SODM1_ARATH
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 03-AUG-2022, entry version 165.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; 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., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., 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., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., 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 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 reference
RT 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., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA 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 SCALE
RP 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 highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific 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 of
RT 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 BY
RP 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 using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT 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 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. {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 family.
CC {ECO:0000305}.
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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 PDB; 4C7U; X-ray; 1.95 A; A/B/C/D/E/F/G/H=30-231.
DR PDBsum; 4C7U; -.
DR AlphaFoldDB; O81235; -.
DR SMR; O81235; -.
DR BioGRID; 5597; 14.
DR STRING; 3702.AT3G10920.1; -.
DR iPTMnet; O81235; -.
DR PaxDb; O81235; -.
DR PRIDE; O81235; -.
DR ProteomicsDB; 232665; -. [O81235-1]
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 InParanoid; O81235; -.
DR OMA; KWGSFDK; -.
DR OrthoDB; 1353361at2759; -.
DR PhylomeDB; O81235; -.
DR PRO; PR:O81235; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O81235; baseline and differential.
DR Genevisible; O81235; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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; HDA:TAIR.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IDA:TAIR.
DR GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0010043; P:response to zinc ion; IEP:TAIR.
DR Gene3D; 1.10.287.990; -; 1.
DR Gene3D; 3.55.40.20; -; 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; Manganese; Metal-binding;
KW Mitochondrion; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 30..231
FT /note="Superoxide dismutase [Mn] 1, mitochondrial"
FT /id="PRO_0000032891"
FT BINDING 55
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT CONFLICT 169
FT /note="V -> F (in Ref. 1; AAC24832)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="N -> S (in Ref. 5; AAM62550)"
FT /evidence="ECO:0000305"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:4C7U"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:4C7U"
FT HELIX 49..57
FT /evidence="ECO:0007829|PDB:4C7U"
FT HELIX 59..80
FT /evidence="ECO:0007829|PDB:4C7U"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:4C7U"
FT HELIX 90..108
FT /evidence="ECO:0007829|PDB:4C7U"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:4C7U"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:4C7U"
FT HELIX 123..133
FT /evidence="ECO:0007829|PDB:4C7U"
FT HELIX 136..149
FT /evidence="ECO:0007829|PDB:4C7U"
FT STRAND 152..161
FT /evidence="ECO:0007829|PDB:4C7U"
FT TURN 162..165
FT /evidence="ECO:0007829|PDB:4C7U"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:4C7U"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:4C7U"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:4C7U"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:4C7U"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:4C7U"
FT HELIX 206..212
FT /evidence="ECO:0007829|PDB:4C7U"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:4C7U"
FT HELIX 219..228
FT /evidence="ECO:0007829|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
