Database: UniProt/TrEMBL
Entry: U3K088_FICAL
LinkDB: U3K088_FICAL
Original site: U3K088_FICAL 
ID   U3K088_FICAL            Unreviewed;       154 AA.
AC   U3K088;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   25-OCT-2017, entry version 33.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC= {ECO:0000256|RuleBase:RU000393};
GN   Name=SOD1 {ECO:0000313|Ensembl:ENSFALP00000008442};
OS   Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae;
OC   Ficedula.
OX   NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000008442, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000008442}
RX   PubMed=23103876; DOI=10.1038/nature11584;
RA   Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N.,
RA   Kawakami T., Kunstner A., Makinen H., Nadachowska-Brzyska K.,
RA   Qvarnstrom A., Uebbing S., Wolf J.B.;
RT   "The genomic landscape of species divergence in Ficedula
RT   flycatchers.";
RL   Nature 491:756-760(2012).
RN   [2] {ECO:0000313|Ensembl:ENSFALP00000008442}
RG   Ensembl;
RL   Submitted (SEP-2013) 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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000393}.
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       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: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSFALP00000008442}.
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DR   EMBL; AGTO01011545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005038997.1; XM_005038940.1.
DR   Ensembl; ENSFALT00000008480; ENSFALP00000008442; ENSFALG00000008092.
DR   GeneID; 101805831; -.
DR   KEGG; fab:101805831; -.
DR   CTD; 6647; -.
DR   GeneTree; ENSGT00530000063226; -.
DR   KO; K04565; -.
DR   OrthoDB; EOG091G0OG2; -.
DR   Proteomes; UP000016665; Unplaced.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0032839; C:dendrite cytoplasm; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005777; C:peroxisome; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0043234; C:protein complex; IEA:Ensembl.
DR   GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
DR   GO; GO:0005507; F:copper ion binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0030346; F:protein phosphatase 2B binding; IEA:Ensembl.
DR   GO; GO:0048365; F:Rac GTPase binding; IEA:Ensembl.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR   GO; GO:0000187; P:activation of MAPK activity; IEA:Ensembl.
DR   GO; GO:0008089; P:anterograde axonal transport; IEA:Ensembl.
DR   GO; GO:0060088; P:auditory receptor cell stereocilium organization; IEA:Ensembl.
DR   GO; GO:0007569; P:cell aging; IEA:Ensembl.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:Ensembl.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:Ensembl.
DR   GO; GO:0060047; P:heart contraction; IEA:Ensembl.
DR   GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:Ensembl.
DR   GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
DR   GO; GO:0002262; P:myeloid cell homeostasis; IEA:Ensembl.
DR   GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; IEA:Ensembl.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0060052; P:neurofilament cytoskeleton organization; IEA:Ensembl.
DR   GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
DR   GO; GO:0032287; P:peripheral nervous system myelin maintenance; IEA:Ensembl.
DR   GO; GO:0001819; P:positive regulation of cytokine production; IEA:Ensembl.
DR   GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR   GO; GO:0043087; P:regulation of GTPase activity; IEA:Ensembl.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:Ensembl.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0060087; P:relaxation of vascular smooth muscle; IEA:Ensembl.
DR   GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
DR   GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   GO; GO:0009408; P:response to heat; IEA:Ensembl.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR   GO; GO:0001895; P:retina homeostasis; IEA:Ensembl.
DR   GO; GO:0008090; P:retrograde axonal transport; IEA:Ensembl.
DR   GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR   GO; GO:0042554; P:superoxide anion generation; IEA:Ensembl.
DR   GO; GO:0019226; P:transmission of nerve impulse; IEA:Ensembl.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D;; -; 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; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000016665};
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:UP000016665};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       13    149       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   154 AA;  15910 MW;  E8460CFB5EF89936 CRC64;
DBGET integrated database retrieval system