NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar;
TISSUE=Colon, and Lung;
DOI=10.1111/j.1432-1033.1993.tb18188.x; PubMed=8375402 [NCBI, ExPASy, EBI, Israel, Japan]
Lingueglia E., Renard S., Voilley N., Waldmann R., Chassande O., Lazdunski M., Barbry P.;
"Molecular cloning and functional expression of different molecular forms of rat amiloride-binding proteins.";
Eur. J. Biochem. 216:679-687(1993).

[2]

NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8023885 [NCBI, ExPASy, EBI, Israel, Japan]
Verity K., Fuller P.J.;
"Isolation of a rat amiloride-binding protein cDNA clone: tissue distribution and regulation of expression.";
Am. J. Physiol. 266:C1505-C1512(1994).

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).
COFACTOR: Binds 2 calcium ions per subunit (By similarity).
COFACTOR: Contains 1 topaquinone per subunit (By similarity).
SUBCELLULAR LOCATION: Secreted, extracellular space.
PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
MISCELLANEOUS: Inhibited by amiloride in a competitive manner (By similarity).
SIMILARITY: Belongs to the copper/topaquinone oxidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X73911; CAA52116.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X73912; CAA52117.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S70383; AAB31157.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S36847; S34656.

UniGene

Rn.54493

3D structure databases

ModBase

P36633.

PTM databases

PhosphoSite

P36633; -.

Organism-specific databases

RGD

61296; Abp1.

Gene expression databases

ArrayExpress

P36633; -.

GermOnline

ENSRNOG00000008575; Rattus norvegicus.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0008131;	Molecular function: amine oxidase activity (inferred from electronic annotation from InterPro).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005507;	Molecular function: copper ion binding (inferred from electronic annotation from InterPro).
GO:0008201;	Molecular function: heparin binding (inferred from electronic annotation from UniProtKB-KW).
GO:0048038;	Molecular function: quinone binding (inferred from electronic annotation from InterPro).
GO:0009308;	Biological process: cellular amine metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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 of domain structure.

Gene3D

G3DSA:3.10.450.40; CuNH_oxidase; 2.
G3DSA:2.70.98.20; Lyase_8_central; 1.

PANTHER

PTHR10638; CuNH_oxidase; 1.

Pfam

PF01179; Cu_amine_oxid; 1.
PF02727; Cu_amine_oxidN2; 1.
PF02728; Cu_amine_oxidN3; 1.
Pfam graphical view of domain structure.

PRINTS

PR00766; CUDAOXIDASE.

PROSITE

PS01164; COPPER_AMINE_OXID_1; 1.
PS01165; COPPER_AMINE_OXID_2; 1.

ProtoNet

P36633.

Genome annotation databases

Ensembl

ENSRNOG00000008575; Rattus norvegicus. [Contig view]

Phylogenomic databases

HOVERGEN

P36633; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Calcium; Copper; Glycoprotein; Heparin-binding; Metal-binding; Oxidoreductase; Secreted; Signal; TPQ.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 22`	`22`	`Potential.`
`CHAIN`	`23 746`	`724`	`Amiloride-sensitive amine oxidase [copper-containing].`	`PRO_0000035668`
`REGION`	`563 570`	`8`	`Heparin-binding (By similarity).`
`ACT_SITE`	`368 368`		`Proton acceptor (By similarity).`
`ACT_SITE`	`456 456`		`Schiff-base intermediate with substrate; via topaquinone (By similarity).`
`METAL`	`505 505`		`Copper (By similarity).`
`METAL`	`507 507`		`Copper (By similarity).`
`METAL`	`514 514`		`Calcium 1 (By similarity).`
`METAL`	`515 515`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`516 516`		`Calcium 1 (By similarity).`
`METAL`	`557 557`		`Calcium 2 (By similarity).`
`METAL`	`648 648`		`Calcium 2; via carbonyl oxygen (By similarity).`
`METAL`	`651 651`		`Calcium 2 (By similarity).`
`METAL`	`653 653`		`Calcium 2 (By similarity).`
`METAL`	`659 659`		`Calcium 1 (By similarity).`
`METAL`	`660 660`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`670 670`		`Copper (By similarity).`
`MOD_RES`	`456 456`		`2',4',5'-topaquinone (By similarity).`
`CARBOHYD`	`110 110`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`269 269`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`533 533`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`740 740`		`N-linked (GlcNAc...) (Potential).`
`CONFLICT`	`587 587`		`S -> T (in Ref. 2; AAB31157).`

Sequence information

Length: 746 AA [This is the length of the unprocessed precursor]

Molecular weight: 85021 Da [This is the MW of the unprocessed precursor]

CRC64: 6C564D044D07BCB2 [This is a checksum on the sequence]

        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

P36633 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools