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Amiloride-sensitive amine oxidase [copper-containing] (DAO) (Diamine oxidase) (EC 1.4.3.22) (Amiloride-binding protein 1) (Amine oxidase copper domain-containing protein 1) (Histaminase) (Kidney amine oxidase) (KAO)

 AOC1_HUMAN              Reviewed;         751 AA.
P19801; C9J690; Q16683; Q16684; Q56II4; Q6GU42;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
07-JUL-2009, sequence version 4.
25-OCT-2017, entry version 181.
RecName: Full=Amiloride-sensitive amine oxidase [copper-containing];
Short=DAO;
Short=Diamine oxidase;
EC=1.4.3.22 {ECO:0000269|PubMed:19764817};
AltName: Full=Amiloride-binding protein 1;
AltName: Full=Amine oxidase copper domain-containing protein 1;
AltName: Full=Histaminase;
AltName: Full=Kidney amine oxidase;
Short=KAO;
Flags: Precursor;
Name=AOC1; Synonyms=ABP1, DAO1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT
ASP-645.
TISSUE=Kidney;
PubMed=2217167; DOI=10.1073/pnas.87.19.7347;
Barbry P., Champe M., Chassande O., Munemitsu S., Champigny G.,
Lingueglia E., Maes P., Frelin C., Tartar A., Ullrich A.,
Lazdunski M.;
"Human kidney amiloride-binding protein: cDNA structure and functional
expression.";
Proc. Natl. Acad. Sci. U.S.A. 87:7347-7351(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8182053;
Chassande O., Renard S., Barbry P., Lazdunski M.;
"The human gene for diamine oxidase, an amiloride binding protein.
Molecular cloning, sequencing, and characterization of the promoter.";
J. Biol. Chem. 269:14484-14489(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS PHE-332
AND ASP-645.
TISSUE=Placenta;
PubMed=8595053; DOI=10.1007/BF00553624;
Zhang X., Kim J., McIntire W.S.;
"cDNA sequences of variant forms of human placenta diamine oxidase.";
Biochem. Genet. 33:261-268(1995).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-16; PHE-332;
ILE-479; ASP-645 AND HIS-659.
NIEHS SNPs program;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ASP-645.
TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 20-39, AND CHARACTERIZATION.
TISSUE=Placenta;
PubMed=8144586;
Novotny W.F., Chassande O., Baker M., Lazdunski M., Barbry P.;
"Diamine oxidase is the amiloride-binding protein and is inhibited by
amiloride analogues.";
J. Biol. Chem. 269:9921-9925(1994).
[8]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX
WITH CALCIUM; COPPER AND IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538
AND ASN-745, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES,
DISULFIDE BONDS, TOPAQUINONE AT TYR-461, SUBUNIT, ENZYME REGULATION,
AND CATALYTIC ACTIVITY.
PubMed=19764817; DOI=10.1021/bi9014192;
McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O.,
Brown D.E., Dooley D.M., Guss J.M.;
"Structure and inhibition of human diamine oxidase.";
Biochemistry 48:9810-9822(2009).
-!- FUNCTION: Catalyzes the degradation of compounds such as
putrescine, histamine, spermine, and spermidine, substances
involved in allergic and immune responses, cell proliferation,
tissue differentiation, tumor formation, and possibly apoptosis.
Placental DAO is thought to play a role in the regulation of the
female reproductive function.
-!- CATALYTIC ACTIVITY: Histamine + H(2)O + O(2) = (imidazol-4-
yl)acetaldehyde + NH(3) + H(2)O(2). {ECO:0000269|PubMed:19764817}.
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378;
Evidence={ECO:0000269|PubMed:19764817};
Note=Binds 1 copper ion per subunit.
{ECO:0000269|PubMed:19764817};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:19764817};
Note=Binds 2 calcium ions per subunit.
{ECO:0000269|PubMed:19764817};
-!- COFACTOR:
Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
Evidence={ECO:0000269|PubMed:19764817};
Note=Contains 1 topaquinone per subunit.
{ECO:0000269|PubMed:19764817};
-!- ENZYME REGULATION: Inhibited by isoniazid, cimetidine, clonidine,
pentamidine, berenil and pentamidine.
