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Cell surface Cu-only superoxide dismutase 5 (EC 1.15.1.1) (Predicted GPI-anchored protein 3)

 SOD5_CANAL              Reviewed;         228 AA.
Q5AD07; A0A1D8PG56;
11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 1.
20-DEC-2017, entry version 100.
RecName: Full=Cell surface Cu-only superoxide dismutase 5;
EC=1.15.1.1;
AltName: Full=Predicted GPI-anchored protein 3;
Flags: Precursor;
Name=SOD5; Synonyms=PGA3, SOD31; OrderedLocusNames=CAALFM_C200680CA;
ORFNames=CaO19.2060, CaO19.9607;
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]
PREDICTION OF GPI-ANCHOR.
PubMed=12845604; DOI=10.1002/yea.1007;
De Groot P.W., Hellingwerf K.J., Klis F.M.;
"Genome-wide identification of fungal GPI proteins.";
Yeast 20:781-796(2003).
[5]
FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
PubMed=14617819; DOI=10.1091/mbc.E03-03-0179;
Martchenko M., Alarco A.M., Harcus D., Whiteway M.;
"Superoxide dismutases in Candida albicans: transcriptional regulation
and functional characterization of the hyphal-induced SOD5 gene.";
Mol. Biol. Cell 15:456-467(2004).
[6]
INDUCTION.
PubMed=15814840; DOI=10.1091/mbc.E05-01-0073;
Kadosh D., Johnson A.D.;
"Induction of the Candida albicans filamentous growth program by
relief of transcriptional repression: a genome-wide analysis.";
Mol. Biol. Cell 16:2903-2912(2005).
[7]
INDUCTION.
PubMed=15813733; DOI=10.1111/j.1365-2958.2005.04557.x;
Fradin C., De Groot P., MacCallum D., Schaller M., Klis F., Odds F.C.,
Hube B.;
"Granulocytes govern the transcriptional response, morphology and
proliferation of Candida albicans in human blood.";
Mol. Microbiol. 56:397-415(2005).
[8]
FUNCTION.
PubMed=19019164; DOI=10.1111/j.1365-2958.2008.06528.x;
Frohner I.E., Bourgeois C., Yatsyk K., Majer O., Kuchler K.;
"Candida albicans cell surface superoxide dismutases degrade host-
derived reactive oxygen species to escape innate immune
surveillance.";
Mol. Microbiol. 71:240-252(2009).
[9]
FUNCTION.
PubMed=21746956; DOI=10.1128/AAC.00280-11;
Bink A., Vandenbosch D., Coenye T., Nelis H., Cammue B.P.,
Thevissen K.;
"Superoxide dismutases are involved in Candida albicans biofilm
persistence against miconazole.";
Antimicrob. Agents Chemother. 55:4033-4037(2011).
[10]
INDUCTION.
PubMed=23123467; DOI=10.1248/bpb.b12-00338;
Miao H., Zhao L., Li C., Shang Q., Lu H., Fu Z., Wang L., Jiang Y.,
Cao Y.;
"Inhibitory effect of Shikonin on Candida albicans growth.";
Biol. Pharm. Bull. 35:1956-1963(2012).
[11]
INDUCTION.
PubMed=23285201; DOI=10.1371/journal.pone.0052850;
Miramon P., Dunker C., Windecker H., Bohovych I.M., Brown A.J.,
Kurzai O., Hube B.;
"Cellular responses of Candida albicans to phagocytosis and the
extracellular activities of neutrophils are critical to counteract
carbohydrate starvation, oxidative and nitrosative stress.";
PLoS ONE 7:E52850-E52850(2012).
[12]
INDUCTION.
PubMed=23125349; DOI=10.1128/EC.00236-12;
Pierce J.V., Dignard D., Whiteway M., Kumamoto C.A.;
"Normal adaptation of Candida albicans to the murine gastrointestinal
tract requires Efg1p-dependent regulation of metabolic and host
defense genes.";
Eukaryot. Cell 12:37-49(2013).
[13]
IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
PubMed=23948566; DOI=10.1016/j.jprot.2013.07.031;
Aoki W., Tatsukami Y., Kitahara N., Matsui K., Morisaka H., Kuroda K.,
Ueda M.;
"Elucidation of potentially virulent factors of Candida albicans
during serum adaptation by using quantitative time-course
proteomics.";
J. Proteomics 91:417-429(2013).
[14]
IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
INDUCTION.
