SOD6_CANAL
ID SOD6_CANAL Reviewed; 316 AA.
AC Q5ACV9; A0A1D8PG15;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cell surface superoxide dismutase [Cu-Zn] 6;
DE EC=1.15.1.1;
DE AltName: Full=Predicted GPI-anchored protein 9;
DE Flags: Precursor;
GN Name=SOD6; Synonyms=PGA9, SOD33; OrderedLocusNames=CAALFM_C200240CA;
GN ORFNames=CaO19.2108, CaO19.9656;
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.
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 [6]
RP INDUCTION.
RX PubMed=16151249; DOI=10.1128/ec.4.9.1562-1573.2005;
RA Murillo L.A., Newport G., Lan C.Y., Habelitz S., Dungan J., Agabian N.M.;
RT "Genome-wide transcription profiling of the early phase of biofilm
RT formation by Candida albicans.";
RL Eukaryot. Cell 4:1562-1573(2005).
RN [7]
RP INDUCTION.
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 [8]
RP INDUCTION.
RX PubMed=21592964; DOI=10.1074/jbc.m111.233569;
RA Singh R.P., Prasad H.K., Sinha I., Agarwal N., Natarajan K.;
RT "Cap2-HAP complex is a critical transcriptional regulator that has dual but
RT contrasting roles in regulation of iron homeostasis in Candida albicans.";
RL J. Biol. Chem. 286:25154-25170(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. May be involved
CC protection against extracellular stress.
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. Membrane {ECO:0000250};
CC Lipid-anchor, GPI-anchor {ECO:0000250}. Note=Covalently-linked GPI-
CC modified cell wall protein (GPI-CWP). {ECO:0000250}.
CC -!- INDUCTION: Unlike SOD4 and SOD5, SOD6 is not regulated during yeast to
CC hyphae transition or by temperature. Up-regulated during biofilm
CC formation and expression is controlled by HAP43.
CC {ECO:0000269|PubMed:16151249, ECO:0000269|PubMed:19019164,
CC ECO:0000269|PubMed:21592964}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; CP017624; AOW27078.1; -; Genomic_DNA.
DR RefSeq; XP_719554.2; XM_714461.2.
DR AlphaFoldDB; Q5ACV9; -.
DR SMR; Q5ACV9; -.
DR STRING; 237561.Q5ACV9; -.
DR GeneID; 3638899; -.
DR KEGG; cal:CAALFM_C200240CA; -.
DR CGD; CAL0000199539; SOD6.
DR VEuPathDB; FungiDB:C2_00240C_A; -.
DR eggNOG; ENOG502S5NX; Eukaryota.
DR HOGENOM; CLU_063073_2_0_1; -.
DR InParanoid; Q5ACV9; -.
DR OMA; TKIACAD; -.
DR OrthoDB; 1504692at2759; -.
DR PRO; PR:Q5ACV9; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:1903561; C:extracellular vesicle; IDA:CGD.
DR GO; GO:0005507; F:copper ion binding; ISS:CGD.
DR GO; GO:0004784; F:superoxide dismutase activity; ISS: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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..288
FT /note="Cell surface superoxide dismutase [Cu-Zn] 6"
FT /id="PRO_0000424638"
FT PROPEP 289..316
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424639"
FT REGION 243..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 78
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT LIPID 288
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 316 AA; 35110 MW; 81911D3A4C104344 CRC64;
MIFIPIIILI YLVSIAASDK SPKIKKNPRN VVAVADFPFG GDTQVKGNVV FSAKEGKHVN
VHIDMTGLPK DEGPFFYHIH ERSVPGNGNC EAVGLHFNPY NASPVCDEQK NDAYCQVGDL
SGKHGCINTT CFELKYSDPY LSLNRKSKSY IIGKSVVFHY PNLTKIACAD IEEANELRLQ
SLIDEYTQTD DAIQLKELNT PLETDYKFDE VEALSSEIYH SDTDSDPPQQ ELISTEKLYN
KTDNVYSPEE TRPSDQNKKS HRHSLLPLAK WKKNSPKNYS NISIHGISSD CLNDGMMVTG
SVFGSLVLGI AAGIFV
