ID   SODE_HUMAN              Reviewed;         240 AA.
AC   P08294; Q5U781; Q6FHA2;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   02-SEP-2026, entry version 236.
DE   RecName: Full=Extracellular superoxide dismutase [Cu-Zn];
DE            Short=EC-SOD;
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=SOD3 {ECO:0000312|HGNC:HGNC:11181};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT THR-58.
RX   PubMed=3476950; DOI=10.1073/pnas.84.18.6340;
RA   Hjalmarsson K., Marklund S.L., Engstroem A., Edlund T.;
RT   "Isolation and sequence of complementary DNA encoding human extracellular
RT   superoxide dismutase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:6340-6344(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-58, AND TISSUE SPECIFICITY.
RC   TISSUE=Blood;
RX   PubMed=7959763; DOI=10.1006/geno.1994.1357;
RA   Folz R.J., Crapo J.D.;
RT   "Extracellular superoxide dismutase (SOD3): tissue-specific expression,
RT   genomic characterization, and computer-assisted sequence analysis of the
RT   human EC SOD gene.";
RL   Genomics 22:162-171(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-58.
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA   Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA   LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-58; THR-91 AND GLY-231.
RG   NIEHS SNPs program;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-58.
RC   TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   GLYCATION AT LYS-229 AND LYS-230.
RX   PubMed=1505778; DOI=10.1016/0891-5849(92)90016-a;
RA   Adachi T., Ohta H., Hayashi K., Hirano K., Marklund S.L.;
RT   "The site of nonenzymic glycation of human extracellular-superoxide
RT   dismutase in vitro.";
RL   Free Radic. Biol. Med. 13:205-210(1992).
RN   [7]
RP   FUNCTION.
RX   PubMed=12933702; DOI=10.1161/01.res.0000092140.81594.a8;
RA   Jung O., Marklund S.L., Geiger H., Pedrazzini T., Busse R., Brandes R.P.;
RT   "Extracellular superoxide dismutase is a major determinant of nitric oxide
RT   bioavailability: in vivo and ex vivo evidence from ecSOD-deficient mice.";
RL   Circ. Res. 93:622-629(2003).
RN   [8]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=15761197; DOI=10.1161/01.res.0000162001.57896.66;
RA   Jeney V., Itoh S., Wendt M., Gradek Q., Ushio-Fukai M., Harrison D.G.,
RA   Fukai T.;
RT   "Role of antioxidant-1 in extracellular superoxide dismutase function and
RT   expression.";
RL   Circ. Res. 96:723-729(2005).
RN   [9]
RP   REVIEW.
RX   PubMed=16087389; DOI=10.1016/j.biocel.2005.06.012;
RA   Nozik-Grayck E., Suliman H.B., Piantadosi C.A.;
RT   "Extracellular superoxide dismutase.";
RL   Int. J. Biochem. Cell Biol. 37:2466-2471(2005).
RN   [10]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-107.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [11]
RP   INTERACTION WITH ATP7A.
RX   PubMed=16371425; DOI=10.1096/fj.05-4564fje;
RA   Qin Z., Itoh S., Jeney V., Ushio-Fukai M., Fukai T.;
RT   "Essential role for the Menkes ATPase in activation of extracellular
RT   superoxide dismutase: implication for vascular oxidative stress.";
RL   FASEB J. 20:334-336(2006).
RN   [12]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-107.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [13]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=31326693; DOI=10.1016/j.redox.2019.101268;
RA   Hu L., Zachariae E.D., Larsen U.G., Vilhardt F., Petersen S.V.;
RT   "The dynamic uptake and release of SOD3 from intracellular stores in
RT   macrophages modulates the inflammatory response.";
RL   Redox Biol. 26:101268-101268(2019).
RN   [14] {ECO:0007744|PDB:2JLP}
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 19-240, SUBUNIT, METAL-BINDING
RP   SITES, AND DISULFIDE BONDS.
