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pH-regulated antigen PRA1 (58 kDa fibrinogen-binding mannoprotein)

 PRA1_CANAL              Reviewed;         299 AA.
P87020; A0A1D8PMQ8; P78598; Q5A0Y5; Q5A156;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
15-MAR-2017, sequence version 3.
22-NOV-2017, entry version 74.
RecName: Full=pH-regulated antigen PRA1;
AltName: Full=58 kDa fibrinogen-binding mannoprotein;
Flags: Precursor;
Name=PRA1; Synonyms=FBP1; OrderedLocusNames=CAALFM_C406980WA;
ORFNames=CaO19.10623, CaO19.3111;
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
Candida/Lodderomyces clade; Candida.
NCBI_TaxID=237561;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, FUNCTION, DISRUPTION
PHENOTYPE, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=9440517;
Sentandreu M., Elorza M.V., Sentandreu R., Fonzi W.A.;
"Cloning and characterization of PRA1, a gene encoding a novel pH-
regulated antigen of Candida albicans.";
J. Bacteriol. 180:282-289(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=15123810; DOI=10.1073/pnas.0401648101;
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
Davis R.W., Scherer S.;
"The diploid genome sequence of Candida albicans.";
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
[3]
GENOME REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
Chibana H., Nantel A., Magee P.T.;
"Assembly of the Candida albicans genome into sixteen supercontigs
aligned on the eight chromosomes.";
Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
"Assembly of a phased diploid Candida albicans genome facilitates
allele-specific measurements and provides a simple model for repeat
and indel structure.";
Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 8-299.
STRAIN=ATCC 26555;
PubMed=9435108; DOI=10.1111/j.1574-6968.1997.tb12784.x;
Lopez-Ribot J.L., Sepulveda P., Cervera A.M., Roig P., Gozalbo D.,
Martinez J.P.;
"Cloning of a cDNA fragment encoding part of the protein moiety of the
58-kDa fibrinogen-binding mannoprotein of Candida albicans.";
FEMS Microbiol. Lett. 157:273-278(1997).
[6]
IDENTIFICATION, SUBCELLULAR LOCATION, GLYCOSYLATION, AND
FIBRINOGEN-BINDING.
PubMed=1398933;
Casanova M., Lopez-Ribot J.L., Monteagudo C., Llombart-Bosch A.,
Sentandreu R., Martinez J.P.;
"Identification of a 58-kilodalton cell surface fibrinogen-binding
mannoprotein from Candida albicans.";
Infect. Immun. 60:4221-4229(1992).
[7]
SUBCELLULAR LOCATION.
PubMed=8300229;
Martinez J.P., Lopez-Ribot J.L., Chaffin W.L.;
"Heterogeneous surface distribution of the fibrinogen-binding protein
on Candida albicans.";
Infect. Immun. 62:709-712(1994).
[8]
SUBCELLULAR LOCATION.
PubMed=7768591;
Lopez-Ribot J.L., Martinez J.P., Chaffin W.L.;
"Comparative study of the C3d receptor and 58-kilodalton fibrinogen-
binding mannoproteins of Candida albicans.";
Infect. Immun. 63:2126-2132(1995).
[9]
SUBCELLULAR LOCATION.
PubMed=8759797; DOI=10.1111/j.1574-6968.1996.tb08417.x;
Lopez-Ribot J.L., Monteagudo C., Sepulveda P., Casanova M.,
Martinez J.P., Chaffin W.L.;
"Expression of the fibrinogen binding mannoprotein and the laminin
receptor of Candida albicans in vitro and in infected tissues.";
FEMS Microbiol. Lett. 142:117-122(1996).
[10]
INDUCTION.
PubMed=10629054; DOI=10.1128/MCB.20.3.971-978.2000;
Davis D.A., Wilson R.B., Mitchell A.P.;
"RIM101-dependent and -independent pathways govern pH responses in
Candida albicans.";
Mol. Cell. Biol. 20:971-978(2000).
[11]
IDENTIFICATION AS A DOMINANT ANTIGEN.
PubMed=11292706; DOI=10.1128/IAI.69.5.2909-2919.2001;
Viudes A., Perea S., Lopez-Ribot J.L.;
"Identification of continuous B-cell epitopes on the protein moiety of
the 58-kiloDalton cell wall mannoprotein of Candida albicans belonging
to a family of immunodominant fungal antigens.";
Infect. Immun. 69:2909-2919(2001).
