[1]	NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. STRAIN=Wistar; TISSUE=Aorta; DOI=10.1248/bpb.28.413; PubMed=15744061 [NCBI, ExPASy, EBI, Israel, Japan] Ochiai Y., Itoh K., Sakurai E., Tanaka Y.; "Molecular cloning and characterization of rat semicarbazide-sensitive amine oxidase."; Biol. Pharm. Bull. 28:413-418(2005).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Prostate; 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).
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-322, PARTIAL PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION. STRAIN=Sprague-Dawley; TISSUE=Adipocyte; DOI=10.1074/jbc.272.14.9388; PubMed=9083076 [NCBI, ExPASy, EBI, Israel, Japan] Morris N.J., Ducret A., Aebersold R., Ross S.A., Keller S.R., Lienhard G.E.; "Membrane amine oxidase cloning and identification as a major protein in the adipocyte plasma membrane."; J. Biol. Chem. 272:9388-9392(1997).
[4]	PROTEIN SEQUENCE OF 2-20, AND SUBCELLULAR LOCATION. TISSUE=Adipocyte; PubMed=8520629 [NCBI, ExPASy, EBI, Israel, Japan] Jochen A., Guven S., Hays J.; "The major integral membrane glycoprotein in adipocytes is a novel 200-kDa heterodimer."; Mol. Membr. Biol. 12:277-281(1995).

Comments

FUNCTION: Cell adhesion protein that participate 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.
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.
TISSUE SPECIFICITY: Highly expressed in adipocytes, aorta and lung. Expressed at lower levels in heart, kidney, large intestine, liver, small intestine and stomach.
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

AB195675; BAD74047.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC100613; AAI00614.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U72632; AAC53189.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_113770.2; -.

UniGene

Rn.198327

3D structure databases

SMR

O08590; 58-716.

ModBase

O08590.

Organism-specific databases

RGD

62058; Aoc3.

Gene expression databases

ArrayExpress

O08590; -.

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.

Genome annotation databases

Ensembl

ENSRNOG00000030114; Rattus norvegicus. [Contig view]

GeneID

29473; -.

KEGG

rno:29473; -.

Phylogenomic databases

HOVERGEN

O08590; -.

Other

609300; -.

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

Keywords

Calcium; Cell adhesion; Copper; Direct protein sequencing; 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`	`2 763`	`762`	`Membrane primary amine oxidase.`	`PRO_0000064105`
`TOPO_DOM`	`2 6`	`5`	`Cytoplasmic (Potential).`
`TRANSMEM`	`7 27`	`21`	`Signal-anchor for type II membrane protein (Potential).`
`TOPO_DOM`	`28 763`	`736`	`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`	`666 666`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`198 199`		`By similarity.`
`DISULFID`	`734 741`		`By similarity.`
`DISULFID`	`748 748`		`Interchain (By similarity).`
`CONFLICT`	`54 54`		`P -> S (in Ref. 3; AAC53189).`
`CONFLICT`	`329 329`		`Q -> R (in Ref. 1; BAD74047).`
`CONFLICT`	`645 645`		`S -> F (in Ref. 1; BAD74047).`

Sequence information

Length: 763 AA [This is the length of the unprocessed precursor]

Molecular weight: 84981 Da [This is the MW of the unprocessed precursor]

CRC64: 5FD739AF43F39039 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTQKTTLVLL ALAVITIFAL VCVLLAGRSG DGGRLSQPLH CPSVLPSVQP QTHPGQSQPF 

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

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

       190        200        210        220        230        240 
EMIFHRELPQ ASGLLHHCCF YKRQGHNLLK MTTAPRGLQS GDRATWFGIY YNLSGAGFYP 

       250        260        270        280        290        300 
HPIGLELLVD HKALDPALWT IQKVFYQGRY YESLTQLEDM FEAGLVNVVL VPDNGTGGSW 

       310        320        330        340        350        360 
SLKSSVPPGR APPLQFHPEG PRFSVQGSQV RSSLWAFSFG LGAFSGPRIF DIRFQGERVA 

       370        380        390        400        410        420 
YEISVQEAIA LYGGNSPASM STCYMDGSFG IGKYSTPLTR GVDCPYLATY VDWHFLLESQ 

       430        440        450        460        470        480 
TPKTLRDAFC VFEQNQGLPL RRHHSDFYSH YFGGVVETVL VVRSVATLLN YDYVWDMVFH 

       490        500        510        520        530        540 
SNGAIEVKFH ATGYITSAFF FGAGEKFGNR VAEHTLGTVH THNAHFKVDL DVAGLKNWAW 

       550        560        570        580        590        600 
AEDLAFVPMN VPWQPEFQMQ RLQVTRKLLE TEEEAAFPLG NATPRYLYLA SNHSNKWGHR 

       610        620        630        640        650        660 
RGYRIQILSF AGKPLPQESP IEKAFTWGRY HLAVTQRKEE EPSSSSIYNQ NDPWTPTVDF 

       670        680        690        700        710        720 
TDFISNETIA GEDLVAWVTA GFLHIPHAED IPNTVTVGNG VGFFLRPYNF FDEDPSFYSP 

       730        740        750        760 
DSIYFRKDQD VTDCEVNSLA CLSQTANCVP DLPAFSHGGF TYK

O08590 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