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O75106

- AOC2_HUMAN

UniProt

O75106 - AOC2_HUMAN

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Protein

Retina-specific copper amine oxidase

Gene

AOC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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.2 Publications

Catalytic activityi

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

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

Kineticsi

  1. KM=0.056 mM for tryptamine1 Publication
  2. KM=0.077 mM for 2-phenylethylamine1 Publication
  3. KM=0.167 mM for benzylamine1 Publication
  4. KM=0.178 mM for p-tyramine1 Publication
  5. KM=1.7 mM for methylamine1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei380 – 3801Proton acceptorBy similarity
Active sitei465 – 4651Schiff-base intermediate with substrate; via topaquinoneBy similarity
Metal bindingi516 – 5161CopperBy similarity
Metal bindingi518 – 5181CopperBy similarity
Metal bindingi525 – 5251Calcium 1By similarity
Metal bindingi526 – 5261Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi527 – 5271Calcium 1By similarity
Metal bindingi568 – 5681Calcium 2By similarity
Metal bindingi634 – 6341Calcium 2By similarity
Metal bindingi659 – 6591Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi661 – 6611Calcium 2By similarity
Metal bindingi663 – 6631Calcium 2By similarity
Metal bindingi669 – 6691Calcium 1By similarity
Metal bindingi670 – 6701Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi680 – 6801CopperBy similarity

GO - Molecular functioni

  1. aliphatic-amine oxidase activity Source: UniProtKB-EC
  2. aminoacetone:oxygen oxidoreductase(deaminating) activity Source: UniProtKB-EC
  3. copper ion binding Source: InterPro
  4. electron carrier activity Source: UniProtKB
  5. phenethylamine:oxygen oxidoreductase (deaminating) activity Source: UniProtKB-EC
  6. primary amine oxidase activity Source: UniProtKB-EC
  7. quinone binding Source: InterPro
  8. tryptamine:oxygen oxidoreductase (deaminating) activity Source: UniProtKB-EC

GO - Biological processi

  1. amine metabolic process Source: InterPro
  2. catecholamine metabolic process Source: UniProtKB-KW
  3. visual perception Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Catecholamine metabolism

Keywords - Ligandi

Calcium, Copper, Metal-binding

Enzyme and pathway databases

SABIO-RKO75106.

Names & Taxonomyi

Protein namesi
Recommended name:
Retina-specific copper amine oxidase (EC:1.4.3.21)
Short name:
RAO
Alternative name(s):
Amine oxidase [copper-containing]
Semicarbazide-sensitive amine oxidase
Short name:
SSAO
Gene namesi
Name:AOC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:549. AOC2.

Subcellular locationi

Isoform 1 : Cell membrane; Peripheral membrane protein
Note: Present on the surface of the cells.
Isoform 2 : Cytoplasm
Note: Either not translocated to the plasma membrane or below detection level.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24839.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Sequence AnalysisAdd
BLAST
Chaini33 – 756724Retina-specific copper amine oxidasePRO_0000035671Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi133 – 1331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi198 – 1981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi226 – 2261N-linked (GlcNAc...)Sequence Analysis
Modified residuei465 – 46512',4',5'-topaquinoneBy similarity
Glycosylationi588 – 5881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi662 – 6621N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

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

Keywords - PTMi

Glycoprotein, TPQ

Proteomic databases

PaxDbiO75106.
PRIDEiO75106.

PTM databases

PhosphoSiteiO75106.

Expressioni

Tissue specificityi

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.3 Publications

Inductioni

Up-regulated during in vitro adipocyte differentiation.1 Publication

Gene expression databases

BgeeiO75106.
CleanExiHS_AOC2.
GenevestigatoriO75106.

Organism-specific databases

HPAiHPA057779.

Interactioni

Subunit structurei

Forms a heterodimer with AOC3, in vitro.1 Publication

Protein-protein interaction databases

STRINGi9606.ENSP00000253799.

Structurei

3D structure databases

ProteinModelPortaliO75106.
SMRiO75106. Positions 51-756.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the copper/topaquinone oxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3733.
GeneTreeiENSGT00510000046461.
HOGENOMiHOG000233919.
HOVERGENiHBG004164.
InParanoidiO75106.
KOiK00276.
OMAiPLESDME.
OrthoDBiEOG7353W8.
PhylomeDBiO75106.
TreeFamiTF314750.

Family and domain databases

Gene3Di2.70.98.20. 1 hit.
3.10.450.40. 2 hits.
InterProiIPR000269. 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]
PANTHERiPTHR10638. PTHR10638. 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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: O75106-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MHLKIVLAFL ALSLITIFAL AYVLLTSPGG SSQPPHCPSV SHRAQPWPHP
60 70 80 90 100
GQSQLFADLS REELTAVMRF LTQRLGPGLV DAAQAQPSDN CIFSVELQLP
110 120 130 140 150
PKAAALAHLD RGSPPPAREA LAIVLFGGQP QPNVSELVVG PLPHPSYMRD
160 170 180 190 200
VTVERHGGPL PYHRRPVLRA EFTQMWRHLK EVELPKAPIF LSSTFNYNGS
210 220 230 240 250
TLAAVHATPR GLRSGDRATW MALYHNISGV GLFLHPVGLE LLLDHRALDP
260 270 280 290 300
AHWTVQQVFY LGHYYADLGQ LEREFKSGRL EVVRVPLPPP NGASSLRSRN
310 320 330 340 350
SPGPLPPLQF SPQGSQYSVQ GNLVVSSLWS FTFGHGVFSG LRIFDVRFQG
360 370 380 390 400
ERIAYEVSVQ ECVSIYGADS PKTMLTRYLD SSFGLGRNSR GLVRGVDCPY
410 420 430 440 450
QATMVDIHIL VGKGAVQLLP GAVCVFEEAQ GLPLRRHHNY LQNHFYGGLA
460 470 480 490 500
SSALVVRSVS SVGNYDYIWD FVLYPNGALE GRVHATGYIN TAFLKGGEEG
510 520 530 540 550
LLFGNRVGER VLGTVHTHAF HFKLDLDVAG LKNWVVAEDV VFKPVAAPWN
560 570 580 590 600
PEHWLQRPQL TRQVLGKEDL TAFSLGSPLP RYLYLASNQT NAWGHQRGYR
610 620 630 640 650
IQIHSPLGIH IPLESDMERA LSWGRYQLVV TQRKEEESQS SSIYHQNDIW
660 670 680 690 700
TPTVTFADFI NNETLLGEDL VAWVTASFLH IPHAEDIPNT VTLGNRVGFL
710 720 730 740 750
LRPYNFFDED PSIFSPGSVY FEKGQDAGLC SINPVACLPD LAACVPDLPP

FSYHGF
Length:756
Mass (Da):83,673
Last modified:January 24, 2006 - v2
Checksum:i10263D8D56D3BD25
GO
Isoform 2 (identifier: O75106-2) [UniParc]FASTAAdd to Basket

Also known as: Short

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

Show »
Length:729
Mass (Da):80,516
Checksum:i5F28CCC8EE353415
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti181 – 1811E → D(PubMed:9119395)Curated
Sequence conflicti181 – 1811E → D(PubMed:9722954)Curated
Sequence conflicti215 – 2184GDRA → RERT(PubMed:9119395)Curated
Sequence conflicti215 – 2184GDRA → RERT(PubMed:9722954)Curated
Sequence conflicti221 – 2222MA → IG(PubMed:9119395)Curated
Sequence conflicti610 – 6101H → Q(PubMed:9119395)Curated
Sequence conflicti610 – 6101H → Q(PubMed:9722954)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51I → V.1 Publication
Corresponds to variant rs34230945 [ dbSNP | Ensembl ].
VAR_025022
Natural varianti22 – 221Y → C.1 Publication
Corresponds to variant rs34435306 [ dbSNP | Ensembl ].
VAR_025023
Natural varianti141 – 1411P → L.1 Publication
Corresponds to variant rs35833794 [ dbSNP | Ensembl ].
VAR_025024
Natural varianti273 – 2731R → Q.1 Publication
Corresponds to variant rs35508987 [ dbSNP | Ensembl ].
VAR_025025
Natural varianti427 – 4271E → D.1 Publication
Corresponds to variant rs34351794 [ dbSNP | Ensembl ].
VAR_025026

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei599 – 62527Missing in isoform 2. 1 PublicationVSP_006549Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11443.1. [O75106-1]
CCDS45690.1. [O75106-2]
RefSeqiNP_001149.2. NM_001158.3. [O75106-2]
NP_033720.2. NM_009590.2. [O75106-1]
UniGeneiHs.143102.

Genome annotation databases

EnsembliENST00000253799; ENSP00000253799; ENSG00000131480. [O75106-1]
ENST00000452774; ENSP00000406134; ENSG00000131480. [O75106-2]
GeneIDi314.
KEGGihsa:314.
UCSCiuc002ibt.3. human. [O75106-2]
uc002ibu.3. human. [O75106-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS11443.1. [O75106-1 ]
CCDS45690.1. [O75106-2 ]
RefSeqi NP_001149.2. NM_001158.3. [O75106-2 ]
NP_033720.2. NM_009590.2. [O75106-1 ]
UniGenei Hs.143102.

3D structure databases

ProteinModelPortali O75106.
SMRi O75106. Positions 51-756.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000253799.

Chemistry

BindingDBi O75106.
ChEMBLi CHEMBL4112.

PTM databases

PhosphoSitei O75106.

Proteomic databases

PaxDbi O75106.
PRIDEi O75106.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000253799 ; ENSP00000253799 ; ENSG00000131480 . [O75106-1 ]
ENST00000452774 ; ENSP00000406134 ; ENSG00000131480 . [O75106-2 ]
GeneIDi 314.
KEGGi hsa:314.
UCSCi uc002ibt.3. human. [O75106-2 ]
uc002ibu.3. human. [O75106-1 ]

Organism-specific databases

CTDi 314.
GeneCardsi GC17P040996.
HGNCi HGNC:549. AOC2.
HPAi HPA057779.
MIMi 602268. gene.
neXtProti NX_O75106.
PharmGKBi PA24839.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3733.
GeneTreei ENSGT00510000046461.
HOGENOMi HOG000233919.
HOVERGENi HBG004164.
InParanoidi O75106.
KOi K00276.
OMAi PLESDME.
OrthoDBi EOG7353W8.
PhylomeDBi O75106.
TreeFami TF314750.

Enzyme and pathway databases

SABIO-RK O75106.

Miscellaneous databases

GenomeRNAii 314.
NextBioi 1277.
PROi O75106.
SOURCEi Search...

Gene expression databases

Bgeei O75106.
CleanExi HS_AOC2.
Genevestigatori O75106.

Family and domain databases

Gene3Di 2.70.98.20. 1 hit.
3.10.450.40. 2 hits.
InterProi IPR000269. 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 ]
PANTHERi PTHR10638. PTHR10638. 1 hit.
Pfami PF01179. Cu_amine_oxid. 1 hit.
PF02727. Cu_amine_oxidN2. 1 hit.
PF02728. Cu_amine_oxidN3. 1 hit.
[Graphical view ]
PRINTSi PR00766. CUDAOXIDASE.
SUPFAMi SSF49998. SSF49998. 1 hit.
SSF54416. SSF54416. 2 hits.
PROSITEi PS01164. COPPER_AMINE_OXID_1. 1 hit.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiAOC2_HUMAN
AccessioniPrimary (citable) accession number: O75106
Secondary accession number(s): A5PKW2
, O00120, O75105, Q4TTW5, Q9UNY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 24, 2006
Last modified: November 26, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3