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O75106 (AOC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Retina-specific copper amine oxidase

Short name=RAO
EC=1.4.3.21
Alternative name(s):
Amine oxidase [copper-containing]
Semicarbazide-sensitive amine oxidase
Short name=SSAO
Gene names
Name:AOC2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length756 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.10

Catalytic activity

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

Cofactor

Binds 1 copper ion per subunit By similarity.

Binds 2 calcium ions per subunit By similarity.

Contains 1 topaquinone per subunit By similarity.

Subunit structure

Forms a heterodimer with AOC3, in vitro. Ref.10

Subcellular location

Isoform 1: Cell membrane; Peripheral membrane protein. Note: Present on the surface of the cells. Ref.10

Isoform 2: Cytoplasm. Note: Either not translocated to the plasma membrane or below detection level. Ref.10

Tissue specificity

Expressed in many tissues with much higher expression in retina. Isoform 1 and isoform 2 are expressed in adipose tissue, whereas isoform 1 only seems to be present in thymus, and isoform 2 only in testis. Ref.8 Ref.9 Ref.10

Induction

Up-regulated during in vitro adipocyte differentiation. Ref.9

Post-translational modification

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

Sequence similarities

Belongs to the copper/topaquinone oxidase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.056 mM for tryptamine Ref.10

KM=0.077 mM for 2-phenylethylamine

KM=0.167 mM for benzylamine

KM=0.178 mM for p-tyramine

KM=1.7 mM for methylamine

Ontologies

Keywords
   Biological processCatecholamine metabolism
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
   LigandCalcium
Copper
Metal-binding
   Molecular functionOxidoreductase
   PTMGlycoprotein
TPQ
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processamine metabolic process

Inferred from electronic annotation. Source: InterPro

catecholamine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

visual perception

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaliphatic-amine oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

aminoacetone:oxygen oxidoreductase(deaminating) activity

Inferred from electronic annotation. Source: UniProtKB-EC

copper ion binding

Inferred from electronic annotation. Source: InterPro

electron carrier activity

Traceable author statement Ref.1. Source: UniProtKB

phenethylamine:oxygen oxidoreductase (deaminating) activity

Inferred from electronic annotation. Source: UniProtKB-EC

primary amine oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

quinone binding

Inferred from electronic annotation. Source: InterPro

tryptamine:oxygen oxidoreductase (deaminating) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: O75106-1)

Also known as: Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O75106-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     599-625: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Potential
Chain33 – 756724Retina-specific copper amine oxidase
PRO_0000035671

Sites

Active site3801Proton acceptor By similarity
Active site4651Schiff-base intermediate with substrate; via topaquinone By similarity
Metal binding5161Copper By similarity
Metal binding5181Copper By similarity
Metal binding5251Calcium 1 By similarity
Metal binding5261Calcium 1; via carbonyl oxygen By similarity
Metal binding5271Calcium 1 By similarity
Metal binding5681Calcium 2 By similarity
Metal binding6341Calcium 2 By similarity
Metal binding6591Calcium 2; via carbonyl oxygen By similarity
Metal binding6611Calcium 2 By similarity
Metal binding6631Calcium 2 By similarity
Metal binding6691Calcium 1 By similarity
Metal binding6701Calcium 1; via carbonyl oxygen By similarity
Metal binding6801Copper By similarity

Amino acid modifications

Modified residue46512',4',5'-topaquinone By similarity
Glycosylation1331N-linked (GlcNAc...) Potential
Glycosylation1981N-linked (GlcNAc...) Potential
Glycosylation2261N-linked (GlcNAc...) Potential
Glycosylation5881N-linked (GlcNAc...) Potential
Glycosylation6621N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence599 – 62527Missing in isoform 2.
VSP_006549
Natural variant51I → V. Ref.4
Corresponds to variant rs34230945 [ dbSNP | Ensembl ].
VAR_025022
Natural variant221Y → C. Ref.4
Corresponds to variant rs34435306 [ dbSNP | Ensembl ].
VAR_025023
Natural variant1411P → L. Ref.4
Corresponds to variant rs35833794 [ dbSNP | Ensembl ].
VAR_025024
Natural variant2731R → Q. Ref.4
Corresponds to variant rs35508987 [ dbSNP | Ensembl ].
VAR_025025
Natural variant4271E → D. Ref.4
Corresponds to variant rs34351794 [ dbSNP | Ensembl ].
VAR_025026

Experimental info

Sequence conflict1811E → D Ref.1
Sequence conflict1811E → D Ref.2
Sequence conflict215 – 2184GDRA → RERT Ref.1
Sequence conflict215 – 2184GDRA → RERT Ref.2
Sequence conflict221 – 2222MA → IG Ref.1
Sequence conflict6101H → Q Ref.1
Sequence conflict6101H → Q Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) [UniParc].

