eukaryot. Cell 3:776-784(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=15302828; DOI=10.1128/ec.3.4.955-965.2004;
RA de Groot P.W., de Boer A.D., Cunningham J., Dekker H.L., de Jong L.,
RA Hellingwerf K.J., de Koster C., Klis F.M.;
RT "Proteomic analysis of Candida albicans cell walls reveals covalently bound
RT carbohydrate-active enzymes and adhesins.";
RL Eukaryot. Cell 3:955-965(2004).
RN [9]
RP FUNCTION, GLYCOSYLATION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=15470096; DOI=10.1099/mic.0.27220-0;
RA Martinez A.I., Castillo L., Garcera A., Elorza M.V., Valentin E.,
RA Sentandreu R.;
RT "Role of Pir1 in the construction of the Candida albicans cell wall.";
RL Microbiology 150:3151-3161(2004).
RN [10]
RP INDUCTION.
RX PubMed=15387822; DOI=10.1111/j.1365-2958.2004.04214.x;
RA Lan C.Y., Rodarte G., Murillo L.A., Jones T., Davis R.W., Dungan J.,
RA Newport G., Agabian N.;
RT "Regulatory networks affected by iron availability in Candida albicans.";
RL Mol. Microbiol. 53:1451-1469(2004).
RN [11]
RP GLYCOSYLATION BY PMT1.
RX PubMed=15659169; DOI=10.1111/j.1365-2958.2004.04401.x;
RA Prill S.K., Klinkert B., Timpel C., Gale C.A., Schroppel K., Ernst J.F.;
RT "PMT family of Candida albicans: five protein mannosyltransferase isoforms
RT affect growth, morphogenesis and antifungal resistance.";
RL Mol. Microbiol. 55:546-560(2005).
RN [12]
RP INDUCTION.
RX PubMed=16998073; DOI=10.1128/ec.00155-06;
RA Mulhern S.M., Logue M.E., Butler G.;
RT "Candida albicans transcription factor Ace2 regulates metabolism and is
RT required for filamentation in hypoxic conditions.";
RL Eukaryot. Cell 5:2001-2013(2006).
RN [13]
RP INDUCTION.
RX PubMed=16339080; DOI=10.1091/mbc.e05-06-0501;
RA Enjalbert B., Smith D.A., Cornell M.J., Alam I., Nicholls S., Brown A.J.P.,
RA Quinn J.;
RT "Role of the Hog1 stress-activated protein kinase in the global
RT transcriptional response to stress in the fungal pathogen Candida
RT albicans.";
RL Mol. Biol. Cell 17:1018-1032(2006).
RN [14]
RP INDUCTION.
RX PubMed=19477921; DOI=10.1091/mbc.e09-03-0210;
RA Cote P., Hogues H., Whiteway M.;
RT "Transcriptional analysis of the Candida albicans cell cycle.";
RL Mol. Biol. Cell 20:3363-3373(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=18227255; DOI=10.1099/mic.0.2007/012617-0;
RA Sosinska G.J., de Groot P.W., Teixeira de Mattos M.J., Dekker H.L.,
RA de Koster C.G., Hellingwerf K.J., Klis F.M.;
RT "Hypoxic conditions and iron restriction affect the cell-wall proteome of
RT Candida albicans grown under vagina-simulative conditions.";
RL Microbiology 154:510-520(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=20641015; DOI=10.1002/yea.1775;
RA Sorgo A.G., Heilmann C.J., Dekker H.L., Brul S., de Koster C.G., Klis F.M.;
RT "Mass spectrometric analysis of the secretome of Candida albicans.";
RL Yeast 27:661-672(2010).
CC -!- FUNCTION: Component of the outer cell wall layer required for stability
CC of the cell wall and specifically for cell wall rigidity.
CC {ECO:0000269|PubMed:15470096}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:10672182,
CC ECO:0000269|PubMed:10802178, ECO:0000269|PubMed:15302828,
CC ECO:0000269|PubMed:15470096, ECO:0000269|PubMed:18227255,
CC ECO:0000269|PubMed:20641015}. Note=Covalently attached to the cell
CC wall.
CC -!- INDUCTION: Expression varies during the cell-cycle with a peak at the
CC beginning of G1. Expression increases in hypoxic and acidic conditions
CC and is down-regulated during the switch from yeast to hyphal growth and
CC under low-iron conditions. The promoter contains E-box consensus
CC sequences (CANNTG) suggesting that PIR1 is directly regulated by EFG1.