[12]
INDUCTION.
PubMed=17042758; DOI=10.1111/j.1567-1364.2006.00130.x;
Sohn K., Senyurek I., Fertey J., Konigsdorfer A., Joffroy C.,
Hauser N., Zelt G., Brunner H., Rupp S.;
"An in vitro assay to study the transcriptional response during
adherence of Candida albicans to different human epithelia.";
FEMS Yeast Res. 6:1085-1093(2006).
[13]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=17905924; DOI=10.1128/EC.00285-07;
Hiller E., Heine S., Brunner H., Rupp S.;
"Candida albicans Sun41p, a putative glycosidase, is involved in
morphogenesis, cell wall biogenesis, and biofilm formation.";
Eukaryot. Cell 6:2056-2065(2007).
[14]
IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION,
IDENTIFICATION IN A COMPLEX WITH MP65 AND HYR1, AND INTERACTION WITH
HUMAN INTEGRIN ALPHA-M/BETA-2.
PubMed=17277107; DOI=10.4049/jimmunol.178.4.2038;
Soloviev D.A., Fonzi W.A., Sentandreu R., Pluskota E., Forsyth C.B.,
Yadav S., Plow E.F.;
"Identification of pH-regulated antigen 1 released from Candida
albicans as the major ligand for leukocyte integrin alphaMbeta2.";
J. Immunol. 178:2038-2046(2007).
[15]
SUBCELLULAR LOCATION, AND GLYCOSYLATION.
PubMed=19098294; DOI=10.1093/jac/dkn515;
Pierce C.G., Thomas D.P., Lopez-Ribot J.L.;
"Effect of tunicamycin on Candida albicans biofilm formation and
maintenance.";
J. Antimicrob. Chemother. 63:473-479(2009).
[16]
FUNCTION, AND INTERACTION WITH HUMAN CFH; CFHR1 AND PLG.
PubMed=19850343; DOI=10.1016/j.molimm.2009.07.017;
Luo S., Poltermann S., Kunert A., Rupp S., Zipfel P.F.;
"Immune evasion of the human pathogenic yeast Candida albicans: Pra1
is a Factor H, FHL-1 and plasminogen binding surface protein.";
Mol. Immunol. 47:541-550(2009).
[17]
FUNCTION.
PubMed=20504767; DOI=10.1074/jbc.M110.142703;
Agarwal V., Asmat T.M., Luo S., Jensch I., Zipfel P.F.,
Hammerschmidt S.;
"Complement regulator Factor H mediates a two-step uptake of
Streptococcus pneumoniae by human cells.";
J. Biol. Chem. 285:23486-23495(2010).
[18]
FUNCTION, AND INTERACTION WITH HUMAN COMPLEMENT C3.
PubMed=20644161; DOI=10.4049/jimmunol.1001011;
Luo S., Hartmann A., Dahse H.M., Skerka C., Zipfel P.F.;
"Secreted pH-regulated antigen 1 of Candida albicans blocks activation
and conversion of complement C3.";
J. Immunol. 185:2164-2173(2010).
[19]
FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH HUMAN INTEGRIN
ALPHA-M/BETA-2.
PubMed=21245270; DOI=10.1128/IAI.00650-10;
Soloviev D.A., Jawhara S., Fonzi W.A.;
"Regulation of innate immune response to Candida albicans infections
by alphaMbeta2-Pra1p interaction.";
Infect. Immun. 79:1546-1558(2011).
[20]
FUNCTION, AND INTERACTION WITH HUMAN C4BPA.
PubMed=21212281; DOI=10.1074/jbc.M110.130138;
Luo S., Blom A.M., Rupp S., Hipler U.C., Hube B., Skerka C.,
Zipfel P.F.;
"The pH-regulated antigen 1 of Candida albicans binds the human
complement inhibitor C4b-binding protein and mediates fungal
complement evasion.";
J. Biol. Chem. 286:8021-8029(2011).
[21]
FUNCTION.
PubMed=21820180; DOI=10.1016/j.molimm.2011.07.007;
Losse J., Svobodova E., Heyken A., Hube B., Zipfel P.F., Jozsi M.;
"Role of pH-regulated antigen 1 of Candida albicans in the fungal
recognition and antifungal response of human neutrophils.";
Mol. Immunol. 48:2135-2143(2011).
[22]
IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
FUNCTION.
