GenomeNet

Database: UniProt
Entry: P19801
LinkDB: P19801
Original site: P19801 
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   17-JUN-2020, entry version 201.
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;
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;
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; 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; Q96HA8: WDYHV1; NbExp=3; IntAct=EBI-12826295, EBI-741158;
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/";
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   SMR; P19801; -.
DR   BioGRID; 106544; 5.
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   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; 369 antibodies.
DR   DNASU; 26; -.
DR   Ensembl; ENST00000360937; ENSP00000354193; ENSG00000002726. [P19801-1]
DR   Ensembl; ENST00000416793; ENSP00000411613; ENSG00000002726. [P19801-2]
DR   Ensembl; ENST00000467291; ENSP00000418328; ENSG00000002726. [P19801-1]
DR   Ensembl; ENST00000493429; ENSP00000418614; ENSG00000002726. [P19801-1]
DR   GeneID; 26; -.
DR   KEGG; hsa:26; -.
DR   UCSC; uc003whz.3; human. [P19801-1]
DR   CTD; 26; -.
DR   DisGeNET; 26; -.
DR   EuPathDB; HostDB:ENSG00000002726.19; -.
DR   GeneCards; AOC1; -.
DR   HGNC; HGNC:80; AOC1.
DR   HPA; ENSG00000002726; Group enriched (intestine, placenta).
DR   MIM; 104610; gene.
DR   neXtProt; NX_P19801; -.
DR   OpenTargets; ENSG00000002726; -.
DR   PharmGKB; PA24416; -.
DR   eggNOG; KOG1186; Eukaryota.
DR   eggNOG; COG3733; LUCA.
DR   GeneTree; ENSGT00950000183207; -.
DR   HOGENOM; CLU_015739_1_0_1; -.
DR   InParanoid; P19801; -.
DR   KO; K11182; -.
DR   OMA; GKKFPRY; -.
DR   OrthoDB; 1320015at2759; -.
DR   PhylomeDB; P19801; -.
DR   TreeFam; TF314750; -.
DR   BioCyc; MetaCyc:HS00083-MONOMER; -.
DR   BRENDA; 1.4.3.22; 2681.
DR   Reactome; R-HSA-211945; Phase I - Functionalization of compounds.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 26; 3 hits in 775 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 decidua and 97 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:0008144; F:drug binding; 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:0043312; P:neutrophil degranulation; TAS:Reactome.
DR   GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
DR   GO; GO:0046677; P:response to antibiotic; IDA:UniProtKB.
DR   GO; GO:0042493; P:response to drug; IDA:UniProtKB.
DR   GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
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; Polymorphism; Reference proteome; Secreted;
KW   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   REGION          371..381
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000244|PDB:3HII,
FT                   ECO:0000269|PubMed:19764817"
FT   REGION          458..463
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000244|PDB:3HII,
FT                   ECO:0000269|PubMed:19764817"
FT   REGION          568..575
FT                   /note="Heparin-binding"
FT                   /evidence="ECO:0000250"
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:0000244|PDB:3HI7, ECO:0000244|PDB:3HIG,
FT                   ECO:0000244|PDB:3HII, ECO:0000244|PDB:3K5T,
FT                   ECO:0000269|PubMed:19764817"
FT   METAL           510
FT                   /note="Copper; via tele nitrogen"
FT                   /evidence="ECO:0000244|PDB:3HI7, ECO:0000244|PDB:3HIG,
FT                   ECO:0000244|PDB:3HII, ECO:0000244|PDB:3K5T,
FT                   ECO:0000244|PDB:3MPH, ECO:0000269|PubMed:19764817"
FT   METAL           512
FT                   /note="Copper; via tele nitrogen"
FT                   /evidence="ECO:0000244|PDB:3HI7, ECO:0000244|PDB:3HIG,
FT                   ECO:0000244|PDB:3HII, ECO:0000244|PDB:3K5T,
FT                   ECO:0000244|PDB:3MPH, ECO:0000269|PubMed:19764817"
FT   METAL           519
FT                   /note="Calcium 1"
FT                   /evidence="ECO:0000244|PDB:3HI7, ECO:0000244|PDB:3HIG,
FT                   ECO:0000244|PDB:3HII, ECO:0000244|PDB:3K5T,
FT                   ECO:0000244|PDB:3MPH, ECO:0000269|PubMed:19764817"
FT   METAL           520
FT                   /note="Calcium 1; via carbonyl oxygen"
FT                   /evidence="ECO:0000244|PDB:3HI7, ECO:0000244|PDB:3HIG,
FT                   ECO:0000244|PDB:3HII, ECO:0000244|PDB:3K5T,
FT                   ECO:0000244|PDB:3MPH, ECO:0000269|PubMed:19764817"
FT   METAL           521
FT                   /note="Calcium 1"
FT                   /evidence="ECO:0000244|PDB:3HI7, ECO:0000244|PDB:3HIG,
FT                   ECO:0000244|PDB:3HII, ECO:0000244|PDB:3K5T,
FT                   ECO:0000244|PDB:3MPH, ECO:0000269|PubMed:19764817"
FT   METAL           562
FT                   /note="Calcium 2"
FT                   /evidence="ECO:0000244|PDB:3HI7, ECO:0000244|PDB:3HIG,
FT                   ECO:0000244|PDB:3HII, ECO:0000244|PDB:3K5T,
FT                   ECO:0000244|PDB:3MPH, ECO:0000269|PubMed:19764817"
FT   METAL           653
FT                   /note="Calcium 2; via carbonyl oxygen"
FT                   /evidence="ECO:0000244|PDB:3HI7, ECO:0000244|PDB:3HIG,
FT                   ECO:0000244|PDB:3HII, ECO:0000244|PDB:3K5T,
FT                   ECO:0000244|PDB:3MPH, ECO:0000269|PubMed:19764817"
FT   METAL           656
FT                   /note="Calcium 2"
FT                   /evidence="ECO:0000244|PDB:3HI7, ECO:0000244|PDB:3HIG,
FT                   ECO:0000244|PDB:3HII, ECO:0000244|PDB:3K5T,
FT                   ECO:0000244|PDB:3MPH, ECO:0000269|PubMed:19764817"
FT   METAL           658
FT                   /note="Calcium 2"
FT                   /evidence="ECO:0000244|PDB:3HI7, ECO:0000244|PDB:3HIG,
FT                   ECO:0000244|PDB:3HII, ECO:0000244|PDB:3K5T,
FT                   ECO:0000244|PDB:3MPH, ECO:0000269|PubMed:19764817"
FT   METAL           664
FT                   /note="Calcium 1"
FT                   /evidence="ECO:0000244|PDB:3HI7, ECO:0000244|PDB:3HIG,
FT                   ECO:0000244|PDB:3HII, ECO:0000244|PDB:3K5T,
FT                   ECO:0000244|PDB:3MPH, ECO:0000269|PubMed:19764817"
FT   METAL           665
FT                   /note="Calcium 1; via carbonyl oxygen"
FT                   /evidence="ECO:0000244|PDB:3HI7, ECO:0000244|PDB:3HIG,
FT                   ECO:0000244|PDB:3HII, ECO:0000244|PDB:3K5T,
FT                   ECO:0000244|PDB:3MPH, ECO:0000269|PubMed:19764817"
FT   METAL           675
FT                   /note="Copper; via pros nitrogen"
FT                   /evidence="ECO:0000244|PDB:3HI7, ECO:0000244|PDB:3HIG,
