AOC1_HUMAN
ID AOC1_HUMAN Reviewed; 751 AA.
AC P19801; C9J690; Q16683; Q16684; Q56II4; Q6GU42;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 4.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Amiloride-sensitive amine oxidase [copper-containing];
DE Short=DAO;
DE Short=Diamine oxidase;
DE EC=1.4.3.22 {ECO:0000269|PubMed:19764817};
DE AltName: Full=Amiloride-binding protein 1;
DE AltName: Full=Amine oxidase copper domain-containing protein 1;
DE AltName: Full=Histaminase;
DE AltName: Full=Kidney amine oxidase;
DE Short=KAO;
DE Flags: Precursor;
GN Name=AOC1; Synonyms=ABP1, DAO1;
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 ASP-645.
RC TISSUE=Kidney;
RX PubMed=2217167; DOI=10.1073/pnas.87.19.7347;
RA Barbry P., Champe M., Chassande O., Munemitsu S., Champigny G.,
RA Lingueglia E., Maes P., Frelin C., Tartar A., Ullrich A., Lazdunski M.;
RT "Human kidney amiloride-binding protein: cDNA structure and functional
RT expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:7347-7351(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8182053; DOI=10.1016/s0021-9258(17)36648-6;
RA Chassande O., Renard S., Barbry P., Lazdunski M.;
RT "The human gene for diamine oxidase, an amiloride binding protein.
RT Molecular cloning, sequencing, and characterization of the promoter.";
RL J. Biol. Chem. 269:14484-14489(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS PHE-332 AND
RP ASP-645.
RC TISSUE=Placenta;
RX PubMed=8595053; DOI=10.1007/bf00553624;
RA Zhang X., Kim J., McIntire W.S.;
RT "cDNA sequences of variant forms of human placenta diamine oxidase.";
RL Biochem. Genet. 33:261-268(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-16; PHE-332; ILE-479;
RP ASP-645 AND HIS-659.
RG NIEHS SNPs program;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-645.
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 [7]
RP PROTEIN SEQUENCE OF 20-39, AND CHARACTERIZATION.
RC TISSUE=Placenta;
RX PubMed=8144586; DOI=10.1016/s0021-9258(17)36970-3;
RA Novotny W.F., Chassande O., Baker M., Lazdunski M., Barbry P.;
RT "Diamine oxidase is the amiloride-binding protein and is inhibited by
RT amiloride analogues.";
RL J. Biol. Chem. 269:9921-9925(1994).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX WITH
RP CALCIUM; COPPER AND IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538 AND
RP ASN-745, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES,
RP DISULFIDE BONDS, TOPAQUINONE AT TYR-461, SUBUNIT, ACTIVITY REGULATION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=19764817; DOI=10.1021/bi9014192;
RA McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O.,
RA Brown D.E., Dooley D.M., Guss J.M.;
RT "Structure and inhibition of human diamine oxidase.";
RL Biochemistry 48:9810-9822(2009).
CC -!- FUNCTION: Catalyzes the degradation of compounds such as putrescine,
CC histamine, spermine, and spermidine, substances involved in allergic
CC and immune responses, cell proliferation, tissue differentiation, tumor
CC formation, and possibly apoptosis. Placental DAO is thought to play a
CC role in the regulation of the female reproductive function.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + histamine + O2 = H2O2 + imidazole-4-acetaldehyde +
CC NH4(+); Xref=Rhea:RHEA:25625, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:27398, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58432; EC=1.4.3.22;
CC Evidence={ECO:0000269|PubMed:19764817};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:19764817};
CC Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:19764817};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:19764817};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000269|PubMed:19764817};
CC -!- COFACTOR:
CC Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC Evidence={ECO:0000269|PubMed:19764817};
CC Note=Contains 1 topaquinone per subunit. {ECO:0000269|PubMed:19764817};
CC -!- ACTIVITY REGULATION: Inhibited by isoniazid, cimetidine, clonidine,
CC pentamidine, berenil and pentamidine. {ECO:0000269|PubMed:19764817}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:19764817}.
