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Protein

Membrane primary amine oxidase

Gene

AOC3

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

Functioni

Cell adhesion protein that participates in lymphocyte extravasation and recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion. Has semicarbazide-sensitive (SSAO) monoamine oxidase activity. May play a role in adipogenesis.4 Publications

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Cu cationNote: Binds 1 copper ion per subunit.
  • Ca2+Note: Binds 2 calcium ions per subunit.
  • L-topaquinoneNote: Contains 1 topaquinone per subunit.

Kineticsi

  1. KM=1.94 mM for 2-phenylethylamine1 Publication
  2. KM=0.67 mM for methylamine1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei386 – 3861Proton acceptorBy similarity
    Active sitei471 – 4711Schiff-base intermediate with substrate; via topaquinoneBy similarity
    Metal bindingi520 – 5201Copper1 Publication
    Metal bindingi522 – 5221Copper1 Publication
    Metal bindingi529 – 5291Calcium 1
    Metal bindingi530 – 5301Calcium 1; via carbonyl oxygen
    Metal bindingi531 – 5311Calcium 1
    Metal bindingi572 – 5721Calcium 2
    Metal bindingi638 – 6381Calcium 2
    Metal bindingi663 – 6631Calcium 2; via carbonyl oxygen
    Metal bindingi665 – 6651Calcium 2
    Metal bindingi667 – 6671Calcium 2
    Metal bindingi673 – 6731Calcium 1
    Metal bindingi674 – 6741Calcium 1; via carbonyl oxygen
    Metal bindingi684 – 6841Copper1 Publication

    GO - Molecular functioni

    • aliphatic-amine oxidase activity Source: UniProtKB-EC
    • aminoacetone:oxygen oxidoreductase(deaminating) activity Source: UniProtKB-EC
    • calcium ion binding Source: UniProtKB
    • cation channel activity Source: UniProtKB
    • copper ion binding Source: UniProtKB
    • phenethylamine:oxygen oxidoreductase (deaminating) activity Source: UniProtKB-EC
    • primary amine oxidase activity Source: UniProtKB
    • protein heterodimerization activity Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB
    • quinone binding Source: UniProtKB
    • tryptamine:oxygen oxidoreductase (deaminating) activity Source: UniProtKB-EC

    GO - Biological processi

    • amine metabolic process Source: UniProtKB
    • cation transmembrane transport Source: GOC
    • cation transport Source: GOC
    • cell adhesion Source: UniProtKB
    • inflammatory response Source: UniProtKB
    • response to antibiotic Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Calcium, Copper, Metal-binding

    Enzyme and pathway databases

    BRENDAi1.4.3.21. 2681.
    SABIO-RKQ16853.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Membrane primary amine oxidase (EC:1.4.3.21)
    Alternative name(s):
    Copper amine oxidase
    HPAO
    Semicarbazide-sensitive amine oxidase
    Short name:
    SSAO
    Vascular adhesion protein 1
    Short name:
    VAP-1
    Gene namesi
    Name:AOC3
    Synonyms:VAP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:550. AOC3.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 54CytoplasmicSequence Analysis
    Transmembranei6 – 2621Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST
    Topological domaini27 – 763737ExtracellularSequence AnalysisAdd
    BLAST

    GO - Cellular componenti

    • cell surface Source: UniProtKB
    • cytoplasm Source: UniProtKB
    • early endosome Source: CACAO
    • endoplasmic reticulum Source: CACAO
    • Golgi apparatus Source: CACAO
    • integral component of membrane Source: UniProtKB
    • microvillus Source: UniProtKB
    • plasma membrane Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi211 – 2111M → V: Increased activity towards 2-phenylethylamine, and decreased activity towards methylamine; when associated with N-394 and G-469. 1 Publication
    Mutagenesisi394 – 3941Y → N: Increased activity towards 2-phenylethylamine, and decreased activity towards methylamine; when associated with V-211 and G-469. 1 Publication
    Mutagenesisi469 – 4691L → G: Increased activity towards 2-phenylethylamine, and decreased activity towards methylamine; when associated with V-211 and N-394. 1 Publication

    Organism-specific databases

    PharmGKBiPA24840.

