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SOD5_CANAL
ID   SOD5_CANAL              Reviewed;         228 AA.
AC   Q5AD07; A0A1D8PG56;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Cell surface Cu-only superoxide dismutase 5;
DE            EC=1.15.1.1;
DE   AltName: Full=Predicted GPI-anchored protein 3;
DE   Flags: Precursor;
GN   Name=SOD5; Synonyms=PGA3, SOD31; OrderedLocusNames=CAALFM_C200680CA;
GN   ORFNames=CaO19.2060, CaO19.9607;
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   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
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=15814840; DOI=10.1091/mbc.e05-01-0073;
RA   Kadosh D., Johnson A.D.;
RT   "Induction of the Candida albicans filamentous growth program by relief of
RT   transcriptional repression: a genome-wide analysis.";
RL   Mol. Biol. Cell 16:2903-2912(2005).
RN   [7]
RP   INDUCTION.
RX   PubMed=15813733; DOI=10.1111/j.1365-2958.2005.04557.x;
RA   Fradin C., De Groot P., MacCallum D., Schaller M., Klis F., Odds F.C.,
RA   Hube B.;
RT   "Granulocytes govern the transcriptional response, morphology and
RT   proliferation of Candida albicans in human blood.";
RL   Mol. Microbiol. 56:397-415(2005).
RN   [8]
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   [9]
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   [10]
RP   INDUCTION.
RX   PubMed=23123467; DOI=10.1248/bpb.b12-00338;
RA   Miao H., Zhao L., Li C., Shang Q., Lu H., Fu Z., Wang L., Jiang Y., Cao Y.;
RT   "Inhibitory effect of Shikonin on Candida albicans growth.";
RL   Biol. Pharm. Bull. 35:1956-1963(2012).
RN   [11]
RP   INDUCTION.
RX   PubMed=23285201; DOI=10.1371/journal.pone.0052850;
RA   Miramon P., Dunker C., Windecker H., Bohovych I.M., Brown A.J., Kurzai O.,
RA   Hube B.;
RT   "Cellular responses of Candida albicans to phagocytosis and the
RT   extracellular activities of neutrophils are critical to counteract
RT   carbohydrate starvation, oxidative and nitrosative stress.";
RL   PLoS ONE 7:E52850-E52850(2012).
RN   [12]
RP   INDUCTION.
RX   PubMed=23125349; DOI=10.1128/ec.00236-12;
RA   Pierce J.V., Dignard D., Whiteway M., Kumamoto C.A.;
RT   "Normal adaptation of Candida albicans to the murine gastrointestinal tract
RT   requires Efg1p-dependent regulation of metabolic and host defense genes.";
RL   Eukaryot. Cell 12:37-49(2013).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RX   PubMed=23948566; DOI=10.1016/j.jprot.2013.07.031;
RA   Aoki W., Tatsukami Y., Kitahara N., Matsui K., Morisaka H., Kuroda K.,
RA   Ueda M.;
RT   "Elucidation of potentially virulent factors of Candida albicans during
RT   serum adaptation by using quantitative time-course proteomics.";
RL   J. Proteomics 91:417-429(2013).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=23136884; DOI=10.1111/mmi.12087;
RA   Rohm M., Lindemann E., Hiller E., Ermert D., Lemuth K., Trkulja D.,
RA   Sogukpinar O., Brunner H., Rupp S., Urban C.F., Sohn K.;
RT   "A family of secreted pathogenesis-related proteins in Candida albicans.";
RL   Mol. Microbiol. 87:132-151(2013).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 27-181, COFACTOR, DISULFIDE BOND,
RP   SUBUNIT, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND FUNCTION.
RX   PubMed=24711423; DOI=10.1073/pnas.1400137111;
RA   Gleason J.E., Galaleldeen A., Peterson R.L., Taylor A.B., Holloway S.P.,
RA   Waninger-Saroni J., Cormack B.P., Cabelli D.E., Hart P.J., Culotta V.C.;
RT   "Candida albicans SOD5 represents the prototype of an unprecedented class
RT   of Cu-only superoxide dismutases required for pathogen defense.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:5866-5871(2014).
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       The unusual attributes of SOD5-like fungal proteins, including the
CC       absence of zinc and an open active site that readily captures
CC       extracellular copper, make these SODs well suited to meet challenges in
CC       zinc and copper availability at the host-pathogen interface.
CC       {ECO:0000269|PubMed:14617819, ECO:0000269|PubMed:19019164,
CC       ECO:0000269|PubMed:21746956, ECO:0000269|PubMed:24711423}.
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         Evidence={ECO:0000269|PubMed:24711423};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000269|PubMed:24711423};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:24711423};
CC   -!- ACTIVITY REGULATION: Secreted in a disulfide-oxidized form and apo-
CC       pools of secreted SOD5 can readily capture extracellular copper for
CC       rapid induction of enzyme activity. {ECO:0000269|PubMed:24711423}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:24711423}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000269|PubMed:23136884}. Membrane {ECO:0000250}; Lipid-anchor,
CC       GPI-anchor {ECO:0000250}. Note=Covalently-linked GPI-modified cell wall
CC       protein (GPI-CWP). {ECO:0000250}.