PubMed=23136884; DOI=10.1111/mmi.12087;
Rohm M., Lindemann E., Hiller E., Ermert D., Lemuth K., Trkulja D.,
Sogukpinar O., Brunner H., Rupp S., Urban C.F., Sohn K.;
"A family of secreted pathogenesis-related proteins in Candida
albicans.";
Mol. Microbiol. 87:132-151(2013).
[15]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 27-181, COFACTOR, DISULFIDE
BOND, SUBUNIT, CATALYTIC ACTIVITY, ENZYME REGULATION, AND FUNCTION.
PubMed=24711423; DOI=10.1073/pnas.1400137111;
Gleason J.E., Galaleldeen A., Peterson R.L., Taylor A.B.,
Holloway S.P., Waninger-Saroni J., Cormack B.P., Cabelli D.E.,
Hart P.J., Culotta V.C.;
"Candida albicans SOD5 represents the prototype of an unprecedented
class of Cu-only superoxide dismutases required for pathogen
defense.";
Proc. Natl. Acad. Sci. U.S.A. 111:5866-5871(2014).
-!- FUNCTION: Superoxide dismutases serve to convert damaging
superoxide radicals, a key form of ROS, to less damaging hydrogen
peroxide that can be converted into water by catalase action.
Degrades host-derived reactive oxygen species to escape innate
immune surveillance. Involved in the occurrence of miconazole-
tolerant persisters in biofilms. Persisters are cells that survive
high doses of an antimicrobial agent. The unusual attributes of
SOD5-like fungal proteins, including the absence of zinc and an
open active site that readily captures extracellular copper, make
these SODs well suited to meet challenges in zinc and copper
availability at the host-pathogen interface.
{ECO:0000269|PubMed:14617819, ECO:0000269|PubMed:19019164,
ECO:0000269|PubMed:21746956, ECO:0000269|PubMed:24711423}.
-!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
{ECO:0000269|PubMed:24711423}.
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378;
Evidence={ECO:0000269|PubMed:24711423};
Note=Binds 1 copper ion per subunit.
{ECO:0000269|PubMed:24711423};
-!- ENZYME REGULATION: Secreted in a disulfide-oxidized form and apo-
pools of secreted SOD5 can readily capture extracellular copper
for rapid induction of enzyme activity.
{ECO:0000269|PubMed:24711423}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:24711423}.
-!- SUBCELLULAR LOCATION: Secreted, cell wall
{ECO:0000269|PubMed:23136884}. Membrane {ECO:0000250}; Lipid-
anchor, GPI-anchor {ECO:0000250}. Note=Covalently-linked GPI-
modified cell wall protein (GPI-CWP). {ECO:0000250}.
-!- INDUCTION: Induced during yeast-to-hyphal transition and by
osmotic and oxidative stresses. Expression is also increased when
cells were grown on nonfermentable substrates as the only carbon
source, in serum, and in the presence of neutrophils. Down-
regulated by shikonin. Expression is controlled by EFG1, NRG1 and
RIM101. {ECO:0000269|PubMed:14617819, ECO:0000269|PubMed:15813733,
ECO:0000269|PubMed:15814840, ECO:0000269|PubMed:23123467,
ECO:0000269|PubMed:23125349, ECO:0000269|PubMed:23136884,
ECO:0000269|PubMed:23285201, ECO:0000269|PubMed:23948566}.
-!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
reticulum and serves to target the protein to the cell surface.
There, the glucosamine-inositol phospholipid moiety is cleaved off
and the GPI-modified mannoprotein is covalently attached via its
lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer
cell wall layer (By similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Leads to sensitivity to hydrogen peroxide
when cells were grown in nutrient-limited conditions.
{ECO:0000269|PubMed:14617819}.
-!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
{ECO:0000305}.
-!- CAUTION: Although the beta-barrel of Cu/Zn SODs is largely
preserved, SOD5 is a monomeric copper protein that lacks a zinc-
binding site and is missing the electrostatic loop element
proposed to promote catalysis through superoxide guidance. Without
an electrostatic loop, the copper site of SOD5 is not recessed and
is readily accessible to bulk solvent (PubMed:24711423).
{ECO:0000305|PubMed:24711423}.
-----------------------------------------------------------------------
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EMBL; CP017624; AOW27120.1; -; Genomic_DNA.
RefSeq; XP_719507.1; XM_714414.1.
PDB; 4N3T; X-ray; 1.40 A; A=27-181.
PDB; 4N3U; X-ray; 1.75 A; A=27-181.
PDB; 5CU9; X-ray; 1.48 A; A=27-181.
PDB; 5KBK; X-ray; 1.41 A; A=27-181.
PDB; 5KBL; X-ray; 1.41 A; A=27-181.
PDB; 5KBM; X-ray; 1.42 A; A=27-181.
PDBsum; 4N3T; -.
PDBsum; 4N3U; -.
PDBsum; 5CU9; -.
PDBsum; 5KBK; -.
PDBsum; 5KBL; -.
PDBsum; 5KBM; -.
ProteinModelPortal; Q5AD07; -.
SMR; Q5AD07; -.
PRIDE; Q5AD07; -.
EnsemblFungi; AOW27120; AOW27120; CAALFM_C200680CA.
GeneID; 3638886; -.
KEGG; cal:CAALFM_C200680CA; -.
CGD; CAL0000188676; SOD5.
InParanoid; Q5AD07; -.
OrthoDB; EOG092C4T7P; -.
PRO; PR:Q5AD07; -.
Proteomes; UP000000559; Chromosome 2.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
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:0005507; F:copper ion binding; IDA:CGD.
GO; GO:0004784; F:superoxide dismutase activity; IDA:CGD.
GO; GO:0034599; P:cellular response to oxidative stress; IMP:CGD.
GO; GO:0071451; P:cellular response to superoxide; IMP:CGD.
GO; GO:0052059; P:evasion or tolerance by symbiont of host-produced reactive oxygen species; IMP:CGD.
GO; GO:0020012; P:evasion or tolerance of host immune response; IMP:CGD.
GO; GO:0009405; P:pathogenesis; IMP:CGD.
GO; GO:0006801; P:superoxide metabolic process; IDA:CGD.
Gene3D; 2.60.40.200; -; 1.
InterPro; IPR017868; Filamin/ABP280_repeat-like.
InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
InterPro; IPR001424; SOD_Cu_Zn_dom.
PANTHER; PTHR10003; PTHR10003; 1.
Pfam; PF00080; Sod_Cu; 1.
SUPFAM; SSF49329; SSF49329; 1.
1: Evidence at protein level;
3D-structure; Antioxidant; Cell wall; Complete proteome; Copper;
Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
Metal-binding; Oxidoreductase; Reference proteome; Secreted; Signal;
Virulence.
SIGNAL 1 15 {ECO:0000255}.
CHAIN 16 205 Cell surface Cu-only superoxide dismutase
5.
/FTId=PRO_0000424636.
PROPEP 206 228 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000424637.
COMPBIAS 180 189 Poly-Ser.
METAL 75 75 Copper; catalytic.
METAL 77 77 Copper; catalytic.
METAL 93 93 Copper; catalytic.
METAL 153 153 Copper; catalytic.
LIPID 205 205 GPI-anchor amidated asparagine.
{ECO:0000255}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 156 156 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 164 164 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 176 176 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 181 181 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 192 192 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 87 162 {ECO:0000269|PubMed:24711423}.
STRAND 30 34 {ECO:0000244|PDB:4N3T}.
STRAND 43 51 {ECO:0000244|PDB:4N3T}.
TURN 52 54 {ECO:0000244|PDB:4N3T}.
STRAND 55 63 {ECO:0000244|PDB:4N3T}.
HELIX 67 69 {ECO:0000244|PDB:4N3T}.
STRAND 74 79 {ECO:0000244|PDB:4N3T}.
HELIX 87 90 {ECO:0000244|PDB:4N3T}.
STRAND 100 102 {ECO:0000244|PDB:5CU9}.
HELIX 106 108 {ECO:0000244|PDB:4N3T}.
HELIX 114 118 {ECO:0000244|PDB:4N3T}.
STRAND 123 136 {ECO:0000244|PDB:4N3T}.
STRAND 149 153 {ECO:0000244|PDB:4N3T}.
STRAND 159 168 {ECO:0000244|PDB:4N3T}.
SEQUENCE 228 AA; 23589 MW; 2724BF2E7B9FAC91 CRC64;
MKYLSIFLLA TFALAGDAPI STDSKGSPSL IAKFEKTSKS NIEGTIKFTP ANNGTVSVSV
DLKGLPSDIG PFPYHVHEKP VPASKNCSAT ENHFNPYNGT VRAATPAAHE VGDLAGKHGN
IMGESYKTEY DDSYISLNEK SRSYIGGLSI VIHANNGTRL NCANITLLDE GHGNANTTMS
NSSSSSSQSA VNTSSSMAST APQGNGAERA VVNGLLAAGV VGVIAALI


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