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Entry version 147 (16 Jan 2019)
Sequence version 4 (23 Jan 2007)
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Protein

Membrane primary amine oxidase

Gene

Aoc3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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. May play a role in adipogenesis (By similarity).By similarity1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei386Proton acceptorBy similarity1
Active sitei471Schiff-base intermediate with substrate; via topaquinoneBy similarity1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi520Copper; via tele nitrogenBy similarity1
Metal bindingi522Copper; via tele nitrogenBy similarity1
Metal bindingi529Calcium 1By similarity1
Metal bindingi530Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi531Calcium 1By similarity1
Metal bindingi572Calcium 2By similarity1
Metal bindingi663Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi667Calcium 2By similarity1
Metal bindingi673Calcium 1By similarity1
Metal bindingi674Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi684Copper; via pros nitrogenBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
Biological processCell adhesion
LigandCalcium, Copper, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.4.3.21 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-211945 Phase I - Functionalization of compounds

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Membrane primary amine oxidase (EC:1.4.3.21By similarity)
Alternative name(s):
Copper amine oxidase
Semicarbazide-sensitive amine oxidase
Short name:
SSAO
VP97
Vascular adhesion protein 1
Short name:
VAP-1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Aoc3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 10

Organism-specific databases

Rat genome database

More...
RGDi
62058 Aoc3

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini2 – 6CytoplasmicSequence analysis5
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei7 – 27Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini28 – 763ExtracellularSequence analysisAdd BLAST736

Keywords - Cellular componenti

Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4592

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000641052 – 763Membrane primary amine oxidaseAdd BLAST762

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi137N-linked (GlcNAc...) asparagineBy similarity1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi198 ↔ 199By similarity
Glycosylationi212O-linked (GalNAc...) threonineBy similarity1
Glycosylationi232N-linked (GlcNAc...) asparagineBy similarity1
Glycosylationi294N-linked (GlcNAc...) asparagineBy similarity1
Disulfide bondi404 ↔ 430By similarity
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei4712',4',5'-topaquinoneBy similarity1
Glycosylationi592N-linked (GlcNAc...) (complex) asparagineBy similarity1
Glycosylationi666N-linked (GlcNAc...) asparagineBy similarity1
Disulfide bondi734 ↔ 741By similarity
Disulfide bondi748InterchainBy similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, TPQ

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
O08590

PRoteomics IDEntifications database

More...
PRIDEi
O08590

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O08590

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
O08590

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Highly expressed in adipocytes, aorta and lung. Expressed at lower levels in heart, kidney, large intestine, liver, small intestine and stomach.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000051307 Expressed in 9 organ(s), highest expression level in lung

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
O08590 RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; disulfide-linked (By similarity). Forms a heterodimer with AOC2 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
248115, 1 interactor

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000059889

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
O08590

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
O08590

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni384 – 394Substrate bindingBy similarityAdd BLAST11
Regioni468 – 473Substrate bindingBy similarity6
Regioni578 – 585Heparin-bindingBy similarity8

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the copper/topaquinone oxidase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1186 Eukaryota
KOG4470 Eukaryota
COG3733 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000153738

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000233919

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG004164

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O08590

KEGG Orthology (KO)

More...
KOi
K00276

Database of Orthologous Groups

More...
OrthoDBi
1320015at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.70.98.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000269 Cu_amine_oxidase
IPR015798 Cu_amine_oxidase_C
IPR036460 Cu_amine_oxidase_C_sf
IPR016182 Cu_amine_oxidase_N-reg
IPR015800 Cu_amine_oxidase_N2
IPR015802 Cu_amine_oxidase_N3

The PANTHER Classification System

More...
PANTHERi
PTHR10638 PTHR10638, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01179 Cu_amine_oxid, 1 hit
PF02727 Cu_amine_oxidN2, 1 hit
PF02728 Cu_amine_oxidN3, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00766 CUDAOXIDASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49998 SSF49998, 1 hit
SSF54416 SSF54416, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01164 COPPER_AMINE_OXID_1, 1 hit
PS01165 COPPER_AMINE_OXID_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

