SODC_MOUSE
ID SODC_MOUSE Reviewed; 154 AA.
AC P08228;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 224.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1;
GN Name=Sod1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SWR/J; TISSUE=Liver;
RX PubMed=3362683; DOI=10.1093/nar/16.6.2728;
RA Bewley G.C.;
RT "cDNA and deduced amino acid sequence of murine Cu-Zn superoxide
RT dismutase.";
RL Nucleic Acids Res. 16:2728-2728(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2022332; DOI=10.1016/0378-1119(91)90126-v;
RA Benedetto M.T., Anzai Y., Gordon J.W.;
RT "Isolation and analysis of the mouse genomic sequence encoding Cu(2+)-Zn2+
RT superoxide dismutase.";
RL Gene 99:191-195(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Ovary, Urinary bladder, and Uterus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver, Mammary gland, and Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 4-23.
RX PubMed=2391363; DOI=10.1083/jcb.111.3.1217;
RA Pluthero F.G., Shreeve M., Eskinazi D., van der Gaag H., Huang K.S.,
RA Hulmes J.D., Blum M., Axelrad A.A.;
RT "Purification of an inhibitor of erythroid progenitor cell cycling and
RT antagonist to interleukin 3 from mouse marrow cell supernatants and its
RT identification as cytosolic superoxide dismutase.";
RL J. Cell Biol. 111:1217-1223(1990).
RN [6]
RP PROTEIN SEQUENCE OF 11-24 AND 104-116, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Klug S., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP DISRUPTION PHENOTYPE.
RC TISSUE=Liver;
RX PubMed=21420488; DOI=10.1016/j.freeradbiomed.2011.03.018;
RA Wang S.K., Weaver J.D., Zhang S., Lei X.G.;
RT "Knockout of SOD1 promotes conversion of selenocysteine to dehydroalanine
RT in murine hepatic GPX1 protein.";
RL Free Radic. Biol. Med. 51:197-204(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-123, SUCCINYLATION
RP [LARGE SCALE ANALYSIS] AT LYS-4; LYS-10; LYS-92; LYS-123 AND LYS-137,
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-154 IN COMPLEX WITH ZINC.
RX PubMed=20727846; DOI=10.1016/j.abb.2010.08.014;
RA Seetharaman S.V., Taylor A.B., Holloway S., Hart P.J.;
RT "Structures of mouse SOD1 and human/mouse SOD1 chimeras.";
RL Arch. Biochem. Biophys. 503:183-190(2010).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC 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=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20727846}.
CC -!- INTERACTION:
CC P08228; P99029: Prdx5; NbExp=2; IntAct=EBI-1635090, EBI-2735704;
CC P08228; P63001: Rac1; NbExp=4; IntAct=EBI-1635090, EBI-413646;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.
CC -!- PTM: Palmitoylation helps nuclear targeting and decreases catalytic
CC activity. {ECO:0000250}.
CC -!- PTM: Succinylation, adjacent to copper catalytic site, probably
CC inhibits activity. Desuccinylation by SIRT5 enhances activity.
CC {ECO:0000250|UniProtKB:P00441}.
CC -!- DISRUPTION PHENOTYPE: 40% reduction in hepatic GPX1 activity.
CC {ECO:0000269|PubMed:21420488}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X06683; CAA29880.1; -; mRNA.
DR EMBL; M60798; AAA40121.1; -; Genomic_DNA.
DR EMBL; M60794; AAA40121.1; JOINED; Genomic_DNA.
DR EMBL; M60795; AAA40121.1; JOINED; Genomic_DNA.
DR EMBL; M60796; AAA40121.1; JOINED; Genomic_DNA.
DR EMBL; M60797; AAA40121.1; JOINED; Genomic_DNA.
DR EMBL; M35725; AAA37518.1; -; mRNA.
DR EMBL; AK020624; BAB32154.1; -; mRNA.
