CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000211
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Extracellular superoxide dismutase [Cu-Zn] 
Protein Synonyms/Alias
 EC-SOD 
Gene Name
 Sod3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
203AGEDDLGKGGNQASLubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen (By similarity). 
Sequence Annotation
 METAL 128 128 Copper; catalytic (By similarity).
 METAL 130 130 Copper; catalytic (By similarity).
 METAL 145 145 Copper; catalytic (By similarity).
 METAL 145 145 Zinc; structural (By similarity).
 METAL 153 153 Zinc; structural (By similarity).
 METAL 156 156 Zinc; structural (By similarity).
 METAL 159 159 Zinc; structural (By similarity).
 METAL 195 195 Copper; catalytic (By similarity).
 CARBOHYD 121 121 N-linked (GlcNAc...) (Potential).
 DISULFID 77 222 By similarity.
 DISULFID 139 221 By similarity.  
Keyword
 3D-structure; Antioxidant; Complete proteome; Copper; Direct protein sequencing; Disulfide bond; Glycoprotein; Metal-binding; Oxidoreductase; Reference proteome; Secreted; Signal; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 251 AA 
Protein Sequence
MLAFLFYGLL LAACGSVTMS NPGESSFDLA DRLDPVEKID RLDLVEKIGD THAKVLEIWM 60
ELGRRREVDA AEMHAICRVQ PSATLPPDQP QITGLVLFRQ LGPGSRLEAY FSLEGFPAEQ 120
NASNRAIHVH EFGDLSQGCD STGPHYNPME VPHPQHPGDF GNFVVRNGQL WRHRVGLTAS 180
LAGPHAILGR SVVVHAGEDD LGKGGNQASL QNGNAGRRLA CCVVGTSSSA AWESQTKERK 240
KRRRESECKT T 251 
Gene Ontology
 GO:0005829; C:cytosol; IBA:RefGenome.
 GO:0031012; C:extracellular matrix; IEA:Compara.
 GO:0005615; C:extracellular space; IDA:MGI.
 GO:0005739; C:mitochondrion; IBA:RefGenome.
 GO:0005634; C:nucleus; IBA:RefGenome.
 GO:0005802; C:trans-Golgi network; IDA:MGI.
 GO:0005507; F:copper ion binding; IBA:RefGenome.
 GO:0004784; F:superoxide dismutase activity; IDA:MGI.
 GO:0008270; F:zinc ion binding; IBA:RefGenome.
 GO:0019430; P:removal of superoxide radicals; IBA:RefGenome.
 GO:0046688; P:response to copper ion; IEA:Compara.
 GO:0001666; P:response to hypoxia; IMP:MGI. 
Interpro
 IPR024134; SOD_Cu/Zn_/chaperones.
 IPR018152; SOD_Cu/Zn_BS.
 IPR024141; SOD_Cu/Zn_extracel.
 IPR001424; SOD_Cu_Zn_dom. 
Pfam
 PF00080; Sod_Cu 
SMART
  
PROSITE
 PS00087; SOD_CU_ZN_1
 PS00332; SOD_CU_ZN_2 
PRINTS
 PR00068; CUZNDISMTASE.