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P08761 (MSRA_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptide methionine sulfoxide reductase

EC=1.8.4.11
Alternative name(s):
Ecdysone-induced protein 28/29 kDa
Methionine-S-sulfoxide reductase
Peptide-methionine (S)-S-oxide reductase
Gene names
Name:Eip71CD
Synonyms:Eip28/29, MsrA
ORF Names:CG7266
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. Ref.2

Catalytic activity

Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin.

L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin.

Induction

By ecdysone.

Sequence similarities

Belongs to the MsrA Met sulfoxide reductase family.

Sequence caution

The sequence CAA28205.1 differs from that shown. Reason: Frameshift at position 222.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Eip28 (identifier: P08761-1)

Also known as: A;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Eip29 (identifier: P08761-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     79-82: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 246246Peptide methionine sulfoxide reductase
PRO_0000138629

Natural variations

Alternative sequence79 – 824Missing in isoform Eip29.
VSP_003279

Experimental info

Sequence conflict218 – 2192EA → V in AAO45213. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform Eip28 (A) [UniParc].

Last modified March 15, 2004. Version 2.
Checksum: 8BB13B2092227D3E

FASTA24627,698
        10         20         30         40         50         60 
MSLTITSSVT HPELKDLSTV RNEQKELNIS PVHDVNVTKA TATFGMGCFW GAESLYGATR 

        70         80         90        100        110        120 
GVLRTTVGYA GGSSDLPTYR KMGDHTEVLE IDYDPTVISF KELLDLFWNN HEYGLTTPIK 

       130        140        150        160        170        180 
RQYASLILYH DEEQKQVAHA SKLEEQERRA PEIITTEIAS KENFYPAEAY HQKYRLQGHK 

       190        200        210        220        230        240 
DLASSLNLSP KLLQTSYVAT KLNGYLAGVG GIEQFKAEAE TMGLTPTQRQ YCYYHVEQNE 


GQGLYC 

« Hide

Isoform Eip29 (B) [UniParc].

Checksum: 29C4EE6B9742E50F
Show »

FASTA24227,119

References

« Hide 'large scale' references
[1]"Structure of the Eip28/29 gene, an ecdysone-inducible gene from Drosophila."
Cherbas L., Schulz R.A., Koehler M.M.D., Savakis C., Cherbas P.
J. Mol. Biol. 189:617-631(1986) [PubMed: 3097323] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS EIP28 AND EIP29).
Strain: Canton-S.
[2]"Reaction mechanism, evolutionary analysis, and role of zinc in Drosophila methionine-R-sulfoxide reductase."
Kumar R.A., Koc A., Cerny R.L., Gladyshev V.N.
J. Biol. Chem. 277:37527-37535(2002) [PubMed: 12145281] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EIP28), FUNCTION.
[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. expand/collapse author list , 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. expand/collapse author list , 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, ALTERNATIVE SPLICING.
Strain: Berkeley.
[5]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM EIP29).
Strain: Berkeley.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X58286 Genomic DNA. Translation: CAA41223.1. Frameshift.
X04024 Genomic DNA. Translation: CAA27657.1. Frameshift.
X04024 Genomic DNA. Translation: CAA27658.1. Frameshift.
X04521 mRNA. Translation: CAA28205.1. Frameshift.
AF541958 mRNA. Translation: AAN28311.1.
AE014296 Genomic DNA. Translation: AAF49630.2.
AE014296 Genomic DNA. Translation: AAN11775.1.
BT004857 mRNA. Translation: AAO45213.1.
PIRA24254.
RefSeqNP_524085.2. NM_079361.2.
NP_730047.1. NM_168622.1.
UniGeneDm.2545.

3D structure databases

ProteinModelPortalP08761.
SMRP08761. Positions 7-242.
ModBaseSearch...

Protein-protein interaction databases

IntActP08761. 2 interactions.
MINTMINT-345143.
STRINGP08761.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0075553; FBpp0075308; FBgn0000565.
GeneID39675.
KEGGdme:Dmel_CG7266.

Organism-specific databases

CTD39675.
FlyBaseFBgn0000565. Eip71CD.

Phylogenomic databases

eggNOGinNOG04478.
InParanoidP08761.
OMAVGNQYRS.
OrthoDBEOG4SQVCR.
PhylomeDBP08761.

Enzyme and pathway databases

BRENDA1.8.4.11. 1994.

Gene expression databases

ArrayExpressP08761.
BgeeP08761.
GermOnlineCG7266. Drosophila melanogaster.

Family and domain databases

InterProIPR002569. Peptide_Met_Sox_Rdtase_MsrA.
[Graphical view]
Gene3DG3DSA:3.30.1060.10. MsrA. 1 hit.
KOK07304.
PfamPF01625. PMSR. 1 hit.
[Graphical view]
SUPFAMSSF55068. MsrA. 1 hit.
TIGRFAMsTIGR00401. MsrA. 1 hit.
ProtoNetSearch...

Other

NextBio814812.

Entry information

Entry nameMSRA_DROME
AccessionPrimary (citable) accession number: P08761
Secondary accession number(s): Q86NL3 expand/collapse secondary AC list , Q8IQM6, Q8IT52, Q9VUP3, Q9VUP4, Q9VUP5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: March 15, 2004
Last modified: January 25, 2012
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families