CC Expression is also regulated by ACE2, HOG1, and RIM101.
CC {ECO:0000269|PubMed:12492856, ECO:0000269|PubMed:15189998,
CC ECO:0000269|PubMed:15387822, ECO:0000269|PubMed:16339080,
CC ECO:0000269|PubMed:16998073, ECO:0000269|PubMed:18227255,
CC ECO:0000269|PubMed:19477921, ECO:0000269|PubMed:20641015}.
CC -!- DOMAIN: The PIR1/2/3 repeats are required for covalent linkage to the
CC cell wall. {ECO:0000250}.
CC -!- PTM: Covalently linked to beta-1,3-glucan of the inner cell wall layer
CC via an alkali-sensitive ester linkage between the gamma-carboxyl group
CC of glutamic acids, arising from specific glutamines within the PIR1/2/3
CC repeats, and hydroxyl groups of glucoses of beta-1,3-glucan chains.
CC {ECO:0000250}.
CC -!- PTM: Highly O-glycosylated by PMT1 and contains one N-mannosylated
CC chain. {ECO:0000269|PubMed:15470096, ECO:0000269|PubMed:15659169}.
CC -!- DISRUPTION PHENOTYPE: Increases sensitivity to calcofluor white and
CC Congo red. {ECO:0000269|PubMed:15470096}.
CC -!- SIMILARITY: Belongs to the PIR protein family. {ECO:0000305}.
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DR EMBL; CP017624; AOW27875.1; -; Genomic_DNA.
DR RefSeq; XP_712603.2; XM_707510.2.
DR AlphaFoldDB; Q59SF7; -.
DR STRING; 237561.Q59SF7; -.
DR GeneID; 3645801; -.
DR KEGG; cal:CAALFM_C208870CA; -.
DR CGD; CAL0000186859; PIR1.
DR VEuPathDB; FungiDB:C2_08870C_A; -.
DR HOGENOM; CLU_039662_0_0_1; -.
DR OrthoDB; 1472005at2759; -.
DR PRO; PR:Q59SF7; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; IDA:CGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0030445; C:yeast-form cell wall; IDA:CGD.
DR GO; GO:0005199; F:structural constituent of cell wall; IMP:CGD.
DR GO; GO:0071502; P:cellular response to temperature stimulus; IDA:CGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR InterPro; IPR000420; Yeast_PIR.
DR PROSITE; PS50256; PIR_REPEAT_2; 5.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation; Glycoprotein;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..385
FT /note="Cell wall mannoprotein PIR1"
FT /id="PRO_0000428629"
FT REPEAT 78..96
FT /note="PIR1/2/3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149"
FT REPEAT 97..115
FT /note="PIR1/2/3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149"
FT REPEAT 116..133
FT /note="PIR1/2/3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149"
FT REPEAT 136..153
FT /note="PIR1/2/3 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149"
FT REPEAT 154..171
FT /note="PIR1/2/3 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149"
FT REPEAT 173..190
FT /note="PIR1/2/3 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149"
FT REPEAT 191..208
FT /note="PIR1/2/3 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149"
FT REPEAT 210..228
FT /note="PIR1/2/3 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149"
FT REPEAT 233..251
FT /note="PIR1/2/3 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149"
FT REGION 257..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 88
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 107
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 125
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 146
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 163
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 183
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 200
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 220
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 243
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 385 AA; 40621 MW; 2A24722AFC101884 CRC64;
MKYSTLVSIA AFISTSLAAT VPDEHYSTLS PSAKIPSGAS TDFSGTFGIQ VVTVESASAL
STDTATSTLT RNDNKKEATP VAQITDGQVQ HQTTGGVSAI KQISDGQVQH QTNAAQPIAQ
ISDGQIQHQT TAKATATPVQ QINDGQIQHQ TTVQPVAQIS DGQIQHQTAK ATATPVQQIG
DGQIQHQTTV QPVAQISDGQ IQHQTVKASA TPVQQIGDGQ IQHQTTAAAA TTASAVKQIN
DGQIQHQTTT AENVAKAQSD GQAIATGSPS SNSTLSDDDD LSSTIPKACS SANNLEMTLH
DSVLKDTHER WGAIVANHQF QFDGPIPQAG TIYSAGWSIK DGYLYLGDSN IFYQCLSGDF
YNLYDENVAK QCSAVKLSVI EFVNC
