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Peroxiredoxin 1 (EC 1.11.1.15) (Cytosolic thioredoxin peroxidase) (DPx-4783) (DmTPx-1) (Thioredoxin peroxidase)

 PRDX1_DROME             Reviewed;         194 AA.
Q9V3P0; Q0KHT0;
10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 149.
RecName: Full=Peroxiredoxin 1;
EC=1.11.1.15 {ECO:0000269|PubMed:11677042};
AltName: Full=Cytosolic thioredoxin peroxidase;
Short=DPx-4783;
Short=DmTPx-1;
AltName: Full=Thioredoxin peroxidase;
Name=Jafrac1; Synonyms=TPX-1; ORFNames=CG1633;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10632718; DOI=10.1046/j.1432-1327.2000.01022.x;
Rodriguez J., Agudo M., Van Damme J., Vandekerckhove J.,
Santaren J.F.;
"Polypeptides differentially expressed in imaginal discs define the
peroxiredoxin family of genes in Drosophila.";
Eur. J. Biochem. 267:487-497(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
AND DEVELOPMENTAL STAGE.
PubMed=11677042; DOI=10.1016/S0891-5849(01)00692-X;
Radyuk S.N., Klichko V.I., Spinola B., Sohal R.S., Orr W.C.;
"The peroxiredoxin gene family in Drosophila melanogaster.";
Free Radic. Biol. Med. 31:1090-1100(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Ovary;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A.,
Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[7]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=11877442; DOI=10.1074/jbc.M200636200;
Bauer H., Kanzok S.M., Schirmer R.H.;
"Thioredoxin-2 but not thioredoxin-1 is a substrate of thioredoxin
peroxidase-1 from Drosophila melanogaster: isolation and
characterization of a second thioredoxin in D.melanogaster and
evidence for distinct biological functions of Trx-1 and Trx-2.";
J. Biol. Chem. 277:17457-17463(2002).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-193 AND SER-194, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction
of hydrogen peroxide and organic hydroperoxides to water and
alcohols, respectively. Plays a role in cell protection against
oxidative stress by detoxifying peroxides and as sensor of
hydrogen peroxide-mediated signaling events. Might participate in
the signaling cascades of growth factors and tumor necrosis
factor-alpha by regulating the intracellular concentrations of
H(2)O(2) (By similarity). Reduces an intramolecular disulfide bond
in GDPD5 that gates the ability to GDPD5 to drive postmitotic
motor neuron differentiation (By similarity).
{ECO:0000250|UniProtKB:P0CB50, ECO:0000250|UniProtKB:Q06830}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000269|PubMed:11677042}.
-!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 5 homodimers
assemble to form a ring-like decamer (By similarity). Interacts
with GDPD5; forms a mixed-disulfide with GDPD5 (By similarity).
Interacts with SESN1 and SESN2 (By similarity).
{ECO:0000250|UniProtKB:P0CB50, ECO:0000250|UniProtKB:Q06830}.
-!- INTERACTION:
P11956:MtnB; NbExp=2; IntAct=EBI-82319, EBI-88468;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11677042}.
-!- DEVELOPMENTAL STAGE: Highly expressed during embryogenesis, weakly
expressed during larval stages. {ECO:0000269|PubMed:11677042,
ECO:0000269|PubMed:11877442}.
-!- PTM: The enzyme can be inactivated by further oxidation of the
cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H)
instead of its condensation to a disulfide bond. It can be
reactivated by forming a transient disulfide bond with
sulfiredoxin SRXN1, which reduces the cysteine sulfinic acid in an
ATP- and Mg-dependent manner. {ECO:0000250|UniProtKB:Q06830}.
-!- MISCELLANEOUS: The active site is a conserved redox-active
cysteine residue, the peroxidatic cysteine (C(P)), which makes the
nucleophilic attack on the peroxide substrate. The peroxide
oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which
then reacts with another cysteine residue, the resolving cysteine
(C(R)), to form a disulfide bridge. The disulfide is subsequently
reduced by an appropriate electron donor to complete the catalytic
cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by
the other dimeric subunit to form an intersubunit disulfide. The
disulfide is subsequently reduced by thioredoxin (By similarity).
As a reducing substrate, thioredoxin 2 is preferred over
thioredoxin 1 (PubMed:11877442). {ECO:0000250|UniProtKB:Q06830,
ECO:0000269|PubMed:11877442}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF167098; AAF42985.1; -; mRNA.
