ID SODC_BOVIN Reviewed; 152 AA. AC P00442; Q3ZCF4; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 202. DE RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000250|UniProtKB:P00441}; DE EC=1.15.1.1 {ECO:0000269|PubMed:518876}; GN Name=SOD1 {ECO:0000250|UniProtKB:P00441}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2263495; DOI=10.1093/nar/18.23.7171; RA Gibbs L.S., Shaffer J.B.; RT "Nucleotide sequence of bovine copper/zinc superoxide dismutase cDNA RT generated by the polymerase chain reaction."; RL Nucleic Acids Res. 18:7171-7171(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1958215; DOI=10.1016/s0006-291x(05)81443-3; RA Hallewell R.A., Imlay K.C., Lee P., Fong N.M., Gallegos C., Getzoff E.D., RA Tainer J.A., Cabelli D.E., Tekamp-Olson P., Mullenbach G.T., Cousens L.S.; RT "Thermostabilization of recombinant human and bovine CuZn superoxide RT dismutases by replacement of free cysteines."; RL Biochem. Biophys. Res. Commun. 181:474-480(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Ileum; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP PROTEIN SEQUENCE OF 2-152, AND ACETYLATION AT ALA-2. RX PubMed=4279916; DOI=10.1016/s0021-9258(19)42108-x; RA Steinman H.M., Naik V.R., Abernethy J.L., Hill R.L.; RT "Bovine erythrocyte superoxide dismutase. Complete amino acid sequence."; RL J. Biol. Chem. 249:7326-7338(1974). RN [5] RP DISULFIDE BOND. RX PubMed=4436313; DOI=10.1016/s0021-9258(19)42109-1; RA Abernethy J.L., Steinman H.M., Hill R.L.; RT "Bovine erythrocyte superoxide dismutase. Subunit structure and sequence RT location of the intrasubunit disulfide bond."; RL J. Biol. Chem. 249:7339-7347(1974). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, AND INHIBITION BY CHEMICAL MODIFICATION. RX PubMed=518876; DOI=10.1021/bi00593a023; RA Malinowski D.P., Friedovich I.; RT "Chemical modification of arginine at the active site of the bovine RT erythrocyte superoxide dismutase."; RL Biochemistry 18:5909-5917(1979). RN [7] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). RX PubMed=1055410; DOI=10.1073/pnas.72.4.1349; RA Richardson J.S., Thomas K.A., Rubin B.H., Richardson D.C.; RT "Crystal structure of bovine Cu,Zn superoxide dismutase at 3-A resolution: RT chain tracing and metal ligands."; RL Proc. Natl. Acad. Sci. U.S.A. 72:1349-1353(1975). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=7175933; DOI=10.1016/0022-2836(82)90174-7; RA Tainer J.A., Getzoff E.D., Beem K.M., Richardson J.S., Richardson D.C.; RT "Determination and analysis of the 2 A-structure of copper, zinc superoxide RT dismutase."; RL J. Mol. Biol. 160:181-217(1982). RN [9] RP STRUCTURE, AND MECHANISM. RX PubMed=6316150; DOI=10.1038/306284a0; RA Tainer J.A., Getzoff E.D., Richardson J.S., Richardson D.C.; RT "Structure and mechanism of copper, zinc superoxide dismutase."; RL Nature 306:284-287(1983). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=1619651; DOI=10.1016/0022-2836(92)90135-7; RA Djinovic K., Coda A., Antolini L., Pelosi G., Desideri A., Falconi M., RA Rotilio G., Bolognesi M.; RT "Crystal structure solution and refinement of the semisynthetic cobalt- RT substituted bovine erythrocyte superoxide dismutase at 2.0-A resolution."; RL J. Mol. Biol. 226:227-238(1992). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RX PubMed=7643403; DOI=10.1006/jmbi.1995.0434; RA Rypniewski W.R., Mangani S., Bruni B., Orioli P.L., Casati M., Wilson K.S.; RT "Crystal structure of reduced bovine erythrocyte superoxide dismutase at RT 1.9-A resolution."; RL J. Mol. Biol. 251:282-296(1995). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX PubMed=10092461; DOI=10.1006/jmbi.1999.2610; RA Hough M.A., Hasnain S.S.; RT "Crystallographic structures of bovine copper-zinc superoxide dismutase RT reveal asymmetry in two subunits: functionally important three and five RT coordinate copper sites captured in the same crystal."; RL J. Mol. Biol. 287:579-592(1999). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEX WITH COPPER AND ZINC RP IONS, AND SUBUNIT. RX PubMed=12906825; DOI=10.1016/s0969-2126(03)00155-2; RA Hough M.A., Hasnain S.S.; RT "Structure of fully reduced bovine copper zinc superoxide dismutase at 1.15 RT A."; RL Structure 11:937-946(2003). CC -!- FUNCTION: Destroys radicals which are normally produced within the CC cells and which are toxic to biological systems. CC {ECO:0000269|PubMed:518876}. 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; Evidence={ECO:0000269|PubMed:518876}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Note=Binds 1 copper ion per subunit.; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 zinc ion per subunit.; CC -!- SUBUNIT: Homodimer; non-disulfide-linked (By similarity). Heterodimer CC with SOD1. The heterodimer CCS:SOD1 interacts with SLC31A1; this CC heterotrimer is Cu(1+)-mediated and its maintenance is regulated CC through SOD1 activation (By similarity). {ECO:0000250|UniProtKB:P00441, CC ECO:0000250|UniProtKB:P08228}. CC -!- INTERACTION: CC P00442; P62998: RAC1; NbExp=2; IntAct=EBI-6654424, EBI-6654511; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. CC -!- PTM: Palmitoylation helps nuclear targeting and decreases catalytic CC activity. {ECO:0000250}. CC -!- PTM: Succinylation, adjacent to copper catalytic site, probably CC inhibits activity. Desuccinylation by SIRT5 enhances activity. CC {ECO:0000250|UniProtKB:P00441}. CC -!- MISCELLANEOUS: Chemical modification of Arg-142 reduces activity by 80- CC 90%. {ECO:0000269|PubMed:518876}. CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Worthington enzyme manual; CC URL="https://www.worthington-biochem.com/SODBE/"; 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; X54799; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; M81129; AAA73164.1; -; mRNA. DR EMBL; BC102432; AAI02433.1; -; mRNA. DR PIR; I45883; DSBOCZ. DR RefSeq; NP_777040.1; NM_174615.2. DR PDB; 1CB4; X-ray; 2.30 A; A/B=2-152. DR PDB; 1CBJ; X-ray; 1.65 A; A/B=2-152. DR PDB; 1COB; X-ray; 2.00 A; A/B=2-152. DR PDB; 1E9O; X-ray; 1.85 A; A/B=2-152. DR PDB; 1E9P; X-ray; 1.70 A; A/B=2-151. DR PDB; 1E9Q; X-ray; 1.75 A; A/B=2-152. DR PDB; 1Q0E; X-ray; 1.15 A; A/B=2-152. DR PDB; 1SDA; X-ray; 2.50 A; B/G/O/Y=2-152. DR PDB; 1SXA; X-ray; 1.90 A; A/B=2-152. DR PDB; 1SXB; X-ray; 2.00 A; A/B=2-152. DR PDB; 1SXC; X-ray; 1.90 A; A/B=2-152. DR PDB; 1SXN; X-ray; 1.90 A; A/B=2-152. DR PDB; 1SXS; X-ray; 2.00 A; A/B=2-152. DR PDB; 1SXZ; X-ray; 2.05 A; A/B=2-152. DR PDB; 2AEO; X-ray; 1.80 A; A/B=2-152. DR PDB; 2SOD; X-ray; 2.00 A; B/G/O/Y=2-152. DR PDB; 2Z7U; X-ray; 2.10 A; A/B=2-152. DR PDB; 2Z7W; X-ray; 1.80 A; A/B=2-152. DR PDB; 2Z7Y; X-ray; 1.55 A; A/B=2-152. DR PDB; 2Z7Z; X-ray; 1.85 A; A/B=2-152. DR PDB; 2ZOW; X-ray; 1.45 A; A/B=2-152. DR PDB; 3HW7; X-ray; 2.00 A; A/B=2-152. DR PDB; 3SOD; X-ray; 2.10 A; B/G/O/Y=2-152. DR PDB; 8IQ0; X-ray; 1.88 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=2-152. DR PDB; 8IQ1; X-ray; 1.80 A; A/B/C/D/E/F/G/H=2-152. DR PDBsum; 1CB4; -. DR PDBsum; 1CBJ; -. DR PDBsum; 1COB; -. DR PDBsum; 1E9O; -. DR PDBsum; 1E9P; -. DR PDBsum; 1E9Q; -. DR