[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Retina; DOI=10.1006/geno.1996.4570; PubMed=9119395 [NCBI, ExPASy, EBI, Israel, Japan] Imamura Y., Kubota R., Wang Y., Asakawa S., Kudoh J., Mashima Y., Oguchi Y., Shimizu N.; "Human retina-specific amine oxidase (RAO): cDNA cloning, tissue expression, and chromosomal mapping."; Genomics 40:277-283(1997).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING. DOI=10.1006/geno.1998.5357; PubMed=9722954 [NCBI, ExPASy, EBI, Israel, Japan] Imamura Y., Noda S., Mashima Y., Kudoh J., Oguchi Y., Shimizu N.; "Human retina-specific amine oxidase: genomic structure of the gene (AOC2), alternatively spliced variant, and mRNA expression in retina."; Genomics 51:293-298(1998).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. TISSUE=Retina; Zhang X., McIntire W.S.; "Human copper-containing amine oxidases."; Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-5; CYS-22; LEU-141; GLN-273 AND ASP-427. NIEHS SNPs program; Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: May be a critical modulator of signal transmission in retina, possibly by degrading the biogenic amines dopamine, histamine, and putrescine.
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).
ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing. Additional isoforms seem to exist.

Name Long

Isoform ID O75106-1

This is the isoform sequence displayed in this entry.

Name Short

Isoform ID O75106-2

Features which should be applied to build the isoform sequence: VSP_006549.
TISSUE SPECIFICITY: Retinal specific.
PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
SIMILARITY: Belongs to the copper/topaquinone oxidase family.
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/aoc2/";.

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

D88213; BAA19001.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB012943; BAA32590.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB012943; BAA32589.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF081363; AAD39345.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ060035; AAY43129.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001149.2; -.
NP_033720.2; -.

UniGene

Hs.143102

3D structure databases

ModBase

O75106.

PTM databases

PhosphoSite

O75106; -.

Organism-specific databases

GC17P038250; -.

HIX0039050; -.

HGNC:549; AOC2.

602268; gene. [NCBI / EBI]

PharmGKB

PA24839; -.

GeneCards

O75106.

Gene expression databases

ArrayExpress

O75106; -.

CleanEx

HS_AOC2; -.

GermOnline

ENSG00000131480; Homo sapiens.

Ontologies

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:0009055;	Molecular function: electron carrier activity (traceable author statement from UniProtKB).
GO:0048038;	Molecular function: quinone binding (inferred from electronic annotation from InterPro).
GO:0006584;	Biological process: catecholamine metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0007601;	Biological process: visual perception (traceable author statement from ProtInc).
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

O75106; -.

Genome annotation databases

Ensembl

ENSG00000131480; Homo sapiens. [Contig view]

GeneID

314; -.

KEGG

hsa:314; -.

NMPDR

fig|9606.3.peg.13800; -.

Phylogenomic databases

HOGENOM

O75106; -.

HOVERGEN

O75106; -.

Other

1277; -.

AOC2; Homo sapiens.

