GenomeNet

Database: UniProt
Entry: Q9LYK8
LinkDB: Q9LYK8
Original site: Q9LYK8 
ID   SODM2_ARATH             Reviewed;         241 AA.
AC   Q9LYK8; Q84W70;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   16-JAN-2019, entry version 131.
DE   RecName: Full=Superoxide dismutase [Mn] 2, mitochondrial;
DE            EC=1.15.1.1;
DE   AltName: Full=Protein MANGANESE SUPEROXIDE DISMUTASE 2;
DE            Short=AtMSD2;
DE   Flags: Precursor;
GN   Name=MSD2; OrderedLocusNames=At3g56350; ORFNames=F18O21_310;
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].
RC   STRAIN=cv. Columbia;
RA   Pan S.-M., Chung M.-H.;
RT   "The character of manganese superoxide dismutases in Arabidopsis.";
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
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] OF 8-241.
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   GENE FAMILY.
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).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems. {ECO:0000250}.
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   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; AY151395; AAN46857.1; -; mRNA.
DR   EMBL; AL163763; CAB87434.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79512.1; -; Genomic_DNA.
DR   EMBL; BT004168; AAO42188.1; -; mRNA.
DR   PIR; T47752; T47752.
DR   RefSeq; NP_191194.1; NM_115493.4.
DR   UniGene; At.34942; -.
DR   ProteinModelPortal; Q9LYK8; -.
DR   SMR; Q9LYK8; -.
DR   BioGrid; 10118; 1.
DR   STRING; 3702.AT3G56350.1; -.
DR   PaxDb; Q9LYK8; -.
DR   PRIDE; Q9LYK8; -.
DR   ProMEX; Q9LYK8; -.
DR   EnsemblPlants; AT3G56350.1; AT3G56350.1; AT3G56350.
DR   GeneID; 824802; -.
DR   Gramene; AT3G56350.1; AT3G56350.1; AT3G56350.
DR   KEGG; ath:AT3G56350; -.
DR   Araport; AT3G56350; -.
DR   TAIR; locus:2078356; AT3G56350.
DR   eggNOG; KOG0876; Eukaryota.
DR   eggNOG; COG0605; LUCA.
DR   HOGENOM; HOG000013583; -.
DR   InParanoid; Q9LYK8; -.
DR   KO; K04564; -.
DR   OMA; KPPHDPL; -.
DR   OrthoDB; 1353361at2759; -.
DR   PhylomeDB; Q9LYK8; -.
DR   BioCyc; ARA:AT3G56350-MONOMER; -.
DR   Reactome; R-ATH-3299685; Detoxification of Reactive Oxygen Species.
DR   PRO; PR:Q9LYK8; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LYK8; baseline and differential.
DR   Genevisible; Q9LYK8; AT.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR   GO; GO:0010227; P:floral organ abscission; 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   2: Evidence at transcript level;
KW   Complete proteome; Manganese; Metal-binding; Mitochondrion;
KW   Oxidoreductase; Reference proteome; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion. {ECO:0000250}.
FT   CHAIN         ?    241       Superoxide dismutase [Mn] 2,
FT                                mitochondrial. {ECO:0000255}.
FT                                /FTId=PRO_5000237373.
FT   METAL        60     60       Manganese. {ECO:0000250}.
FT   METAL       108    108       Manganese. {ECO:0000250}.
FT   METAL       197    197       Manganese. {ECO:0000250}.
FT   METAL       201    201       Manganese. {ECO:0000250}.
SQ   SEQUENCE   241 AA;  26892 MW;  22E5F2FB84DD99D4 CRC64;
     MTTTVIIIIF VAIFATTLHD ARGATMEPCL ESMKTASLPD LPYAYDALEP AISEEIMRLH
     HQKHHQTYVT QYNKALNSLR SAMADGDHSS VVKLQSLIKF NGGGHVNHAI FWKNLAPVHE
     GGGKPPHDPL ASAIDAHFGS LEGLIQKMNA EGAAVQGSGW VWFGLDRELK RLVVETTANQ
     DPLVTKGSHL VPLIGIDVWE HAYYPQYKNA RAEYLKNIWT VINWKYAADV FEKHTRDLDI
     N
//
DBGET integrated database retrieval system