PubMed=22074954; DOI=10.1016/j.peptides.2011.10.021;
Karkowska-Kuleta J., Kedracka-Krok S., Rapala-Kozik M., Kamysz W.,
Bielinska S., Karafova A., Kozik A.;
"Molecular determinants of the interaction between human high
molecular weight kininogen and Candida albicans cell wall:
Identification of kininogen-binding proteins on fungal cell wall and
mapping the cell wall-binding regions on kininogen molecule.";
Peptides 32:2488-2496(2011).
[23]
FUNCTION.
PubMed=22844116; DOI=10.4049/jimmunol.1200524;
Jawhara S., Pluskota E., Verbovetskiy D., Skomorovska-Prokvolit O.,
Plow E.F., Soloviev D.A.;
"Integrin alphaXbeta(2) is a leukocyte receptor for Candida albicans
and is essential for protection against fungal infections.";
J. Immunol. 189:2468-2477(2012).
[24]
FUNCTION.
PubMed=22761575; DOI=10.1371/journal.ppat.1002777;
Citiulo F., Jacobsen I.D., Miramon P., Schild L., Brunke S.,
Zipfel P., Brock M., Hube B., Wilson D.;
"Candida albicans scavenges host zinc via Pra1 during endothelial
invasion.";
PLoS Pathog. 8:E1002777-E1002777(2012).
-!- FUNCTION: Cell surface protein involved in the host-parasite
interaction during candidal infection. With MP65, represents a
major component of the biofilm matrix. Sequesters zinc from host
tissue and mediates leukocyte adhesion and migration. As a surface
protein, binds the two human complement regulators CFH and CFHR1,
as well as plasminogen PLG, mediates complement evasion and extra-
cellular matrix interaction and/or degradation. As a released
protein, enhances complement control in direct vicinity of the
yeast and thus generates an additional protective layer which
controls host complement attack, assisting the fungus in escaping
host surveillance. Binds to host fluid-phase C3 and blocks
cleavage of C3 to C3a and C3b, leading to inhibition of complement
activation. Mediates also human complement control and complement
evasion through binding to C4BPA, another human complement
inhibitor, as well as through binding to host integrin alpha-
M/beta-2. Decreases complement-mediated adhesion, as well as
uptake of C.albicans by human macrophages.
{ECO:0000269|PubMed:19850343, ECO:0000269|PubMed:20504767,
ECO:0000269|PubMed:20644161, ECO:0000269|PubMed:21212281,
ECO:0000269|PubMed:21245270, ECO:0000269|PubMed:21820180,
ECO:0000269|PubMed:22074954, ECO:0000269|PubMed:22761575,
ECO:0000269|PubMed:22844116, ECO:0000269|PubMed:9440517}.
-!- SUBUNIT: Component of a multiprotein complex of 250 kDa composed
of at least HYR1, MP65, and PRA1. Interacts with host Integrin
alpha-M/beta-2 heterodimer. Binds also human factor H (CFH),
CFHR1, plasminogen (PLG), complement C3, and C4BPA.
{ECO:0000269|PubMed:17277107, ECO:0000269|PubMed:19850343,
ECO:0000269|PubMed:20644161, ECO:0000269|PubMed:21212281,
ECO:0000269|PubMed:21245270}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1398933,
ECO:0000269|PubMed:17277107, ECO:0000269|PubMed:17905924,
ECO:0000269|PubMed:19098294, ECO:0000269|PubMed:22074954,
ECO:0000269|PubMed:7768591, ECO:0000269|PubMed:8300229,
ECO:0000269|PubMed:8759797, ECO:0000269|PubMed:9440517}.
Note=Found primarily on the cell surface of filamentous forms and
enriched at hyphal tips.
-!- INDUCTION: Differentially expressed in response to changes in the
pH with aximal expression at neutral pH and no expression detected
below pH 6.0. Expression is controlled by RIM101. Expression is
also increased during adhesion onto human epithelia.
{ECO:0000269|PubMed:10629054, ECO:0000269|PubMed:17042758,
ECO:0000269|PubMed:9440517}.
-!- PTM: N- and O-glycosylated. The N- and 0-glycosidically linked
carbohydrates represent 18 to 20 percent and 3 to 4 percent,
respectively, of the molecular mass of PRA1. 0-linked sugar
residues may be involved in the interaction with fibrinogen.
Contributes highly to the carbohydrate component of the matrix.
Treatment with tunicamycin impairs glycosylation.
{ECO:0000269|PubMed:1398933, ECO:0000269|PubMed:19098294,
ECO:0000269|PubMed:9440517}.
