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P15107

- SOD1B_XENLA

UniProt

P15107 - SOD1B_XENLA

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Protein

Superoxide dismutase [Cu-Zn] B

Gene

sod1-b

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Protein has several cofactor binding sites:
  • Cu cationNote: Binds 1 copper ion per subunit.
  • Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi45 – 451Copper; catalytic
Metal bindingi47 – 471Copper; catalytic
Metal bindingi62 – 621Copper; catalytic
Metal bindingi62 – 621Zinc; structural
Metal bindingi70 – 701Zinc; structural
Metal bindingi79 – 791Zinc; structural
Metal bindingi82 – 821Zinc; structural
Metal bindingi118 – 1181Copper; catalytic

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. superoxide dismutase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Cu-Zn] B (EC:1.15.1.1)
Short name:
XSODB
Gene namesi
Name:sod1-b
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6254670. sod1.

Subcellular locationi

Cytoplasm. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 151150Superoxide dismutase [Cu-Zn] BPRO_0000164077Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi6 – 61S-palmitoyl cysteineBy similarity
Disulfide bondi56 ↔ 144

Keywords - PTMi

Disulfide bond, Lipoprotein, Palmitate

Proteomic databases

PRIDEiP15107.

Interactioni

Subunit structurei

Homodimer, and heterodimer of Superoxide dismutase [Cu-Zn] A and B.1 Publication

Structurei

Secondary structure

1
151
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 97Combined sources
Beta strandi11 – 133Combined sources
Beta strandi15 – 239Combined sources
Beta strandi28 – 369Combined sources
Beta strandi39 – 4810Combined sources
Helixi55 – 595Combined sources
Beta strandi76 – 783Combined sources
Beta strandi82 – 898Combined sources
Beta strandi92 – 10110Combined sources
Beta strandi103 – 1064Combined sources
Beta strandi113 – 1208Combined sources
Beta strandi127 – 1293Combined sources
Helixi132 – 1354Combined sources
Beta strandi141 – 1466Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XSOX-ray1.49A/B2-151[»]
ProteinModelPortaliP15107.
SMRiP15107. Positions 2-151.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15107.

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Phylogenomic databases

HOVERGENiHBG000062.
KOiK04565.

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15107-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVKAVCVLAG SGDVKGVVHF EQQDEGAVSV EGKIEGLTDG LHGFHIHVFG
60 70 80 90 100
DNTNGCMSAG SHFNPENKNH GAPGDTDRHV GDLGNVTAEG GVAQFKITDS
110 120 130 140 150
LISLKGPNSI IGRTAVVHEK ADDLGKGGND ESLKTGNAGG RLACGVIGYS

P
Length:151
Mass (Da):15,418
Last modified:January 23, 2007 - v3
Checksum:i8DA6A8FDA1C7FB36
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611S → P AA sequence (PubMed:2751312)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51518 mRNA. Translation: CAA35890.1.
BC070696 mRNA. Translation: AAH70696.1.
PIRiS09568.
RefSeqiNP_001080933.1. NM_001087464.1.
UniGeneiXl.42.

Genome annotation databases

GeneIDi394274.
KEGGixla:394274.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51518 mRNA. Translation: CAA35890.1 .
BC070696 mRNA. Translation: AAH70696.1 .
PIRi S09568.
RefSeqi NP_001080933.1. NM_001087464.1.
UniGenei Xl.42.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1XSO X-ray 1.49 A/B 2-151 [» ]
ProteinModelPortali P15107.
SMRi P15107. Positions 2-151.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P15107.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 394274.
KEGGi xla:394274.

Organism-specific databases

CTDi 394274.
Xenbasei XB-GENE-6254670. sod1.

Phylogenomic databases

HOVERGENi HBG000062.
KOi K04565.

Miscellaneous databases

EvolutionaryTracei P15107.

Family and domain databases

Gene3Di 2.60.40.200. 1 hit.
InterProi IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view ]
Pfami PF00080. Sod_Cu. 1 hit.
[Graphical view ]
PRINTSi PR00068. CUZNDISMTASE.
SUPFAMi SSF49329. SSF49329. 1 hit.
PROSITEi PS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Xenopus laevis Cu,Zn superoxide dismutase B cDNA sequence."
    Carri M.T., Battistoni A., Mariottini P., Rotilio G.
    Nucleic Acids Res. 18:1641-1641(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Tadpole.
  2. NIH - Xenopus Gene Collection (XGC) project
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Gastrula.
  3. "Primary structure from amino acid and cDNA sequences of two Cu,Zn superoxide dismutase variants from Xenopus laevis."
    Schinina M.E., Barra D., Bossa F., Calabrese L., Montesano L., Carri M.T., Mariottini P., Amaldi F., Rotilio G.
    Arch. Biochem. Biophys. 272:507-515(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-151.
  4. "The Cu,Zn superoxide dismutase isoenzymes of Xenopus laevis: purification, identification of a heterodimer and differential heat sensitivity."
    Capo C.R., Polticelli F., Calabrese L., Schinina M.E., Carri M.T., Rotilio G.
    Biochem. Biophys. Res. Commun. 173:1186-1193(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-31, SUBUNIT.
  5. "Modelling the three-dimensional structure and electrostatic potential field of the two Cu,Zn superoxide dismutase variants from Xenopus laevis."
    Falconi M., Rotilio G., Desideri A.
    Proteins 10:149-155(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  6. "Three-dimensional structure of Xenopus laevis Cu,Zn superoxide dismutase b determined by X-ray crystallography at 1.5-A resolution."
    Djinovic Carugo K., Battistoni A., Carri M.T., Polticelli F., Desideri A., Rotilio G., Coda A., Wilson K.S., Bolognesi M.
    Acta Crystallogr. D 52:176-188(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS).

Entry informationi

Entry nameiSOD1B_XENLA
AccessioniPrimary (citable) accession number: P15107
Secondary accession number(s): Q5D025
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3