RX   PubMed=19289127; DOI=10.1016/j.jmb.2009.03.026;
RA   Antonyuk S.V., Strange R.W., Marklund S.L., Hasnain S.S.;
RT   "The structure of human extracellular copper-zinc superoxide dismutase at
RT   1.7 A resolution: insights into heparin and collagen binding.";
RL   J. Mol. Biol. 388:310-326(2009).
RN   [15]
RP   VARIANT GLY-231.
RX   PubMed=8034674; DOI=10.1016/s0021-9258(17)32289-5;
RA   Sandstrom J., Nilsson P., Karlsson K., Marklund S.L.;
RT   "10-fold increase in human plasma extracellular superoxide dismutase
RT   content caused by a mutation in heparin-binding domain.";
RL   J. Biol. Chem. 269:19163-19166(1994).
RN   [16]
RP   VARIANT GLY-231.
RX   PubMed=7662997; DOI=10.1007/bf01883574;
RA   Yamada H., Yamada Y., Adachi T., Goto H., Ogasawara N., Futenma A.,
RA   Kitano M., Hirano K., Kato K.;
RT   "Molecular analysis of extracellular-superoxide dismutase gene associated
RT   with high level in serum.";
RL   Jpn. J. Hum. Genet. 40:177-184(1995).
RN   [17]
RP   VARIANT GLY-231, AND SUBCELLULAR LOCATION.
RX   PubMed=8546689; DOI=10.1042/bj3130235;
RA   Adachi T., Yamada H., Yamada Y., Morihara N., Yamazaki N., Murakami T.,
RA   Futenma A., Kato K., Hirano K.;
RT   "Substitution of glycine for arginine-213 in extracellular-superoxide
RT   dismutase impairs affinity for heparin and endothelial cell surface.";
RL   Biochem. J. 313:235-239(1996).
RN   [18]
RP   VARIANT GLY-231.
RX   PubMed=8864862; DOI=10.1093/oxfordjournals.jbchem.a021383;
RA   Adachi T., Morihara N., Yamazaki N., Yamada H., Futenma A., Kato K.,
RA   Hirano K.;
RT   "An arginine-213 to glycine mutation in human extracellular-superoxide
RT   dismutase reduces susceptibility to trypsin-like proteinases.";
RL   J. Biochem. 120:184-188(1996).
CC   -!- FUNCTION: Secreted antioxidant enzyme that acts as the primary
CC       scavenger of superoxide radicals in the extracellular space, converting
CC       them to hydrogen peroxide and thereby protecting tissues from oxidative
CC       damage (PubMed:12933702, PubMed:15761197). Also preserves nitric oxide
CC       bioavailability by preventing the formation of harmful peroxynitrite
CC       (PubMed:12933702). Stored in intracellular pre-formed vesicles of
CC       macrophages and neutrophils and released upon stimulation by
CC       inflammatory mediators (PubMed:31326693). {ECO:0000269|PubMed:12933702,
CC       ECO:0000269|PubMed:15761197, ECO:0000269|PubMed:31326693}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 superoxide + 2 H(+) = 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:0000269|PubMed:15761197};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000269|PubMed:19289127};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:19289127};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:19289127};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:19289127};
CC   -!- SUBUNIT: Homotetramer (PubMed:19289127). Directly interacts with ATP7A;
CC       this interaction is copper-dependent and is required for SOD3 activity
CC       (PubMed:16371425). {ECO:0000269|PubMed:16371425,
CC       ECO:0000269|PubMed:19289127}.
CC   -!- INTERACTION:
CC       P08294; Q12797-6: ASPH; NbExp=3; IntAct=EBI-10195782, EBI-12092171;
CC       P08294; Q9NZI2-2: KCNIP1; NbExp=3; IntAct=EBI-10195782, EBI-22452746;
CC       P08294; Q9Y2W7: KCNIP3; NbExp=6; IntAct=EBI-10195782, EBI-751501;
CC       P08294; O43765: SGTA; NbExp=3; IntAct=EBI-10195782, EBI-347996;
CC       P08294; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-10195782, EBI-744081;
CC       P08294; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-10195782, EBI-741480;
CC       P08294; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-10195782, EBI-947187;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000269|PubMed:8546689}. Golgi apparatus, trans-Golgi network
CC       {ECO:0000250|UniProtKB:O09164}. Vesicle {ECO:0000269|PubMed:31326693}.
CC       Note=99% of SOD3/EC-SOD is anchored to heparan sulfate proteoglycans in
CC       the tissue interstitium, and 1% is located in the vasculature in
CC       equilibrium between the plasma and the endothelium (PubMed:8546689). In
CC       macrophages and neutrophiles, extracellular SOD2 in endocytosed and
CC       stored in intracellular vesicles (PubMed:31326693).
CC       {ECO:0000269|PubMed:31326693, ECO:0000269|PubMed:8546689}.
CC   -!- TISSUE SPECIFICITY: Expressed in blood vessels, heart, lung, kidney and
CC       placenta. Major SOD isoenzyme in extracellular fluids such as plasma,
CC       lymph and synovial fluid (PubMed:7959763). Stored in macrophages
CC       intracellular compartments (PubMed:31326693).
CC       {ECO:0000269|PubMed:31326693, ECO:0000269|PubMed:7959763}.
CC   -!- POLYMORPHISM: The variant Gly-231 which is found in about 2.2% of
CC       individual displays a 10-fold increased plasma EC-SOD content due to
CC       reduced heparin-binding affinity and thus the impairment of its binding
CC       ability to endothelial cell surface. {ECO:0000269|PubMed:7662997,
CC       ECO:0000269|PubMed:8034674, ECO:0000269|PubMed:8546689}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Superoxide dismutase entry;
CC       URL="https://en.wikipedia.org/wiki/Superoxide_dismutase";
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DR   EMBL; J02947; AAA66000.1; -; mRNA.
DR   EMBL; U10116; AAA62278.1; -; Genomic_DNA.
DR   EMBL; CR541853; CAG46651.1; -; mRNA.
DR   EMBL; AY787834; AAV40827.1; -; Genomic_DNA.
DR   EMBL; BC014418; AAH14418.1; -; mRNA.
DR   CCDS; CCDS3430.1; -.
DR   PIR; A28301; DSHUEC.
DR   RefSeq; NP_003093.2; NM_003102.4.
DR   PDB; 2JLP; X-ray; 1.70 A; A/B/C/D=19-240.
DR   AlphaFoldDB; P08294; -.
DR   SMR; P08294; -.
DR   BioGRID; 112532; 11.
DR   FunCoup; P08294; 83.
DR   IntAct; P08294; 8.
DR   NDEx; IQUERY-CP-SOD3; 10 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000371554; -.
DR   BindingDB; P08294; -.
DR   ChEMBL; CHEMBL2069159; -.
DR   DrugBank; DB09096; Benzoyl peroxide.
DR   GlyConnect; P08294; 4 N-Linked glycans (1 site).
DR   GlyCosmos; P08294; 4 sites, 3 glycans.
DR   GlyGen; P08294; 2 sites, 90 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; P08294; -.
DR   PhosphoSitePlus; P08294; -.
DR   BioMuta; SOD3; -.
DR   DMDM; 108885292; -.
DR   jPOST; P08294; -.
DR   MassIVE; P08294; -.
DR   PaxDb; 9606-ENSP00000371554; -.
DR   PeptideAtlas; P08294; -.
DR   ProteomicsDB; 52104; -.
DR   Antibodypedia; 3278; 557 antibodies from 39 providers.
DR   DNASU; 6649; -.
DR   Ensembl; ENST00000382120.4; ENSP00000371554.3; ENSG00000109610.7.
DR   Ensembl; ENST00000880265.1; ENSP00000550324.1; ENSG00000109610.7.
