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P19801 (AOC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Amiloride-sensitive amine oxidase [copper-containing]

Short name=DAO
Short name=Diamine oxidase
EC=1.4.3.22
Alternative name(s):
Amiloride-binding protein 1
Amine oxidase copper domain-containing protein 1
Histaminase
Kidney amine oxidase
Short name=KAO
Gene names
Name:AOC1
Synonyms:ABP1, DAO1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length751 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 + H2O + O2 = (imidazol-4-yl)acetaldehyde + NH3 + H2O2.

Cofactor

Binds 1 copper ion per subunit. Ref.8

Binds 2 calcium ions per subunit. Ref.8

Contains 1 topaquinone per subunit. Ref.8

Subunit structure

Homodimer; disulfide-linked. Ref.8

Subcellular location

Secretedextracellular space.

Tissue specificity

Placenta and kidney.

Post-translational modification

Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.

Miscellaneous

Inhibited by amiloride in a competitive manner By similarity.

Sequence similarities

Belongs to the copper/topaquinone oxidase family.

Sequence caution

The sequence AAA58358.1 differs from that shown. Reason: Frameshift at positions 266, 284, 328, 494, 497, 514, 707 and 729.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
   LigandCalcium
Copper
Heparin-binding
Metal-binding
   Molecular functionOxidoreductase
   PTMDisulfide bond
Glycoprotein
TPQ
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processamine metabolic process

Inferred from electronic annotation. Source: InterPro

cellular response to azide

Inferred from direct assay PubMed 16846222. Source: UniProtKB

cellular response to copper ion

Inferred from direct assay PubMed 9399025. Source: UniProtKB

cellular response to copper ion starvation

Inferred from direct assay PubMed 9399025. Source: UniProtKB

cellular response to heparin

Traceable author statement Ref.8. Source: UniProtKB

cellular response to histamine

Inferred from direct assay PubMed 12072962. Source: UniProtKB

oxidation-reduction process

Inferred from direct assay PubMed 16846222Ref.7. Source: UniProtKB

response to antibiotic

Inferred from direct assay Ref.8PubMed 7626074. Source: UniProtKB

response to drug

Inferred from direct assay Ref.7. Source: UniProtKB

sodium ion transmembrane transport

Traceable author statement Ref.1. Source: UniProtKB

   Cellular_componentextracellular space

Inferred from direct assay PubMed 12072962PubMed 9399025. Source: UniProtKB

peroxisome

Non-traceable author statement PubMed 1356107. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.1Ref.7. Source: UniProtKB

tight junction

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncalcium ion binding

Inferred from direct assay PubMed 12072962Ref.8. Source: UniProtKB

cation channel activity

Inferred from direct assay Ref.8. Source: UniProtKB

copper ion binding

Inferred from direct assay PubMed 12072962Ref.8. Source: UniProtKB

diamine oxidase activity

Inferred from direct assay PubMed 12072962PubMed 16846222Ref.7PubMed 9399025. Source: UniProtKB

drug binding

Inferred from direct assay Ref.1Ref.7. Source: UniProtKB

heparin binding

Inferred from direct assay PubMed 12072962Ref.8. Source: UniProtKB

histamine oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

methylputrescine oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

primary amine oxidase activity

Inferred from direct assay Ref.8. Source: UniProtKB

propane-1,3-diamine oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein complex binding

Inferred from direct assay Ref.8. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.8. Source: UniProtKB

quinone binding

Inferred from direct assay PubMed 12072962Ref.8. Source: UniProtKB

receptor activity

Inferred from direct assay Ref.1. Source: UniProtKB

sodium channel activity

Traceable author statement Ref.1. Source: UniProtKB

zinc ion binding

Inferred from direct assay PubMed 12072962. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P19801-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P19801-2)

Also known as: DAO2;

The sequence of this isoform differs from the canonical sequence as follows:
     618-618: A → ARTEGGQPRALSQAASPVPG

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.7
Chain20 – 751732Amiloride-sensitive amine oxidase [copper-containing]
PRO_0000035666

Regions

Region568 – 5758Heparin-binding By similarity

Sites

Active site3731Proton acceptor Ref.8
Active site4611Schiff-base intermediate with substrate; via topaquinone Ref.8
Metal binding5101Copper
Metal binding5121Copper
Metal binding5191Calcium 1
Metal binding5201Calcium 1; via carbonyl oxygen
Metal binding5211Calcium 1
Metal binding5621Calcium 2
Metal binding6531Calcium 2; via carbonyl oxygen
Metal binding6561Calcium 2
Metal binding6581Calcium 2
Metal binding6641Calcium 1
Metal binding6651Calcium 1; via carbonyl oxygen
Metal binding6751Copper

Amino acid modifications

Modified residue46112',4',5'-topaquinone
Glycosylation1101N-linked (GlcNAc...) Ref.8
Glycosylation1681N-linked (GlcNAc...) Potential
Glycosylation5381N-linked (GlcNAc...) Ref.8
Glycosylation7451N-linked (GlcNAc...) Ref.8
Disulfide bond177 ↔ 181 Ref.8
Disulfide bond391 ↔ 417 Ref.8
Disulfide bond736Interchain Ref.8

Natural variations

Alternative sequence6181A → ARTEGGQPRALSQAASPVPG in isoform 2.
VSP_055190
Natural variant161T → M. Ref.4
Corresponds to variant rs10156191 [ dbSNP | Ensembl ].
VAR_025078
Natural variant3321S → F. Ref.3 Ref.4
Corresponds to variant rs1049742 [ dbSNP | Ensembl ].
VAR_025079
Natural variant4791M → I. Ref.4
Corresponds to variant rs45558339 [ dbSNP | Ensembl ].
VAR_025080
Natural variant6451H → D. Ref.1 Ref.3 Ref.4 Ref.6
Corresponds to variant rs1049793 [ dbSNP | Ensembl ].
VAR_007542
Natural variant6591N → H. Ref.4
Corresponds to variant rs35070995 [ dbSNP | Ensembl ].
VAR_025081

Experimental info

Sequence conflict281R → A AA sequence Ref.7
Sequence conflict2801P → A in AAA58358. Ref.1
Sequence conflict2901D → T in AAA58358. Ref.1
Sequence conflict5721K → R in AAA58358. Ref.1
Sequence conflict5921T → S in AAA58358. Ref.1
Sequence conflict5921T → S in CAA55046. Ref.2
Sequence conflict5921T → S in AAC50270. Ref.3
Sequence conflict5921T → S in AAB60381. Ref.3
Sequence conflict5921T → S in AAH14093. Ref.6
Isoform 2:
Sequence conflict6321A → R in AAB60381. Ref.3

Secondary structure

................................................................................................................................. 751
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 7, 2009. Version 4.
Checksum: 37114CD0D446639C

FASTA75185,378
        10         20         30         40         50         60 
MPALGWAVAA ILMLQTAMAE PSPGTLPRKA GVFSDLSNQE LKAVHSFLWS KKELRLQPSS 

        70         80         90        100        110        120 
TTTMAKNTVF LIEMLLPKKY HVLRFLDKGE RHPVREARAV IFFGDQEHPN VTEFAVGPLP 

       130        140        150        160        170        180 
GPCYMRALSP RPGYQSSWAS RPISTAEYAL LYHTLQEATK PLHQFFLNTT GFSFQDCHDR 

       190        200        210        220        230        240 
CLAFTDVAPR GVASGQRRSW LIIQRYVEGY FLHPTGLELL VDHGSTDAGH WAVEQVWYNG 

       250        260        270        280        290        300 
KFYGSPEELA RKYADGEVDV VVLEDPLPGG KGHDSTEEPP LFSSHKPRGD FPSPIHVSGP 

       310        320        330        340        350        360 
RLVQPHGPRF RLEGNAVLYG GWSFAFRLRS SSGLQVLNVH FGGERIAYEV SVQEAVALYG 

       370        380        390        400        410        420 
GHTPAGMQTK YLDVGWGLGS VTHELAPGID CPETATFLDT FHYYDADDPV HYPRALCLFE 

       430        440        450        460        470        480 
MPTGVPLRRH FNSNFKGGFN FYAGLKGQVL VLRTTSTVYN YDYIWDFIFY PNGVMEAKMH 

       490        500        510        520        530        540 
ATGYVHATFY TPEGLRHGTR LHTHLIGNIH THLVHYRVDL DVAGTKNSFQ TLQMKLENIT 

       550        560        570        580        590        600 
NPWSPRHRVV QPTLEQTQYS WERQAAFRFK RKLPKYLLFT SPQENPWGHK RTYRLQIHSM 

       610        620        630        640        650        660 
ADQVLPPGWQ EEQAITWARY PLAVTKYRES ELCSSSIYHQ NDPWHPPVVF EQFLHNNENI 

       670        680        690        700        710        720 
ENEDLVAWVT VGFLHIPHSE DIPNTATPGN SVGFLLRPFN FFPEDPSLAS RDTVIVWPRD 

       730        740        750 
NGPNYVQRWI PEDRDCSMPP PFSYNGTYRP V 

« Hide

Isoform 2 (DAO2) [UniParc].

Checksum: CA4864D23DB6D7CC
Show »

FASTA77087,239

References

« Hide 'large scale' references
[1]"Human kidney amiloride-binding protein: cDNA structure and functional expression."
Barbry P., Champe M., Chassande O., Munemitsu S., Champigny G., Lingueglia E., Maes P., Frelin C., Tartar A., Ullrich A., Lazdunski M.
Proc. Natl. Acad. Sci. U.S.A. 87:7347-7351(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT ASP-645.
Tissue: Kidney.
[2]"The human gene for diamine oxidase, an amiloride binding protein. Molecular cloning, sequencing, and characterization of the promoter."
Chassande O., Renard S., Barbry P., Lazdunski M.
J. Biol. Chem. 269:14484-14489(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"cDNA sequences of variant forms of human placenta diamine oxidase."
Zhang X., Kim J., McIntire W.S.
Biochem. Genet. 33:261-268(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS PHE-332 AND ASP-645.
Tissue: Placenta.
[4]NIEHS SNPs program
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-16; PHE-332; ILE-479; ASP-645 AND HIS-659.
[5]"The DNA sequence of human chromosome 7."
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. expand/collapse author list , 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.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASP-645.
Tissue: Colon.
[7]"Diamine oxidase is the amiloride-binding protein and is inhibited by amiloride analogues."
Novotny W.F., Chassande O., Baker M., Lazdunski M., Barbry P.
J. Biol. Chem. 269:9921-9925(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-39, CHARACTERIZATION.
Tissue: Placenta.
[8]"Structure and inhibition of human diamine oxidase."
McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O., Brown D.E., Dooley D.M., Guss J.M.
Biochemistry 48:9810-9822(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX WITH IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538 AND ASN-745, COFACTOR, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES, DISULFIDE BONDS.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M55602 mRNA. Translation: AAA58358.1. Frameshift.
X78212 Genomic DNA. Translation: CAA55046.1.
U11862 mRNA. Translation: AAC50270.1.
U11863 mRNA. Translation: AAB60381.1.
AY948960 Genomic DNA. Translation: AAX81409.1.
AC006343 Genomic DNA. No translation available.
AC006479 Genomic DNA. No translation available.
BC014093 mRNA. Translation: AAH14093.1.
CCDSCCDS43679.1. [P19801-1]
CCDS64797.1. [P19801-2]
PIRA54053.
RefSeqNP_001082.2. NM_001091.3. [P19801-1]
NP_001259001.1. NM_001272072.1.
XP_005250024.1. XM_005249967.2. [P19801-1]
UniGeneHs.647097.
Hs.733889.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3HI7X-ray1.80A/B21-751[»]
3HIGX-ray2.09A/B21-751[»]
3HIIX-ray2.15A/B21-751[»]
3K5TX-ray2.11A21-751[»]
3MPHX-ray2.05A/B21-751[»]
ProteinModelPortalP19801.
SMRP19801. Positions 27-751.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000354193.

Chemistry

BindingDBP19801.
ChEMBLCHEMBL2118.
DrugBankDB00594. Amiloride.
DB00127. Spermine.

PTM databases

PhosphoSiteP19801.

Polymorphism databases

DMDM251757489.

Proteomic databases

PaxDbP19801.
PRIDEP19801.

Protocols and materials databases

DNASU26.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360937; ENSP00000354193; ENSG00000002726. [P19801-1]
ENST00000416793; ENSP00000411613; ENSG00000002726.
ENST00000467291; ENSP00000418328; ENSG00000002726. [P19801-1]
ENST00000493429; ENSP00000418614; ENSG00000002726. [P19801-1]
GeneID26.
KEGGhsa:26.
UCSCuc003why.1. human. [P19801-1]

Organism-specific databases

CTD26.
GeneCardsGC07P150523.
H-InvDBHIX0007216.
HGNCHGNC:80. AOC1.
HPAHPA031032.
HPA031033.
MIM104610. gene.
neXtProtNX_P19801.
PharmGKBPA24416.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3733.
HOGENOMHOG000233919.
HOVERGENHBG004164.
InParanoidP19801.
KOK11182.
OrthoDBEOG78WKR2.
PhylomeDBP19801.
TreeFamTF314750.

Enzyme and pathway databases

BioCycMetaCyc:HS00083-MONOMER.

Gene expression databases

ArrayExpressP19801.
BgeeP19801.
CleanExHS_ABP1.
GenevestigatorP19801.

Family and domain databases

Gene3D2.70.98.20. 1 hit.
3.10.450.40. 1 hit.
InterProIPR000269. Cu_amine_oxidase.
IPR015798. Cu_amine_oxidase_C.
IPR016182. Cu_amine_oxidase_N-reg.
IPR015800. Cu_amine_oxidase_N2.
IPR015801. Cu_amine_oxidase_N2/3.
IPR015802. Cu_amine_oxidase_N3.
[Graphical view]
PANTHERPTHR10638. PTHR10638. 1 hit.
PfamPF01179. Cu_amine_oxid. 1 hit.
PF02727. Cu_amine_oxidN2. 1 hit.
PF02728. Cu_amine_oxidN3. 1 hit.
[Graphical view]
PRINTSPR00766. CUDAOXIDASE.
SUPFAMSSF49998. SSF49998. 1 hit.
SSF54416. SSF54416. 2 hits.
PROSITEPS01164. COPPER_AMINE_OXID_1. 1 hit.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP19801.
GenomeRNAi26.
NextBio85.
PROP19801.
SOURCESearch...

Entry information

Entry nameAOC1_HUMAN
AccessionPrimary (citable) accession number: P19801
Secondary accession number(s): C9J690 expand/collapse secondary AC list , Q16683, Q16684, Q56II4, Q6GU42
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 7, 2009
Last modified: July 9, 2014
This is version 151 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM