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Database: UniProt
Entry: A0A077DB40_LARCR
LinkDB: A0A077DB40_LARCR
Original site: A0A077DB40_LARCR 
ID   A0A077DB40_LARCR        Unreviewed;       154 AA.
AC   A0A077DB40;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=SOD1 {ECO:0000313|EMBL:AIL29307.1};
GN   ORFNames=D5F01_LYC13505 {ECO:0000313|EMBL:KAE8287461.1};
OS   Larimichthys crocea (Large yellow croaker) (Pseudosciaena crocea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Sciaenidae; Larimichthys.
OX   NCBI_TaxID=215358 {ECO:0000313|EMBL:AIL29307.1};
RN   [1] {ECO:0000313|EMBL:AIL29307.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=EC01 {ECO:0000313|EMBL:AIL29307.1};
RC   TISSUE=Liver {ECO:0000313|EMBL:AIL29307.1};
RX   PubMed=25652289; DOI=10.1016/j.fsi.2015.01.032;
RA   Liu H., He J., Chi C., Gu Y.;
RT   "Identification and analysis of icCu/Zn-SOD, Mn-SOD and ecCu/Zn-SOD in
RT   superoxide dismutase multigene family of Pseudosciaena crocea.";
RL   Fish Shellfish Immunol. 43:491-501(2015).
RN   [2] {ECO:0000313|EMBL:KAE8287461.1, ECO:0000313|Proteomes:UP000424527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMULYC20181020 {ECO:0000313|EMBL:KAE8287461.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:KAE8287461.1};
RA   Xiao S.;
RT   "Chromosome genome assembly for large yellow croaker.";
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|ARBA:ARBA00003917, ECO:0000256|RuleBase:RU000393}.
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         Evidence={ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00010457, ECO:0000256|RuleBase:RU000393}.
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DR   EMBL; KJ908287; AIL29307.1; -; mRNA.
DR   EMBL; REGW02000013; KAE8287461.1; -; Genomic_DNA.
DR   RefSeq; NP_001290289.1; NM_001303360.1.
DR   AlphaFoldDB; A0A077DB40; -.
DR   GeneID; 104923808; -.
DR   KEGG; lco:104923808; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   OrthoDB; 3470597at2759; -.
DR   Proteomes; UP000424527; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0070050; P:neuron cellular homeostasis; IEA:Ensembl.
DR   GO; GO:0010038; P:response to metal ion; IEA:Ensembl.
DR   GO; GO:0051597; P:response to methylmercury; IEA:Ensembl.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
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; IPR018152; SOD_Cu/Zn_BS.
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.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   2: Evidence at transcript level;
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023139};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Reference proteome {ECO:0000313|Proteomes:UP000424527};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN          15..150
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
SQ   SEQUENCE   154 AA;  15794 MW;  EFC0A8A4EA5667ED CRC64;
     MVLKAVCVLK GDGEVGGTVF FEQENDSAPV TVTGEIKGLQ PGDHGFHVHA FGDNTNGCIS
     AGPHFNPHNK NHAGPTDAER HVGDLGNVTA GADNVAKISI TDSMITLTGP ISIIGRTMVI
     HEKADDLGKG GNEESLKTGN AGSRLACGVI GIAQ
//
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