[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). STRAIN=129/SvJ, and BALB/c; PubMed=9743358 [NCBI, ExPASy, EBI, Israel, Japan] Bono P., Salmi M., Smith D.J., Leppanen I., Horelli-Kuitunen N., Palotie A., Jalkanen S.; "Isolation, structural characterization, and chromosomal mapping of the mouse vascular adhesion protein-1 gene and promoter."; J. Immunol. 161:2953-2960(1998).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). DOI=10.1074/jbc.274.14.9515; PubMed=10092636 [NCBI, ExPASy, EBI, Israel, Japan] Moldes M., Feve B., Pairault J.; "Molecular cloning of a major mRNA species in murine 3T3 adipocyte lineage. differentiation-dependent expression, regulation, and identification as semicarbazide-sensitive amine oxidase."; J. Biol. Chem. 274:9515-9523(1999).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). STRAIN=C57BL/6; TISSUE=Brain; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

FUNCTION: Cell adhesion protein that participates in lymphocyte recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion. Has a monoamine oxidase activity (By similarity).
CATALYTIC ACTIVITY: RCH₂NH₂ + H₂O + O₂ = RCHO + 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).
SUBUNIT: Homodimer; disulfide-linked (By similarity).
SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein (By similarity).

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	O70423-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	O70423-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_016604.

PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
PTM: N- and O-glycosylated (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

AF054831; AAC23747.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF078705; AAC35839.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF115411; AAD09199.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC080857; AAH80857.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_033805.1; -.

UniGene

Mm.67281

3D structure databases

SMR

O70423; 57-715, 58-716.

ModBase

O70423.

Organism-specific databases

MGI

MGI:1306797; Aoc3.

Gene expression databases

ArrayExpress

O70423; -.

CleanEx

MM_AOC3; -.

GermOnline

ENSMUSG00000019326; Mus musculus.

Ontologies

GO:0009986;	Cellular component: cell surface (inferred from sequence or structural similarity from UniProtKB).
GO:0016021;	Cellular component: integral to membrane (inferred from sequence or structural similarity from UniProtKB).
GO:0005886;	Cellular component: plasma membrane (inferred from sequence or structural similarity from UniProtKB).
GO:0008131;	Molecular function: amine oxidase activity (inferred from sequence or structural similarity from UniProtKB).
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:0005515;	Molecular function: protein binding (inferred from electronic annotation from UniProtKB-KW).
GO:0048038;	Molecular function: quinone binding (inferred from sequence or structural similarity from UniProtKB).
GO:0007155;	Biological process: cell adhesion (inferred from sequence or structural similarity from UniProtKB).
GO:0009308;	Biological process: cellular amine metabolic process (inferred from sequence or structural similarity from UniProtKB).
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.

Proteomics databases

PRIDE

O70423; -.

Genome annotation databases

Ensembl

ENSMUSG00000019326; Mus musculus. [Contig view]

GeneID

11754; -.

KEGG

mmu:11754; -.

NMPDR

fig|10090.3.peg.25341; -.

Phylogenomic databases

HOGENOM

O70423; -.

HOVERGEN

O70423; -.

Other

279503; -.

Aoc3; Mus musculus.