{ECO:0000269|PubMed:19764817}.
-!- SUBUNIT: Homodimer; disulfide-linked.
{ECO:0000269|PubMed:19764817}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P19801-1; Sequence=Displayed;
Name=2; Synonyms=DAO2;
IsoId=P19801-2; Sequence=VSP_055190;
Note=Ref.3 (AAB60381) sequence is in conflict in position:
632:A->R. {ECO:0000305};
-!- TISSUE SPECIFICITY: Placenta and kidney.
-!- PTM: Topaquinone (TPQ) is generated by copper-dependent
autoxidation of a specific tyrosyl residue.
{ECO:0000250|UniProtKB:P12807}.
-!- MISCELLANEOUS: Inhibited by amiloride in a competitive manner.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA58358.1; Type=Frameshift; Positions=266, 284, 328, 494, 497, 514, 707, 729; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/abp1/";
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EMBL; M55602; AAA58358.1; ALT_FRAME; mRNA.
EMBL; X78212; CAA55046.1; -; Genomic_DNA.
EMBL; U11862; AAC50270.1; -; mRNA.
EMBL; U11863; AAB60381.1; -; mRNA.
EMBL; AY948960; AAX81409.1; -; Genomic_DNA.
EMBL; AC006343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC006479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC014093; AAH14093.1; -; mRNA.
CCDS; CCDS43679.1; -. [P19801-1]
CCDS; CCDS64797.1; -. [P19801-2]
PIR; A54053; A54053.
RefSeq; NP_001082.2; NM_001091.3. [P19801-1]
RefSeq; NP_001259001.1; NM_001272072.1. [P19801-2]
RefSeq; XP_016867433.1; XM_017011944.1. [P19801-2]
RefSeq; XP_016867434.1; XM_017011945.1. [P19801-2]
RefSeq; XP_016867435.1; XM_017011946.1. [P19801-2]
RefSeq; XP_016867436.1; XM_017011947.1. [P19801-1]
UniGene; Hs.647097; -.
UniGene; Hs.733889; -.
PDB; 3HI7; X-ray; 1.80 A; A/B=21-751.
PDB; 3HIG; X-ray; 2.09 A; A/B=21-751.
PDB; 3HII; X-ray; 2.15 A; A/B=21-751.
PDB; 3K5T; X-ray; 2.11 A; A=21-751.
PDB; 3MPH; X-ray; 2.05 A; A/B=21-751.
PDBsum; 3HI7; -.
PDBsum; 3HIG; -.
PDBsum; 3HII; -.
PDBsum; 3K5T; -.
PDBsum; 3MPH; -.
ProteinModelPortal; P19801; -.
SMR; P19801; -.
BioGrid; 106544; 1.
IntAct; P19801; 9.
STRING; 9606.ENSP00000354193; -.
BindingDB; P19801; -.
ChEMBL; CHEMBL2118; -.
DrugBank; DB00594; Amiloride.
DrugBank; DB03608; Diminazene.
iPTMnet; P19801; -.
PhosphoSitePlus; P19801; -.
DMDM; 251757489; -.
PaxDb; P19801; -.
PeptideAtlas; P19801; -.
PRIDE; P19801; -.
TopDownProteomics; P19801-1; -. [P19801-1]
DNASU; 26; -.
Ensembl; ENST00000360937; ENSP00000354193; ENSG00000002726. [P19801-1]
Ensembl; ENST00000416793; ENSP00000411613; ENSG00000002726. [P19801-2]
Ensembl; ENST00000467291; ENSP00000418328; ENSG00000002726. [P19801-1]
Ensembl; ENST00000493429; ENSP00000418614; ENSG00000002726. [P19801-1]
GeneID; 26; -.
KEGG; hsa:26; -.
UCSC; uc003whz.3; human. [P19801-1]
CTD; 26; -.
DisGeNET; 26; -.
EuPathDB; HostDB:ENSG00000002726.19; -.
GeneCards; AOC1; -.
H-InvDB; HIX0007216; -.
HGNC; HGNC:80; AOC1.