    Chemistry

    DrugBankiDB01275. Hydralazine.
    DB00780. Phenelzine.

    Polymorphism and mutation databases

    DMDMi2501336.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 763762Membrane primary amine oxidasePRO_0000064102Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi137 – 1371N-linked (GlcNAc...)2 Publications
    Disulfide bondi198 ↔ 1991 Publication
    Glycosylationi212 – 2121O-linked (GalNAc...)1 Publication
    Glycosylationi232 – 2321N-linked (GlcNAc...)1 Publication
    Glycosylationi294 – 2941N-linked (GlcNAc...)2 Publications
    Modified residuei471 – 47112',4',5'-topaquinone
    Glycosylationi592 – 5921N-linked (GlcNAc...) (complex)4 Publications
    Glycosylationi618 – 6181N-linked (GlcNAc...)3 Publications
    Glycosylationi666 – 6661N-linked (GlcNAc...)3 Publications
    Disulfide bondi734 ↔ 7411 Publication
    Disulfide bondi748 – 748Interchain1 Publication

    Post-translational modificationi

    Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
    N- and O-glycosylated.4 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, TPQ

    Proteomic databases

    PaxDbiQ16853.
    PeptideAtlasiQ16853.
    PRIDEiQ16853.

    Expressioni

    Tissue specificityi

    Strongly expressed on the high endothelial venules of peripheral lymph nodes and on hepatic endothelia. Also highly expressed in appendix, lung and small intestine. Expressed also in adipose tissue, in bone marrow, colon, heart, kidney, ovary, pancreas, placenta, prostate, skeletal muscle, spleen and testis. Isoform 2 seems to be the predominant transcript in fetal kidneys, fetal cartilage and fetal tonsils. The highest relative expression of isoform 2 occurs in skeletal muscle, heart, pancreas, kidney, and lung.3 Publications

    Inductioni

    Up-regulated during in vitro adipocyte differentiation.1 Publication

    Gene expression databases

    BgeeiQ16853.
    CleanExiHS_AOC3.
    ExpressionAtlasiQ16853. baseline and differential.
    GenevisibleiQ16853. HS.

    Organism-specific databases

    HPAiCAB025797.
    HPA000980.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Can heterodimerize with isoform 2 leading to reduced surface expression. Forms a heterodimer with AOC2.3 Publications

    Protein-protein interaction databases

    BioGridi114192. 2 interactions.
    IntActiQ16853. 2 interactions.
    STRINGi9606.ENSP00000312326.

    Structurei

    Secondary structure

    1
    763
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi65 – 7814Combined sources
    Beta strandi83 – 853Combined sources
    Helixi86 – 883Combined sources
    Beta strandi93 – 10210Combined sources
    Helixi106 – 11510Combined sources
    Beta strandi123 – 1308Combined sources
    Beta strandi132 – 1354Combined sources
    Beta strandi137 – 1448Combined sources
    Beta strandi146 – 1483Combined sources
    Beta strandi151 – 1544Combined sources
    Helixi156 – 1605Combined sources
    Helixi166 – 1683Combined sources
    Helixi173 – 18513Combined sources
    Helixi188 – 1914Combined sources
    Helixi192 – 1998Combined sources
    Turni203 – 2064Combined sources
    Beta strandi208 – 2114Combined sources
    Beta strandi217 – 2193Combined sources
    Beta strandi224 – 2318Combined sources
    Beta strandi234 – 2363Combined sources
    Helixi238 – 2403Combined sources
    Beta strandi242 – 2509Combined sources
    Beta strandi253 – 2553Combined sources
    Helixi256 – 2583Combined sources
    Beta strandi260 – 2667Combined sources
    Beta strandi269 – 2724Combined sources
    Helixi274 – 2829Combined sources
    Turni283 – 2853Combined sources
    Turni298 – 3003Combined sources
    Beta strandi314 – 3163Combined sources
    Beta strandi318 – 3203Combined sources
    Beta strandi322 – 3265Combined sources
    Beta strandi329 – 34214Combined sources
    Turni343 – 3453Combined sources
    Beta strandi346 – 3549Combined sources
    Beta strandi357 – 37216Combined sources
    Helixi377 – 3804Combined sources
    Beta strandi383 – 3853Combined sources
    Helixi386 – 3883Combined sources
    Turni391 – 3944Combined sources
    Turni400 – 4023Combined sources
    Beta strandi408 – 42114Combined sources
    Beta strandi423 – 44523Combined sources
    Beta strandi447 – 4493Combined sources
    Beta strandi451 – 46818Combined sources
    Beta strandi471 – 4799Combined sources
    Turni481 – 4833Combined sources
    Beta strandi485 – 4939Combined sources
    Beta strandi497 – 4993Combined sources
    Beta strandi506 – 5127Combined sources
    Beta strandi515 – 5184Combined sources
    Beta strandi520 – 53011Combined sources
    Beta strandi534 – 55118Combined sources
    Beta strandi554 – 56916Combined sources
    Helixi572 – 5754Combined sources
    Beta strandi577 – 5815Combined sources
    Beta strandi585 – 59410Combined sources
    Beta strandi600 – 6089Combined sources
    Beta strandi617 – 6193Combined sources
    Helixi622 – 6298Combined sources
    Beta strandi630 – 6367Combined sources
    Turni647 – 6515Combined sources
    Beta strandi653 – 6553Combined sources
    Helixi660 – 6634Combined sources
    Beta strandi670 – 68415Combined sources
    Helixi688 – 6903Combined sources
    Beta strandi700 – 71314Combined sources
    Helixi715 – 7184Combined sources
    Beta strandi723 – 7297Combined sources
    Turni734 – 7363Combined sources
    Helixi738 – 7414Combined sources
    Helixi742 – 7454Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PU4X-ray3.20A/B1-763[»]
    1US1X-ray2.90A/B1-763[»]
    2C10X-ray2.50A/B/C/D29-763[»]
    2C11X-ray2.90A/B/C/D29-763[»]
    2Y73X-ray2.60A/B1-763[»]
    2Y74X-ray2.95A/B1-763[»]
    3ALAX-ray2.90A/B/C/D/E/F/G33-763[»]
    4BTWX-ray2.80A/B27-763[»]
    4BTXX-ray2.78A/B27-763[»]
    4BTYX-ray3.10A/B27-763[»]
    ProteinModelPortaliQ16853.
    SMRiQ16853. Positions 58-761.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16853.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the copper/topaquinone oxidase family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG3733.
    GeneTreeiENSGT00510000046461.
    HOGENOMiHOG000233919.
    HOVERGENiHBG004164.
    InParanoidiQ16853.
    KOiK00276.
    OMAiDEGRFNW.
    OrthoDBiEOG7353W8.
    PhylomeDBiQ16853.
    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 (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q16853-1) [UniParc]FASTAAdd to basket

