Reviewed, UniProtKB/Swiss-Prot Q9V3P0 (PRDX1_DROME)

Names and origin

Protein names

Recommended name:
    Peroxiredoxin 1
    EC=1.11.1.15
Alternative name(s):
    Thioredoxin peroxidase
    Cytosolic thioredoxin peroxidase
      Short name=DmTPx-1
      Short name=DPx-4783

Gene names

Name:	Jafrac1
Synonyms:	TPX-1
ORF Names:	CG1633

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	194 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. As a reducing substrate, thioredoxin 2 is preferred over thioredoxin 1. Ref.2 Ref.7
Catalytic activity	2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
Subunit structure	Homodimer; disulfide-linked, upon oxidation By similarity. UniProtKB Q06830
Subcellular location	Cytoplasm. Ref.2
Developmental stage	Highly expressed during embryogenesis, weakly expressed during larval stages. Ref.2 Ref.7
Miscellaneous	The active site is the redox-active Cys-47 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-168-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin By similarity. UniProtKB Q06830 Irreversibly inactivated by overoxidation of Cys-47 (to Cys-SO3H) upon oxidative stress By similarity.
Sequence similarities	Belongs to the ahpC/TSA family. UniProtKB Q06830 Contains 1 thioredoxin domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Redox-active center
Molecular function	Antioxidant Oxidoreductase Peroxidase
PTM	Disulfide bond Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Ref.7 Inferred from direct assay. Source: UniProtKB hydrogen peroxide catabolic process Ref.2 Inferred from direct assay. Source: FlyBase oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Ref.2 Inferred from direct assay. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction. Source: IntAct thioredoxin peroxidase activity Ref.1 Ref.2 Ref.7 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q9VCJ3	1	EBI-82319,EBI-179284
	Q9VX10	1	EBI-82319,EBI-110159
MtnA	P04357	1	EBI-82319,EBI-172200
MtnB	P11956	1	EBI-82319,EBI-88468
XRCC1	Q9Y095	1	EBI-82319,EBI-165571

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 194	194	Peroxiredoxin 1		PRO_0000135085
Regions
	Domain	2 – 160	159	Thioredoxin
Sites
	Active site	47	1	Cysteine sulfenic acid (-SOH) intermediate By similarity UniProtKB Q06830
Amino acid modifications
	Modified residue	193	1	Phosphothreonine Ref.8
	Modified residue	194	1	Phosphoserine Ref.8
	Disulfide bond	47		Interchain (with C-168); in linked form By similarity
	Disulfide bond	168		Interchain (with C-47); in linked form By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9V3P0-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 93ED319BE144E8D1	FASTA	194	21,738
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Polypeptides differentially expressed in imaginal discs define the peroxiredoxin family of genes in Drosophila." Rodriguez J., Agudo M., Van Damme J., Vandekerckhove J., Santaren J.F. Eur. J. Biochem. 267:487-497(2000) [PubMed: 10632718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The peroxiredoxin gene family in Drosophila melanogaster." Radyuk S.N., Klichko V.I., Spinola B., Sohal R.S., Orr W.C. Free Radic. Biol. Med. 31:1090-1100(2001) [PubMed: 11677042] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[3]	"The genome sequence of Drosophila melanogaster." 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. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." 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. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[5]	"A Drosophila full-length cDNA resource." 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. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Ovary.
[6]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[7]	"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." Bauer H., Kanzok S.M., Schirmer R.H. J. Biol. Chem. 277:17457-17463(2002) [PubMed: 11877442] [Abstract] Cited for: FUNCTION, DEVELOPMENTAL STAGE.
[8]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-193 AND SER-194, MASS SPECTROMETRY. Tissue: Embryo.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF167098 mRNA. Translation: AAF42985.1. AF321615 mRNA. Translation: AAK06770.1. AF321616 mRNA. Translation: AAK06771.1. AE014298 Genomic DNA. Translation: AAF48253.1. AY070534 mRNA. Translation: AAL48005.1. BT014630 mRNA. Translation: AAT27254.1.
RefSeq	NP_477510.1. NP_727689.1.
UniGene	Dm.3464
3D structure databases
HSSP	HSSP built from PDB template 1QQ2 based on UniProtKB Q63716.
SMR	Q9V3P0. Positions 3-190.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:17916N.
IntAct	Q9V3P0. 5 interactions.
Proteomic databases
PRIDE	Q9V3P0.
Genome annotation databases
Ensembl	FBgn0040309. Drosophila melanogaster. [Contig view]
GeneID	53578.
KEGG	dme:Dmel_CG1633.
Organism-specific databases
FlyBase	FBgn0040309. Jafrac1.
Phylogenomic databases
HOGENOM	Q9V3P0.
OMA	Q9V3P0. AAEFRKI.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-001731-MON. DMEL-XXX-02:DMEL-XXX-02-001732-MON.
BRENDA	1.11.1.15. 48.
Gene expression databases
ArrayExpress	Q9V3P0.
GermOnline	CG1633. Drosophila melanogaster.
Family and domain databases
InterPro	IPR000866. Alkyl_hydroperoxide_Rdtase. IPR019479. Peroxiredoxin_C. IPR017936. Thioredoxin-like. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF10417. 1-cysPrx_C. 1 hit. PF00578. AhpC-TSA. 1 hit. [Graphical view]
PROSITE	PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	841448.

Entry information

Entry name

PRDX1_DROME

Accession

Primary (citable) accession number: Q9V3P0
Secondary accession number(s): Q0KHT0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2003
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project