P13926 (SOD1A_XENLA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Superoxide dismutase [Cu-Zn] A
Short name=XSODA
EC=1.15.1.1

Gene names

Name:

sod1-a

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	151 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic activity	2 superoxide + 2 H+ = O2 + H2O2.
Cofactor	Binds 1 copper ion per subunit By similarity. Binds 1 zinc ion per subunit By similarity.
Subunit structure	Homodimer, and heterodimer of Superoxide dismutase [Cu-Zn] A and B. Ref.4
Subcellular location	Cytoplasm.
Developmental stage	Expressed both maternally and zygotically. Expression accumulates through oogenesis, remaining more or less constant at the beginning of embryogenesis, to slightly increase later on (at protein level).
Sequence similarities	Belongs to the Cu-Zn superoxide dismutase family.
Sequence caution	The sequence AAI22467.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Copper Metal-binding Zinc
Molecular function	Antioxidant Oxidoreductase
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	superoxide metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW superoxide dismutase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.3 Ref.4
	Chain	2 – 151	150	Superoxide dismutase [Cu-Zn] A		PRO_0000164076
Sites
	Metal binding	45	1	Copper; catalytic By similarity
	Metal binding	47	1	Copper; catalytic By similarity
	Metal binding	62	1	Copper; catalytic By similarity
	Metal binding	62	1	Zinc; structural By similarity
	Metal binding	70	1	Zinc; structural By similarity
	Metal binding	79	1	Zinc; structural By similarity
	Metal binding	82	1	Zinc; structural By similarity
	Metal binding	118	1	Copper; catalytic By similarity
Amino acid modifications
	Disulfide bond	56 ↔ 144		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P13926 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 6ABE0B23C120E77E	FASTA	151	15,721
	10 20 30 40 50 60 MVKAVCVLAG SGDVKGVVRF EQQDDGDVTV EGKIEGLTDG NHGFHIHVFG DNTNGCLSAG 70 80 90 100 110 120 PHFNPQNKNH GSPKDADRHV GDLGNVTAEG GVAQFKFTDP QISLKGERSI IGRTAVVHEK 130 140 150 QDDLGKGGDD ESLKTGNAGG RLACGVIGFC P

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Developmental expression of Cu,Zn superoxide dismutase in Xenopus. Constant level of the enzyme in oogenesis and embryogenesis." Montesano L., Carri M.T., Mariottini P., Amaldi F., Rotilio G. Eur. J. Biochem. 186:421-426(1989) [PubMed: 2598938] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPENTAL STAGE. Tissue: Oocyte.
[2]	NIH - Xenopus Gene Collection (XGC) project Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[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: 2751312] [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: 2268321] [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: 1896428] [Abstract] Cited for: 3D-STRUCTURE MODELING.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X16585 mRNA. Translation: CAA34602.1. BC108610 mRNA. Translation: AAI08611.1. BC122466 mRNA. Translation: AAI22467.1. Different initiation.
PIR	S05021.
UniGene	Xl.1162. Xl.85768.
3D structure databases
ProteinModelPortal	P13926.
SMR	P13926. Positions 2-151.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
Xenbase	XB-GENE-6252314. sod1.
Phylogenomic databases
HOVERGEN	HBG000062.
Family and domain databases
InterPro	IPR024134. SOD_Cu/Zn_/chaperones. IPR018152. SOD_Cu/Zn_BS. IPR001424. SOD_Cu_Zn_dom. [Graphical view]
Gene3D	G3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit.
PANTHER	PTHR10003. SOD_Cu_Zn. 1 hit.
Pfam	PF00080. Sod_Cu. 1 hit. [Graphical view]
PRINTS	PR00068. CUZNDISMTASE.
SUPFAM	SSF49329. SOD_Cu_Zn. 1 hit.
PROSITE	PS00087. SOD_CU_ZN_1. 1 hit. PS00332. SOD_CU_ZN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SOD1A_XENLA

Accession

Primary (citable) accession number: P13926
Secondary accession number(s): Q0P3T2, Q2VPM0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 23, 2007
Last modified:	July 27, 2011
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program