CC -!- INTERACTION:
CC P19801; Q15038: DAZAP2; NbExp=3; IntAct=EBI-12826295, EBI-724310;
CC P19801; O75593: FOXH1; NbExp=3; IntAct=EBI-12826295, EBI-1759806;
CC P19801; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-12826295, EBI-10261141;
CC P19801; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-12826295, EBI-741158;
CC P19801; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-12826295, EBI-1389308;
CC P19801; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-12826295, EBI-11987469;
CC P19801; Q01085-2: TIAL1; NbExp=3; IntAct=EBI-12826295, EBI-11064654;
CC P19801; O43711: TLX3; NbExp=3; IntAct=EBI-12826295, EBI-3939165;
CC P19801; Q96K80: ZC3H10; NbExp=3; IntAct=EBI-12826295, EBI-742550;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P19801-1; Sequence=Displayed;
CC Name=2; Synonyms=DAO2;
CC IsoId=P19801-2; Sequence=VSP_055190;
CC -!- TISSUE SPECIFICITY: Placenta and kidney.
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000250|UniProtKB:P12807}.
CC -!- MISCELLANEOUS: Inhibited by amiloride in a competitive manner.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58358.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/abp1/";
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DR EMBL; M55602; AAA58358.1; ALT_FRAME; mRNA.
DR EMBL; X78212; CAA55046.1; -; Genomic_DNA.
DR EMBL; U11862; AAC50270.1; -; mRNA.
DR EMBL; U11863; AAB60381.1; -; mRNA.
DR EMBL; AY948960; AAX81409.1; -; Genomic_DNA.
DR EMBL; AC006343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014093; AAH14093.1; -; mRNA.
DR CCDS; CCDS43679.1; -. [P19801-1]
DR CCDS; CCDS64797.1; -. [P19801-2]
DR PIR; A54053; A54053.
DR RefSeq; NP_001082.2; NM_001091.3. [P19801-1]
DR RefSeq; NP_001259001.1; NM_001272072.1. [P19801-2]
DR RefSeq; XP_016867433.1; XM_017011944.1. [P19801-2]
DR RefSeq; XP_016867434.1; XM_017011945.1. [P19801-2]
DR RefSeq; XP_016867435.1; XM_017011946.1. [P19801-2]
DR RefSeq; XP_016867436.1; XM_017011947.1. [P19801-1]
DR PDB; 3HI7; X-ray; 1.80 A; A/B=21-751.
DR PDB; 3HIG; X-ray; 2.09 A; A/B=21-751.
DR PDB; 3HII; X-ray; 2.15 A; A/B=21-751.
DR PDB; 3K5T; X-ray; 2.11 A; A=21-751.
DR PDB; 3MPH; X-ray; 2.05 A; A/B=21-751.
DR PDBsum; 3HI7; -.
DR PDBsum; 3HIG; -.
DR PDBsum; 3HII; -.
DR PDBsum; 3K5T; -.
DR PDBsum; 3MPH; -.
DR AlphaFoldDB; P19801; -.
DR SMR; P19801; -.
DR BioGRID; 106544; 15.
DR IntAct; P19801; 10.
DR STRING; 9606.ENSP00000411613; -.
DR BindingDB; P19801; -.
DR ChEMBL; CHEMBL2118; -.
DR DrugBank; DB00594; Amiloride.
DR DrugBank; DB01373; Calcium.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB03608; Diminazene.
DR DrugCentral; P19801; -.
DR GlyGen; P19801; 5 sites, 2 O-linked glycans (1 site).
DR iPTMnet; P19801; -.
DR PhosphoSitePlus; P19801; -.
DR BioMuta; AOC1; -.
DR DMDM; 251757489; -.
DR CPTAC; CPTAC-2204; -.
DR jPOST; P19801; -.
DR MassIVE; P19801; -.
DR PaxDb; P19801; -.
DR PeptideAtlas; P19801; -.
DR PRIDE; P19801; -.
DR ProteomicsDB; 53688; -. [P19801-1]
DR ProteomicsDB; 53689; -. [P19801-2]
DR ProteomicsDB; 8732; -.
DR TopDownProteomics; P19801-1; -. [P19801-1]
DR Antibodypedia; 10528; 399 antibodies from 28 providers.
DR DNASU; 26; -.
