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Surface antigen protein 2

 CSA2_CANAL              Reviewed;         147 AA.
Q5A0X8; A0A1D8PMP6;
07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 1.
22-NOV-2017, entry version 62.
RecName: Full=Surface antigen protein 2 {ECO:0000305};
Flags: Precursor;
Name=CSA2; Synonyms=CRW1; OrderedLocusNames=CAALFM_C406920CA;
ORFNames=CaO19.10629, CaO19.3117;
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 [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).
[2]
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).
[3]
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).
[4]
INDUCTION.
PubMed=15554973; DOI=10.1111/j.1365-2958.2004.04350.x;
Bensen E.S., Martin S.J., Li M., Berman J., Davis D.A.;
"Transcriptional profiling in Candida albicans reveals new adaptive
responses to extracellular pH and functions for Rim101p.";
Mol. Microbiol. 54:1335-1351(2004).
[5]
INDUCTION.
PubMed=15917516; DOI=10.1128/AAC.49.6.2226-2236.2005;
Liu T.T., Lee R.E., Barker K.S., Lee R.E., Wei L., Homayouni R.,
Rogers P.D.;
"Genome-wide expression profiling of the response to azole, polyene,
echinocandin, and pyrimidine antifungal agents in Candida albicans.";
Antimicrob. Agents Chemother. 49:2226-2236(2005).
[6]
INDUCTION.
PubMed=16030247; DOI=10.1091/mbc.E05-05-0435;
Hromatka B.S., Noble S.M., Johnson A.D.;
"Transcriptional response of Candida albicans to nitric oxide and the
role of the YHB1 gene in nitrosative stress and virulence.";
Mol. Biol. Cell 16:4814-4826(2005).
[7]
INDUCTION.
PubMed=16102003; DOI=10.1111/j.1365-2958.2005.04771.x;
Urban C., Xiong X., Sohn K., Schroppel K., Brunner H., Rupp S.;
"The moonlighting protein Tsa1p is implicated in oxidative stress
response and in cell wall biogenesis in Candida albicans.";
Mol. Microbiol. 57:1318-1341(2005).
[8]
IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
INDUCTION.
PubMed=20641015; DOI=10.1002/yea.1775;
Sorgo A.G., Heilmann C.J., Dekker H.L., Brul S., de Koster C.G.,
Klis F.M.;
"Mass spectrometric analysis of the secretome of Candida albicans.";
Yeast 27:661-672(2010).
[9]
INDUCTION.
PubMed=21592964; DOI=10.1074/jbc.M111.233569;
Singh R.P., Prasad H.K., Sinha I., Agarwal N., Natarajan K.;
"Cap2-HAP complex is a critical transcriptional regulator that has
dual but contrasting roles in regulation of iron homeostasis in
Candida albicans.";
J. Biol. Chem. 286:25154-25170(2011).
[10]
INDUCTION.
PubMed=23563485; DOI=10.1128/EC.00071-13;
Srikantha T., Daniels K.J., Pujol C., Kim E., Soll D.R.;
"Identification of genes upregulated by the transcription factor Bcr1
that are involved in impermeability, impenetrability, and drug
resistance of Candida albicans a/alpha biofilms.";
Eukaryot. Cell 12:875-888(2013).
[11]
DISRUPTION PHENOTYPE, FUNCTION, AND HEME-BINDING.
PubMed=24796871; DOI=10.1111/1567-1364.12160;
Okamoto-Shibayama K., Kikuchi Y., Kokubu E., Sato Y., Ishihara K.;
"Csa2, a member of the Rbt5 protein family, is involved in the
utilization of iron from human hemoglobin during Candida albicans
hyphal growth.";
FEMS Yeast Res. 14:674-677(2014).
[12]
BIOTECHNOLOGY.
PubMed=25001939;
Liu L., Cai J., Liu C., Guo Y., Pan Y., Wang Y., Che X.;
"Establishment and evaluation of a double antibody sandwich ELISA to
detect Csa2 protein of Candida albicans.";
Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 30:732-735(2014).