Last modified January 24, 2006. Version 2.
Checksum: 10263D8D56D3BD25

FASTA75683,673
        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 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: 5F28CCC8EE353415
Show »

FASTA72980,516

References

« Hide 'large scale' references
[1]"Human retina-specific amine oxidase (RAO): cDNA cloning, tissue expression, and chromosomal mapping."
Imamura Y., Kubota R., Wang Y., Asakawa S., Kudoh J., Mashima Y., Oguchi Y., Shimizu N.
Genomics 40:277-283(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Retina.
[2]"Human retina-specific amine oxidase: genomic structure of the gene (AOC2), alternatively spliced variant, and mRNA expression in retina."
Imamura Y., Noda S., Mashima Y., Kudoh J., Oguchi Y., Shimizu N.
Genomics 51:293-298(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
[3]"Human copper-containing amine oxidases."
Zhang X., McIntire W.S.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Retina.
[4]NIEHS SNPs program
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-5; CYS-22; LEU-141; GLN-273 AND ASP-427.
[5]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] (ISOFORM 1).
[8]"High expression of semicarbazide-sensitive amine oxidase genes AOC2 and AOC3, but not the diamine oxidase gene AOC1 in human adipocytes."
Heniquez A., Meissonnier G., Visentin V., Prevot D., Carpene C.
Inflamm. Res. 52:S74-S75(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[9]"Adipogenesis-related increase of semicarbazide-sensitive amine oxidase and monoamine oxidase in human adipocytes."
Bour S., Daviaud D., Gres S., Lefort C., Prevot D., Zorzano A., Wabitsch M., Saulnier-Blache J.-S., Valet P., Carpene C.
Biochimie 89:916-925(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
[10]"The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase."
Kaitaniemi S., Elovaara H., Groen K., Kidron H., Liukkonen J., Salminen T., Salmi M., Jalkanen S., Elima K.
Cell. Mol. Life Sci. 66:2743-2757(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D88213 mRNA. Translation: BAA19001.1.
AB012943 Genomic DNA. Translation: BAA32590.1.
AB012943 Genomic DNA. Translation: BAA32589.1.
AF081363 mRNA. Translation: AAD39345.1.
DQ060035 Genomic DNA. Translation: AAY43129.1.
AC016889 Genomic DNA. No translation available.
CH471152 Genomic DNA. Translation: EAW60895.1.
BC142641 mRNA. Translation: AAI42642.1.
RefSeqNP_001149.2. NM_001158.3.
NP_033720.2. NM_009590.2.
UniGeneHs.143102.

3D structure databases

ProteinModelPortalO75106.
SMRO75106. Positions 51-756.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000253799.

Chemistry

BindingDBO75106.
ChEMBLCHEMBL4112.

PTM databases

PhosphoSiteO75106.

Proteomic databases

PaxDbO75106.
PRIDEO75106.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000253799; ENSP00000253799; ENSG00000131480. [O75106-1]
ENST00000452774; ENSP00000406134; ENSG00000131480. [O75106-2]
GeneID314.
KEGGhsa:314.
UCSCuc002ibt.3. human. [O75106-2]
uc002ibu.3. human. [O75106-1]

Organism-specific databases

CTD314.
GeneCardsGC17P040996.
HGNCHGNC:549. AOC2.
HPAHPA057779.
MIM602268. gene.
neXtProtNX_O75106.
PharmGKBPA24839.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3733.
HOGENOMHOG000233919.
HOVERGENHBG004164.
InParanoidO75106.
KOK00276.
OMAPLESDME.
OrthoDBEOG7353W8.
PhylomeDBO75106.
TreeFamTF314750.

Enzyme and pathway databases

SABIO-RKO75106.

Gene expression databases

BgeeO75106.
CleanExHS_AOC2.
GenevestigatorO75106.

Family and domain databases

Gene3D2.70.98.20. 1 hit.
3.10.450.40. 2 hits.
InterProIPR000269. Cu_amine_oxidase.
IPR015798. Cu_amine_oxidase_C.
IPR016182. Cu_amine_oxidase_N-reg.
IPR015800. Cu_amine_oxidase_N2.
IPR015801. Cu_amine_oxidase_N2/3.
IPR015802. Cu_amine_oxidase_N3.
[Graphical view]
PANTHERPTHR10638. PTHR10638. 1 hit.
PfamPF01179. Cu_amine_oxid. 1 hit.
PF02727. Cu_amine_oxidN2. 1 hit.
PF02728. Cu_amine_oxidN3. 1 hit.
[Graphical view]
PRINTSPR00766. CUDAOXIDASE.
SUPFAMSSF49998. SSF49998. 1 hit.
SSF54416. SSF54416. 2 hits.
PROSITEPS01164. COPPER_AMINE_OXID_1. 1 hit.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi314.
NextBio1277.
PROO75106.
SOURCESearch...

Entry information

Entry nameAOC2_HUMAN
AccessionPrimary (citable) accession number: O75106
Secondary accession number(s): A5PKW2 expand/collapse secondary AC list , O00120, O75105, Q4TTW5, Q9UNY0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 24, 2006
Last modified: March 19, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM