ID   MSRA_DROME              Reviewed;         246 AA.
AC   P08761; Q86NL3; Q8IQM6; Q8IT52; Q9VUP3; Q9VUP4; Q9VUP5;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 2.
DT   25-NOV-2008, entry version 80.
DE   RecName: Full=Peptide methionine sulfoxide reductase;
DE            EC=1.8.4.11;
DE   AltName: Full=Peptide-methionine (S)-S-oxide reductase;
DE   AltName: Full=Methionine-S-sulfoxide reductase;
DE   AltName: Full=Ecdysone-induced protein 28/29 kDa;
GN   Name=Eip71CD; Synonyms=Eip28/29, MsrA; ORFNames=CG7266;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS EIP28 AND EIP29).
RC   STRAIN=Canton-S;
RX   MEDLINE=87060956; PubMed=3097323; DOI=10.1016/0022-2836(86)90492-4;
RA   Cherbas L., Schulz R.A., Koehler M.M.D., Savakis C., Cherbas P.;
RT   "Structure of the Eip28/29 gene, an ecdysone-inducible gene from
RT   Drosophila.";
RL   J. Mol. Biol. 189:617-631(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EIP28), AND FUNCTION.
RX   MEDLINE=22241889; PubMed=12145281; DOI=10.1074/jbc.M203496200;
RA   Kumar R.A., Koc A., Cerny R.L., Gladyshev V.N.;
RT   "Reaction mechanism, evolutionary analysis, and role of zinc in
RT   Drosophila methionine-R-sulfoxide reductase.";
RL   J. Biol. Chem. 277:37527-37535(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RX   MEDLINE=22426069; PubMed=12537572;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM EIP29).
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W.,
RA   Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA   George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
RA   Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA   Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA   Celniker S.E.;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has an important function as a repair enzyme for
CC       proteins that have been inactivated by oxidation. Catalyzes the
CC       reversible oxidation-reduction of methionine sulfoxide in proteins
CC       to methionine.
CC   -!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide +
CC       H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin.
CC   -!- CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H(2)O =
CC       L-methionine (S)-S-oxide + thioredoxin.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Eip28; Synonyms=A;
CC         IsoId=P08761-1; Sequence=Displayed;
CC       Name=Eip29; Synonyms=B;
CC         IsoId=P08761-2; Sequence=VSP_003279;
CC   -!- INDUCTION: By ecdysone.
CC   -!- SIMILARITY: Belongs to the msrA Met sulfoxide reductase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA28205.1; Type=Frameshift; Positions=222;
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DR   EMBL; X58286; CAA41223.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; X04024; CAA27657.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; X04024; CAA27658.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; X04521; CAA28205.1; ALT_FRAME; mRNA.
DR   EMBL; AF541958; AAN28311.1; -; mRNA.
DR   EMBL; AE014296; AAF49630.2; -; Genomic_DNA.
DR   EMBL; AE014296; AAN11775.1; -; Genomic_DNA.
DR   EMBL; BT004857; AAO45213.1; -; mRNA.
DR   PIR; A24254; A24254.
DR   RefSeq; NP_524085.2; -.
DR   RefSeq; NP_730047.1; -.
DR   UniGene; Dm.2545; -.
DR   HSSP; P54149; 1FVA.
DR   IntAct; P08761; -.
DR   Ensembl; CG7266; Drosophila melanogaster.
DR   GeneID; 39675; -.
DR   KEGG; dme:Dmel_CG7266; -.
DR   FlyBase; FBgn0000565; Eip71CD.
DR   BioCyc; DMEL-XXX-02:DMEL-XXX-02-016766-MON; -.
DR   NextBio; 814812; -.
DR   ArrayExpress; P08761; -.
DR   GermOnline; CG7266; Drosophila melanogaster.
DR   GO; GO:0008113; F:peptide-methionine-(S)-S-oxide reductase ac...; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0019538; P:protein metabolic process; IEA:InterPro.
DR   GO; GO:0035071; P:salivary gland cell autophagic cell death; IEP:FlyBase.
DR   GO; GO:0000096; P:sulfur amino acid metabolic process; NAS:FlyBase.
DR   InterPro; IPR002569; MsrA.
DR   Gene3D; G3DSA:3.30.1060.10; MsrA; 1.
DR   Pfam; PF01625; PMSR; 1.
DR   ProDom; PD003489; PMSR; 1.
DR   TIGRFAMs; TIGR00401; msrA; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Complete proteome; Oxidoreductase.
FT   CHAIN         1    246       Peptide methionine sulfoxide reductase.
FT                                /FTId=PRO_0000138629.
FT   VAR_SEQ      79     82       Missing (in isoform Eip29).
FT                                /FTId=VSP_003279.
FT   CONFLICT    218    219       EA -> V (in Ref. 5; AAO45213).
SQ   SEQUENCE   246 AA;  27698 MW;  8BB13B2092227D3E CRC64;
     MSLTITSSVT HPELKDLSTV RNEQKELNIS PVHDVNVTKA TATFGMGCFW GAESLYGATR
     GVLRTTVGYA GGSSDLPTYR KMGDHTEVLE IDYDPTVISF KELLDLFWNN HEYGLTTPIK
     RQYASLILYH DEEQKQVAHA SKLEEQERRA PEIITTEIAS KENFYPAEAY HQKYRLQGHK
     DLASSLNLSP KLLQTSYVAT KLNGYLAGVG GIEQFKAEAE TMGLTPTQRQ YCYYHVEQNE
     GQGLYC
//