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Superoxide dismutase [Mn] 1, mitochondrial (EC 1.15.1.1) (Protein MANGANESE SUPEROXIDE DISMUTASE 1) (AtMSD1) (Protein MATERNAL EFFECT EMBRYO ARREST 33)

 SODM1_ARATH             Reviewed;         231 AA.
O81235; Q8LEP0; Q9SRK3;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
20-JUN-2002, sequence version 2.
25-OCT-2017, entry version 143.
RecName: Full=Superoxide dismutase [Mn] 1, mitochondrial;
EC=1.15.1.1;
AltName: Full=Protein MANGANESE SUPEROXIDE DISMUTASE 1;
Short=AtMSD1;
AltName: Full=Protein MATERNAL EFFECT EMBRYO ARREST 33;
Flags: Precursor;
Name=MSD1; Synonyms=MEE3, SODA; OrderedLocusNames=At3g10920;
ORFNames=F9F8.26;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND GENE FAMILY.
STRAIN=cv. Columbia;
PubMed=9765550; DOI=10.1104/pp.118.2.637;
Kliebenstein D.J., Monde R.A., Last R.L.;
"Superoxide dismutase in Arabidopsis: an eclectic enzyme family with
disparate regulation and protein localization.";
Plant Physiol. 118:637-650(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=14671022; DOI=10.1105/tpc.016055;
Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
Millar A.H.;
"Experimental analysis of the Arabidopsis mitochondrial proteome
highlights signaling and regulatory components, provides assessment of
targeting prediction programs, and indicates plant-specific
mitochondrial proteins.";
Plant Cell 16:241-256(2004).
[7]
ENZYME REGULATION.
PubMed=17522887; DOI=10.1007/s00425-007-0547-6;
Su Z., Chai M.F., Lu P.L., An R., Chen J., Wang X.C.;
"AtMTM1, a novel mitochondrial protein, may be involved in activation
of the manganese-containing superoxide dismutase in Arabidopsis.";
Planta 226:1031-1039(2007).
[8]
INDUCTION BY SALT.
PubMed=18275461; DOI=10.1111/j.1399-3054.2007.01009.x;
Attia H., Arnaud N., Karray N., Lachaal M.;
"Long-term effects of mild salt stress on growth, ion accumulation and
superoxide dismutase expression of Arabidopsis rosette leaves.";
Physiol. Plantarum 132:293-305(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22092075; DOI=10.1021/pr200917t;
Aryal U.K., Krochko J.E., Ross A.R.;
"Identification of phosphoproteins in Arabidopsis thaliana leaves
using polyethylene glycol fractionation, immobilized metal-ion
affinity chromatography, two-dimensional gel electrophoresis and mass
spectrometry.";
J. Proteome Res. 11:425-437(2012).
-!- FUNCTION: Destroys superoxide anion radicals which are normally
produced within the cells and which are toxic to biological
systems.
-!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Activated by MTM1.
{ECO:0000269|PubMed:17522887}.
-!- SUBUNIT: Homotetramer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:14671022}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=O81235-1; Sequence=Displayed;
-!- INDUCTION: Induced by salt stress. {ECO:0000269|PubMed:18275461}.
-!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF061518; AAC24832.1; -; mRNA.
EMBL; AC009991; AAF01529.1; -; Genomic_DNA.
EMBL; CP002686; AEE74977.1; -; Genomic_DNA.
EMBL; AY072495; AAL66910.1; -; mRNA.
EMBL; AY059807; AAL24289.1; -; mRNA.
EMBL; AY085319; AAM62550.1; -; mRNA.
PIR; PA0012; PA0012.
PIR; T50827; T50827.
RefSeq; NP_187703.1; NM_111929.4. [O81235-1]
UniGene; At.11023; -.
PDB; 4C7U; X-ray; 1.95 A; A/B/C/D/E/F/G/H=30-231.
PDBsum; 4C7U; -.
ProteinModelPortal; O81235; -.
SMR; O81235; -.
STRING; 3702.AT3G10920.1; -.
iPTMnet; O81235; -.
PaxDb; O81235; -.
PRIDE; O81235; -.
EnsemblPlants; AT3G10920.1; AT3G10920.1; AT3G10920. [O81235-1]
GeneID; 820263; -.