    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
    MNQKTILVLL ILAVITIFAL VCVLLVGRGG DGGEPSQLPH CPSVSPSAQP
    60 70 80 90 100
    WTHPGQSQLF ADLSREELTA VMRFLTQRLG PGLVDAAQAR PSDNCVFSVE
    110 120 130 140 150
    LQLPPKAAAL AHLDRGSPPP AREALAIVFF GRQPQPNVSE LVVGPLPHPS
    160 170 180 190 200
    YMRDVTVERH GGPLPYHRRP VLFQEYLDID QMIFNRELPQ ASGLLHHCCF
    210 220 230 240 250
    YKHRGRNLVT MTTAPRGLQS GDRATWFGLY YNISGAGFFL HHVGLELLVN
    260 270 280 290 300
    HKALDPARWT IQKVFYQGRY YDSLAQLEAQ FEAGLVNVVL IPDNGTGGSW
    310 320 330 340 350
    SLKSPVPPGP APPLQFYPQG PRFSVQGSRV ASSLWTFSFG LGAFSGPRIF
    360 370 380 390 400
    DVRFQGERLV YEISLQEALA IYGGNSPAAM TTRYVDGGFG MGKYTTPLTR
    410 420 430 440 450
    GVDCPYLATY VDWHFLLESQ APKTIRDAFC VFEQNQGLPL RRHHSDLYSH
    460 470 480 490 500
    YFGGLAETVL VVRSMSTLLN YDYVWDTVFH PSGAIEIRFY ATGYISSAFL
    510 520 530 540 550
    FGATGKYGNQ VSEHTLGTVH THSAHFKVDL DVAGLENWVW AEDMVFVPMA
    560 570 580 590 600
    VPWSPEHQLQ RLQVTRKLLE MEEQAAFLVG SATPRYLYLA SNHSNKWGHP
    610 620 630 640 650
    RGYRIQMLSF AGEPLPQNSS MARGFSWERY QLAVTQRKEE EPSSSSVFNQ
    660 670 680 690 700
    NDPWAPTVDF SDFINNETIA GKDLVAWVTA GFLHIPHAED IPNTVTVGNG
    710 720 730 740 750
    VGFFLRPYNF FDEDPSFYSA DSIYFRGDQD AGACEVNPLA CLPQAAACAP
    760
    DLPAFSHGGF SHN
    Length:763
    Mass (Da):84,622
    Last modified:January 23, 2007 - v3
    Checksum:i58AD55605EC9D228
    GO
    Isoform 2 (identifier: Q16853-2) [UniParc]FASTAAdd to basket

    Also known as: VAP-1Delta3

    The sequence of this isoform differs from the canonical sequence as follows:
         630-634: YQLAV → IWWPG
         635-763: Missing.

    Note: Devoid of the semicarbazide-sensitive amine oxidase (SSAO) activity.
    Show »
    Length:634
    Mass (Da):70,675
    Checksum:i3275AE7C61775C99
    GO
    Isoform 3 (identifier: Q16853-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-543: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:220
    Mass (Da):24,533
    Checksum:i37CB1D564AC233E2
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti5 – 51T → R.1 Publication
    Corresponds to variant rs33954211 [ dbSNP | Ensembl ].
    VAR_025035
    Natural varianti78 – 781R → Q.
    Corresponds to variant rs402680 [ dbSNP | Ensembl ].
    VAR_052603
    Natural varianti167 – 1671H → Y.1 Publication
    Corresponds to variant rs2228470 [ dbSNP | Ensembl ].
    VAR_025027
    Natural varianti171 – 1711V → M.
    Corresponds to variant rs408038 [ dbSNP | Ensembl ].
    VAR_052604
    Natural varianti203 – 2031H → R.
    Corresponds to variant rs630079 [ dbSNP | Ensembl ].
    VAR_052605
    Natural varianti317 – 3171Y → H.
    Corresponds to variant rs438287 [ dbSNP | Ensembl ].
    VAR_012064
    Natural varianti329 – 3291R → Q.
    Corresponds to variant rs2229595 [ dbSNP | Ensembl ].
    VAR_024343
    Natural varianti371 – 3711I → T.1 Publication
    Corresponds to variant rs35097308 [ dbSNP | Ensembl ].
    VAR_025028
    Natural varianti408 – 4081A → S.1 Publication
    Corresponds to variant rs35643019 [ dbSNP | Ensembl ].
    VAR_025029
    Natural varianti426 – 4261R → H.1 Publication
    Corresponds to variant rs33986943 [ dbSNP | Ensembl ].
    VAR_025030
    Natural varianti441 – 4411R → W.1 Publication
    Corresponds to variant rs2229596 [ dbSNP | Ensembl ].
    VAR_025031
    Natural varianti582 – 5821A → T.1 Publication
    Corresponds to variant rs34987927 [ dbSNP | Ensembl ].
    VAR_025032
    Natural varianti700 – 7001G → S.1 Publication
    Corresponds to variant rs477207 [ dbSNP | Ensembl ].
    VAR_025033
    Natural varianti749 – 7491A → V.1 Publication
    Corresponds to variant rs34012919 [ dbSNP | Ensembl ].
    VAR_025034

