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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei381 – 3811Proton acceptorBy similarity
Active sitei466 – 4661Schiff-base intermediate with substrate; via topaquinoneBy similarity
Metal bindingi517 – 5171Copper; via tele nitrogenBy similarity
Metal bindingi519 – 5191Copper; via tele nitrogenBy similarity
Metal bindingi526 – 5261Calcium 1By similarity
Metal bindingi527 – 5271Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi528 – 5281Calcium 1By similarity
Metal bindingi569 – 5691Calcium 2By similarity
Metal bindingi660 – 6601Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi662 – 6621Calcium 2By similarity
Metal bindingi664 – 6641Calcium 2By similarity
Metal bindingi670 – 6701Calcium 1By similarity
Metal bindingi671 – 6711Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi681 – 6811Copper; via pros nitrogenBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Sequence analysisAdd
BLAST
Chaini33 – 757725Retina-specific copper amine oxidaseBy similarityPRO_0000035672Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi133 – 1331N-linked (GlcNAc...)By similarity
Glycosylationi198 – 1981N-linked (GlcNAc...)Sequence analysis
Glycosylationi226 – 2261N-linked (GlcNAc...)By similarity
Disulfide bondi399 ↔ 425By similarity
Modified residuei466 – 46612',4',5'-topaquinoneBy similarity
Glycosylationi589 – 5891N-linked (GlcNAc...) (complex)By similarity
Glycosylationi663 – 6631N-linked (GlcNAc...)By similarity
Disulfide bondi731 ↔ 738By similarity
Disulfide bondi745 – 745InterchainBy 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

PaxDbiQ812C9.
PRIDEiQ812C9.

PTM databases

iPTMnetiQ812C9.
PhosphoSiteiQ812C9.

Expressioni

Tissue specificityi

Significantly much highly expressed in retina.

Gene expression databases

BgeeiQ812C9.
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. Positions 48-757.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni379 – 38911Substrate bindingBy similarityAdd
BLAST
Regioni463 – 4686Substrate bindingBy similarity
Regioni575 – 5828Heparin-bindingBy similarity

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.
OrthoDBiEOG7353W8.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531S → N in AAK58865 (PubMed:14585497).Curated
Sequence conflicti117 – 1171V → A in AAK58865 (PubMed:14585497).Curated

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. Positions 48-757.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000040255.

PTM databases

iPTMnetiQ812C9.
PhosphoSiteiQ812C9.

Proteomic databases

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.
OrthoDBiEOG7353W8.
TreeFamiTF314750.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ812C9.
SOURCEiSearch...

Gene expression databases

BgeeiQ812C9.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of AOC2 gene encoding a copper-binding amine oxidase expressed specifically in retina."
    Zhang Q., Mashima Y., Noda S., Imamura Y., Kudoh J., Shimizu N., Nishiyama T., Umeda S., Oguchi Y., Tanaka Y., Iwata T.
    Gene 318:45-53(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.

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: June 8, 2016
This is version 103 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.