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Database: UniProt
Entry: A0A1S3JI77_LINUN
LinkDB: A0A1S3JI77_LINUN
Original site: A0A1S3JI77_LINUN 
ID   A0A1S3JI77_LINUN        Unreviewed;       261 AA.
AC   A0A1S3JI77;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   16-JAN-2019, entry version 7.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=LOC106173497 {ECO:0000313|RefSeq:XP_013410092.1};
OS   Lingula unguis.
OC   Eukaryota; Metazoa; Lophotrochozoa; Brachiopoda; Linguliformea;
OC   Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX   NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013410092.1};
RN   [1] {ECO:0000313|RefSeq:XP_013410092.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_013410092.1};
RG   RefSeq;
RL   Submitted (APR-2018) to UniProtKB.
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {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.
CC       {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.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
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DR   RefSeq; XP_013410092.1; XM_013554638.1.
DR   GeneID; 106173497; -.
DR   OrthoDB; 1574423at2759; -.
DR   Proteomes; UP000085678; Genome assembly.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030414; F:peptidase inhibitor activity; IEA:InterPro.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   Gene3D; 4.10.75.10; -; 1.
DR   InterPro; IPR036645; Elafin-like_sf.
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   InterPro; IPR008197; WAP_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   Pfam; PF00095; WAP; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   SUPFAM; SSF57256; SSF57256; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000085678};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    261       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5010262726.
FT   DOMAIN       30     72       WAP. {ECO:0000259|Pfam:PF00095}.
FT   DOMAIN      111    248       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   261 AA;  27856 MW;  6D5FA7DD634632E2 CRC64;
     MENLIWICLV LTVTSLELKV QAQVFPLADK PGECSTAPFY RVRSRLCNQD HLCPGDWKCC
     PHAYHGYICR PPKFESVPKT ESRIESLAMQ GVFAHCALKP NMGTPEPDRV NVHGNIDMIQ
     RQGVLEVRVN ISGLPLDGSQ EHGLHVHAFG DLSGGCGSTK GHYNPTGVTH GAPTDVVRHI
     GDWGNVPQDK NGQIVTSFFD GIASLVGKNN IVGRAIVLHT GKDDLGRGGN AASLANGNAG
     PRLGCCVIGI TNGQRVAVPA A
//
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