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Database: UniProt
Entry: A0A1S3H1E6_LINUN
LinkDB: A0A1S3H1E6_LINUN
Original site: A0A1S3H1E6_LINUN 
ID   A0A1S3H1E6_LINUN        Unreviewed;       360 AA.
AC   A0A1S3H1E6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   16-JAN-2019, entry version 13.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=LOC106151196 {ECO:0000313|RefSeq:XP_013379762.1};
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_013379762.1};
RN   [1] {ECO:0000313|RefSeq:XP_013379762.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_013379762.1};
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR   RefSeq; XP_013379762.1; XM_013524308.1.
DR   EnsemblMetazoa; g5290.t1; g5290.t1; g5290.
DR   GeneID; 106151196; -.
DR   KEGG; lak:106151196; -.
DR   KO; K04565; -.
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   CDD; cd00112; LDLa; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   Gene3D; 4.10.75.10; -; 1.
DR   InterPro; IPR036645; Elafin-like_sf.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
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; PF00057; Ldl_recept_a; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   Pfam; PF00095; WAP; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SMART; SM00192; LDLa; 1.
DR   SMART; SM00217; WAP; 1.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   SUPFAM; SSF57256; SSF57256; 1.
DR   SUPFAM; SSF57424; SSF57424; 1.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
DR   PROSITE; PS51390; WAP; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000085678};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00124,
KW   ECO:0000256|SAAS:SAAS01050632};
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     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22    360       Superoxide dismutase [Cu-Zn].
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5010288108.
FT   DOMAIN      129    175       WAP. {ECO:0000259|PROSITE:PS51390}.
FT   DISULFID     76     94       {ECO:0000256|PROSITE-ProRule:PRU00124}.
FT   DISULFID     88    103       {ECO:0000256|PROSITE-ProRule:PRU00124}.
SQ   SEQUENCE   360 AA;  39308 MW;  E7D5F5880D4D8373 CRC64;
     MFFGILRCTF LILLIWTSCQ ATPATETPPE TTPVYLNNVK TARLNMRMPT LDINAFYHGY
     AGFQSKDCDS AYEFKCKNRR CIPATWRCDR ENDCGDRSDE ADCVHFTRKS APKPSVKSLT
     FPHGLPIGYP AKTGTCSTFP VYGQKYLWQC TNDHDCILDM KCCNDGKGKV CKPPVLESLR
     PYLSPQQLAR MYTVGHCDMR PNTGVKHGIS GDIYLVQRGN LLEVRVNISG LPTEGNSLKH
     GLHVHTYGDL SDGCASTGGH FNPANVRHGS PTDLPNKRHV GDWGNVERDS DGNVVTAFLD
     SVASLWGPNT IIGRAIVIHA SEDDLGRGGD KGSSLSGNAG PRLACCVIGI SNGNNLLQQG
//
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