Gramene; AT3G10920.1; AT3G10920.1; AT3G10920.
KEGG; ath:AT3G10920; -.
Araport; AT3G10920; -.
TAIR; locus:2085552; AT3G10920.
eggNOG; KOG0876; Eukaryota.
eggNOG; COG0605; LUCA.
HOGENOM; HOG000013583; -.
InParanoid; O81235; -.
KO; K04564; -.
OMA; KWGSFDK; -.
OrthoDB; EOG09360K54; -.
PhylomeDB; O81235; -.
Reactome; R-ATH-3299685; Detoxification of Reactive Oxygen Species.
PRO; PR:O81235; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; O81235; baseline and differential.
Genevisible; O81235; AT.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0005507; F:copper ion binding; IDA:TAIR.
GO; GO:0046872; F:metal ion binding; IDA:TAIR.
GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
GO; GO:0042742; P:defense response to bacterium; IEP:TAIR.
GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
GO; GO:0009651; P:response to salt stress; IEP:TAIR.
GO; GO:0010043; P:response to zinc ion; IEP:TAIR.
InterPro; IPR001189; Mn/Fe_SOD.
InterPro; IPR019833; Mn/Fe_SOD_BS.
InterPro; IPR019832; Mn/Fe_SOD_C.
InterPro; IPR019831; Mn/Fe_SOD_N.
InterPro; IPR036324; Mn/Fe_SOD_N_sf.
InterPro; IPR036314; SOD_C_sf.
Pfam; PF02777; Sod_Fe_C; 1.
Pfam; PF00081; Sod_Fe_N; 1.
PIRSF; PIRSF000349; SODismutase; 1.
PRINTS; PR01703; MNSODISMTASE.
SUPFAM; SSF46609; SSF46609; 1.
SUPFAM; SSF54719; SSF54719; 1.
PROSITE; PS00088; SOD_MN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Manganese;
Metal-binding; Mitochondrion; Oxidoreductase; Phosphoprotein;
Reference proteome; Transit peptide.
TRANSIT 1 29 Mitochondrion. {ECO:0000250}.
CHAIN 30 231 Superoxide dismutase [Mn] 1,
mitochondrial.
/FTId=PRO_0000032891.
METAL 55 55 Manganese. {ECO:0000250}.
METAL 103 103 Manganese. {ECO:0000250}.
METAL 192 192 Manganese. {ECO:0000250}.
METAL 196 196 Manganese. {ECO:0000250}.
MOD_RES 124 124 Phosphoserine.
{ECO:0000244|PubMed:22092075}.
CONFLICT 169 169 V -> F (in Ref. 1; AAC24832).
{ECO:0000305}.
CONFLICT 230 230 N -> S (in Ref. 5; AAM62550).
{ECO:0000305}.
HELIX 40 43 {ECO:0000244|PDB:4C7U}.
TURN 44 46 {ECO:0000244|PDB:4C7U}.
HELIX 49 57 {ECO:0000244|PDB:4C7U}.
HELIX 59 80 {ECO:0000244|PDB:4C7U}.
HELIX 83 88 {ECO:0000244|PDB:4C7U}.
HELIX 90 108 {ECO:0000244|PDB:4C7U}.
HELIX 113 115 {ECO:0000244|PDB:4C7U}.
TURN 116 118 {ECO:0000244|PDB:4C7U}.
HELIX 123 133 {ECO:0000244|PDB:4C7U}.
HELIX 136 149 {ECO:0000244|PDB:4C7U}.
STRAND 152 161 {ECO:0000244|PDB:4C7U}.
TURN 162 165 {ECO:0000244|PDB:4C7U}.
STRAND 166 173 {ECO:0000244|PDB:4C7U}.
HELIX 178 181 {ECO:0000244|PDB:4C7U}.
STRAND 185 192 {ECO:0000244|PDB:4C7U}.
HELIX 195 197 {ECO:0000244|PDB:4C7U}.
HELIX 199 202 {ECO:0000244|PDB:4C7U}.
HELIX 206 212 {ECO:0000244|PDB:4C7U}.
HELIX 213 216 {ECO:0000244|PDB:4C7U}.
HELIX 219 228 {ECO:0000244|PDB:4C7U}.
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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