Amiloride-sensitive amine oxidase [copper-containing] precursor

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Reviewed, UniProtKB/Swiss-Prot P36633 (ABP1_RAT)

Last modified June 16, 2009. Version 80. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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

Gene names

Name:

Abp1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length	746 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

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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 By similarity.
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.
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.

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Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Copper Heparin-binding Metal-binding
Molecular function	Oxidoreductase
PTM	Glycoprotein TPQ
Gene Ontology (GO)
Biological process	cellular 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
Molecular function	amine oxidase activity Inferred from electronic annotation. Source: EC calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW drug binding Ref.1 Inferred from direct assay. Source: RGD heparin binding Inferred from electronic annotation. Source: UniProtKB-KW quinone binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

Potential

Chain

23 – 746

724

Amiloride-sensitive amine oxidase [copper-containing]

PRO_0000035668

Regions

Region

563 – 570

Heparin-binding By similarity

Sites

Active site

368

Proton acceptor By similarity

Active site

456

Schiff-base intermediate with substrate; via topaquinone By similarity

Metal binding

505

Copper By similarity

Metal binding

507

Copper By similarity

Metal binding

514

Calcium 1 By similarity

Metal binding

515

Calcium 1; via carbonyl oxygen By similarity

Metal binding

516

Calcium 1 By similarity

Metal binding

557

Calcium 2 By similarity

Metal binding

648

Calcium 2; via carbonyl oxygen By similarity

Metal binding

651

Calcium 2 By similarity

Metal binding

653

Calcium 2 By similarity

Metal binding

659

Calcium 1 By similarity

Metal binding

660

Calcium 1; via carbonyl oxygen By similarity

Metal binding

670

Copper By similarity

Amino acid modifications

Modified residue

456

2',4',5'-topaquinone By similarity

Glycosylation

110

N-linked (GlcNAc...) Potential

Glycosylation

269

N-linked (GlcNAc...) Potential

Glycosylation

533

N-linked (GlcNAc...) Potential

Glycosylation

740

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

587

S → T in AAB31157. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

P36633-1 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 6C564D044D07BCB2
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FASTA

746

85,021

        10         20         30         40         50         60 
MCLAFGWAAV ILVLQTVDTA SAVRTPYDKA RVFADLSPQE IKAVHSFLMN REELGLQPSK 

        70         80         90        100        110        120 
EPTLAKNSVF LIEMLLPKKK HVLKFLDEGR KGPNREARAV IFFGAQDYPN VTEFAVGPLP 

       130        140        150        160        170        180 
RPYYIRALSP RPGHHLSWSS RPISTAEYDL LYHTLKRATM PLHQFFLDTT GFSFLGCDDR 

       190        200        210        220        230        240 
CLTFTDVAPR GVASGQRRSW FIVQRYVEGY FLHPTGLEIL LDHGSTDVQD WRVEQLWYNG 

       250        260        270        280        290        300 
KFYNNPEELA RKYAVGEVDT VVLEDPLPNG TEKPPLFSSY KPRGEFHTPV NVAGPHVVQP 

       310        320        330        340        350        360 
SGPRYKLEGN TVLYGGWSFS YRLRSSSGLQ IFNVLFGGER VAYEVSVQEA VALYGGHTPA 

       370        380        390        400        410        420 
GMQTKYIDVG WGLGSVTHEL APGIDCPETA TFLDAFHYYD SDGPVHYPHA LCLFEMPTGV 

       430        440        450        460        470        480 
PLRRHFNSNF KGGFNFYAGL KGYVLVLRTT STVYNYDYIW DFIFYSNGVM EAKMHATGYV 

       490        500        510        520        530        540 
HATFYTPEGL RHGTRLQTHL LGNIHTHLVH YRVDMDVAGT KNSFQTLTMK LENLTNPWSP 

       550        560        570        580        590        600 
SHSLVQPTLE QTQYSQEHQA AFRFGQTLPK YLLFSSPQKN CWGHRRSYRL QIHSMAEQVL 

       610        620        630        640        650        660 
PPGWQEERAV TWARYPLAVT KYRESERYSS SLYNQNDPWD PPVVFEEFLR NNENIEDEDL 

       670        680        690        700        710        720 
VAWVTVGFLH IPHSEDVPNT ATPGNSVGFL LRPFNFFPED PSLASRDTVI VWPQDKGLNR 

       730        740 
VQRWIPEDRR CLVSPPFSYN GTYKPV

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References

[1]	"Molecular cloning and functional expression of different molecular forms of rat amiloride-binding proteins." Lingueglia E., Renard S., Voilley N., Waldmann R., Chassande O., Lazdunski M., Barbry P. Eur. J. Biochem. 216:679-687(1993) [PubMed: 8375402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Wistar. Tissue: Colon and Lung.
[2]	"Isolation of a rat amiloride-binding protein cDNA clone: tissue distribution and regulation of expression." Verity K., Fuller P.J. Am. J. Physiol. 266:C1505-C1512(1994) [PubMed: 8023885] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

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Cross-references

Sequence databases
	X73911 mRNA. Translation: CAA52116.1. X73912 mRNA. Translation: CAA52117.1. Different initiation. S70383 mRNA. Translation: AAB31157.1.
IPI	IPI00204571.
PIR	S34656. S36847.
UniGene	Rn.54493
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	ENSRNOG00000008575. Rattus norvegicus. [Contig view]
Organism-specific databases
RGD	61296. Abp1.
Phylogenomic databases
HOVERGEN	P36633.
Enzyme and pathway databases
BRENDA	1.4.3.6. 248.
Gene expression databases
ArrayExpress	P36633.
GermOnline	ENSRNOG00000008575. Rattus norvegicus.
Family and domain databases
InterPro	IPR000269. Cu_amine_oxidase. IPR015798. Cu_amine_oxidase_C. 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...

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Entry information

Entry name

ABP1_RAT

Accession

Primary (citable) accession number: P36633
Secondary accession number(s): Q63973

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	June 16, 2009
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents