SOD4_CANAL
ID SOD4_CANAL Reviewed; 232 AA.
AC Q5AD05; A0A1D8PG54;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Cell surface superoxide dismutase [Cu-Zn] 4;
DE EC=1.15.1.1;
DE AltName: Full=GPI-anchored protein 2;
DE Flags: Precursor;
GN Name=SOD4; Synonyms=PGA2, SOD32; OrderedLocusNames=CAALFM_C200660CA;
GN ORFNames=CaO19.2062, CaO19.9609;
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 PREDICTION OF GPI-ANCHOR.
RX PubMed=12845604; DOI=10.1002/yea.1007;
RA De Groot P.W., Hellingwerf K.J., Klis F.M.;
RT "Genome-wide identification of fungal GPI proteins.";
RL Yeast 20:781-796(2003).
RN [5]
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 [6]
RP IDENTIFICATION.
RX PubMed=14617819; DOI=10.1091/mbc.e03-03-0179;
RA Martchenko M., Alarco A.M., Harcus D., Whiteway M.;
RT "Superoxide dismutases in Candida albicans: transcriptional regulation and
RT functional characterization of the hyphal-induced SOD5 gene.";
RL Mol. Biol. Cell 15:456-467(2004).
RN [7]
RP INDUCTION.
RX PubMed=16215173; DOI=10.1128/ec.4.10.1654-1661.2005;
RA Westwater C., Balish E., Schofield D.A.;
RT "Candida albicans-conditioned medium protects yeast cells from oxidative
RT stress: a possible link between quorum sensing and oxidative stress
RT resistance.";
RL Eukaryot. Cell 4:1654-1661(2005).
RN [8]
RP INDUCTION.
RX PubMed=15790671; DOI=10.1093/jac/dki089;
RA Sigle H.C., Thewes S., Niewerth M., Korting H.C., Schafer-Korting M.,
RA Hube B.;
RT "Oxygen accessibility and iron levels are critical factors for the
RT antifungal action of ciclopirox against Candida albicans.";
RL J. Antimicrob. Chemother. 55:663-673(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
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 [10]
RP FUNCTION.
RX PubMed=19019164; DOI=10.1111/j.1365-2958.2008.06528.x;
RA Frohner I.E., Bourgeois C., Yatsyk K., Majer O., Kuchler K.;
RT "Candida albicans cell surface superoxide dismutases degrade host-derived
RT reactive oxygen species to escape innate immune surveillance.";
RL Mol. Microbiol. 71:240-252(2009).
RN [11]
RP INDUCTION.
RX PubMed=20735781; DOI=10.1111/j.1365-2958.2010.07331.x;
RA Lohse M.B., Johnson A.D.;
RT "Temporal anatomy of an epigenetic switch in cell programming: the white-
RT opaque transition of C. albicans.";
RL Mol. Microbiol. 78:331-343(2010).
RN [12]
RP FUNCTION.
RX PubMed=21746956; DOI=10.1128/aac.00280-11;
RA Bink A., Vandenbosch D., Coenye T., Nelis H., Cammue B.P., Thevissen K.;
RT "Superoxide dismutases are involved in Candida albicans biofilm persistence
RT against miconazole.";
RL Antimicrob. Agents Chemother. 55:4033-4037(2011).
RN [13]
RP INDUCTION.
RX PubMed=22205973; DOI=10.1371/journal.pone.0028830;
RA Zhu J., Krom B.P., Sanglard D., Intapa C., Dawson C.C., Peters B.M.,
RA Shirtliff M.E., Jabra-Rizk M.A.;
RT "Farnesol-induced apoptosis in Candida albicans is mediated by Cdr1-p
RT extrusion and depletion of intracellular glutathione.";
RL PLoS ONE 6:E28830-E28830(2011).
CC -!- FUNCTION: Superoxide dismutases serve to convert damaging superoxide
CC radicals, a key form of ROS, to less damaging hydrogen peroxide that
CC can be converted into water by catalase action. Degrades host-derived
CC reactive oxygen species to escape innate immune surveillance. Involved
CC in the occurrence of miconazole-tolerant persisters in biofilms.
CC Persisters are cells that survive high doses of an antimicrobial agent.
CC {ECO:0000269|PubMed:19019164, ECO:0000269|PubMed:21746956}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:18421; EC=1.15.1.1;
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:15302828}. Membrane {ECO:0000305|PubMed:15302828};
CC Lipid-anchor, GPI-anchor. Note=Covalently-linked GPI-modified cell wall
CC protein (GPI-CWP). {ECO:0000269|PubMed:15302828}.
CC -!- INDUCTION: Induced by farnesol and ciclopirox. Expression is higher in
CC opaque cells compared to white cells. {ECO:0000269|PubMed:15790671,
CC ECO:0000269|PubMed:16215173, ECO:0000269|PubMed:20735781,
CC ECO:0000269|PubMed:22205973}.
CC -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC reticulum and serves to target the protein to the cell surface. There,
CC the glucosamine-inositol phospholipid moiety is cleaved off and the
CC GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; CP017624; AOW27119.1; -; Genomic_DNA.
DR RefSeq; XP_719509.1; XM_714416.1.
DR AlphaFoldDB; Q5AD05; -.
DR SMR; Q5AD05; -.
DR STRING; 237561.Q5AD05; -.
DR GeneID; 3638888; -.
DR KEGG; cal:CAALFM_C200660CA; -.
DR CGD; CAL0000184565; SOD4.
DR VEuPathDB; FungiDB:C2_00660C_A; -.
DR eggNOG; ENOG502S5NX; Eukaryota.
DR HOGENOM; CLU_063073_1_1_1; -.
DR InParanoid; Q5AD05; -.
DR OMA; IVVHYAN; -.
DR OrthoDB; 1504692at2759; -.
DR PRO; PR:Q5AD05; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005576; C:extracellular region; IDA:CGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
DR GO; GO:0030445; C:yeast-form cell wall; IDA:CGD.
DR GO; GO:0005507; F:copper ion binding; IDA:CGD.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:CGD.
DR GO; GO:0071451; P:cellular response to superoxide; IDA:CGD.
DR GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
DR Gene3D; 2.60.40.200; -; 1.
DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR InterPro; IPR001424; SOD_Cu_Zn_dom.
DR PANTHER; PTHR10003; PTHR10003; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR SUPFAM; SSF49329; SSF49329; 1.
PE 1: Evidence at protein level;
KW Antioxidant; Cell wall; Copper; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Metal-binding; Oxidoreductase; Reference proteome; Secreted;
KW Signal; Virulence; Zinc.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..209
FT /note="Cell surface superoxide dismutase [Cu-Zn] 4"
FT /id="PRO_0000424634"
FT PROPEP 210..232
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424635"
FT REGION 174..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT LIPID 209
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 232 AA; 23726 MW; CD945181DFC15842 CRC64;
MKYLSIISIV ALALAGDSPI STDSKGKAPL VARFKKTSKS DIEGTIKFEP ANNGTVLVSV
DLTGLPSGVG PYPYHVHEKP VPESKNCTAT GMHFNPFNGS TTAKTPAALE LGDLSGRHGN
ITSESFEVEY DDSYISLNKD SKAYIGGLSI VVHSNNNTRL NCANITTLDE GDDTASAATW
SNSSSSSSSS SKNSTNGSSG SSTSASQGSG AGRAEISGFL AAGIAGVVAA LI