-!- FUNCTION: Secreted heme-binding protein involved in the
utilization of iron from human hemoglobin during hyphal growth.
May also play a role in non-hemoglobin iron utilization. The
ability to acquire iron from host tissues is a major virulence
factor of pathogenic microorganisms.
{ECO:0000269|PubMed:24796871}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20641015}.
-!- INDUCTION: Expression is induced during hyphal growth, by
ketoconazole, and nitric oxide. Expression is also regulated by
RIM101, TSA1, HAP43 and BCR1. {ECO:0000269|PubMed:15554973,
ECO:0000269|PubMed:15917516, ECO:0000269|PubMed:16030247,
ECO:0000269|PubMed:16102003, ECO:0000269|PubMed:20641015,
ECO:0000269|PubMed:21592964, ECO:0000269|PubMed:23563485}.
-!- DOMAIN: The CFEM domain is involved in heme-binding. It contains 8
cysteines and is found in proteins from several pathogenic fungi,
including both human and plant pathogens.
{ECO:0000250|UniProtKB:Q59UT5}.
-!- DISRUPTION PHENOTYPE: Leads to defects in hemoglobin utilization
as sole source of carbon. {ECO:0000269|PubMed:24796871}.
-!- BIOTECHNOLOGY: CSA2 could be used as a new diagnostic marker of
Candida albicans infection. {ECO:0000269|PubMed:25001939}.
-!- SIMILARITY: Belongs to the RBT5 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CP017626; AOW29413.1; -; Genomic_DNA.
RefSeq; XP_715426.1; XM_710333.1.
PDB; 4Y7S; X-ray; 2.00 A; A/B/C=34-144.
PDBsum; 4Y7S; -.
SMR; Q5A0X8; -.
PRIDE; Q5A0X8; -.
EnsemblFungi; AOW29413; AOW29413; CAALFM_C406920CA.
GeneID; 3642930; -.
KEGG; cal:CAALFM_C406920CA; -.
CGD; CAL0000201350; CSA2.
HOGENOM; HOG000094008; -.
OrthoDB; EOG092C2UGH; -.
PRO; PR:Q5A0X8; -.
Proteomes; UP000000559; Chromosome 4.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0005576; C:extracellular region; IDA:CGD.
GO; GO:0020037; F:heme binding; IDA:CGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035351; P:heme transmembrane transport; IDA:CGD.
GO; GO:0033212; P:iron assimilation; IMP:CGD.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
InterPro; IPR008427; Extracellular_membr_CFEM_dom.
Pfam; PF05730; CFEM; 1.
SMART; SM00747; CFEM; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Heme; Iron; Metal-binding;
Reference proteome; Secreted; Signal; Virulence.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 147 Surface antigen protein 2.
/FTId=PRO_0000431444.
REGION 56 119 CFEM. {ECO:0000250|UniProtKB:Q59UT5}.
HELIX 35 38 {ECO:0000244|PDB:4Y7S}.
HELIX 52 55 {ECO:0000244|PDB:4Y7S}.
TURN 56 58 {ECO:0000244|PDB:4Y7S}.
HELIX 61 63 {ECO:0000244|PDB:4Y7S}.
HELIX 65 68 {ECO:0000244|PDB:4Y7S}.
STRAND 74 76 {ECO:0000244|PDB:4Y7S}.
HELIX 81 86 {ECO:0000244|PDB:4Y7S}.
HELIX 88 101 {ECO:0000244|PDB:4Y7S}.
HELIX 105 120 {ECO:0000244|PDB:4Y7S}.
HELIX 132 143 {ECO:0000244|PDB:4Y7S}.
SEQUENCE 147 AA; 15078 MW; 0E339D80F96CC52C CRC64;
MKFSTILAIP FAIAFANAAA APAVTAAPAP AADNPYTIYP PVPKTASING FADRIYDQIP
KCAQECVKQS TSSTPCPYWD TGCLCVIPNF TGAVGNCVAS KCRGADVTNF RKLAVGACAA
AGVWDPYWII PASVSSALDA AATATGN


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