Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Retina-specific copper amine oxidase

Gene

Aoc2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Has a monoamine oxidase activity with substrate specificity for 2-phenylethylamine and tryptamine. May play a role in adipogenesis. May be a critical modulator of signal transmission in retina (By similarity).By similarity

Catalytic activityi

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2.By similarity

Cofactori

Protein has several cofactor binding sites:
  • Cu cationBy similarityNote: Binds 1 copper ion per subunit.By similarity
  • Ca2+By similarityNote: Binds 2 calcium ions per subunit.By similarity
  • L-topaquinoneBy similarityNote: Contains 1 topaquinone per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei381Proton acceptorBy similarity1
Active sitei466Schiff-base intermediate with substrate; via topaquinoneBy similarity1
Metal bindingi517Copper; via tele nitrogenBy similarity1
Metal bindingi519Copper; via tele nitrogenBy similarity1
Metal bindingi526Calcium 1By similarity1
Metal bindingi527Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi528Calcium 1By similarity1
Metal bindingi569Calcium 2By similarity1
Metal bindingi660Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi662Calcium 2By similarity1
Metal bindingi664Calcium 2By similarity1
Metal bindingi670Calcium 1By similarity1
Metal bindingi671Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi681Copper; via pros nitrogenBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Catecholamine metabolism

Keywords - Ligandi

Calcium, Copper, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-211945. Phase 1 - Functionalization of compounds.

Names & Taxonomyi

Protein namesi
Recommended name:
Retina-specific copper amine oxidase (EC:1.4.3.21By similarity)
Short name:
RAO
Alternative name(s):
Amine oxidase [copper-containing]
Gene namesi
Name:Aoc2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2668431. Aoc2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 32Sequence analysisAdd BLAST32
ChainiPRO_000003567233 – 757Retina-specific copper amine oxidaseBy similarityAdd BLAST725

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi133N-linked (GlcNAc...)By similarity1
Glycosylationi198N-linked (GlcNAc...)Sequence analysis1
Glycosylationi226N-linked (GlcNAc...)By similarity1
Disulfide bondi399 ↔ 425By similarity
Modified residuei4662',4',5'-topaquinoneBy similarity1
Glycosylationi589N-linked (GlcNAc...) (complex)By similarity1
Glycosylationi663N-linked (GlcNAc...)By similarity1
Disulfide bondi731 ↔ 738By similarity
Disulfide bondi745InterchainBy similarity

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, TPQ

Proteomic databases

MaxQBiQ812C9.
PaxDbiQ812C9.
PRIDEiQ812C9.

PTM databases

iPTMnetiQ812C9.
PhosphoSitePlusiQ812C9.

Expressioni

Tissue specificityi

Significantly much highly expressed in retina.

Gene expression databases

BgeeiENSMUSG00000078651.
ExpressionAtlasiQ812C9. baseline and differential.

Interactioni

Subunit structurei

Homodimer; disulfide-linked (By similarity). Forms a heterodimer with AOC3 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000040255.

Structurei

3D structure databases

ProteinModelPortaliQ812C9.
SMRiQ812C9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni379 – 389Substrate bindingBy similarityAdd BLAST11
Regioni463 – 468Substrate bindingBy similarity6
Regioni575 – 582Heparin-bindingBy similarity8

Sequence similaritiesi

Belongs to the copper/topaquinone oxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1186. Eukaryota.
COG3733. LUCA.
GeneTreeiENSGT00510000046461.
HOGENOMiHOG000233919.
HOVERGENiHBG004164.
InParanoidiQ812C9.
KOiK00276.
OMAiVDIHILV.
OrthoDBiEOG091G02WY.
TreeFamiTF314750.

Family and domain databases

Gene3Di2.70.98.20. 1 hit.
InterProiIPR032952. AOC2.
IPR000269. Cu_amine_oxidase.
IPR015798. Cu_amine_oxidase_C.
IPR016182. Cu_amine_oxidase_N-reg.
IPR015800. Cu_amine_oxidase_N2.
IPR015802. Cu_amine_oxidase_N3.
[Graphical view]
PANTHERiPTHR10638. PTHR10638. 1 hit.
PTHR10638:SF4. PTHR10638:SF4. 1 hit.
PfamiPF01179. Cu_amine_oxid. 1 hit.
PF02727. Cu_amine_oxidN2. 1 hit.
PF02728. Cu_amine_oxidN3. 1 hit.
[Graphical view]
PRINTSiPR00766. CUDAOXIDASE.
SUPFAMiSSF49998. SSF49998. 1 hit.
SSF54416. SSF54416. 2 hits.
PROSITEiPS01164. COPPER_AMINE_OXID_1. 1 hit.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q812C9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLKVLLLLL GLSFLTVFAL VYVLLTRQGS FSQSPRCPSI PPRIHPWTHP
60 70 80 90 100
SQSQLFADLT PEELTAVMSF LTKHLGPGLV DAAQARPSDN CVFSVELQLP
110 120 130 140 150
AKAAALAHLD RGGPPPVREA LAIIFFGGQP KPNVSELVVG PLPHPSYMRD
160 170 180 190 200
VTVERHGGPL PYYRRPMQKT EFVQIWRHLK EVELPKAPTF LASVLNYNGS
210 220 230 240 250
TLAPLHSTAS GFHAGDRATW IALYHNISGL GVFLHPVGLE LLLDHGALDP
260 270 280 290 300
ADWVVQQVFY LGHYYADLAQ LEWEFKVGRL EVIRVPLPTP GGASSLRPRV
310 320 330 340 350
TPDPPLPPLQ FSLQGPQYNI QGNSVTSPLW TFTFGHGVFS GLRIFDIRFK
360 370 380 390 400
GERVAYEVSV QECLTVYGAD SPKTMTIRYL DSSYGLGLNS RALVRGVDCP
410 420 430 440 450
YQATMVDIHV LVGTGSVQLL PGAVCVFEEA QGLPLRRHHN GIGGHFYGGL
460 470 480 490 500
ASSSLVVRSV SSVGNYDYIW DFMLHPTGAL EARVHATGYI NTAFMSGGAE
510 520 530 540 550
SLLFGNRVGE RVLGAVHTHA FHFKLDLDVA GLKNWVIAED AVFKPVAAPW
560 570 580 590 600
NPELQLQRPQ LTRQVLSRED LAAFPWGSPL PRYLYLATNQ TNAWGHQRGY
610 620 630 640 650
RIQIHSPPGV HVPLESSEER ALSWGRYQLV VTQRKEAEPH SSSIYYQNDM
660 670 680 690 700
RSPATVFADF INNETLLGED LVAWVTASFL HIPHAEDIPN TVTVGNRVGF
710 720 730 740 750
LLRPYNFFNE DPSIFSPGSV YFERDQDAGL CSINPVACTQ QLADCVPNLP

