SODC_BOVIN
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 03-AUG-2022, entry version 193.
DE RecName: Full=Superoxide dismutase [Cu-Zn];
DE EC=1.15.1.1 {ECO:0000269|PubMed:518876};
GN Name=SOD1;
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. {ECO:0000269|PubMed:12906825}.
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/";
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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 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 AlphaFoldDB; P00442; -.
DR PCDDB; P00442; -.
DR SMR; P00442; -.
DR IntAct; P00442; 2.
DR STRING; 9913.ENSBTAP00000032384; -.
DR BindingDB; P00442; -.
DR iPTMnet; P00442; -.
DR PaxDb; P00442; -.
DR PeptideAtlas; P00442; -.
DR PRIDE; P00442; -.
DR Ensembl; ENSBTAT00000032452; ENSBTAP00000032384; ENSBTAG00000018854.
DR GeneID; 281495; -.
DR KEGG; bta:281495; -.
DR CTD; 6647; -.
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; 1574423at2759; -.
DR TreeFam; TF105131; -.
DR BRENDA; 1.15.1.1; 908.
DR Reactome; R-BTA-114608; Platelet degranulation.
DR Reactome; R-BTA-3299685; Detoxification of Reactive Oxygen Species.
DR SABIO-RK; P00442; -.
DR EvolutionaryTrace; P00442; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000018854; Expressed in oocyte and 106 other 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:0051087; F:chaperone binding; ISS: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: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:0006879; P:cellular iron ion homeostasis; 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: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; -; 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 PRINTS; PR00068; CUZNDISMTASE.
DR SUPFAM; SSF49329; SSF49329; 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
