SOD5_ARTBC
ID SOD5_ARTBC Reviewed; 373 AA.
AC D4B5D4;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Cell surface Cu-only superoxide dismutase ARB_03674 {ECO:0000305};
DE EC=1.15.1.1 {ECO:0000250|UniProtKB:Q5AD07};
DE Flags: Precursor;
GN ORFNames=ARB_03674;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(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 (By similarity).
CC Degrades host-derived reactive oxygen species to escape innate immune
CC surveillance (By similarity). Involved in the occurrence of miconazole-
CC tolerant persisters in biofilms (By similarity). Persisters are cells
CC that survive high doses of an antimicrobial agent. The unusual
CC attributes of SOD5-like fungal proteins, including the absence of zinc
CC and an open active site that readily captures extracellular copper,
CC make these SODs well suited to meet challenges in zinc and copper
CC availability at the host-pathogen interface (By similarity).
CC {ECO:0000250|UniProtKB:Q5AD07}.
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:0000250|UniProtKB:Q5AD07};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:Q5AD07};
CC Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:Q5AD07};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q5AD07}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000250|UniProtKB:Q5AD07}. Secreted {ECO:0000269|PubMed:21919205}.
CC Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}.
CC Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP).
CC {ECO:0000250|UniProtKB:Q5AD07}.
CC -!- INDUCTION: Expression is down-regulated in presence of human
CC keratinocytes. {ECO:0000269|PubMed:21247460}.
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 {ECO:0000305}.
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 {ECO:0000250|UniProtKB:Q5AD07}.
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DR EMBL; ABSU01000039; EFE29467.1; -; Genomic_DNA.
DR RefSeq; XP_003010107.1; XM_003010061.1.
DR AlphaFoldDB; D4B5D4; -.
DR SMR; D4B5D4; -.
DR STRING; 663331.D4B5D4; -.
DR EnsemblFungi; EFE29467; EFE29467; ARB_03674.
DR GeneID; 9525375; -.
DR KEGG; abe:ARB_03674; -.
DR eggNOG; ENOG502S5NX; Eukaryota.
DR HOGENOM; CLU_063073_0_0_1; -.
DR OMA; TRITCAD; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.60.40.200; -; 1.
DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR PANTHER; PTHR10003; PTHR10003; 1.
DR SUPFAM; SSF49329; SSF49329; 1.
PE 1: Evidence at protein level;
KW Antioxidant; Cell membrane; Cell wall; Copper; Disulfide bond;
KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Secreted; Signal; Virulence.
FT SIGNAL 1..55
FT /evidence="ECO:0000255"
FT CHAIN 56..352
FT /note="Cell surface Cu-only superoxide dismutase ARB_03674"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434655"
FT PROPEP 353..373
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434656"
FT REGION 329..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 194
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q5AD07"
FT BINDING 196
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q5AD07"
FT BINDING 212
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q5AD07"
FT BINDING 280
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q5AD07"
FT LIPID 352
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 206..289
FT /evidence="ECO:0000250|UniProtKB:Q5AD07"
SQ SEQUENCE 373 AA; 40234 MW; 92B1B8CA83CA9C0A CRC64;
MIWKQPPRRM GEMGGSLSRR FGNAAASWAV WRVSRSCFSL LFFFYFFLFF SSSSLLPTTN
NYQHLQLHSL IPTLNTTAHL PHQQASSASM KASLFLACSA LGLALATPTQ DAPETVNNPL
GIVYQAKLPE TSRTGIRGTI NATAHSSGRG VVFNLDLWGF DNTEGPFRKL HTCFDQTNKQ
TNKIVKLTTT TAYHIHVDPV PTDGSCGPTK DHLDPFGRGQ TPPCDDSLPQ TCEPGDLSGK
FGRLTTSSME EHFNQTFHDL YTSTRPGLGT FFGNRSIVIH HRNSTRLTCA NFTLVEQPGT
STTYVPRPTG TGIISSIFPT GTGAISTSGH APTISATYTP TPTPSPPAQN NGAGRLVGFS
LGAIMAALVP LAL
