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UniProtKB/Swiss-Prot entry Q9V3P0


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PRDX1_DROME
Primary accession number Q9V3P0
Secondary accession number Q0KHT0
Integrated into Swiss-Prot on January 10, 2003
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 64)
Name and origin of the protein
Protein name Peroxiredoxin 1
Synonyms EC 1.11.1.15
Thioredoxin peroxidase
Cytosolic thioredoxin peroxidase
DmTPx-1
DPx-4783
Gene name
Name: Jafrac1
Synonyms: TPX-1
ORFNames: CG1633
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10632718 [NCBI, ExPASy, EBI, Israel, Japan]
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], FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
DOI=10.1016/S0891-5849(01)00692-X; PubMed=11677042 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
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.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1074/jbc.M200636200; PubMed=11877442 [NCBI, ExPASy, EBI, Israel, Japan]
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 MASS SPECTROMETRY.
TISSUE=Embryo;
DOI=10.1021/pr700696a; PubMed=18327897 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF167098; AAF42985.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321615; AAK06770.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF321616; AAK06771.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014298; AAF48253.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY070534; AAL48005.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT014630; AAT27254.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_477510.1; -.
NP_727689.1; -.
UniGene Dm.3464
3D structure databases
HSSP Q63716; 1QQ2. [HSSP ENTRY / PDB]
SMR Q9V3P0; 3-190.
ModBase Q9V3P0.
Protein-protein interaction databases
DIP DIP:17916N; -.
IntAct Q9V3P0; -.
Enzyme and pathway databases
BioCyc DMEL-XXX-02:DMEL-XXX-02-001731-MON; -.
DMEL-XXX-02:DMEL-XXX-02-001732-MON; -.
Organism-specific databases
FlyBase FBgn0040309; Jafrac1.
Gene expression databases
ArrayExpress Q9V3P0; -.
GermOnline CG1633; Drosophila melanogaster.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0008379; Molecular function: thioredoxin peroxidase activity (inferred from direct assay from UniProtKB).
GO:0045454; Biological process: cell redox homeostasis (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000866; AhpC-TSA.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 1.
Pfam PF00578; AhpC-TSA; 1.
Pfam graphical view of domain structure.
PROSITE PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9V3P0.
Genome annotation databases
Ensembl CG1633; Drosophila melanogaster. [Contig view]
GeneID 53578; -.
KEGG dme:Dmel_CG1633; -.
Phylogenomic databases
HOGENOM Q9V3P0; -.
Other
ProtoNet Q9V3P0.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Antioxidant; Complete proteome; Cytoplasm; Oxidoreductase; Peroxidase; Phosphoprotein; Redox-active center.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   194  194     Peroxiredoxin 1. PRO_0000135085
DOMAIN   2   160  159     Thioredoxin. 
ACT_SITE   47    47        Cysteine sulfenic acid (-SOH) intermediate (By similarity). 
MOD_RES   193   193        Phosphothreonine. 
MOD_RES   194   194        Phosphoserine. 
DISULFID   47    47        Interchain (with C-168); in linked form (By similarity). 
DISULFID   168   168        Interchain (with C-47); in linked form (By similarity). 
Sequence information
Length: 194 AA [This is the length of the unprocessed precursor] Molecular weight: 21738 Da [This is the MW of the unprocessed precursor] CRC64: 93ED319BE144E8D1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPQLQKPAPA FAGTAVVNGV FKDIKLSDYK GKYLVLFFYP LDFTFVCPTE IIAFSESAAE 

        70         80         90        100        110        120 
FRKINCEVIG CSTDSQFTHL AWINTPRKQG GLGSMDIPLL ADKSMKVARD YGVLDEETGI 

       130        140        150        160        170        180 
PFRGLFIIDD KQNLRQITVN DLPVGRSVEE TLRLVQAFQY TDKYGEVCPA NWKPGQKTMV 

       190 
ADPTKSKEYF ETTS 

Q9V3P0 in FASTA format

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