EMBL; AF321615; AAK06770.1; -; mRNA.
EMBL; AF321616; AAK06771.1; -; mRNA.
EMBL; AE014298; AAF48253.1; -; Genomic_DNA.
EMBL; AY070534; AAL48005.1; -; mRNA.
EMBL; BT014630; AAT27254.1; -; mRNA.
RefSeq; NP_001285202.1; NM_001298273.1.
RefSeq; NP_001285203.1; NM_001298274.1.
RefSeq; NP_001285204.1; NM_001298275.1.
RefSeq; NP_477510.1; NM_058162.3.
RefSeq; NP_727689.1; NM_167359.2.
UniGene; Dm.3464; -.
ProteinModelPortal; Q9V3P0; -.
SMR; Q9V3P0; -.
BioGrid; 72802; 21.
DIP; DIP-17916N; -.
IntAct; Q9V3P0; 16.
MINT; MINT-763596; -.
STRING; 7227.FBpp0073594; -.
iPTMnet; Q9V3P0; -.
PaxDb; Q9V3P0; -.
PRIDE; Q9V3P0; -.
EnsemblMetazoa; FBtr0073763; FBpp0073594; FBgn0040309.
EnsemblMetazoa; FBtr0073764; FBpp0073595; FBgn0040309.
EnsemblMetazoa; FBtr0339699; FBpp0308756; FBgn0040309.
EnsemblMetazoa; FBtr0339700; FBpp0308757; FBgn0040309.
EnsemblMetazoa; FBtr0345161; FBpp0311371; FBgn0040309.
GeneID; 53578; -.
KEGG; dme:Dmel_CG1633; -.
CTD; 53578; -.
FlyBase; FBgn0040309; Jafrac1.
eggNOG; KOG0852; Eukaryota.
eggNOG; COG0450; LUCA.
InParanoid; Q9V3P0; -.
KO; K13279; -.
OMA; CPANWEE; -.
OrthoDB; EOG091G0IE5; -.
PhylomeDB; Q9V3P0; -.
Reactome; R-DME-5628897; TP53 Regulates Metabolic Genes.
GenomeRNAi; 53578; -.
PRO; PR:Q9V3P0; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0040309; -.
ExpressionAtlas; Q9V3P0; differential.
Genevisible; Q9V3P0; DM.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:UniProtKB.
GO; GO:0007155; P:cell adhesion; IMP:FlyBase.
GO; GO:0045454; P:cell redox homeostasis; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:FlyBase.
GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
GO; GO:0007281; P:germ cell development; IMP:FlyBase.
GO; GO:0008354; P:germ cell migration; IMP:FlyBase.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:FlyBase.
GO; GO:0010906; P:regulation of glucose metabolic process; IMP:FlyBase.
GO; GO:0006979; P:response to oxidative stress; IMP:FlyBase.
GO; GO:0042594; P:response to starvation; IMP:FlyBase.
InterPro; IPR000866; AhpC/TSA.
InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
InterPro; IPR019479; Peroxiredoxin_C.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF10417; 1-cysPrx_C; 1.
Pfam; PF00578; AhpC-TSA; 1.
PIRSF; PIRSF000239; AHPC; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
Antioxidant; Complete proteome; Cytoplasm; Disulfide bond;
Oxidoreductase; Peroxidase; Phosphoprotein; Redox-active center;
Reference proteome.
CHAIN 1 194 Peroxiredoxin 1.
/FTId=PRO_0000135085.
DOMAIN 2 160 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 47 47 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000250|UniProtKB:Q06830}.
MOD_RES 193 193 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 194 194 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
DISULFID 47 47 Interchain (with C-168); in linked form.
{ECO:0000250|UniProtKB:Q06830}.
DISULFID 168 168 Interchain (with C-47); in linked form.
{ECO:0000250|UniProtKB:Q06830}.
SEQUENCE 194 AA; 21738 MW; 93ED319BE144E8D1 CRC64;
MPQLQKPAPA FAGTAVVNGV FKDIKLSDYK GKYLVLFFYP LDFTFVCPTE IIAFSESAAE
FRKINCEVIG CSTDSQFTHL AWINTPRKQG GLGSMDIPLL ADKSMKVARD YGVLDEETGI
PFRGLFIIDD KQNLRQITVN DLPVGRSVEE TLRLVQAFQY TDKYGEVCPA NWKPGQKTMV
ADPTKSKEYF ETTS


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