O08590-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTQKTTLVLL ALAVITIFAL VCVLLAGRSG DGGRLSQPLH CPSVLPSVQP
60 70 80 90 100
QTHPGQSQPF ADLSPEELTA VMSFLIKHLG PGLVDAAQAR PSDNCVFSVE
110 120 130 140 150
LQLPAKAAAL AHLDRGGPPP VREALAIIFF GGQPKPNVSE LVVGPLPHPS
160 170 180 190 200
YMRDVTVERH GGPLPYYRRP VLTREYQDIQ EMIFHRELPQ ASGLLHHCCF
210 220 230 240 250
YKRQGHNLLK MTTAPRGLQS GDRATWFGIY YNLSGAGFYP HPIGLELLVD
260 270 280 290 300
HKALDPALWT IQKVFYQGRY YESLTQLEDM FEAGLVNVVL VPDNGTGGSW
310 320 330 340 350
SLKSSVPPGR APPLQFHPEG PRFSVQGSQV RSSLWAFSFG LGAFSGPRIF
360 370 380 390 400
DIRFQGERVA YEISVQEAIA LYGGNSPASM STCYMDGSFG IGKYSTPLTR
410 420 430 440 450
GVDCPYLATY VDWHFLLESQ TPKTLRDAFC VFEQNQGLPL RRHHSDFYSH
460 470 480 490 500
YFGGVVETVL VVRSVATLLN YDYVWDMVFH SNGAIEVKFH ATGYITSAFF
510 520 530 540 550
FGAGEKFGNR VAEHTLGTVH THNAHFKVDL DVAGLKNWAW AEDLAFVPMN
560 570 580 590 600
VPWQPEFQMQ RLQVTRKLLE TEEEAAFPLG NATPRYLYLA SNHSNKWGHR
610 620 630 640 650
RGYRIQILSF AGKPLPQESP IEKAFTWGRY HLAVTQRKEE EPSSSSIYNQ
660 670 680 690 700
NDPWTPTVDF TDFISNETIA GEDLVAWVTA GFLHIPHAED IPNTVTVGNG
710 720 730 740 750
VGFFLRPYNF FDEDPSFYSP DSIYFRKDQD VTDCEVNSLA CLSQTANCVP
760
DLPAFSHGGF TYK
Length:763
Mass (Da):84,981
Last modified:January 23, 2007 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5FD739AF43F39039
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti54P → S in AAC53189 (PubMed:9083076).Curated1
Sequence conflicti329Q → R in BAD74047 (PubMed:15744061).Curated1
Sequence conflicti645S → F in BAD74047 (PubMed:15744061).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AB195675 mRNA Translation: BAD74047.1
BC100613 mRNA Translation: AAI00614.1
U72632 mRNA Translation: AAC53189.1

NCBI Reference Sequences

More...
RefSeqi
NP_113770.2, NM_031582.2

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Rn.198327

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000076820; ENSRNOP00000068449; ENSRNOG00000051307

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
29473

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:29473

UCSC genome browser

More...
UCSCi
RGD:62058 rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB195675 mRNA Translation: BAD74047.1
BC100613 mRNA Translation: AAI00614.1
U72632 mRNA Translation: AAC53189.1
RefSeqiNP_113770.2, NM_031582.2
UniGeneiRn.198327

3D structure databases

SMRiO08590
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248115, 1 interactor
STRINGi10116.ENSRNOP00000059889

Chemistry databases

BindingDBiO08590
ChEMBLiCHEMBL4592

PTM databases

iPTMnetiO08590
PhosphoSitePlusiO08590

Proteomic databases

PaxDbiO08590
PRIDEiO08590

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000076820; ENSRNOP00000068449; ENSRNOG00000051307
GeneIDi29473
KEGGirno:29473
UCSCiRGD:62058 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
8639
RGDi62058 Aoc3

Phylogenomic databases

eggNOGiKOG1186 Eukaryota
KOG4470 Eukaryota
COG3733 LUCA
GeneTreeiENSGT00940000153738
HOGENOMiHOG000233919
HOVERGENiHBG004164
InParanoidiO08590
KOiK00276
OrthoDBi1320015at2759

Enzyme and pathway databases

BRENDAi1.4.3.21 5301
ReactomeiR-RNO-211945 Phase I - Functionalization of compounds

Miscellaneous databases

Protein Ontology

More...
PROi
PR:O08590

Gene expression databases

BgeeiENSRNOG00000051307 Expressed in 9 organ(s), highest expression level in lung
GenevisibleiO08590 RN

Family and domain databases

Gene3Di2.70.98.20, 1 hit
InterProiView protein in InterPro
IPR000269 Cu_amine_oxidase
IPR015798 Cu_amine_oxidase_C
IPR036460 Cu_amine_oxidase_C_sf
IPR016182 Cu_amine_oxidase_N-reg
IPR015800 Cu_amine_oxidase_N2
IPR015802 Cu_amine_oxidase_N3
PANTHERiPTHR10638 PTHR10638, 1 hit
PfamiView protein in Pfam
PF01179 Cu_amine_oxid, 1 hit
PF02727 Cu_amine_oxidN2, 1 hit
PF02728 Cu_amine_oxidN3, 1 hit
PRINTSiPR00766 CUDAOXIDASE
SUPFAMiSSF49998 SSF49998, 1 hit
SSF54416 SSF54416, 2 hits
PROSITEiView protein in PROSITE
PS01164 COPPER_AMINE_OXID_1, 1 hit
PS01165 COPPER_AMINE_OXID_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAOC3_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O08590
Secondary accession number(s): Q497D2, Q5R1T5
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 147 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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