TSA1_CANAL
ID TSA1_CANAL Reviewed; 196 AA.
AC Q9Y7F0; A0A1D8PKI8; Q5A2Z4;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Peroxiredoxin TSA1-A;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:P34760};
DE AltName: Full=Thiol-specific antioxidant protein;
DE AltName: Full=Thioredoxin peroxidase;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin TSA1-A {ECO:0000305};
GN Name=TSA1 {ECO:0000303|PubMed:12782322};
GN Synonyms=TSA1A {ECO:0000303|PubMed:16102003};
GN OrderedLocusNames=CAALFM_C306180CA; ORFNames=CaO19.7417;
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 [MRNA].
RA Marchais V., Cottin J.;
RT "Sequence of TSA-like gene in Candida albicans.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=12782322; DOI=10.1016/s0014-5793(03)00455-1;
RA Urban C., Sohn K., Lottspeich F., Brunner H., Rupp S.;
RT "Identification of cell surface determinants in Candida albicans reveals
RT Tsa1p, a protein differentially localized in the cell.";
RL FEBS Lett. 544:228-235(2003).
RN [6]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=16102003; DOI=10.1111/j.1365-2958.2005.04771.x;
RA Urban C., Xiong X., Sohn K., Schroppel K., Brunner H., Rupp S.;
RT "The moonlighting protein Tsa1p is implicated in oxidative stress response
RT and in cell wall biogenesis in Candida albicans.";
RL Mol. Microbiol. 57:1318-1341(2005).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16134099; DOI=10.1002/yea.1283;
RA Shin D.H., Jung S., Park S.J., Kim Y.J., Ahn J.M., Kim W., Choi W.;
RT "Characterization of thiol-specific antioxidant 1 (TSA1) of Candida
RT albicans.";
RL Yeast 22:907-918(2005).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides and as sensor of hydrogen peroxide-mediated
CC signaling events. Also involved in the correct composition of the
CC hyphal cell wall. {ECO:0000269|PubMed:16102003}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24;
CC Evidence={ECO:0000250|UniProtKB:P34760};
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation.
CC {ECO:0000250|UniProtKB:P34760}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:12782322,
CC ECO:0000269|PubMed:16102003}. Nucleus {ECO:0000269|PubMed:12782322,
CC ECO:0000269|PubMed:16134099}. Cytoplasm {ECO:0000269|PubMed:12782322,
CC ECO:0000269|PubMed:16134099}. Note=Localizes to the cell surface in
CC hyphally grown cells, whereas no surface but mainly nuclear
CC localization is found in yeast-form cells.
CC {ECO:0000269|PubMed:12782322, ECO:0000269|PubMed:16102003}.
CC -!- INDUCTION: Induced by oxidative stress. {ECO:0000269|PubMed:16102003}.
CC -!- DISRUPTION PHENOTYPE: Results in delayed hyphal development and
CC enhanced sensitivity to cell wall-perturbing agents, yet does not
CC impair virulence in vivo. {ECO:0000269|PubMed:16102003}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. In this typical 2-Cys
CC peroxiredoxin, C(R) is provided by the other dimeric subunit to form an
CC intersubunit disulfide. The disulfide is subsequently reduced by
CC thioredoxin. {ECO:0000250|UniProtKB:P34760}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF149421; AAD34017.1; -; mRNA.
DR EMBL; CP017625; AOW28625.1; -; Genomic_DNA.
DR RefSeq; XP_019330878.1; XM_019475333.1.
DR RefSeq; XP_716082.1; XM_710989.1.
DR AlphaFoldDB; Q9Y7F0; -.
DR SMR; Q9Y7F0; -.
DR BioGRID; 1225363; 1.
DR STRING; 237561.Q9Y7F0; -.
DR MoonDB; Q9Y7F0; Curated.
DR MoonProt; Q9Y7F0; -.
DR PeroxiBase; 4472; Cal2CysPrx01.
DR PRIDE; Q9Y7F0; -.
DR GeneID; 30515214; -.
DR GeneID; 3642269; -.
DR KEGG; cal:CAALFM_C306180CA; -.
DR KEGG; cal:CAALFM_C306330WA; -.
DR CGD; CAL0000174369; TSA1.
DR CGD; CAL0000189947; TSA1B.
DR VEuPathDB; FungiDB:C3_06180C_A; -.
DR VEuPathDB; FungiDB:C3_06330W_A; -.
DR HOGENOM; CLU_042529_21_1_1; -.
DR InParanoid; Q9Y7F0; -.
DR OMA; FWYPKDF; -.
DR OrthoDB; 1326484at2759; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005737; C:cytoplasm; IDA:CGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
DR GO; GO:0005634; C:nucleus; IDA:CGD.
DR GO; GO:0030985; F:high molecular weight kininogen binding; IDA:CGD.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
DR GO; GO:0051701; P:biological process involved in interaction with host; IPI:CGD.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IMP:CGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0036171; P:filamentous growth of a population of unicellular organisms in response to chemical stimulus; IMP:CGD.
DR GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:CGD.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Antioxidant; Cytoplasm; Disulfide bond; Nucleus; Oxidoreductase;
KW Peroxidase; Redox-active center; Reference proteome.
FT CHAIN 1..196
FT /note="Peroxiredoxin TSA1-A"
FT /id="PRO_0000135094"
FT DOMAIN 3..161
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 173..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 48
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P34760"
FT BINDING 45..47
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P34760"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P34760"
FT DISULFID 48
FT /note="Interchain (with C-169); in linked form"
FT /evidence="ECO:0000250|UniProtKB:P34760"
FT DISULFID 169
FT /note="Interchain (with C-48); in linked form"
FT /evidence="ECO:0000250|UniProtKB:P34760"
SQ SEQUENCE 196 AA; 21860 MW; 0BD7B6B4715DCDBB CRC64;
MAPVVQQPAP SFKKTAVVDG VFEEVTLEQY KGKWVLLAFI PLAFTFVCPS EIIAYSEAVK
KFAEKDAQVL FASTDSEYTW LAWTNVARKD GGIGKVDFPV LADTNHSLSR DYGVLIEEEG
VALRGIFLID PKGVLRQITI NDLPVGRSVE ESLRLLEAFQ FTEKYGEVCP ANWHPGDETI
KPSPEASKEY FNKVNK
