ID A0A401RV98_CHIPU Unreviewed; 171 AA.
AC A0A401RV98;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=superoxide dismutase {ECO:0000256|ARBA:ARBA00012682};
DE EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682};
GN ORFNames=chiPu_0000469 {ECO:0000313|EMBL:GCC22084.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC22084.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC22084.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
CC {ECO:0000256|ARBA:ARBA00003917}.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000256|ARBA:ARBA00010457}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCC22084.1}.
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DR EMBL; BEZZ01000006; GCC22084.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401RV98; -.
DR STRING; 137246.A0A401RV98; -.
DR OMA; CGIILET; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProt.
DR CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 1.
DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR InterPro; IPR001424; SOD_Cu_Zn_dom.
DR PANTHER; PTHR10003:SF103; SUPEROXIDE DISMUTASE [CU-ZN]; 1.
DR PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR PRINTS; PR00068; CUZNDISMTASE.
DR SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
PE 3: Inferred from homology;
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023139};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000287033}.
FT DOMAIN 29..163
FT /note="Superoxide dismutase copper/zinc binding"
FT /evidence="ECO:0000259|Pfam:PF00080"
SQ SEQUENCE 171 AA; 18334 MW; A6F0132648988621 CRC64;
MEIKAVCVLK DQHDVYPYVH DLSDPISGVN GVVVFESQAN GQVLIKGTFT GLTRGKHGLH
VCTFGNLFNG YHSVGPHFNP RKRIHGGQQD NERHVGDLGN VEANEDGVAE FQIEDQLISL
SGIESIIGRA MVIQAEEDDL GKGENEESLS TGNAITGLAW GVIGIADVTA N
//
