ID F6V6S8_CIOIN Unreviewed; 217 AA. AC F6V6S8; A0A1W2WJ09; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-MAR-2024, entry version 70. DE RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414}; DE EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414}; GN Name=LOC100182293 {ECO:0000313|Ensembl:ENSCINP00000008803.3}; OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis). OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia; OC Cionidae; Ciona. OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000008803.3, ECO:0000313|Proteomes:UP000008144}; RN [1] {ECO:0000313|Proteomes:UP000008144} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12481130; DOI=10.1126/science.1080049; RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A., RA Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N., RA Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P., RA Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S., RA Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K., RA Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P., RA Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S., RA Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G., RA Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A., RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M., RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D., RA Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F., RA Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N., RA Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M., RA Satoh N., Rokhsar D.S.; RT "The draft genome of Ciona intestinalis: insights into chordate and RT vertebrate origins."; RL Science 298:2157-2167(2002). RN [2] {ECO:0000313|Ensembl:ENSCINP00000008803.3} 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|RuleBase:RU000414}. CC -!- FUNCTION: Destroys superoxide anion radicals which are normally CC produced within the cells and which are toxic to biological systems. CC {ECO:0000256|ARBA:ARBA00002170}. 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|ARBA:ARBA00001605, CC ECO:0000256|RuleBase:RU000414}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix CC {ECO:0000256|ARBA:ARBA00004305}. CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family. CC {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EAAA01001024; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_002128490.1; XM_002128454.4. DR AlphaFoldDB; F6V6S8; -. DR STRING; 7719.ENSCINP00000008803; -. DR Ensembl; ENSCINT00000008803.3; ENSCINP00000008803.3; ENSCING00000004261.3. DR GeneID; 100182293; -. DR KEGG; cin:100182293; -. DR GeneTree; ENSGT00390000011877; -. DR HOGENOM; CLU_031625_2_0_1; -. DR InParanoid; F6V6S8; -. DR OMA; DSLINWD; -. DR OrthoDB; 4839at2759; -. DR TreeFam; TF105132; -. DR Proteomes; UP000008144; Chromosome 12. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central. DR GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central. DR GO; GO:0045087; P:innate immune response; IEA:Ensembl. DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl. DR GO; GO:0051597; P:response to methylmercury; IEA:Ensembl. DR Gene3D; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1. DR Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1. DR InterPro; IPR001189; Mn/Fe_SOD. DR InterPro; IPR019833; Mn/Fe_SOD_BS. DR InterPro; IPR019832; Mn/Fe_SOD_C. DR InterPro; IPR019831; Mn/Fe_SOD_N. DR InterPro; IPR036324; Mn/Fe_SOD_N_sf. DR InterPro; IPR036314; SOD_C_sf. DR PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 1. DR PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 1. DR Pfam; PF02777; Sod_Fe_C; 1. DR Pfam; PF00081; Sod_Fe_N; 1. DR PIRSF; PIRSF000349; SODismutase; 1. DR PRINTS; PR01703; MNSODISMTASE. DR SUPFAM; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1. DR SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1. DR PROSITE; PS00088; SOD_MN; 1. PE 3: Inferred from homology; KW Manganese {ECO:0000256|ARBA:ARBA00023211}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR000349-1}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU000414}; KW Reference proteome {ECO:0000313|Proteomes:UP000008144}. FT DOMAIN 22..103 FT /note="Manganese/iron superoxide dismutase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00081" FT DOMAIN 111..213 FT /note="Manganese/iron superoxide dismutase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02777" FT BINDING 47 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 95 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 180 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" FT BINDING 184 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000256|PIRSR:PIRSR000349-1" SQ SEQUENCE 217 AA; 24072 MW; BFC77966CAA60C30 CRC64; MLRLLSSRCT SKVVPVWASR GKHTLPDLPY DYSALEPHIS AEIMETHYAK HHATYVNNLN IAEEKLHEAE AKNDISSIIS LGPALKFNGG GHINHSIFWE TLSPNGGSEP CGELKTAIDR DFGSFENLKA KLTAASVGVQ GSGWSWLGLD KEKGQLQVVA CPNQDPLHAT TGLVPLFGID VWEHAYYLQY KNVRPDYIKA IFNVVNWENV GKRFTDA //