PMP20_SCHPO
ID PMP20_SCHPO Reviewed; 156 AA.
AC O14313; O74877;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Peroxisomal membrane associated protein 20;
DE AltName: Full=Peroxiredoxin homolog pmp20 {ECO:0000303|PubMed:20356456};
DE Short=Prx {ECO:0000303|PubMed:20356456};
GN Name=pmp20 {ECO:0000303|PubMed:20356456};
GN ORFNames=SPCC330.06c {ECO:0000312|PomBase:SPCC330.06c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=972 / ATCC 24843;
RA Lenaers G., Perret E., Delpech B., Picard A., Caput D.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP FUNCTION, LACK OF CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=20356456; DOI=10.5483/bmbrep.2010.43.3.170;
RA Kim J.S., Bang M.A., Lee S., Chae H.Z., Kim K.;
RT "Distinct functional roles of peroxiredoxin isozymes and glutathione
RT peroxidase from fission yeast, Schizosaccharomyces pombe.";
RL BMB Rep. 43:170-175(2010).
CC -!- FUNCTION: May act as a chaperone rather than a peroxidase. Has no
CC thioredoxin-dependent peroxidase activity. Shows weak chaperone
CC activity. {ECO:0000269|PubMed:20356456}.
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation.
CC {ECO:0000269|PubMed:20356456}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
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 the typical 2-Cys
CC Prx5 family, C(R) is provided by the other dimeric subunit to form an
CC intersubunit disulfide. Pmp20 lacks the resolving cysteine residue.
CC {ECO:0000305|PubMed:20356456}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ002536; CAA05528.1; -; mRNA.
DR EMBL; CU329672; CAA20911.1; -; Genomic_DNA.
DR PIR; T41316; T41316.
DR RefSeq; NP_587706.1; NM_001022701.2.
DR AlphaFoldDB; O14313; -.
DR SMR; O14313; -.
DR BioGRID; 275555; 11.
DR STRING; 4896.SPCC330.06c.1; -.
DR iPTMnet; O14313; -.
DR MaxQB; O14313; -.
DR PaxDb; O14313; -.
DR PRIDE; O14313; -.
DR EnsemblFungi; SPCC330.06c.1; SPCC330.06c.1:pep; SPCC330.06c.
DR GeneID; 2538981; -.
DR KEGG; spo:SPCC330.06c; -.
DR PomBase; SPCC330.06c; pmp20.
DR VEuPathDB; FungiDB:SPCC330.06c; -.
DR eggNOG; KOG0541; Eukaryota.
DR HOGENOM; CLU_072440_3_0_1; -.
DR InParanoid; O14313; -.
DR OMA; GTPIHFI; -.
DR PhylomeDB; O14313; -.
DR Reactome; R-SPO-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-SPO-5628897; TP53 Regulates Metabolic Genes.
DR PRO; PR:O14313; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IDA:PomBase.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IC:PomBase.
DR CDD; cd03013; PRX5_like; 1.
DR InterPro; IPR037944; PRX5-like.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10430; PTHR10430; 1.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Antioxidant; Cytoplasm; Disulfide bond; Nucleus; Oxidoreductase;
KW Peroxidase; Redox-active center; Reference proteome.
FT CHAIN 1..156
FT /note="Peroxisomal membrane associated protein 20"
FT /id="PRO_0000056609"
FT DOMAIN 2..156
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 43
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P38013"
FT DISULFID 43
FT /note="Interchain; in linked form"
FT /evidence="ECO:0000269|PubMed:20356456"
FT CONFLICT 20
FT /note="E -> K (in Ref. 1; CAA05528)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 156 AA; 16675 MW; 234DC024251F41D2 CRC64;
MVAVGSTLPK VTLWENKPEE VVEFPSQGKF IIVGVPGAFT PPCSSQVPGY IANEKQFAAK
GISGIYVVAV NDVFVTKAWK KSFDGGEQSG VHFVADWNGE FTKAFDAGFD ASGLLGPLRS
KRYAAVVENG KVVKVFIENE VTDVDISSAD KVLSSL
