ID Q4PMB7_IXOSC Unreviewed; 154 AA.
AC Q4PMB7; A0A6P7WM57;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
OS Ixodes scapularis (Black-legged tick) (Deer tick).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX NCBI_TaxID=6945 {ECO:0000313|EMBL:AAY66847.1};
RN [1] {ECO:0000313|EMBL:AAY66847.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ISUFL293 {ECO:0000313|EMBL:AAY66847.1};
RC TISSUE=Salivary glands {ECO:0000313|EMBL:AAY66847.1};
RA Tseng H.-P., Hseu T.-H., Buhler D.R., Wang W.-D., Tsai H.-L., Hu C.-H.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAY66847.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ISUFL293 {ECO:0000313|EMBL:AAY66847.1};
RC TISSUE=Salivary glands {ECO:0000313|EMBL:AAY66847.1};
RX PubMed=16431279; DOI=10.1016/j.ibmb.2005.11.005;
RA Ribeiro J.M., Alarcon-Chaidez F., Francischetti I.M., Mans B.J.,
RA Mather T.N., Valenzuela J.G., Wikel S.K.;
RT "An annotated catalog of salivary gland transcripts from Ixodes scapularis
RT ticks.";
RL Insect Biochem. Mol. Biol. 36:111-129(2006).
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. {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|RuleBase:RU000393}.
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DR EMBL; DQ066210; AAY66847.1; -; mRNA.
DR AlphaFoldDB; Q4PMB7; -.
DR VEuPathDB; VectorBase:ISCI008219; -.
DR VEuPathDB; VectorBase:ISCP_013667; -.
DR VEuPathDB; VectorBase:ISCW008219; -.
DR HOGENOM; CLU_056632_4_1_1; -.
DR OrthoDB; 3470597at2759; -.
DR GO; GO:0005507; F:copper ion binding; 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; 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 Metal-binding {ECO:0000256|RuleBase:RU000393};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW Zinc {ECO:0000256|RuleBase:RU000393}.
FT DOMAIN 16..150
FT /note="Superoxide dismutase copper/zinc binding"
FT /evidence="ECO:0000259|Pfam:PF00080"
SQ SEQUENCE 154 AA; 15629 MW; 98FA53B5B782D3BF CRC64;
MSVKAVCVLK GSEKTTGTVY FTQAGPNQPV VVTGEITGLD QGLHGFHVHE FGDNTNGCTS
AGPHFNPLGK EHGAPTDTNR HVGDLGNVIA GDDGVAKVAI TDSQISLSGP HSIIGRSVVI
HADPDDLGKG GHELSKTTGN AGARLACGVV GVTK
//