HPA; HPA031032; -.
HPA; HPA031033; -.
MIM; 104610; gene.
neXtProt; NX_P19801; -.
OpenTargets; ENSG00000002726; -.
PharmGKB; PA24416; -.
eggNOG; KOG1186; Eukaryota.
eggNOG; COG3733; LUCA.
GeneTree; ENSGT00510000046461; -.
HOGENOM; HOG000233919; -.
HOVERGEN; HBG004164; -.
InParanoid; P19801; -.
KO; K11182; -.
OMA; PLRRHFN; -.
OrthoDB; EOG091G0C1O; -.
PhylomeDB; P19801; -.
TreeFam; TF314750; -.
BioCyc; MetaCyc:HS00083-MONOMER; -.
BRENDA; 1.4.3.22; 2681.
Reactome; R-HSA-211945; Phase I - Functionalization of compounds.
Reactome; R-HSA-6798695; Neutrophil degranulation.
EvolutionaryTrace; P19801; -.
GenomeRNAi; 26; -.
PRO; PR:P19801; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000002726; -.
CleanEx; HS_ABP1; -.
ExpressionAtlas; P19801; baseline and differential.
Genevisible; P19801; HS.
GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005777; C:peroxisome; NAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
GO; GO:0052597; F:diamine oxidase activity; IDA:UniProtKB.
GO; GO:0008144; F:drug binding; IDA:UniProtKB.
GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
GO; GO:0052598; F:histamine oxidase activity; TAS:Reactome.
GO; GO:0052599; F:methylputrescine oxidase activity; IEA:UniProtKB-EC.
GO; GO:0008131; F:primary amine oxidase activity; IDA:UniProtKB.
GO; GO:0052600; F:propane-1,3-diamine oxidase activity; IEA:UniProtKB-EC.
GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0048038; F:quinone binding; IDA:UniProtKB.
GO; GO:0004872; F:receptor activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0009308; P:amine metabolic process; IEA:InterPro.
GO; GO:0097185; P:cellular response to azide; IDA:UniProtKB.
GO; GO:0071280; P:cellular response to copper ion; IDA:UniProtKB.
GO; GO:0035874; P:cellular response to copper ion starvation; IDA:UniProtKB.
GO; GO:0071504; P:cellular response to heparin; TAS:UniProtKB.
GO; GO:0071420; P:cellular response to histamine; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
GO; GO:0046677; P:response to antibiotic; IDA:UniProtKB.
GO; GO:0042493; P:response to drug; IDA:UniProtKB.
GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
Gene3D; 2.70.98.20; -; 1.
InterPro; IPR000269; Cu_amine_oxidase.
InterPro; IPR015798; Cu_amine_oxidase_C.
InterPro; IPR036460; Cu_amine_oxidase_C_sf.
InterPro; IPR016182; Cu_amine_oxidase_N-reg.
InterPro; IPR015800; Cu_amine_oxidase_N2.
InterPro; IPR015802; Cu_amine_oxidase_N3.
PANTHER; PTHR10638; PTHR10638; 1.
Pfam; PF01179; Cu_amine_oxid; 1.
Pfam; PF02727; Cu_amine_oxidN2; 1.
Pfam; PF02728; Cu_amine_oxidN3; 1.
PRINTS; PR00766; CUDAOXIDASE.
SUPFAM; SSF49998; SSF49998; 1.
SUPFAM; SSF54416; SSF54416; 2.
PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Complete proteome;
Copper; Direct protein sequencing; Disulfide bond; Glycoprotein;
Heparin-binding; Metal-binding; Oxidoreductase; Polymorphism;
Reference proteome; Secreted; Signal; TPQ.
SIGNAL 1 19 {ECO:0000269|PubMed:8144586}.
CHAIN 20 751 Amiloride-sensitive amine oxidase
[copper-containing].
/FTId=PRO_0000035666.
REGION 371 381 Substrate binding. {ECO:0000244|PDB:3HII,
ECO:0000269|PubMed:19764817}.
REGION 458 463 Substrate binding. {ECO:0000244|PDB:3HII,
ECO:0000269|PubMed:19764817}.
REGION 568 575 Heparin-binding. {ECO:0000250}.
ACT_SITE 373 373 Proton acceptor.
{ECO:0000269|PubMed:19764817}.
ACT_SITE 461 461 Schiff-base intermediate with substrate;
via topaquinone. {ECO:0000244|PDB:3HI7,
ECO:0000244|PDB:3HIG,
ECO:0000244|PDB:3HII,
ECO:0000244|PDB:3K5T,
ECO:0000269|PubMed:19764817}.
METAL 510 510 Copper; via tele nitrogen.
{ECO:0000244|PDB:3HI7,
ECO:0000244|PDB:3HIG,
ECO:0000244|PDB:3HII,
ECO:0000244|PDB:3K5T,
ECO:0000244|PDB:3MPH,
ECO:0000269|PubMed:19764817}.
METAL 512 512 Copper; via tele nitrogen.
{ECO:0000244|PDB:3HI7,
ECO:0000244|PDB:3HIG,
ECO:0000244|PDB:3HII,
ECO:0000244|PDB:3K5T,
ECO:0000244|PDB:3MPH,
ECO:0000269|PubMed:19764817}.
METAL 519 519 Calcium 1. {ECO:0000244|PDB:3HI7,
ECO:0000244|PDB:3HIG,
ECO:0000244|PDB:3HII,
ECO:0000244|PDB:3K5T,
ECO:0000244|PDB:3MPH,
ECO:0000269|PubMed:19764817}.
METAL 520 520 Calcium 1; via carbonyl oxygen.
{ECO:0000244|PDB:3HI7,
ECO:0000244|PDB:3HIG,
ECO:0000244|PDB:3HII,
ECO:0000244|PDB:3K5T,
ECO:0000244|PDB:3MPH,
ECO:0000269|PubMed:19764817}.
METAL 521 521 Calcium 1. {ECO:0000244|PDB:3HI7,
ECO:0000244|PDB:3HIG,
ECO:0000244|PDB:3HII,
ECO:0000244|PDB:3K5T,
ECO:0000244|PDB:3MPH,
ECO:0000269|PubMed:19764817}.
METAL 562 562 Calcium 2. {ECO:0000244|PDB:3HI7,
ECO:0000244|PDB:3HIG,
ECO:0000244|PDB:3HII,
ECO:0000244|PDB:3K5T,
ECO:0000244|PDB:3MPH,
ECO:0000269|PubMed:19764817}.
METAL 653 653 Calcium 2; via carbonyl oxygen.
{ECO:0000244|PDB:3HI7,
ECO:0000244|PDB:3HIG,
ECO:0000244|PDB:3HII,
ECO:0000244|PDB:3K5T,
ECO:0000244|PDB:3MPH,
ECO:0000269|PubMed:19764817}.
METAL 656 656 Calcium 2. {ECO:0000244|PDB:3HI7,
ECO:0000244|PDB:3HIG,
ECO:0000244|PDB:3HII,
ECO:0000244|PDB:3K5T,
ECO:0000244|PDB:3MPH,
ECO:0000269|PubMed:19764817}.
METAL 658 658 Calcium 2. {ECO:0000244|PDB:3HI7,
ECO:0000244|PDB:3HIG,
ECO:0000244|PDB:3HII,
ECO:0000244|PDB:3K5T,
ECO:0000244|PDB:3MPH,
ECO:0000269|PubMed:19764817}.
METAL 664 664 Calcium 1. {ECO:0000244|PDB:3HI7,
ECO:0000244|PDB:3HIG,
ECO:0000244|PDB:3HII,
ECO:0000244|PDB:3K5T,
ECO:0000244|PDB:3MPH,
ECO:0000269|PubMed:19764817}.
METAL 665 665 Calcium 1; via carbonyl oxygen.
{ECO:0000244|PDB:3HI7,
ECO:0000244|PDB:3HIG,
ECO:0000244|PDB:3HII,
ECO:0000244|PDB:3K5T,
ECO:0000244|PDB:3MPH,
ECO:0000269|PubMed:19764817}.
METAL 675 675 Copper; via pros nitrogen.
{ECO:0000244|PDB:3HI7,
ECO:0000244|PDB:3HIG,
ECO:0000244|PDB:3HII,
ECO:0000244|PDB:3K5T,
ECO:0000244|PDB:3MPH,
ECO:0000269|PubMed:19764817}.
MOD_RES 461 461 2',4',5'-topaquinone.
{ECO:0000269|PubMed:19764817}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3HI7,
ECO:0000244|PDB:3HIG,
ECO:0000244|PDB:3HII,
ECO:0000244|PDB:3K5T,
ECO:0000244|PDB:3MPH,
ECO:0000269|PubMed:19764817}.
CARBOHYD 168 168 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 538 538 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3HI7,
ECO:0000244|PDB:3HIG,
ECO:0000244|PDB:3HII,
ECO:0000244|PDB:3K5T,
ECO:0000244|PDB:3MPH,
ECO:0000269|PubMed:19764817}.
CARBOHYD 745 745 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3HI7,
ECO:0000244|PDB:3HIG,
ECO:0000244|PDB:3HII,
ECO:0000244|PDB:3K5T,
ECO:0000244|PDB:3MPH,
ECO:0000269|PubMed:19764817}.
DISULFID 177 181 {ECO:0000244|PDB:3HI7,
ECO:0000244|PDB:3HIG,
ECO:0000244|PDB:3HII,
ECO:0000269|PubMed:19764817}.
DISULFID 391 417 {ECO:0000244|PDB:3HI7,
ECO:0000244|PDB:3HIG,
ECO:0000244|PDB:3HII,
ECO:0000269|PubMed:19764817}.
DISULFID 736 736 Interchain. {ECO:0000244|PDB:3HI7,
ECO:0000244|PDB:3HIG,
ECO:0000244|PDB:3HII,
ECO:0000269|PubMed:19764817}.
VAR_SEQ 618 618 A -> ARTEGGQPRALSQAASPVPG (in isoform 2).
{ECO:0000303|PubMed:8595053}.
/FTId=VSP_055190.
VARIANT 16 16 T -> M (in dbSNP:rs10156191).
{ECO:0000269|Ref.4}.
/FTId=VAR_025078.
VARIANT 332 332 S -> F (in dbSNP:rs1049742).
{ECO:0000269|PubMed:8595053,
ECO:0000269|Ref.4}.
/FTId=VAR_025079.
VARIANT 479 479 M -> I (in dbSNP:rs45558339).
{ECO:0000269|Ref.4}.
/FTId=VAR_025080.
VARIANT 645 645 H -> D (in dbSNP:rs1049793).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2217167,
ECO:0000269|PubMed:8595053,
ECO:0000269|Ref.4}.
/FTId=VAR_007542.
VARIANT 659 659 N -> H (in dbSNP:rs35070995).
{ECO:0000269|Ref.4}.
/FTId=VAR_025081.
CONFLICT 28 28 R -> A (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 280 280 P -> A (in Ref. 1; AAA58358).
{ECO:0000305}.
CONFLICT 290 290 D -> T (in Ref. 1; AAA58358).
{ECO:0000305}.
CONFLICT 572 572 K -> R (in Ref. 1; AAA58358).
{ECO:0000305}.
CONFLICT 592 592 T -> S (in Ref. 1; AAA58358, 2; CAA55046,
3; AAC50270/AAB60381 and 6; AAH14093).
{ECO:0000305}.
HELIX 29 33 {ECO:0000244|PDB:3HI7}.
HELIX 38 49 {ECO:0000244|PDB:3HI7}.
HELIX 52 54 {ECO:0000244|PDB:3HI7}.
STRAND 64 75 {ECO:0000244|PDB:3HI7}.
HELIX 79 88 {ECO:0000244|PDB:3HI7}.
STRAND 96 103 {ECO:0000244|PDB:3HI7}.
STRAND 105 108 {ECO:0000244|PDB:3HI7}.
STRAND 110 117 {ECO:0000244|PDB:3HI7}.
STRAND 119 121 {ECO:0000244|PDB:3HI7}.
STRAND 124 129 {ECO:0000244|PDB:3HI7}.
HELIX 137 140 {ECO:0000244|PDB:3HI7}.
HELIX 145 158 {ECO:0000244|PDB:3HI7}.
HELIX 160 162 {ECO:0000244|PDB:3HI7}.
HELIX 163 170 {ECO:0000244|PDB:3HI7}.
STRAND 173 176 {ECO:0000244|PDB:3HI7}.
STRAND 178 186 {ECO:0000244|PDB:3HI7}.
STRAND 191 193 {ECO:0000244|PDB:3HI7}.
STRAND 198 205 {ECO:0000244|PDB:3HI7}.
HELIX 210 212 {ECO:0000244|PDB:3HI7}.
STRAND 214 222 {ECO:0000244|PDB:3HI7}.
STRAND 225 227 {ECO:0000244|PDB:3HI7}.
HELIX 228 230 {ECO:0000244|PDB:3HI7}.
STRAND 232 238 {ECO:0000244|PDB:3HI7}.
HELIX 246 254 {ECO:0000244|PDB:3HI7}.
STRAND 301 303 {ECO:0000244|PDB:3HI7}.
STRAND 309 313 {ECO:0000244|PDB:3HI7}.
STRAND 316 320 {ECO:0000244|PDB:3HI7}.
STRAND 322 329 {ECO:0000244|PDB:3HI7}.
TURN 330 332 {ECO:0000244|PDB:3HI7}.
STRAND 333 341 {ECO:0000244|PDB:3HI7}.
STRAND 344 359 {ECO:0000244|PDB:3HI7}.
HELIX 364 368 {ECO:0000244|PDB:3HI7}.
STRAND 370 372 {ECO:0000244|PDB:3HI7}.
HELIX 373 376 {ECO:0000244|PDB:3HI7}.
HELIX 378 380 {ECO:0000244|PDB:3HI7}.
TURN 387 389 {ECO:0000244|PDB:3HI7}.
STRAND 395 405 {ECO:0000244|PDB:3HI7}.
STRAND 410 422 {ECO:0000244|PDB:3HI7}.
STRAND 427 433 {ECO:0000244|PDB:3HI7}.
STRAND 435 445 {ECO:0000244|PDB:3HI7}.
STRAND 448 456 {ECO:0000244|PDB:3HI7}.
STRAND 458 469 {ECO:0000244|PDB:3HI7}.
STRAND 475 483 {ECO:0000244|PDB:3HI7}.
STRAND 487 489 {ECO:0000244|PDB:3HI7}.
HELIX 492 496 {ECO:0000244|PDB:3HI7}.
STRAND 497 502 {ECO:0000244|PDB:3HI7}.
STRAND 505 508 {ECO:0000244|PDB:3HI7}.
STRAND 510 520 {ECO:0000244|PDB:3HI7}.
STRAND 524 540 {ECO:0000244|PDB:3HI7}.
STRAND 547 559 {ECO:0000244|PDB:3HI7}.
HELIX 562 565 {ECO:0000244|PDB:3HI7}.
STRAND 569 571 {ECO:0000244|PDB:3MPH}.
STRAND 575 584 {ECO:0000244|PDB:3HI7}.
STRAND 590 598 {ECO:0000244|PDB:3HI7}.
HELIX 610 619 {ECO:0000244|PDB:3HI7}.
STRAND 621 626 {ECO:0000244|PDB:3HI7}.
HELIX 629 631 {ECO:0000244|PDB:3HI7}.
TURN 637 641 {ECO:0000244|PDB:3HI7}.
STRAND 643 645 {ECO:0000244|PDB:3HI7}.
HELIX 652 655 {ECO:0000244|PDB:3HI7}.
STRAND 661 675 {ECO:0000244|PDB:3HI7}.
HELIX 679 681 {ECO:0000244|PDB:3HI7}.
STRAND 691 704 {ECO:0000244|PDB:3HI7}.
HELIX 706 709 {ECO:0000244|PDB:3HI7}.
STRAND 714 717 {ECO:0000244|PDB:3HI7}.
STRAND 720 723 {ECO:0000244|PDB:3K5T}.
STRAND 725 727 {ECO:0000244|PDB:3HI7}.
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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