FT                   ECO:0000244|PDB:3HII, ECO:0000244|PDB:3K5T,
FT                   ECO:0000244|PDB:3MPH, ECO:0000269|PubMed:19764817"
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:0000244|PDB:3HI7, ECO:0000244|PDB:3HIG,
FT                   ECO:0000244|PDB:3HII, ECO:0000244|PDB:3K5T,
FT                   ECO:0000244|PDB:3MPH, ECO:0000269|PubMed:19764817"
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:0000244|PDB:3HI7, ECO:0000244|PDB:3HIG,
FT                   ECO:0000244|PDB:3HII, ECO:0000244|PDB:3K5T,
FT                   ECO:0000244|PDB:3MPH, ECO:0000269|PubMed:19764817"
FT   CARBOHYD        745
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000244|PDB:3HI7, ECO:0000244|PDB:3HIG,
FT                   ECO:0000244|PDB:3HII, ECO:0000244|PDB:3K5T,
FT                   ECO:0000244|PDB:3MPH, ECO:0000269|PubMed:19764817"
FT   DISULFID        177..181
FT                   /evidence="ECO:0000244|PDB:3HI7, ECO:0000244|PDB:3HIG,
FT                   ECO:0000244|PDB:3HII, ECO:0000269|PubMed:19764817"
FT   DISULFID        391..417
FT                   /evidence="ECO:0000244|PDB:3HI7, ECO:0000244|PDB:3HIG,
FT                   ECO:0000244|PDB:3HII, ECO:0000269|PubMed:19764817"
FT   DISULFID        736
FT                   /note="Interchain"
FT                   /evidence="ECO:0000244|PDB:3HI7, ECO:0000244|PDB:3HIG,
FT                   ECO:0000244|PDB:3HII, ECO:0000269|PubMed:19764817"
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:0000244|PDB:3HI7"
FT   HELIX           38..49
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   HELIX           52..54
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          64..75
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   HELIX           79..88
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          96..103
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          105..108
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          110..117
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          119..121
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          124..129
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   HELIX           137..140
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   HELIX           145..158
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   HELIX           160..162
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   HELIX           163..170
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          173..176
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          178..186
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          191..193
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          198..205
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   HELIX           210..212
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          214..222
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          225..227
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   HELIX           228..230
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          232..238
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   HELIX           246..254
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          301..303
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          309..313
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          316..320
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          322..329
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   TURN            330..332
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          333..341
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          344..359
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   HELIX           364..368
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          370..372
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   HELIX           373..376
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   HELIX           378..380
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   TURN            387..389
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          395..405
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          410..422
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          427..433
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          435..445
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          448..456
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          458..469
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          475..483
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          487..489
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   HELIX           492..496
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          497..502
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          505..508
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          510..520
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          524..540
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          547..559
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   HELIX           562..565
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          569..571
FT                   /evidence="ECO:0000244|PDB:3MPH"
FT   STRAND          575..584
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          590..598
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   HELIX           610..619
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          621..626
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   HELIX           629..631
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   TURN            637..641
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          643..645
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   HELIX           652..655
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          661..675
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   HELIX           679..681
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          691..704
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   HELIX           706..709
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          714..717
FT                   /evidence="ECO:0000244|PDB:3HI7"
FT   STRAND          720..723
FT                   /evidence="ECO:0000244|PDB:3K5T"
FT   STRAND          725..727
FT                   /evidence="ECO:0000244|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
//
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