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 543543Missing in isoform 3. 1 PublicationVSP_055201Add
    BLAST
    Alternative sequencei630 – 6345YQLAV → IWWPG in isoform 2. 1 PublicationVSP_053751
    Alternative sequencei635 – 763129Missing in isoform 2. 1 PublicationVSP_053752Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U39447 mRNA. Translation: AAC50919.1.
    AF067406 mRNA. Translation: AAC25170.1.
    AB050502 Genomic DNA. Translation: BAB18866.1.
    JX020506 mRNA. Translation: AGB67480.1.
    AK025727 mRNA. No translation available.
    AK315129 mRNA. Translation: BAG37582.1.
    DQ143944 Genomic DNA. Translation: AAZ38716.1.
    AC016889 Genomic DNA. No translation available.
    BC050549 mRNA. Translation: AAH50549.1.
    CCDSiCCDS11444.1. [Q16853-1]
    CCDS62198.1. [Q16853-3]
    CCDS74071.1. [Q16853-2]
    PIRiJC5234.
    RefSeqiNP_001264660.1. NM_001277731.1. [Q16853-2]
    NP_001264661.1. NM_001277732.1. [Q16853-3]
    NP_003725.1. NM_003734.3. [Q16853-1]
    UniGeneiHs.198241.

    Genome annotation databases

    EnsembliENST00000308423; ENSP00000312326; ENSG00000131471.
    ENST00000591562; ENSP00000468632; ENSG00000131471. [Q16853-3]
    ENST00000613571; ENSP00000484312; ENSG00000131471. [Q16853-2]
    ENST00000617500; ENSP00000477686; ENSG00000131471. [Q16853-3]
    GeneIDi8639.
    KEGGihsa:8639.
    UCSCiuc002ibv.4. human. [Q16853-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U39447 mRNA. Translation: AAC50919.1.
    AF067406 mRNA. Translation: AAC25170.1.
    AB050502 Genomic DNA. Translation: BAB18866.1.
    JX020506 mRNA. Translation: AGB67480.1.
    AK025727 mRNA. No translation available.
    AK315129 mRNA. Translation: BAG37582.1.
    DQ143944 Genomic DNA. Translation: AAZ38716.1.
    AC016889 Genomic DNA. No translation available.
    BC050549 mRNA. Translation: AAH50549.1.
    CCDSiCCDS11444.1. [Q16853-1]
    CCDS62198.1. [Q16853-3]
    CCDS74071.1. [Q16853-2]
    PIRiJC5234.
    RefSeqiNP_001264660.1. NM_001277731.1. [Q16853-2]
    NP_001264661.1. NM_001277732.1. [Q16853-3]
    NP_003725.1. NM_003734.3. [Q16853-1]
    UniGeneiHs.198241.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PU4X-ray3.20A/B1-763[»]
    1US1X-ray2.90A/B1-763[»]
    2C10X-ray2.50A/B/C/D29-763[»]
    2C11X-ray2.90A/B/C/D29-763[»]
    2Y73X-ray2.60A/B1-763[»]
    2Y74X-ray2.95A/B1-763[»]
    3ALAX-ray2.90A/B/C/D/E/F/G33-763[»]
    4BTWX-ray2.80A/B27-763[»]
    4BTXX-ray2.78A/B27-763[»]
    4BTYX-ray3.10A/B27-763[»]
    ProteinModelPortaliQ16853.
    SMRiQ16853. Positions 58-761.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi114192. 2 interactions.
    IntActiQ16853. 2 interactions.
    STRINGi9606.ENSP00000312326.

    Chemistry

    BindingDBiQ16853.
    ChEMBLiCHEMBL3437.
    DrugBankiDB01275. Hydralazine.
    DB00780. Phenelzine.
    GuidetoPHARMACOLOGYi2767.

    Polymorphism and mutation databases

    DMDMi2501336.

