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Database: UniProt
Entry: B5G2V2_TAEGU
LinkDB: B5G2V2_TAEGU
Original site: B5G2V2_TAEGU 
ID   B5G2V2_TAEGU            Unreviewed;       109 AA.
AC   B5G2V2;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=superoxide dismutase {ECO:0000256|ARBA:ARBA00012682};
DE            EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682};
GN   Name=SOD1 {ECO:0000313|Ensembl:ENSTGUP00000021909.1};
OS   Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC   Estrildinae; Taeniopygia.
OX   NCBI_TaxID=59729 {ECO:0000313|EMBL:ACH45613.1};
RN   [1] {ECO:0000313|EMBL:ACH45613.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Whole brain {ECO:0000313|EMBL:ACH45613.1};
RX   PubMed=17018643; DOI=10.1073/pnas.0607098103;
RA   Wada K., Howard J.T., McConnell P., Whitney O., Lints T., Rivas M.V.,
RA   Horita H., Patterson M.A., White S.A., Scharff C., Haesler S., Zhao S.,
RA   Sakaguchi H., Hagiwara M., Shiraki T., Hirozane-Kishikawa T., Skene P.,
RA   Hayashizaki Y., Carninci P., Jarvis E.D.;
RT   "A molecular neuroethological approach for identifying and characterizing a
RT   cascade of behaviorally regulated genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15212-15217(2006).
RN   [2] {ECO:0000313|Ensembl:ENSTGUP00000021909.1, ECO:0000313|Proteomes:UP000007754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20360741; DOI=10.1038/nature08819;
RA   Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA   Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA   Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA   Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA   Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA   Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA   Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA   McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA   Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA   Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA   Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA   Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA   Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA   Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT   "The genome of a songbird.";
RL   Nature 464:757-762(2010).
RN   [3] {ECO:0000313|Ensembl:ENSTGUP00000021909.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|ARBA:ARBA00003917}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00010457}.
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DR   EMBL; DQ216317; ACH45613.1; -; mRNA.
DR   Ensembl; ENSTGUT00000035057.1; ENSTGUP00000021909.1; ENSTGUG00000013463.2.
DR   GeneTree; ENSGT00940000155551; -.
DR   Proteomes; UP000007754; Chromosome 1.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProt.
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   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
PE   2: Evidence at transcript level;
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023139};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007754}.
FT   DOMAIN          16..80
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
FT   REGION          53..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   109 AA;  11408 MW;  090C8AE0695F7A53 CRC64;
     MAAMRAVCVM QGEGAVKGVI HFEQQGTGPV KVTGEITGLA DGEHGFHVHE FGDNTNGCTS
     AGPHFNPEQK KHGGPSDAER CTRGGTTWAE GAMTRACSLE MQGPAWPAE
//
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