DR   Ensembl; ENST00000952028.1; ENSP00000622087.1; ENSG00000109610.7.
DR   Ensembl; ENST00000952029.1; ENSP00000622088.1; ENSG00000109610.7.
DR   Ensembl; ENST00000952030.1; ENSP00000622089.1; ENSG00000109610.7.
DR   Ensembl; ENST00000952031.1; ENSP00000622090.1; ENSG00000109610.7.
DR   GeneID; 6649; -.
DR   KEGG; hsa:6649; -.
DR   MANE-Select; ENST00000382120.4; ENSP00000371554.3; NM_003102.4; NP_003093.2.
DR   UCSC; uc003gqz.4; human.
DR   AGR; HGNC:11181; -.
DR   ClinPGx; PA36018; -.
DR   CTD; 6649; -.
DR   DisGeNET; 6649; -.
DR   GeneCards; SOD3; -.
DR   HGNC; HGNC:11181; SOD3.
DR   HPA; ENSG00000109610; Group enriched (blood vessel, choroid plexus).
DR   MIM; 185490; gene.
DR   OpenTargets; ENSG00000109610; -.
DR   VEuPathDB; HostDB:ENSG00000109610; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   GeneTree; ENSGT00940000162224; -.
DR   HOGENOM; CLU_056632_3_1_1; -.
DR   InParanoid; P08294; -.
DR   OMA; DGSLWKY; -.
DR   OrthoDB; 666972at2759; -.
DR   PAN-GO; P08294; 3 GO annotations based on evolutionary models.
DR   PhylomeDB; P08294; -.
DR   BioCyc; MetaCyc:HS03242-MONOMER; -.
DR   BRENDA; 1.15.1.1; 2681.
DR   PathwayCommons; P08294; -.
DR   Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
DR   Reactome; R-HSA-9818027; NFE2L2 regulating anti-oxidant/detoxification enzymes.
DR   SignaLink; P08294; -.
DR   SIGNOR; P08294; -.
DR   Agora; ENSG00000109610; -.
DR   BioGRID-ORCS; 6649; 11 hits in 1153 CRISPR screens.
DR   ChiTaRS; SOD3; human.
DR   EvolutionaryTrace; P08294; -.
DR   GeneWiki; SOD3; -.
DR   GenomeRNAi; 6649; -.
DR   Pharos; P08294; Tbio.
DR   PRO; PR:P08294; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; P08294; protein.
DR   Bgee; ENSG00000109610; Expressed in descending thoracic aorta and 150 other cell types or tissues.
DR   ExpressionAtlas; P08294; baseline and differential.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0060090; F:molecular adaptor activity; EXP:DisProt.
DR   GO; GO:0004784; F:superoxide dismutase activity; IDA:UniProtKB.
DR   GO; GO:0046209; P:nitric oxide metabolic process; IMP:UniProtKB.
DR   GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   DisProt; DP02656; -.
DR   FunFam; 2.60.40.200:FF:000008; Superoxide dismutase [Cu-Zn]; 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; 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.
DR   PDBsum; 2JLP; -.