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

Keywords

Alternative splicing; Calcium; Catecholamine metabolism; Copper; Glycoprotein; Metal-binding; Oxidoreductase; Polymorphism; Signal; TPQ.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 32`	`32`	`Potential.`
`CHAIN`	`33 756`	`724`	`Retina-specific copper amine oxidase.`	`PRO_0000035671`
`ACT_SITE`	`380 380`		`Proton acceptor (By similarity).`
`ACT_SITE`	`465 465`		`Schiff-base intermediate with substrate; via topaquinone (By similarity).`
`METAL`	`516 516`		`Copper (By similarity).`
`METAL`	`518 518`		`Copper (By similarity).`
`METAL`	`525 525`		`Calcium 1 (By similarity).`
`METAL`	`526 526`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`527 527`		`Calcium 1 (By similarity).`
`METAL`	`568 568`		`Calcium 2 (By similarity).`
`METAL`	`634 634`		`Calcium 2 (By similarity).`
`METAL`	`659 659`		`Calcium 2; via carbonyl oxygen (By similarity).`
`METAL`	`661 661`		`Calcium 2 (By similarity).`
`METAL`	`663 663`		`Calcium 2 (By similarity).`
`METAL`	`669 669`		`Calcium 1 (By similarity).`
`METAL`	`670 670`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`680 680`		`Copper (By similarity).`
`MOD_RES`	`465 465`		`2',4',5'-topaquinone (By similarity).`
`CARBOHYD`	`133 133`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`198 198`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`226 226`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`588 588`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`662 662`		`N-linked (GlcNAc...) (Potential).`
`VAR_SEQ`	`599 625`		`Missing (in isoform Short).`	`VSP_006549`
`VARIANT`	`5 5`	`1`	`I -> V.`	`VAR_025022`
`VARIANT`	`22 22`	`1`	`Y -> C.`	`VAR_025023`
`VARIANT`	`141 141`	`1`	`P -> L.`	`VAR_025024`
`VARIANT`	`273 273`	`1`	`R -> Q.`	`VAR_025025`
`VARIANT`	`427 427`	`1`	`E -> D.`	`VAR_025026`
`CONFLICT`	`181 181`		`E -> D (in Ref. 1 and 2).`
`CONFLICT`	`215 218`		`GDRA -> RERT (in Ref. 1 and 2).`
`CONFLICT`	`221 222`		`MA -> IG (in Ref. 1).`
`CONFLICT`	`610 610`		`H -> Q (in Ref. 1 and 2).`

Sequence information

Length: 756 AA [This is the length of the unprocessed precursor]

Molecular weight: 83673 Da [This is the MW of the unprocessed precursor]

CRC64: 10263D8D56D3BD25 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MHLKIVLAFL ALSLITIFAL AYVLLTSPGG SSQPPHCPSV SHRAQPWPHP GQSQLFADLS 

        70         80         90        100        110        120 
REELTAVMRF LTQRLGPGLV DAAQAQPSDN CIFSVELQLP PKAAALAHLD RGSPPPAREA 

       130        140        150        160        170        180 
LAIVLFGGQP QPNVSELVVG PLPHPSYMRD VTVERHGGPL PYHRRPVLRA EFTQMWRHLK 

       190        200        210        220        230        240 
EVELPKAPIF LSSTFNYNGS TLAAVHATPR GLRSGDRATW MALYHNISGV GLFLHPVGLE 

       250        260        270        280        290        300 
LLLDHRALDP AHWTVQQVFY LGHYYADLGQ LEREFKSGRL EVVRVPLPPP NGASSLRSRN 

       310        320        330        340        350        360 
SPGPLPPLQF SPQGSQYSVQ GNLVVSSLWS FTFGHGVFSG LRIFDVRFQG ERIAYEVSVQ 

       370        380        390        400        410        420 
ECVSIYGADS PKTMLTRYLD SSFGLGRNSR GLVRGVDCPY QATMVDIHIL VGKGAVQLLP 

       430        440        450        460        470        480 
GAVCVFEEAQ GLPLRRHHNY LQNHFYGGLA SSALVVRSVS SVGNYDYIWD FVLYPNGALE 

       490        500        510        520        530        540 
GRVHATGYIN TAFLKGGEEG LLFGNRVGER VLGTVHTHAF HFKLDLDVAG LKNWVVAEDV 

       550        560        570        580        590        600 
VFKPVAAPWN PEHWLQRPQL TRQVLGKEDL TAFSLGSPLP RYLYLASNQT NAWGHQRGYR 

       610        620        630        640        650        660 
IQIHSPLGIH IPLESDMERA LSWGRYQLVV TQRKEEESQS SSIYHQNDIW TPTVTFADFI 

       670        680        690        700        710        720 
NNETLLGEDL VAWVTASFLH IPHAEDIPNT VTLGNRVGFL LRPYNFFDED PSIFSPGSVY 

       730        740        750 
FEKGQDAGLC SINPVACLPD LAACVPDLPP FSYHGF

O75106 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