DR Ensembl; ENST00000360937.9; ENSP00000354193.4; ENSG00000002726.21. [P19801-1]
DR Ensembl; ENST00000416793.6; ENSP00000411613.2; ENSG00000002726.21. [P19801-2]
DR Ensembl; ENST00000467291.5; ENSP00000418328.1; ENSG00000002726.21. [P19801-1]
DR Ensembl; ENST00000493429.5; ENSP00000418614.1; ENSG00000002726.21. [P19801-1]
DR GeneID; 26; -.
DR KEGG; hsa:26; -.
DR MANE-Select; ENST00000360937.9; ENSP00000354193.4; NM_001091.4; NP_001082.2.
DR UCSC; uc003whz.3; human. [P19801-1]
DR CTD; 26; -.
DR DisGeNET; 26; -.
DR GeneCards; AOC1; -.
DR HGNC; HGNC:80; AOC1.
DR HPA; ENSG00000002726; Group enriched (intestine, kidney, placenta).
DR MIM; 104610; gene.
DR neXtProt; NX_P19801; -.
DR OpenTargets; ENSG00000002726; -.
DR PharmGKB; PA24416; -.
DR VEuPathDB; HostDB:ENSG00000002726; -.
DR eggNOG; KOG1186; Eukaryota.
DR GeneTree; ENSGT00950000183207; -.
DR HOGENOM; CLU_015739_1_0_1; -.
DR InParanoid; P19801; -.
DR OMA; HRTEHKT; -.
DR OrthoDB; 1320015at2759; -.
DR PhylomeDB; P19801; -.
DR TreeFam; TF314750; -.
DR BioCyc; MetaCyc:HS00083-MON; -.
DR BRENDA; 1.4.3.22; 2681.
DR PathwayCommons; P19801; -.
DR Reactome; R-HSA-211945; Phase I - Functionalization of compounds.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P19801; -.
DR BioGRID-ORCS; 26; 7 hits in 1038 CRISPR screens.
DR ChiTaRS; AOC1; human.
DR EvolutionaryTrace; P19801; -.
DR GenomeRNAi; 26; -.
DR Pharos; P19801; Tchem.
DR PRO; PR:P19801; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P19801; protein.
DR Bgee; ENSG00000002726; Expressed in ileal mucosa and 102 other tissues.
DR ExpressionAtlas; P19801; baseline and differential.
DR Genevisible; P19801; HS.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0052597; F:diamine oxidase activity; IDA:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
DR GO; GO:0052598; F:histamine oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0052599; F:methylputrescine oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008131; F:primary amine oxidase activity; IDA:UniProtKB.
DR GO; GO:0052600; F:propane-1,3-diamine oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0048038; F:quinone binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0009308; P:amine metabolic process; IBA:GO_Central.
DR GO; GO:0097185; P:cellular response to azide; IDA:UniProtKB.
DR GO; GO:0071280; P:cellular response to copper ion; IDA:UniProtKB.
DR GO; GO:0035874; P:cellular response to copper ion starvation; IDA:UniProtKB.
DR GO; GO:0071504; P:cellular response to heparin; TAS:UniProtKB.
DR GO; GO:0071420; P:cellular response to histamine; IDA:UniProtKB.
DR GO; GO:0009445; P:putrescine metabolic process; IMP:UniProtKB.
DR GO; GO:0046677; P:response to antibiotic; IDA:UniProtKB.
DR Gene3D; 2.70.98.20; -; 1.
DR InterPro; IPR000269; Cu_amine_oxidase.
DR InterPro; IPR015798; Cu_amine_oxidase_C.
DR InterPro; IPR036460; Cu_amine_oxidase_C_sf.
DR InterPro; IPR016182; Cu_amine_oxidase_N-reg.
DR InterPro; IPR015800; Cu_amine_oxidase_N2.
DR InterPro; IPR015802; Cu_amine_oxidase_N3.
DR PANTHER; PTHR10638; PTHR10638; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR Pfam; PF02727; Cu_amine_oxidN2; 1.
DR Pfam; PF02728; Cu_amine_oxidN3; 1.
DR PRINTS; PR00766; CUDAOXIDASE.
DR SUPFAM; SSF49998; SSF49998; 1.
DR SUPFAM; SSF54416; SSF54416; 2.
DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
DR PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Copper;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Heparin-binding;
KW Metal-binding; Oxidoreductase; Reference proteome; Secreted; Signal; TPQ.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:8144586"
FT CHAIN 20..751
FT /note="Amiloride-sensitive amine oxidase [copper-
FT containing]"
FT /id="PRO_0000035666"
FT ACT_SITE 373
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:19764817"
FT ACT_SITE 461
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000269|PubMed:19764817,
FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG,
FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T"
FT BINDING 371..381
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19764817,
FT ECO:0007744|PDB:3HII"
FT BINDING 458..463
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19764817,
FT ECO:0007744|PDB:3HII"
FT BINDING 510
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:19764817,
FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG,
FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T,
FT ECO:0007744|PDB:3MPH"
FT BINDING 512
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:19764817,
FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG,
FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T,
FT ECO:0007744|PDB:3MPH"
FT BINDING 519
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19764817,
FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG,
FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T,
FT ECO:0007744|PDB:3MPH"
FT BINDING 520
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19764817,
FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG,
FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T,
FT ECO:0007744|PDB:3MPH"
FT BINDING 521
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19764817,
FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG,
FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T,
FT ECO:0007744|PDB:3MPH"
FT BINDING 562
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19764817,
FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG,
FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T,
FT ECO:0007744|PDB:3MPH"
FT BINDING 568..575
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT BINDING 653
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19764817,
FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG,
FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T,
FT ECO:0007744|PDB:3MPH"
FT BINDING 656
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19764817,
FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG,
FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T,
FT ECO:0007744|PDB:3MPH"
FT BINDING 658
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19764817,
FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG,
FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T,
FT ECO:0007744|PDB:3MPH"
FT BINDING 664
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19764817,
FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG,
FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T,
FT ECO:0007744|PDB:3MPH"
FT BINDING 665
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19764817,
FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG,
FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T,
FT ECO:0007744|PDB:3MPH"
FT BINDING 675
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:19764817,
FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG,
FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T,
FT ECO:0007744|PDB:3MPH"
FT MOD_RES 461
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000269|PubMed:19764817"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19764817,
FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG,
FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T,
FT ECO:0007744|PDB:3MPH"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19764817,
FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG,
FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T,
FT ECO:0007744|PDB:3MPH"
FT CARBOHYD 745
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19764817,
FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG,
FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T,
FT ECO:0007744|PDB:3MPH"
FT DISULFID 177..181
FT /evidence="ECO:0000269|PubMed:19764817,
FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG,
FT ECO:0007744|PDB:3HII"
FT DISULFID 391..417
FT /evidence="ECO:0000269|PubMed:19764817,
FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG,
FT ECO:0007744|PDB:3HII"
FT DISULFID 736
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:19764817,
FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG,
FT ECO:0007744|PDB:3HII"
FT VAR_SEQ 618
FT /note="A -> ARTEGGQPRALSQAASPVPG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8595053"
FT /id="VSP_055190"
FT VARIANT 16
FT /note="T -> M (in dbSNP:rs10156191)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_025078"
FT VARIANT 332
FT /note="S -> F (in dbSNP:rs1049742)"
FT /evidence="ECO:0000269|PubMed:8595053, ECO:0000269|Ref.4"
FT /id="VAR_025079"
FT VARIANT 479
FT /note="M -> I (in dbSNP:rs45558339)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_025080"
FT VARIANT 645
FT /note="H -> D (in dbSNP:rs1049793)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2217167, ECO:0000269|PubMed:8595053,
FT ECO:0000269|Ref.4"
FT /id="VAR_007542"
FT VARIANT 659
FT /note="N -> H (in dbSNP:rs35070995)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_025081"
FT CONFLICT 28
FT /note="R -> A (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="P -> A (in Ref. 1; AAA58358)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="D -> T (in Ref. 1; AAA58358)"
FT /evidence="ECO:0000305"
FT CONFLICT 572
FT /note="K -> R (in Ref. 1; AAA58358)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="T -> S (in Ref. 1; AAA58358, 2; CAA55046, 3;
FT AAC50270/AAB60381 and 6; AAH14093)"
FT /evidence="ECO:0000305"
FT HELIX 29..33
FT /evidence="ECO:0007829|PDB:3HI7"
FT HELIX 38..49
FT /evidence="ECO:0007829|PDB:3HI7"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 64..75
FT /evidence="ECO:0007829|PDB:3HI7"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:3HI7"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:3HI7"
FT HELIX 145..158
FT /evidence="ECO:0007829|PDB:3HI7"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:3HI7"
FT HELIX 163..170
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 178..186
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:3HI7"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 214..222
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:3HI7"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 232..238
FT /evidence="ECO:0007829|PDB:3HI7"
FT HELIX 246..254
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 322..329
FT /evidence="ECO:0007829|PDB:3HI7"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 333..341
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 344..359
FT /evidence="ECO:0007829|PDB:3HI7"
FT HELIX 364..368
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:3HI7"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:3HI7"
FT HELIX 378..380
FT /evidence="ECO:0007829|PDB:3HI7"
FT TURN 387..389
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 395..405
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 410..422
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 427..433
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 435..445
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 448..456
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 458..469
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 475..483
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:3HI7"
FT HELIX 492..496
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 497..502
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 505..508
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 510..520
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 524..540
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 547..559
FT /evidence="ECO:0007829|PDB:3HI7"
FT HELIX 562..565
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:3MPH"
FT STRAND 575..584
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 590..598
FT /evidence="ECO:0007829|PDB:3HI7"
FT HELIX 610..619
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 621..626
FT /evidence="ECO:0007829|PDB:3HI7"
FT HELIX 629..631
FT /evidence="ECO:0007829|PDB:3HI7"
FT TURN 637..641
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 643..645
FT /evidence="ECO:0007829|PDB:3HI7"
FT HELIX 652..655
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 661..675
FT /evidence="ECO:0007829|PDB:3HI7"
FT HELIX 679..681
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 691..704
FT /evidence="ECO:0007829|PDB:3HI7"
FT HELIX 706..709
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 714..717
FT /evidence="ECO:0007829|PDB:3HI7"
FT STRAND 720..723
FT /evidence="ECO:0007829|PDB:3K5T"
FT STRAND 725..727
FT /evidence="ECO:0007829|PDB:3HI7"
FT CONFLICT P19801-2:632
FT /note="A -> R (in Ref. 3; AAB60381)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 751 AA; 85378 MW; 37114CD0D446639C CRC64;
MPALGWAVAA ILMLQTAMAE PSPGTLPRKA GVFSDLSNQE LKAVHSFLWS KKELRLQPSS
TTTMAKNTVF LIEMLLPKKY HVLRFLDKGE RHPVREARAV IFFGDQEHPN VTEFAVGPLP
GPCYMRALSP RPGYQSSWAS RPISTAEYAL LYHTLQEATK PLHQFFLNTT GFSFQDCHDR
CLAFTDVAPR GVASGQRRSW LIIQRYVEGY FLHPTGLELL VDHGSTDAGH WAVEQVWYNG
KFYGSPEELA RKYADGEVDV VVLEDPLPGG KGHDSTEEPP LFSSHKPRGD FPSPIHVSGP
RLVQPHGPRF RLEGNAVLYG GWSFAFRLRS SSGLQVLNVH FGGERIAYEV SVQEAVALYG
GHTPAGMQTK YLDVGWGLGS VTHELAPGID CPETATFLDT FHYYDADDPV HYPRALCLFE
MPTGVPLRRH FNSNFKGGFN FYAGLKGQVL VLRTTSTVYN YDYIWDFIFY PNGVMEAKMH
ATGYVHATFY TPEGLRHGTR LHTHLIGNIH THLVHYRVDL DVAGTKNSFQ TLQMKLENIT
NPWSPRHRVV QPTLEQTQYS WERQAAFRFK RKLPKYLLFT SPQENPWGHK RTYRLQIHSM
ADQVLPPGWQ EEQAITWARY PLAVTKYRES ELCSSSIYHQ NDPWHPPVVF EQFLHNNENI
ENEDLVAWVT VGFLHIPHSE DIPNTATPGN SVGFLLRPFN FFPEDPSLAS RDTVIVWPRD
NGPNYVQRWI PEDRDCSMPP PFSYNGTYRP V
