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Database: UniProt
Entry: SOD6_CANAL
LinkDB: SOD6_CANAL
Original site: 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   10-APR-2019, entry version 104.
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;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   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.,
RA   Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
RA   Davis R.W., 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
RT   aligned on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
RP   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
RT   allele-specific measurements and provides a simple model for repeat
RT   and indel 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
RT   and 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.,
RA   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-
RT   derived reactive oxygen species to escape innate immune
RT   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
RT   dual but contrasting roles in regulation of iron homeostasis in
RT   Candida albicans.";
RL   J. Biol. Chem. 286:25154-25170(2011).
CC   -!- FUNCTION: Superoxide dismutases serve to convert damaging
CC       superoxide radicals, a key form of ROS, to less damaging hydrogen
CC       peroxide that can be converted into water by catalase action. May
CC       be involved 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
CC       GPI-modified cell wall protein (GPI-CWP). {ECO:0000250}.
CC   -!- INDUCTION: Unlike SOD4 and SOD5, SOD6 is not regulated during
CC       yeast to hyphae transition or by temperature. Up-regulated during
CC       biofilm 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.
CC       There, the glucosamine-inositol phospholipid moiety is cleaved off
CC       and the GPI-modified mannoprotein is covalently attached via its
CC       lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer
CC       cell wall layer (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
DR   EMBL; CP017624; AOW27078.1; -; Genomic_DNA.
DR   RefSeq; XP_719554.2; XM_714461.2.
DR   ProteinModelPortal; Q5ACV9; -.
DR   SMR; Q5ACV9; -.
DR   STRING; 5476.C4YIZ2; -.
DR   GeneID; 3638899; -.
DR   KEGG; cal:CAALFM_C200240CA; -.
DR   CGD; CAL0000199539; SOD6.
DR   EuPathDB; FungiDB:C2_00240C_A; -.
DR   HOGENOM; HOG000093535; -.
DR   InParanoid; Q5ACV9; -.
DR   OMA; AVGLHFN; -.
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:0005618; C:cell wall; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005507; F:copper ion binding; ISS:CGD.
DR   GO; GO:0004784; F:superoxide dismutase activity; ISS:CGD.
DR   GO; GO:0016532; F:superoxide dismutase copper chaperone activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
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; Complete proteome; Copper; Glycoprotein;
KW   GPI-anchor; Lipoprotein; Membrane; Metal-binding; Oxidoreductase;
KW   Reference proteome; Secreted; Signal; Virulence; Zinc.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19    288       Cell surface superoxide dismutase [Cu-Zn]
FT                                6.
FT                                /FTId=PRO_0000424638.
FT   PROPEP      289    316       Removed in mature form. {ECO:0000255}.
FT                                /FTId=PRO_0000424639.
FT   METAL        78     78       Copper; catalytic. {ECO:0000250}.
FT   METAL        80     80       Copper; catalytic. {ECO:0000250}.
FT   METAL        96     96       Copper; catalytic. {ECO:0000250}.
FT   METAL        96     96       Zinc; structural. {ECO:0000250}.
FT   METAL       119    119       Zinc; structural. {ECO:0000250}.
FT   METAL       159    159       Copper; catalytic. {ECO:0000250}.
FT   LIPID       288    288       GPI-anchor amidated serine.
FT                                {ECO:0000255}.
FT   CARBOHYD    128    128       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    162    162       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    240    240       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    278    278       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    281    281       N-linked (GlcNAc...) asparagine.
FT                                {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
//
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