-!- DISRUPTION PHENOTYPE: Impairs hypha formation. Protects the fungus
against leukocyte killing in vitro and in vivo, impedes the innate
immune response to the infection, and increases fungal virulence
and organ invasion in vivo. {ECO:0000269|PubMed:21245270,
ECO:0000269|PubMed:9440517}.
-!- SIMILARITY: Belongs to the ZPS1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U84261; AAC00525.1; -; Genomic_DNA.
EMBL; CP017626; AOW29419.1; -; Genomic_DNA.
EMBL; U83997; AAC49898.1; -; mRNA.
RefSeq; XP_715420.2; XM_710327.2.
ProteinModelPortal; P87020; -.
SMR; P87020; -.
TCDB; 2.A.5.1.15; the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.
PRIDE; P87020; -.
EnsemblFungi; AOW29419; AOW29419; CAALFM_C406980WA.
GeneID; 3642969; -.
KEGG; cal:CAALFM_C406980WA; -.
CGD; CAL0000174610; PRA1.
HOGENOM; HOG000190015; -.
InParanoid; P87020; -.
OrthoDB; EOG092C4NHF; -.
PRO; PR:P87020; -.
Proteomes; UP000000559; Chromosome 4.
GO; GO:0009986; C:cell surface; IDA:CGD.
GO; GO:0005576; C:extracellular region; IDA:CGD.
GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
GO; GO:0001411; C:hyphal tip; IDA:CGD.
GO; GO:0070051; F:fibrinogen binding; IDA:CGD.
GO; GO:0030985; F:high molecular weight kininogen binding; IDA:CGD.
GO; GO:0005178; F:integrin binding; IDA:CGD.
GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IDA:CGD.
GO; GO:0042784; P:active evasion of host immune response via regulation of host complement system; IPI:CGD.
GO; GO:0044406; P:adhesion of symbiont to host; IDA:CGD.
GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:CGD.
GO; GO:0052155; P:modulation by symbiont of host cell-mediated immune response; IDA:CGD.
GO; GO:0052085; P:negative regulation by symbiont of host T-cell mediated immune response; IDA:CGD.
GO; GO:0045916; P:negative regulation of complement activation; IDA:CGD.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0032119; P:sequestering of zinc ion; IMP:CGD.
CDD; cd11307; M35_Asp_f2_like; 1.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR029482; HRXXH.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
Pfam; PF13933; HRXXH; 1.
1: Evidence at protein level;
Complete proteome; Glycoprotein; Reference proteome; Secreted; Signal;
Virulence.
SIGNAL 1 15 {ECO:0000255}.
CHAIN 16 299 pH-regulated antigen PRA1.
/FTId=PRO_0000041750.
CARBOHYD 48 48 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 89 89 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 135 135 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 208 208 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 8 8 L -> F (in Ref. 5; AAC49898).
{ECO:0000305}.
CONFLICT 25 25 D -> N (in Ref. 1; AAC00525).
{ECO:0000305}.
CONFLICT 90 90 E -> D (in Ref. 1; AAC00525).
{ECO:0000305}.
CONFLICT 101 101 D -> E (in Ref. 1; AAC00525 and 5;
AAC49898). {ECO:0000305}.
CONFLICT 105 105 G -> D (in Ref. 5; AAC49898).
{ECO:0000305}.
CONFLICT 154 154 T -> S (in Ref. 1; AAC00525 and 5;
AAC49898). {ECO:0000305}.
CONFLICT 159 159 S -> G (in Ref. 1; AAC00525 and 5;
AAC49898). {ECO:0000305}.
SEQUENCE 299 AA; 33159 MW; 5DF3AC42FE495E73 CRC64;
MNYLLFCLFF AFSVAAPVTV TRFVDASPTG YDWRADWVKG FPIDSSCNAT QYNQLSTGLQ
EAQLLAEHAR DHTLRFGSKS PFFRKYFGNE TASAEVVGHF DNVVGADKSS ILFLCDDLDD
KCKNDGWAGY WRGSNHSDQT IICDLSFVTR RYLTQLCSSG YTVSKSKTNI FWAGDLLHRF
WHLKSIGQLV IEHYADTYEE VLELAQENST YAVRNSNSLI YYALDVYAYD VTIPGEGCNG
DGTSYKKSDF SSFEDSDSGS DSGASSTASS SHQHTDSNPS ATTDANSHCH THADGEVHC


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