PDBsum; 1Q0E; -. DR PDBsum; 1SDA; -. DR PDBsum; 1SXA; -. DR PDBsum; 1SXB; -. DR PDBsum; 1SXC; -. DR PDBsum; 1SXN; -. DR PDBsum; 1SXS; -. DR PDBsum; 1SXZ; -. DR PDBsum; 2AEO; -. DR PDBsum; 2SOD; -. DR PDBsum; 2Z7U; -. DR PDBsum; 2Z7W; -. DR PDBsum; 2Z7Y; -. DR PDBsum; 2Z7Z; -. DR PDBsum; 2ZOW; -. DR PDBsum; 3HW7; -. DR PDBsum; 3SOD; -. DR PDBsum; 8IQ0; -. DR PDBsum; 8IQ1; -. DR AlphaFoldDB; P00442; -. DR PCDDB; P00442; -. DR SMR; P00442; -. DR IntAct; P00442; 2. DR STRING; 9913.ENSBTAP00000032384; -. DR BindingDB; P00442; -. DR iPTMnet; P00442; -. DR PaxDb; 9913-ENSBTAP00000032384; -. DR PeptideAtlas; P00442; -. DR Ensembl; ENSBTAT00000032452.4; ENSBTAP00000032384.3; ENSBTAG00000018854.5. DR GeneID; 281495; -. DR KEGG; bta:281495; -. DR VEuPathDB; HostDB:ENSBTAG00000018854; -. DR eggNOG; KOG0441; Eukaryota. DR GeneTree; ENSGT00940000155551; -. DR HOGENOM; CLU_056632_4_1_1; -. DR InParanoid; P00442; -. DR OMA; AQRGFHI; -. DR OrthoDB; 3470597at2759; -. DR TreeFam; TF105131; -. DR BRENDA; 1.15.1.1; 908. DR SABIO-RK; P00442; -. DR EvolutionaryTrace; P00442; -. DR Proteomes; UP000009136; Chromosome 1. DR Bgee; ENSBTAG00000018854; Expressed in oocyte and 106 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0032839; C:dendrite cytoplasm; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005777; C:peroxisome; IBA:GO_Central. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0030346; F:protein phosphatase 2B binding; ISS:UniProtKB. DR GO; GO:0051087; F:protein-folding chaperone binding; ISS:UniProtKB. DR GO; GO:0004784; F:superoxide dismutase activity; IDA:UniProtKB. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; ISS:UniProtKB. DR GO; GO:0007566; P:embryo implantation; ISS:UniProtKB. DR GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB. DR GO; GO:0060047; P:heart contraction; ISS:UniProtKB. DR GO; GO:0050665; P:hydrogen peroxide biosynthetic process; ISS:UniProtKB. DR GO; GO:0006879; P:intracellular iron ion homeostasis; ISS:UniProtKB. DR GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB. DR GO; GO:0046716; P:muscle cell cellular homeostasis; ISS:UniProtKB. DR GO; GO:0002262; P:myeloid cell homeostasis; ISS:UniProtKB. DR GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; ISS:UniProtKB. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB. DR GO; GO:0060052; P:neurofilament cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB. DR GO; GO:0032287; P:peripheral nervous system myelin maintenance; ISS:UniProtKB. DR GO; GO:0043085; P:positive regulation of catalytic activity; IDA:UniProtKB. DR GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB. DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB. DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB. DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB. DR GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB. DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:UniProtKB. DR GO; GO:0040014; P:regulation of multicellular organism growth; ISS:UniProtKB. DR GO; GO:0045859; P:regulation of protein kinase activity; ISS:UniProtKB. DR GO; GO:0060087; P:relaxation of vascular associated smooth muscle; ISS:UniProtKB. DR GO; GO:0019430; P:removal of superoxide radicals; IDA:UniProtKB. DR GO; GO:0048678; P:response to axon injury; ISS:UniProtKB. DR GO; GO:0045471; P:response to ethanol; ISS:UniProtKB. DR GO; GO:0009408; P:response to heat; ISS:UniProtKB. DR GO; GO:0042542; P:response to hydrogen peroxide; ISS:UniProtKB. DR GO; GO:0010033; P:response to organic substance; ISS:UniProtKB. DR GO; GO:0000303; P:response to superoxide; ISS:UniProtKB. DR GO; GO:0001895; P:retina homeostasis; ISS:UniProtKB. DR GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB. DR GO; GO:0006801; P:superoxide metabolic process; ISS:UniProtKB. DR GO; GO:0019226; P:transmission of nerve impulse; ISS:UniProtKB. 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 1: Evidence at protein level; KW 3D-structure; Acetylation; Antioxidant; Copper; Cytoplasm; KW Direct protein sequencing; Disulfide bond; Lipoprotein; Metal-binding; KW Nucleus; Oxidoreductase; Palmitate; Phosphoprotein; Reference proteome; KW Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:4279916" FT CHAIN 2..152 FT /note="Superoxide dismutase [Cu-Zn]" FT /id="PRO_0000164049" FT BINDING 45 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:1055410, FT ECO:0000269|PubMed:12906825" FT BINDING 47 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:1055410, FT ECO:0000269|PubMed:12906825" FT BINDING 62 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:1055410, FT ECO:0000269|PubMed:12906825" FT BINDING 62 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000269|PubMed:1055410" FT BINDING 70 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000269|PubMed:1055410" FT BINDING 79 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000269|PubMed:1055410" FT BINDING 82 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000269|PubMed:1055410" FT BINDING 119 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:1055410, FT ECO:0000269|PubMed:12906825" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|PubMed:4279916" FT MOD_RES 4 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P08228" FT MOD_RES 10 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P08228" FT MOD_RES 90 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P08228" FT MOD_RES 104 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07632" FT MOD_RES 106 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P08228" FT MOD_RES 121 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P00441" FT MOD_RES 121 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P00441" FT MOD_RES 135 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08228" FT MOD_RES 135 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08228" FT LIPID 7 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT DISULFID 56..145 FT /evidence="ECO:0000269|PubMed:4436313" FT STRAND 4..10 FT /evidence="ECO:0007829|PDB:1Q0E" FT STRAND 12..14 FT /evidence="ECO:0007829|PDB:1Q0E" FT STRAND 16..24 FT /evidence="ECO:0007829|PDB:1Q0E" FT STRAND 27..36 FT /evidence="ECO:0007829|PDB:1Q0E" FT STRAND 39..48 FT /evidence="ECO:0007829|PDB:1Q0E" FT TURN 53..56 FT /evidence="ECO:0007829|PDB:1Q0E" FT HELIX 57..59 FT /evidence="ECO:0007829|PDB:1Q0E" FT STRAND 76..78 FT /evidence="ECO:0007829|PDB:2Z7Y" FT STRAND 82..88 FT /evidence="ECO:0007829|PDB:1Q0E" FT TURN 90..92 FT /evidence="ECO:0007829|PDB:2SOD" FT STRAND 94..102 FT /evidence="ECO:0007829|PDB:1Q0E" FT STRAND 104..107 FT /evidence="ECO:0007829|PDB:1Q0E" FT STRAND 114..121 FT /evidence="ECO:0007829|PDB:1Q0E" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:1Q0E" FT HELIX 133..136 FT /evidence="ECO:0007829|PDB:1Q0E" FT STRAND 141..147 FT /evidence="ECO:0007829|PDB:1Q0E" FT STRAND 149..152 FT /evidence="ECO:0007829|PDB:1SDA" SQ SEQUENCE 152 AA; 15683 MW; A467EE17E4C31CCD CRC64; MATKAVCVLK GDGPVQGTIH FEAKGDTVVV TGSITGLTEG DHGFHVHQFG DNTQGCTSAG PHFNPLSKKH GGPKDEERHV GDLGNVTADK NGVAIVDIVD PLISLSGEYS IIGRTMVVHE KPDDLGRGGN EESTKTGNAG SRLACGVIGI AK //