CC   -!- INDUCTION: Induced during yeast-to-hyphal transition and by osmotic and
CC       oxidative stresses. Expression is also increased when cells were grown
CC       on nonfermentable substrates as the only carbon source, in serum, and
CC       in the presence of neutrophils. Down-regulated by shikonin. Expression
CC       is controlled by EFG1, NRG1 and RIM101. {ECO:0000269|PubMed:14617819,
CC       ECO:0000269|PubMed:15813733, ECO:0000269|PubMed:15814840,
CC       ECO:0000269|PubMed:23123467, ECO:0000269|PubMed:23125349,
CC       ECO:0000269|PubMed:23136884, ECO:0000269|PubMed:23285201,
CC       ECO:0000269|PubMed:23948566}.
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   -!- DISRUPTION PHENOTYPE: Leads to sensitivity to hydrogen peroxide when
CC       cells were grown in nutrient-limited conditions.
CC       {ECO:0000269|PubMed:14617819}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Although the beta-barrel of Cu/Zn SODs is largely preserved,
CC       SOD5 is a monomeric copper protein that lacks a zinc-binding site and
CC       is missing the electrostatic loop element proposed to promote catalysis
CC       through superoxide guidance. Without an electrostatic loop, the copper
CC       site of SOD5 is not recessed and is readily accessible to bulk solvent
CC       (PubMed:24711423). {ECO:0000305|PubMed:24711423}.
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DR   EMBL; CP017624; AOW27120.1; -; Genomic_DNA.
DR   RefSeq; XP_719507.1; XM_714414.1.
DR   PDB; 4N3T; X-ray; 1.40 A; A=27-181.
DR   PDB; 4N3U; X-ray; 1.75 A; A=27-181.
DR   PDB; 5CU9; X-ray; 1.48 A; A=27-181.
DR   PDB; 5KBK; X-ray; 1.41 A; A=27-181.
DR   PDB; 5KBL; X-ray; 1.41 A; A=27-181.
DR   PDB; 5KBM; X-ray; 1.42 A; A=27-181.
DR   PDBsum; 4N3T; -.
DR   PDBsum; 4N3U; -.
DR   PDBsum; 5CU9; -.
DR   PDBsum; 5KBK; -.
DR   PDBsum; 5KBL; -.
DR   PDBsum; 5KBM; -.
DR   AlphaFoldDB; Q5AD07; -.
DR   SMR; Q5AD07; -.
DR   STRING; 237561.Q5AD07; -.
DR   GeneID; 3638886; -.
DR   KEGG; cal:CAALFM_C200680CA; -.
DR   CGD; CAL0000188676; SOD5.
DR   VEuPathDB; FungiDB:C2_00680C_A; -.
DR   eggNOG; ENOG502S5NX; Eukaryota.
DR   HOGENOM; CLU_063073_1_1_1; -.
DR   InParanoid; Q5AD07; -.
DR   OrthoDB; 1504692at2759; -.
DR   PHI-base; PHI:383; -.
DR   PHI-base; PHI:8749; -.
DR   PRO; PR:Q5AD07; -.
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:0005507; F:copper ion binding; IDA:CGD.
DR   GO; GO:0004784; F:superoxide dismutase activity; IDA:CGD.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IMP:CGD.
DR   GO; GO:0071451; P:cellular response to superoxide; IDA:CGD.
DR   GO; GO:0042783; P:evasion of host immune response; IMP:CGD.
DR   GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
DR   GO; GO:0006801; P:superoxide metabolic process; IDA:CGD.
DR   GO; GO:0052164; P:symbiont defense to host-produced reactive oxygen species; IMP:CGD.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR017868; Filamin/ABP280_repeat-like.
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   3D-structure; Antioxidant; Cell wall; Copper; Disulfide bond; Glycoprotein;
KW   GPI-anchor; Lipoprotein; Membrane; Metal-binding; Oxidoreductase;
KW   Reference proteome; Secreted; Signal; Virulence.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..205
FT                   /note="Cell surface Cu-only superoxide dismutase 5"
FT                   /id="PRO_0000424636"
FT   PROPEP          206..228
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000424637"
FT   REGION          176..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..203
FT                   /note="Polar residues"
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   BINDING         77
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT   BINDING         93
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT   BINDING         153
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT   LIPID           205
FT                   /note="GPI-anchor amidated asparagine"
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        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        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        87..162
FT                   /evidence="ECO:0000269|PubMed:24711423"
FT   STRAND          30..34
FT                   /evidence="ECO:0007829|PDB:4N3T"
FT   STRAND          43..51
FT                   /evidence="ECO:0007829|PDB:4N3T"
FT   TURN            52..54
FT                   /evidence="ECO:0007829|PDB:4N3T"
FT   STRAND          55..63
FT                   /evidence="ECO:0007829|PDB:4N3T"
FT   HELIX           67..69
FT                   /evidence="ECO:0007829|PDB:4N3T"
FT   STRAND          74..79
FT                   /evidence="ECO:0007829|PDB:4N3T"
FT   HELIX           87..90
FT                   /evidence="ECO:0007829|PDB:4N3T"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:5CU9"
FT   HELIX           106..108
FT                   /evidence="ECO:0007829|PDB:4N3T"
FT   HELIX           114..118
FT                   /evidence="ECO:0007829|PDB:4N3T"
FT   STRAND          123..136
FT                   /evidence="ECO:0007829|PDB:4N3T"
FT   STRAND          149..153
FT                   /evidence="ECO:0007829|PDB:4N3T"
FT   STRAND          159..168
FT                   /evidence="ECO:0007829|PDB:4N3T"
SQ   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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