    Proteomic databases

    PaxDbiQ16853.
    PeptideAtlasiQ16853.
    PRIDEiQ16853.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000308423; ENSP00000312326; ENSG00000131471.
    ENST00000591562; ENSP00000468632; ENSG00000131471. [Q16853-3]
    ENST00000613571; ENSP00000484312; ENSG00000131471. [Q16853-2]
    ENST00000617500; ENSP00000477686; ENSG00000131471. [Q16853-3]
    GeneIDi8639.
    KEGGihsa:8639.
    UCSCiuc002ibv.4. human. [Q16853-1]

    Organism-specific databases

    CTDi8639.
    GeneCardsiGC17P041003.
    HGNCiHGNC:550. AOC3.
    HPAiCAB025797.
    HPA000980.
    MIMi603735. gene.
    neXtProtiNX_Q16853.
    PharmGKBiPA24840.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG3733.
    GeneTreeiENSGT00510000046461.
    HOGENOMiHOG000233919.
    HOVERGENiHBG004164.
    InParanoidiQ16853.
    KOiK00276.
    OMAiDEGRFNW.
    OrthoDBiEOG7353W8.
    PhylomeDBiQ16853.
    TreeFamiTF314750.

    Enzyme and pathway databases

    BRENDAi1.4.3.21. 2681.
    SABIO-RKQ16853.

    Miscellaneous databases

    EvolutionaryTraceiQ16853.
    GeneWikiiAOC3.
    GenomeRNAii8639.
    NextBioi32389.
    PROiQ16853.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ16853.
    CleanExiHS_AOC3.
    ExpressionAtlasiQ16853. baseline and differential.
    GenevisibleiQ16853. HS.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning and sequencing of a copper-containing, topaquinone-containing monoamine oxidase from human placenta."
      Zhang X., McIntire W.S.
      Gene 179:279-286(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. "Cloning of vascular adhesion protein 1 reveals a novel multifunctional adhesion molecule."
      Smith D.J., Salmi M., Bono P., Hellman J., Leu T., Jalkanen S.
      J. Exp. Med. 188:17-27(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, FUNCTION, SELF-ASSOCIATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Lung.
    3. "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].
    4. "Functional modulation of vascular adhesion protein-1 by a novel splice variant."
      Kaitaniemi S., Gron K., Elovaara H., Salmi M., Jalkanen S., Elima K.
      PLoS ONE 8:E54151-E54151(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBUNIT, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
      Tissue: Placenta.
    6. NIEHS SNPs program
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-5; TYR-167; THR-371; SER-408; HIS-426; TRP-441; THR-582; SER-700 AND VAL-749.
    7. "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].
    8. "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).
      Tissue: PNS.
    9. "Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes."
      Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.
      Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 79-90 AND 123-132.
      Tissue: Adipocyte.
    10. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-592; ASN-618 AND ASN-666.
      Tissue: Plasma.
    11. "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.
    12. "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, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF MET-211; TYR-394 AND LEU-469.
    13. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-137; ASN-294; ASN-592; ASN-618 AND ASN-666.
      Tissue: Liver.
    14. Cited for: GLYCOSYLATION AT ASN-592.
    15. "Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications."
      Airenne T.T., Nymalm Y., Kidron H., Smith D.J., Pihlavisto M., Salmi M., Jalkanen S., Johnson M.S., Salminen T.A.
      Protein Sci. 14:1964-1974(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH COPPER AND CALCIUM IONS, DISULFIDE BONDS, TOPAQUINONE AT TYR-471, GLYCOSYLATION AT ASN-137; THR-212; ASN-232; ASN-294; ASN-592; ASN-618 AND ASN-666.

    Entry informationi

    Entry nameiAOC3_HUMAN
    AccessioniPrimary (citable) accession number: Q16853
    Secondary accession number(s): B2RCI5
    , K7ESB3, L0L8N9, Q45F94
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: July 22, 2015
    This is version 159 of the entry and version 3 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

    3D-structure, Complete proteome, Direct protein sequencing, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.