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

Keywords

Alternative splicing; Calcium; Cell adhesion; Copper; Glycoprotein; Membrane; Metal-binding; Oxidoreductase; Signal-anchor; TPQ; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 765`	`764`	`Membrane primary amine oxidase.`	`PRO_0000064103`
`TOPO_DOM`	`2 6`	`5`	`Cytoplasmic (Potential).`
`TRANSMEM`	`7 27`	`21`	`Signal-anchor for type II membrane protein (Potential).`
`TOPO_DOM`	`28 765`	`738`	`Extracellular (Potential).`
`ACT_SITE`	`386 386`		`Proton acceptor (By similarity).`
`ACT_SITE`	`471 471`		`Schiff-base intermediate with substrate; via topaquinone (By similarity).`
`METAL`	`520 520`		`Copper (By similarity).`
`METAL`	`522 522`		`Copper (By similarity).`
`METAL`	`529 529`		`Calcium 1 (By similarity).`
`METAL`	`530 530`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`531 531`		`Calcium 1 (By similarity).`
`METAL`	`572 572`		`Calcium 2 (By similarity).`
`METAL`	`638 638`		`Calcium 2 (By similarity).`
`METAL`	`663 663`		`Calcium 2; via carbonyl oxygen (By similarity).`
`METAL`	`665 665`		`Calcium 2 (By similarity).`
`METAL`	`667 667`		`Calcium 2 (By similarity).`
`METAL`	`673 673`		`Calcium 1 (By similarity).`
`METAL`	`674 674`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`684 684`		`Copper (By similarity).`
`MOD_RES`	`471 471`		`2',4',5'-topaquinone (By similarity).`
`CARBOHYD`	`137 137`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`212 212`		`O-linked (GalNAc...) (By similarity).`
`CARBOHYD`	`232 232`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`294 294`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`592 592`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`659 659`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`666 666`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`198 199`		`By similarity.`
`DISULFID`	`734 741`		`By similarity.`
`DISULFID`	`748 748`		`Interchain (By similarity).`
`VAR_SEQ`	`630 765`		`Missing (in isoform 2).`	`VSP_016604`
`CONFLICT`	`659 659`		`N -> D (in Ref. 2; AAD09199).`

Sequence information

Length: 765 AA [This is the length of the unprocessed precursor]

Molecular weight: 84534 Da [This is the MW of the unprocessed precursor]

CRC64: 7489ED67D3DBB44D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTQKTTLVLL ALAVITIFAL VCVLLAGRSG DGGGLSQPLH CPSVLPSVQP RTHPSQSQPF 

        70         80         90        100        110        120 
ADLSPEELTA VMSFLTKHLG PGLVDAAQAR PSDNCVFSVE LQLPAKAAAL AHLDRGGPPP 

       130        140        150        160        170        180 
VREALAIIFF GGQPKPNVSE LVVGPLPHPS YMRDVTVERH GGPLPYYRRP VLDREYQDIE 

       190        200        210        220        230        240 
EMIFHRELPQ ASGLLHHCCF YKHQGQNLLT MTTAPRGLQS GDRATWFGLY YNLSGAGFYP 

       250        260        270        280        290        300 
HPIGLELLID HKALDPALWT IQKVFYQGRY YESLTQLEDQ FEAGLVNVVL VPNNGTGGSW 

       310        320        330        340        350        360 
SLKSSVPPGP APPLQFHPQG PRFSVQGSQV SSSLWAFSFG LGAFSGPRIF DIRFQGERVA 

       370        380        390        400        410        420 
YEISVQEAIA LYGGNSPASM STCYVDGSFG IGKYSTPLIR GVDCPYLATY VDWHFLLESQ 

       430        440        450        460        470        480 
APKTLRDAFC VFEQNQGLPL RRHHSDFYSH YFGGVVGTVL VVRSVSTLLN YDYIWDMVFH 

       490        500        510        520        530        540 
PNGAIEVKFH ATGYISSAFF FGAGEKFGNR VGAHTLGTVH THSAHFKVDL DVAGLKNWAW 

       550        560        570        580        590        600 
AEDMAFVPTI VPWQPEYQMQ RLQVTRKLLE TEEEAAFPLG GATPRYLYLA SNHSNKWGHR 

       610        620        630        640        650        660 
RGYRIQILSF AGKPLPQESP IEKAFTWGRY HLAVTQRKEE EPSSSSIFNQ NDPWTPTVNF 

       670        680        690        700        710        720 
TDFISNETIA GEDLVAWVTA GFLHIPHAED IPNTVTAGNS VGFFLRPYNF FDEDPSFHSA 

       730        740        750        760 
DSIYFREGQD ATACEVNPLA CLSQTATCAP EIPAFSHGGF AYRDN

O70423 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