Reviewed, UniProtKB/Swiss-Prot P19801 (ABP1_HUMAN)

Names and origin

Protein names

Recommended name:
    Amiloride-sensitive amine oxidase [copper-containing]
      Short name=Diamine oxidase
      Short name=DAO
    EC=1.4.3.22
Alternative name(s):
    Amiloride-binding protein
      Short name=ABP
    Histaminase
    Kidney amine oxidase
      Short name=KAO

Gene names

Name:	ABP1
Synonyms:	AOC1, DAO1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	751 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 By similarity. Binds 2 calcium ions per subunit By similarity. Contains 1 topaquinone per subunit By similarity.
Subcellular location	Secreted › extracellular 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 component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
Ligand	Calcium Copper Heparin-binding Metal-binding
Molecular function	Oxidoreductase
PTM	Glycoprotein TPQ
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	amine metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell peroxisome Non-traceable author statement. Source: ProtInc
Molecular function	amine oxidase activity Ref.7 Inferred from direct assay. Source: MGI calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW heparin binding Inferred from electronic annotation. Source: UniProtKB-KW quinone binding Inferred from electronic annotation. Source: InterPro
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:
     619-619: R → RTEGGQPRALSQARSPVPGR

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Ref.7
	Chain	20 – 751	732	Amiloride-sensitive amine oxidase [copper-containing]		PRO_0000035666
Regions
	Region	568 – 575	8	Heparin-binding By similarity
Sites
	Active site	373	1	Proton acceptor By similarity
	Active site	461	1	Schiff-base intermediate with substrate; via topaquinone By similarity
	Metal binding	510	1	Copper By similarity
	Metal binding	512	1	Copper By similarity
	Metal binding	519	1	Calcium 1 By similarity
	Metal binding	520	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	521	1	Calcium 1 By similarity
	Metal binding	562	1	Calcium 2 By similarity
	Metal binding	653	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	656	1	Calcium 2 By similarity
	Metal binding	658	1	Calcium 2 By similarity
	Metal binding	664	1	Calcium 1 By similarity
	Metal binding	665	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	675	1	Copper By similarity
Amino acid modifications
	Modified residue	461	1	2',4',5'-topaquinone By similarity
	Glycosylation	110	1	N-linked (GlcNAc...) Potential
	Glycosylation	168	1	N-linked (GlcNAc...) Potential
	Glycosylation	538	1	N-linked (GlcNAc...) Potential
	Glycosylation	745	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	619	1	R → RTEGGQPRALSQARSPVPGR in isoform 2.		VSP_006548
	Natural variant	16	1	T → M: dbSNP rs10156191. Ref.4		VAR_025078
	Natural variant	332	1	S → F: dbSNP rs1049742. Ref.4 Ref.3		VAR_025079
	Natural variant	479	1	M → I: dbSNP rs45558339.		VAR_025080
	Natural variant	645	1	H → D: dbSNP rs1049793. Ref.4 Ref.3 Ref.1 Ref.6		VAR_007542
	Natural variant	659	1	N → H: dbSNP rs35070995. Ref.4		VAR_025081
Experimental info
	Sequence conflict	28	1	R → A AA sequence Ref.7
	Sequence conflict	280	1	P → A in AAA58358. Ref.1
	Sequence conflict	290	1	D → T in AAA58358. Ref.1
	Sequence conflict	572	1	K → R in AAA58358. Ref.1
	Sequence conflict	592	1	T → S in AAA58358. Ref.1
	Sequence conflict	592	1	T → S in CAA55046. Ref.2
	Sequence conflict	592	1	T → S in AAC50270. Ref.3
	Sequence conflict	592	1	T → S in AAB60381. Ref.3
	Sequence conflict	592	1	T → S in AAH14093. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 7, 2009. Version 4. Checksum: 37114CD0D446639C	FASTA	751	85,378
	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
	Isoform 2 (DAO2). Checksum: D592FC97BA29D7CC	FASTA	770	87,324
	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 EEQAITWART EGGQPRALSQ ARSPVPGRYP LAVTKYRESE LCSSSIYHQN 670 680 690 700 710 720 DPWHPPVVFE QFLHNNENIE NEDLVAWVTV GFLHIPHSED IPNTATPGNS VGFLLRPFNF 730 740 750 760 770 FPEDPSLASR DTVIVWPRDN GPNYVQRWIP EDRDCSMPPP FSYNGTYRPV

References

	« Hide 'large scale' referencesShow '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: 2217167] [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: 8182053] [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: 8595053] [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. , 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: 12853948] [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: 15489334] [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: 8144586] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-39, CHARACTERIZATION. Tissue: Placenta.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBLGenBankDDBJ	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. BC014093 mRNA. Translation: AAH14093.1.
IPI	IPI00020982. IPI00219832.
PIR	A54053.
RefSeq	NP_001082.2.
UniGene	Hs.647097
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P19801.
Genome annotation databases
Ensembl	ENST00000360937; ENSP00000354193; ENSG00000002726; Homo sapiens. [Genome view] ENST00000467291; ENSP00000418328; ENSG00000002726; Homo sapiens. [Genome view] ENST00000487631; ENSP00000417051; ENSG00000002726; Homo sapiens. [Genome view] ENST00000493429; ENSP00000418614; ENSG00000002726; Homo sapiens. [Genome view]
GeneID	26.
KEGG	hsa:26.
UCSC	uc003why.1. human. uc003wia.1. human.
Organism-specific databases
CTD	26.
GeneCards	GC07P150180.
H-InvDB	HIX0007216.
HGNC	HGNC:80. ABP1.
MIM	104610. gene.
PharmGKB	PA24416.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P19801.
InParanoid	P19801.
Enzyme and pathway databases
BRENDA	1.4.3.6. 247.
Gene expression databases
ArrayExpress	P19801.
Bgee	P19801.
CleanEx	HS_ABP1.
Genevestigator	P19801.
GermOnline	ENSG00000002726. Homo sapiens.
Family and domain databases
InterPro	IPR000269. 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]
Gene3D	G3DSA:3.10.450.40. CuNH_oxidase. 2 hits. G3DSA:2.70.98.20. Lyase_8_central. 1 hit.
PANTHER	PTHR10638. CuNH_oxidase. 1 hit.
Pfam	PF01179. Cu_amine_oxid. 1 hit. PF02727. Cu_amine_oxidN2. 1 hit. PF02728. Cu_amine_oxidN3. 1 hit. [Graphical view]
PRINTS	PR00766. CUDAOXIDASE.
PROSITE	PS01164. COPPER_AMINE_OXID_1. 1 hit. PS01165. COPPER_AMINE_OXID_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00594. Amiloride. DB00127. Spermine.
NextBio	85.
SOURCE	Search...

Entry information

Entry name

ABP1_HUMAN

Accession

Primary (citable) accession number: P19801
Secondary accession number(s): Q16683 , Q16684, Q56II4, Q6GU42

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	July 7, 2009
Last modified:	December 15, 2009
This is version 109 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.