GenomeNet

Database: UniProt
Entry: O81235
LinkDB: O81235
Original site: O81235 
ID   SODM1_ARATH             Reviewed;         231 AA.
AC   O81235; Q8LEP0; Q9SRK3;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2002, sequence version 2.
DT   16-JAN-2019, entry version 150.
DE   RecName: Full=Superoxide dismutase [Mn] 1, mitochondrial;
DE            EC=1.15.1.1;
DE   AltName: Full=Protein MANGANESE SUPEROXIDE DISMUTASE 1;
DE            Short=AtMSD1;
DE   AltName: Full=Protein MATERNAL EFFECT EMBRYO ARREST 33;
DE   Flags: Precursor;
GN   Name=MSD1; Synonyms=MEE3, SODA; OrderedLocusNames=At3g10920;
GN   ORFNames=F9F8.26;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND GENE FAMILY.
RC   STRAIN=cv. Columbia;
RX   PubMed=9765550; DOI=10.1104/pp.118.2.637;
RA   Kliebenstein D.J., Monde R.A., Last R.L.;
RT   "Superoxide dismutase in Arabidopsis: an eclectic enzyme family with
RT   disparate regulation and protein localization.";
RL   Plant Physiol. 118:637-650(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
RA   Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA   Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA   De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA   Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA   Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA   Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA   Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA   Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA   Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA   Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA   Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
RA   Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA   Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA   Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA   Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA   Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA   Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA   Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA   Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:820-822(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
RP   SCALE ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=14671022; DOI=10.1105/tpc.016055;
RA   Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA   Millar A.H.;
RT   "Experimental analysis of the Arabidopsis mitochondrial proteome
RT   highlights signaling and regulatory components, provides assessment of
RT   targeting prediction programs, and indicates plant-specific
RT   mitochondrial proteins.";
RL   Plant Cell 16:241-256(2004).
RN   [7]
RP   ACTIVITY REGULATION.
RX   PubMed=17522887; DOI=10.1007/s00425-007-0547-6;
RA   Su Z., Chai M.F., Lu P.L., An R., Chen J., Wang X.C.;
RT   "AtMTM1, a novel mitochondrial protein, may be involved in activation
RT   of the manganese-containing superoxide dismutase in Arabidopsis.";
RL   Planta 226:1031-1039(2007).
RN   [8]
RP   INDUCTION BY SALT.
RX   PubMed=18275461; DOI=10.1111/j.1399-3054.2007.01009.x;
RA   Attia H., Arnaud N., Karray N., Lachaal M.;
RT   "Long-term effects of mild salt stress on growth, ion accumulation and
RT   superoxide dismutase expression of Arabidopsis rosette leaves.";
RL   Physiol. Plantarum 132:293-305(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22092075; DOI=10.1021/pr200917t;
RA   Aryal U.K., Krochko J.E., Ross A.R.;
RT   "Identification of phosphoproteins in Arabidopsis thaliana leaves
RT   using polyethylene glycol fractionation, immobilized metal-ion
RT   affinity chromatography, two-dimensional gel electrophoresis and mass
RT   spectrometry.";
RL   J. Proteome Res. 11:425-437(2012).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by MTM1.
CC       {ECO:0000269|PubMed:17522887}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000269|PubMed:14671022}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=O81235-1; Sequence=Displayed;
CC   -!- INDUCTION: Induced by salt stress. {ECO:0000269|PubMed:18275461}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; AF061518; AAC24832.1; -; mRNA.
DR   EMBL; AC009991; AAF01529.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74977.1; -; Genomic_DNA.
DR   EMBL; AY072495; AAL66910.1; -; mRNA.
DR   EMBL; AY059807; AAL24289.1; -; mRNA.
DR   EMBL; AY085319; AAM62550.1; -; mRNA.
DR   PIR; PA0012; PA0012.
DR   PIR; T50827; T50827.
DR   RefSeq; NP_187703.1; NM_111929.4. [O81235-1]
DR   UniGene; At.11023; -.
DR   PDB; 4C7U; X-ray; 1.95 A; A/B/C/D/E/F/G/H=30-231.
DR   PDBsum; 4C7U; -.
DR   ProteinModelPortal; O81235; -.
DR   SMR; O81235; -.
DR   STRING; 3702.AT3G10920.1; -.
DR   iPTMnet; O81235; -.
DR   PaxDb; O81235; -.
DR   PRIDE; O81235; -.
DR   EnsemblPlants; AT3G10920.1; AT3G10920.1; AT3G10920. [O81235-1]
DR   GeneID; 820263; -.
