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UniProtKB/Swiss-Prot entry P08761


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

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Entry information
Entry name MSRA_DROME
Primary accession number P08761
Secondary accession numbers Q86NL3 Q8IQM6 Q8IT52 Q9VUP3 Q9VUP4 Q9VUP5
Integrated into Swiss-Prot on November 1, 1988
Sequence was last modified on March 15, 2004 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 81)
Name and origin of the protein
Protein name Peptide methionine sulfoxide reductase
Synonyms EC 1.8.4.11
Peptide-methionine (S)-S-oxide reductase
Methionine-S-sulfoxide reductase
Ecdysone-induced protein 28/29 kDa
Gene name
Name: Eip71CD
Synonyms: Eip28/29, MsrA
ORFNames: CG7266
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 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS EIP28 AND EIP29).
STRAIN=Canton-S;
DOI=10.1016/0022-2836(86)90492-4; PubMed=3097323 [NCBI, ExPASy, EBI, Israel, Japan]
Cherbas L., Schulz R.A., Koehler M.M.D., Savakis C., Cherbas P.;
"Structure of the Eip28/29 gene, an ecdysone-inducible gene from Drosophila.";
J. Mol. Biol. 189:617-631(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EIP28), AND FUNCTION.
DOI=10.1074/jbc.M203496200; PubMed=12145281 [NCBI, ExPASy, EBI, Israel, Japan]
Kumar R.A., Koc A., Cerny R.L., Gladyshev V.N.;
"Reaction mechanism, evolutionary analysis, and role of zinc in Drosophila methionine-R-sulfoxide reductase.";
J. Biol. Chem. 277:37527-37535(2002).
[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, AND ALTERNATIVE SPLICING.
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] (ISOFORM EIP29).
STRAIN=Berkeley;
TISSUE=Embryo;
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., 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.
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
X58286; CAA41223.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04024; CAA27657.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04024; CAA27658.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04521; CAA28205.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF541958; AAN28311.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014296; AAF49630.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014296; AAN11775.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT004857; AAO45213.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A24254; A24254.
RefSeq NP_524085.2; -.
NP_730047.1; -.
UniGene Dm.2545
3D structure databases
HSSP P54149; 1FVA. [HSSP ENTRY / PDB]
ModBase P08761.
Enzyme and pathway databases
BioCyc DMEL-XXX-02:DMEL-XXX-02-016766-MON; -.
Organism-specific databases
FlyBase FBgn0000565; Eip71CD.
Gene expression databases
ArrayExpress P08761; -.
GermOnline CG7266; Drosophila melanogaster.
Ontologies
GO
GO:0008113; Molecular function: peptide-methionine-(S)-S-oxide reductase activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019538; Biological process: protein metabolic process (inferred from electronic annotation from InterPro).
GO:0035071; Biological process: salivary gland cell autophagic cell death (inferred from expression pattern from FlyBase).
GO:0000096; Biological process: sulfur amino acid metabolic process (non-traceable author statement from FlyBase).
QuickGo view.
Family and domain databases
InterPro IPR002569; MsrA.
Graphical view of domain structure.
Gene3D G3DSA:3.30.1060.10; MsrA; 1.
Pfam PF01625; PMSR; 1.
Pfam graphical view of domain structure.
ProDom PD003489; PMSR; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00401; msrA; 1.
Genome annotation databases
Ensembl CG7266; Drosophila melanogaster. [Contig view]
GeneID 39675; -.
KEGG dme:Dmel_CG7266; -.
Other
NextBio 814812; -.
ProtoNet P08761.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Complete proteome; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   246  246     Peptide methionine sulfoxide reductase. PRO_0000138629
VAR_SEQ   79    82        Missing (in isoform Eip29). VSP_003279
CONFLICT   218   219        EA -> V (in Ref. 5; AAO45213). 
Sequence information
Length: 246 AA [This is the length of the unprocessed precursor] Molecular weight: 27698 Da [This is the MW of the unprocessed precursor] CRC64: 8BB13B2092227D3E [This is a checksum on the sequence]
        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 

P08761 in FASTA format

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View entry in raw text format (no links)
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