SFSYEGL
Length:757
Mass (Da):83,583
Last modified:July 27, 2011 - v2
Checksum:i4D93D9839AD57159
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti53S → N in AAK58865 (PubMed:14585497).Curated1
Sequence conflicti117V → A in AAK58865 (PubMed:14585497).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF350445 mRNA. Translation: AAK58864.2.
AF350446 Genomic DNA. Translation: AAK58865.1.
AL590969 Genomic DNA. Translation: CAM19554.1.
BC150843 mRNA. Translation: AAI50844.1.
BC150848 mRNA. Translation: AAI50849.1.
CCDSiCCDS25464.1.
RefSeqiNP_849263.1. NM_178932.1.
UniGeneiMm.302277.

Genome annotation databases

EnsembliENSMUST00000041095; ENSMUSP00000040255; ENSMUSG00000078651.
GeneIDi237940.
KEGGimmu:237940.
UCSCiuc007loo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF350445 mRNA. Translation: AAK58864.2.
AF350446 Genomic DNA. Translation: AAK58865.1.
AL590969 Genomic DNA. Translation: CAM19554.1.
BC150843 mRNA. Translation: AAI50844.1.
BC150848 mRNA. Translation: AAI50849.1.
CCDSiCCDS25464.1.
RefSeqiNP_849263.1. NM_178932.1.
UniGeneiMm.302277.

3D structure databases

ProteinModelPortaliQ812C9.
SMRiQ812C9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000040255.

PTM databases

iPTMnetiQ812C9.
PhosphoSitePlusiQ812C9.

Proteomic databases

MaxQBiQ812C9.
PaxDbiQ812C9.
PRIDEiQ812C9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041095; ENSMUSP00000040255; ENSMUSG00000078651.
GeneIDi237940.
KEGGimmu:237940.
UCSCiuc007loo.1. mouse.

Organism-specific databases

CTDi314.
MGIiMGI:2668431. Aoc2.

Phylogenomic databases

eggNOGiKOG1186. Eukaryota.
COG3733. LUCA.
GeneTreeiENSGT00510000046461.
HOGENOMiHOG000233919.
HOVERGENiHBG004164.
InParanoidiQ812C9.
KOiK00276.
OMAiVDIHILV.
OrthoDBiEOG091G02WY.
TreeFamiTF314750.

Enzyme and pathway databases

ReactomeiR-MMU-211945. Phase 1 - Functionalization of compounds.

Miscellaneous databases

PROiQ812C9.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000078651.
ExpressionAtlasiQ812C9. baseline and differential.

Family and domain databases

Gene3Di2.70.98.20. 1 hit.
InterProiIPR032952. AOC2.
IPR000269. Cu_amine_oxidase.
IPR015798. Cu_amine_oxidase_C.
IPR016182. Cu_amine_oxidase_N-reg.
IPR015800. Cu_amine_oxidase_N2.
IPR015802. Cu_amine_oxidase_N3.
[Graphical view]
PANTHERiPTHR10638. PTHR10638. 1 hit.
PTHR10638:SF4. PTHR10638:SF4. 1 hit.
PfamiPF01179. Cu_amine_oxid. 1 hit.
PF02727. Cu_amine_oxidN2. 1 hit.
PF02728. Cu_amine_oxidN3. 1 hit.
[Graphical view]
PRINTSiPR00766. CUDAOXIDASE.
SUPFAMiSSF49998. SSF49998. 1 hit.
SSF54416. SSF54416. 2 hits.
PROSITEiPS01164. COPPER_AMINE_OXID_1. 1 hit.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAOC2_MOUSE
AccessioniPrimary (citable) accession number: Q812C9
Secondary accession number(s): A2A4J0, Q80WP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: July 27, 2011
Last modified: November 2, 2016
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.