DR   Gramene; AT3G10920.1; AT3G10920.1; AT3G10920. [O81235-1]
DR   KEGG; ath:AT3G10920; -.
DR   Araport; AT3G10920; -.
DR   TAIR; locus:2085552; AT3G10920.
DR   eggNOG; KOG0876; Eukaryota.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   InParanoid; O81235; -.
DR   KO; K04564; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; 1353361at2759; -.
DR   PhylomeDB; O81235; -.
DR   Reactome; R-ATH-3299685; Detoxification of Reactive Oxygen Species.
DR   PRO; PR:O81235; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; O81235; baseline and differential.
DR   Genevisible; O81235; AT.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0005507; F:copper ion binding; IDA:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IDA:TAIR.
DR   GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR   GO; GO:0042742; P:defense response to bacterium; IEP:TAIR.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR   GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR   GO; GO:0010043; P:response to zinc ion; IEP:TAIR.
DR   Gene3D; 1.10.287.990; -; 1.
DR   Gene3D; 2.40.500.20; -; 1.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019833; Mn/Fe_SOD_BS.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Complete proteome; Manganese;
KW   Metal-binding; Mitochondrion; Oxidoreductase; Phosphoprotein;
KW   Reference proteome; Transit peptide.
FT   TRANSIT       1     29       Mitochondrion. {ECO:0000250}.
FT   CHAIN        30    231       Superoxide dismutase [Mn] 1,
FT                                mitochondrial.
FT                                /FTId=PRO_0000032891.
FT   METAL        55     55       Manganese. {ECO:0000250}.
FT   METAL       103    103       Manganese. {ECO:0000250}.
FT   METAL       192    192       Manganese. {ECO:0000250}.
FT   METAL       196    196       Manganese. {ECO:0000250}.
FT   MOD_RES     124    124       Phosphoserine.
FT                                {ECO:0000244|PubMed:22092075}.
FT   CONFLICT    169    169       V -> F (in Ref. 1; AAC24832).
FT                                {ECO:0000305}.
FT   CONFLICT    230    230       N -> S (in Ref. 5; AAM62550).
FT                                {ECO:0000305}.
FT   HELIX        40     43       {ECO:0000244|PDB:4C7U}.
FT   TURN         44     46       {ECO:0000244|PDB:4C7U}.
FT   HELIX        49     57       {ECO:0000244|PDB:4C7U}.
FT   HELIX        59     80       {ECO:0000244|PDB:4C7U}.
FT   HELIX        83     88       {ECO:0000244|PDB:4C7U}.
FT   HELIX        90    108       {ECO:0000244|PDB:4C7U}.
FT   HELIX       113    115       {ECO:0000244|PDB:4C7U}.
FT   TURN        116    118       {ECO:0000244|PDB:4C7U}.
FT   HELIX       123    133       {ECO:0000244|PDB:4C7U}.
FT   HELIX       136    149       {ECO:0000244|PDB:4C7U}.
FT   STRAND      152    161       {ECO:0000244|PDB:4C7U}.
FT   TURN        162    165       {ECO:0000244|PDB:4C7U}.
FT   STRAND      166    173       {ECO:0000244|PDB:4C7U}.
FT   HELIX       178    181       {ECO:0000244|PDB:4C7U}.
FT   STRAND      185    192       {ECO:0000244|PDB:4C7U}.
FT   HELIX       195    197       {ECO:0000244|PDB:4C7U}.
FT   HELIX       199    202       {ECO:0000244|PDB:4C7U}.
FT   HELIX       206    212       {ECO:0000244|PDB:4C7U}.
FT   HELIX       213    216       {ECO:0000244|PDB:4C7U}.
FT   HELIX       219    228       {ECO:0000244|PDB:4C7U}.
SQ   SEQUENCE   231 AA;  25444 MW;  2DBD5560A9E8AD7D CRC64;
     MAIRCVASRK TLAGLKETSS RLLRIRGIQT FTLPDLPYDY GALEPAISGE IMQIHHQKHH
     QAYVTNYNNA LEQLDQAVNK GDASTVVKLQ SAIKFNGGGH VNHSIFWKNL APSSEGGGEP
     PKGSLGSAID AHFGSLEGLV KKMSAEGAAV QGSGWVWLGL DKELKKLVVD TTANQDPLVT
     KGGSLVPLVG IDVWEHAYYL QYKNVRPEYL KNVWKVINWK YASEVYEKEN N
//
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