DR EMBL; AK077284; BAC36730.1; -; mRNA.
DR EMBL; BC002066; AAH02066.1; -; mRNA.
DR EMBL; BC048874; AAH48874.1; -; mRNA.
DR EMBL; BC086886; AAH86886.1; -; mRNA.
DR CCDS; CCDS37395.1; -.
DR PIR; JQ0915; JQ0915.
DR RefSeq; NP_035564.1; NM_011434.1.
DR PDB; 3GTT; X-ray; 2.40 A; A/B/C/D/E/F=2-154.
DR PDB; 3GTV; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=82-154.
DR PDB; 3LTV; X-ray; 2.45 A; A/B/C/D/E/F=2-81.
DR PDBsum; 3GTT; -.
DR PDBsum; 3GTV; -.
DR PDBsum; 3LTV; -.
DR AlphaFoldDB; P08228; -.
DR SMR; P08228; -.
DR BioGRID; 203387; 38.
DR ComplexPortal; CPX-2898; [Cu-Zn] Superoxide dismutase complex.
DR DIP; DIP-48691N; -.
DR IntAct; P08228; 49.
DR MINT; P08228; -.
DR STRING; 10090.ENSMUSP00000023707; -.
DR iPTMnet; P08228; -.
DR PhosphoSitePlus; P08228; -.
DR SwissPalm; P08228; -.
DR DOSAC-COBS-2DPAGE; P08228; -.
DR REPRODUCTION-2DPAGE; IPI00130589; -.
DR REPRODUCTION-2DPAGE; P08228; -.
DR SWISS-2DPAGE; P08228; -.
DR UCD-2DPAGE; P08228; -.
DR CPTAC; non-CPTAC-3945; -.
DR EPD; P08228; -.
DR jPOST; P08228; -.
DR MaxQB; P08228; -.
DR PaxDb; P08228; -.
DR PeptideAtlas; P08228; -.
DR PRIDE; P08228; -.
DR ProteomicsDB; 258707; -.
DR Antibodypedia; 786; 1525 antibodies from 50 providers.
DR DNASU; 20655; -.
DR Ensembl; ENSMUST00000023707; ENSMUSP00000023707; ENSMUSG00000022982.
DR GeneID; 20655; -.
DR KEGG; mmu:20655; -.
DR UCSC; uc007zvz.1; mouse.
DR CTD; 6647; -.
DR MGI; MGI:98351; Sod1.
DR VEuPathDB; HostDB:ENSMUSG00000022982; -.
DR eggNOG; KOG0441; Eukaryota.
DR GeneTree; ENSGT00940000155551; -.
DR HOGENOM; CLU_056632_4_1_1; -.
DR InParanoid; P08228; -.
DR OMA; AQRGFHI; -.
DR OrthoDB; 1574423at2759; -.
DR PhylomeDB; P08228; -.
DR TreeFam; TF105131; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR BioGRID-ORCS; 20655; 30 hits in 72 CRISPR screens.
DR ChiTaRS; Sod1; mouse.
DR EvolutionaryTrace; P08228; -.
DR PRO; PR:P08228; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P08228; protein.
DR Bgee; ENSMUSG00000022982; Expressed in otolith organ and 271 other tissues.
DR Genevisible; P08228; MM.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0032839; C:dendrite cytoplasm; ISS:UniProtKB.
DR GO; GO:0031045; C:dense core granule; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0051087; F:chaperone binding; ISS:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030346; F:protein phosphatase 2B binding; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0007568; P:aging; IMP:MGI.
DR GO; GO:0008089; P:anterograde axonal transport; IMP:BHF-UCL.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; IMP:MGI.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:MGI.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IMP:MGI.
DR GO; GO:0007566; P:embryo implantation; IMP:MGI.
DR GO; GO:0006749; P:glutathione metabolic process; IMP:MGI.
DR GO; GO:0060047; P:heart contraction; IMP:MGI.
DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:MGI.
DR GO; GO:0002262; P:myeloid cell homeostasis; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
DR GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0051093; P:negative regulation of developmental process; IMP:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IGI:ARUK-UCL.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR GO; GO:2000242; P:negative regulation of reproductive process; IMP:MGI.
DR GO; GO:0060052; P:neurofilament cytoskeleton organization; IMP:MGI.
DR GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
DR GO; GO:0032287; P:peripheral nervous system myelin maintenance; IMP:MGI.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISS:UniProtKB.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:MGI.
DR GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IGI:ARUK-UCL.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; ISO:MGI.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR GO; GO:0043087; P:regulation of GTPase activity; ISO:MGI.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:UniProtKB.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0045859; P:regulation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0060087; P:relaxation of vascular associated smooth muscle; IMP:MGI.
DR GO; GO:0019430; P:removal of superoxide radicals; IMP:MGI.
DR GO; GO:0048678; P:response to axon injury; IMP:MGI.
DR GO; GO:0046688; P:response to copper ion; ISO:MGI.
DR GO; GO:0045471; P:response to ethanol; IMP:MGI.
DR GO; GO:0009408; P:response to heat; IMP:MGI.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:MGI.
DR GO; GO:0031667; P:response to nutrient levels; ISO:MGI.
DR GO; GO:0010033; P:response to organic substance; ISS:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IDA:MGI.
DR GO; GO:0000302; P:response to reactive oxygen species; IMP:MGI.
DR GO; GO:0000303; P:response to superoxide; IMP:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR GO; GO:0001895; P:retina homeostasis; IMP:MGI.
DR GO; GO:0008090; P:retrograde axonal transport; IMP:BHF-UCL.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0042554; P:superoxide anion generation; IDA:MGI.
DR GO; GO:0006801; P:superoxide metabolic process; IMP:MGI.
DR GO; GO:0019226; P:transmission of nerve impulse; IMP:MGI.
DR CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR Gene3D; 2.60.40.200; -; 1.
DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR InterPro; IPR018152; SOD_Cu/Zn_BS.
DR InterPro; IPR001424; SOD_Cu_Zn_dom.
DR PANTHER; PTHR10003; PTHR10003; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR PRINTS; PR00068; CUZNDISMTASE.
DR SUPFAM; SSF49329; SSF49329; 1.
DR PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Antioxidant; Copper; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Lipoprotein; Metal-binding;
KW Nucleus; Oxidoreductase; Palmitate; Phosphoprotein; Reference proteome;
KW Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CHAIN 2..154
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000164062"
FT BINDING 47
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:20727846"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:20727846"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:20727846"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:20727846"
FT BINDING 121
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 4
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 10
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 92
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00441"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07632"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 123
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 123
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 137
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 137
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT LIPID 7
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT DISULFID 58..147
FT /evidence="ECO:0000250"
FT CONFLICT 102
FT /note="D -> H (in Ref. 2; AAA40121)"
FT /evidence="ECO:0000305"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:3GTT"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:3GTT"
FT STRAND 16..25
FT /evidence="ECO:0007829|PDB:3GTT"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:3GTT"
FT STRAND 41..50
FT /evidence="ECO:0007829|PDB:3GTT"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:3GTT"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:3GTT"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:3LTV"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:3GTT"
FT STRAND 96..109
FT /evidence="ECO:0007829|PDB:3GTV"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:3GTV"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:3GTV"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:3GTV"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:3GTV"
SQ SEQUENCE 154 AA; 15943 MW; CAE548C66043BAC4 CRC64;
MAMKAVCVLK GDGPVQGTIH FEQKASGEPV VLSGQITGLT EGQHGFHVHQ YGDNTQGCTS
AGPHFNPHSK KHGGPADEER HVGDLGNVTA GKDGVANVSI EDRVISLSGE HSIIGRTMVV
HEKQDDLGKG GNEESTKTGN AGSRLACGVI GIAQ