PE   1: Evidence at protein level;
KW   3D-structure; Antioxidant; Copper; Direct protein sequencing;
KW   Disulfide bond; Glycation; Glycoprotein; Golgi apparatus; Heparin-binding;
KW   Metal-binding; Oxidoreductase; Proteomics identification;
KW   Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..18
FT   CHAIN           19..240
FT                   /note="Extracellular superoxide dismutase [Cu-Zn]"
FT                   /id="PRO_0000032855"
FT   BINDING         114
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:19289127,
FT                   ECO:0007744|PDB:2JLP"
FT   BINDING         116
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:19289127,
FT                   ECO:0007744|PDB:2JLP"
FT   BINDING         131
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:19289127,
FT                   ECO:0007744|PDB:2JLP"
FT   BINDING         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000269|PubMed:19289127,
FT                   ECO:0007744|PDB:2JLP"
FT   BINDING         139
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000269|PubMed:19289127,
FT                   ECO:0007744|PDB:2JLP"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000269|PubMed:19289127,
FT                   ECO:0007744|PDB:2JLP"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000269|PubMed:19289127,
FT                   ECO:0007744|PDB:2JLP"
FT   BINDING         181
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:19289127,
FT                   ECO:0007744|PDB:2JLP"
FT   SITE            41
FT                   /note="Not glycated"
FT   SITE            92
FT                   /note="Not glycated"
FT   SITE            238
FT                   /note="Not glycated"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19159218"
FT   CARBOHYD        229
FT                   /note="N-linked (Glc) (glycation) lysine; in vitro"
FT                   /evidence="ECO:0000269|PubMed:1505778"
FT   CARBOHYD        230
FT                   /note="N-linked (Glc) (glycation) lysine; in vitro"
FT                   /evidence="ECO:0000269|PubMed:1505778"
FT   DISULFID        63..208
FT                   /evidence="ECO:0000269|PubMed:19289127,
FT                   ECO:0007744|PDB:2JLP"
FT   DISULFID        125..207
FT                   /evidence="ECO:0000269|PubMed:19289127,
FT                   ECO:0007744|PDB:2JLP"
FT   VARIANT         58
FT                   /note="A -> T (in dbSNP:rs2536512)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:3476950, ECO:0000269|PubMed:7959763,
FT                   ECO:0000269|Ref.3, ECO:0000269|Ref.4"
FT                   /id="VAR_020776"
FT   VARIANT         91
FT                   /note="A -> T (in dbSNP:rs17879876)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_020777"
FT   VARIANT         231
FT                   /note="R -> G (in dbSNP:rs1799895)"
FT                   /evidence="ECO:0000269|PubMed:7662997,
FT                   ECO:0000269|PubMed:8034674, ECO:0000269|PubMed:8546689,
FT                   ECO:0000269|PubMed:8864862, ECO:0000269|Ref.4"
FT                   /id="VAR_014705"
FT   STRAND          59..67
FT                   /evidence="ECO:0007829|PDB:2JLP"
FT   STRAND          79..88
FT                   /evidence="ECO:0007829|PDB:2JLP"
FT   STRAND          93..100
FT                   /evidence="ECO:0007829|PDB:2JLP"
FT   STRAND          104..117
FT                   /evidence="ECO:0007829|PDB:2JLP"
FT   HELIX           124..128
FT                   /evidence="ECO:0007829|PDB:2JLP"
FT   STRAND          145..152
FT                   /evidence="ECO:0007829|PDB:2JLP"
FT   STRAND          155..164
FT                   /evidence="ECO:0007829|PDB:2JLP"
FT   STRAND          166..169
FT                   /evidence="ECO:0007829|PDB:2JLP"
FT   STRAND          176..183
FT                   /evidence="ECO:0007829|PDB:2JLP"
FT   STRAND          190..192
FT                   /evidence="ECO:0007829|PDB:2JLP"
FT   HELIX           195..198
FT                   /evidence="ECO:0007829|PDB:2JLP"
FT   STRAND          204..209
FT                   /evidence="ECO:0007829|PDB:2JLP"
FT   HELIX           216..222
FT                   /evidence="ECO:0007829|PDB:2JLP"
SQ   SEQUENCE   240 AA;  25851 MW;  585B8DEBFC506CF4 CRC64;
     MLALLCSCLL LAAGASDAWT GEDSAEPNSD SAEWIRDMYA KVTEIWQEVM QRRDDDGALH
     AACQVQPSAT LDAAQPRVTG VVLFRQLAPR AKLDAFFALE GFPTEPNSSS RAIHVHQFGD
     LSQGCESTGP HYNPLAVPHP QHPGDFGNFA VRDGSLWRYR AGLAASLAGP HSIVGRAVVV
     HAGEDDLGRG GNQASVENGN AGRRLACCVV GVCGPGLWER QAREHSERKK RRRESECKAA
//