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O70423

- AOC3_MOUSE

UniProt

O70423 - AOC3_MOUSE

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Protein

Membrane primary amine oxidase

Gene

Aoc3

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

Functioni

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

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

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  1. amine metabolic process Source: UniProtKB
  2. cell adhesion Source: UniProtKB
  3. response to antibiotic Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Membrane primary amine oxidase (EC:1.4.3.21)
Alternative name(s):
Copper amine oxidase
Semicarbazide-sensitive amine oxidase
Short name:
SSAO
Vascular adhesion protein 1
Short name:
VAP-1
Gene namesi
Name:Aoc3
Synonyms:Vap1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1306797. Aoc3.

Subcellular locationi

Membrane By similarity; Single-pass type II membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 65CytoplasmicSequence Analysis
Transmembranei7 – 2721Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini28 – 765738ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell surface Source: UniProtKB
  2. cytoplasm Source: Ensembl
  3. integral component of membrane Source: UniProtKB
  4. microvillus Source: Ensembl
  5. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 765764Membrane primary amine oxidasePRO_0000064103Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi137 – 1371N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi198 ↔ 199By similarity
Glycosylationi212 – 2121O-linked (GalNAc...)By similarity
Glycosylationi232 – 2321N-linked (GlcNAc...)Sequence Analysis
Glycosylationi294 – 2941N-linked (GlcNAc...)Sequence Analysis
Modified residuei471 – 47112',4',5'-topaquinoneBy similarity
Glycosylationi592 – 5921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi659 – 6591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi666 – 6661N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi734 ↔ 741By similarity
Disulfide bondi748 – 748InterchainBy similarity

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, TPQ

Proteomic databases

MaxQBiO70423.
PaxDbiO70423.
PRIDEiO70423.

Expressioni

Gene expression databases

BgeeiO70423.
CleanExiMM_AOC3.
ExpressionAtlasiO70423. baseline and differential.
GenevestigatoriO70423.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Forms a heterodimer with AOC2 (By similarity).By similarity

Protein-protein interaction databases

BioGridi198116. 1 interaction.
IntActiO70423. 4 interactions.
MINTiMINT-4087892.
STRINGi10090.ENSMUSP00000099394.

Structurei

3D structure databases

ProteinModelPortaliO70423.
SMRiO70423. Positions 58-761.
ModBaseiSearch...
MobiDBiSearch...

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.
InParanoidiO70423.
KOiK00276.
OMAiSWERYQL.
OrthoDBiEOG7353W8.
PhylomeDBiO70423.
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

Isoform 1 (identifier: O70423-1) [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
MTQKTTLVLL ALAVITIFAL VCVLLAGRSG DGGGLSQPLH CPSVLPSVQP
60 70 80 90 100
RTHPSQSQPF ADLSPEELTA VMSFLTKHLG PGLVDAAQAR PSDNCVFSVE
110 120 130 140 150
LQLPAKAAAL AHLDRGGPPP VREALAIIFF GGQPKPNVSE LVVGPLPHPS
160 170 180 190 200
YMRDVTVERH GGPLPYYRRP VLDREYQDIE EMIFHRELPQ ASGLLHHCCF
210 220 230 240 250
YKHQGQNLLT MTTAPRGLQS GDRATWFGLY YNLSGAGFYP HPIGLELLID
260 270 280 290 300
HKALDPALWT IQKVFYQGRY YESLTQLEDQ FEAGLVNVVL VPNNGTGGSW
310 320 330 340 350
SLKSSVPPGP APPLQFHPQG PRFSVQGSQV SSSLWAFSFG LGAFSGPRIF
360 370 380 390 400
DIRFQGERVA YEISVQEAIA LYGGNSPASM STCYVDGSFG IGKYSTPLIR
410 420 430 440 450
GVDCPYLATY VDWHFLLESQ APKTLRDAFC VFEQNQGLPL RRHHSDFYSH
460 470 480 490 500
YFGGVVGTVL VVRSVSTLLN YDYIWDMVFH PNGAIEVKFH ATGYISSAFF
510 520 530 540 550
FGAGEKFGNR VGAHTLGTVH THSAHFKVDL DVAGLKNWAW AEDMAFVPTI
560 570 580 590 600
VPWQPEYQMQ RLQVTRKLLE TEEEAAFPLG GATPRYLYLA SNHSNKWGHR
610 620 630 640 650
RGYRIQILSF AGKPLPQESP IEKAFTWGRY HLAVTQRKEE EPSSSSIFNQ
660 670 680 690 700
NDPWTPTVNF TDFISNETIA GEDLVAWVTA GFLHIPHAED IPNTVTAGNS
710 720 730 740 750
VGFFLRPYNF FDEDPSFHSA DSIYFREGQD ATACEVNPLA CLSQTATCAP
760
EIPAFSHGGF AYRDN
Length:765
Mass (Da):84,534
Last modified:January 23, 2007 - v3
Checksum:i7489ED67D3DBB44D
GO
Isoform 2 (identifier: O70423-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     630-765: Missing.

Note: No experimental confirmation available.

Show »
Length:629
Mass (Da):69,527
Checksum:i96121FDE3D7473F4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti659 – 6591N → D in AAD09199. (PubMed:10092636)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei630 – 765136Missing in isoform 2. 1 PublicationVSP_016604Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF054831 mRNA. Translation: AAC23747.1.
AF078705 Genomic DNA. Translation: AAC35839.1.
AF115411 mRNA. Translation: AAD09199.1.
AL590969 Genomic DNA. Translation: CAM19551.1.
BC080857 mRNA. Translation: AAH80857.1.
CCDSiCCDS25465.1. [O70423-1]
RefSeqiNP_033805.1. NM_009675.2. [O70423-1]
UniGeneiMm.67281.

Genome annotation databases

EnsembliENSMUST00000103105; ENSMUSP00000099394; ENSMUSG00000019326. [O70423-1]
GeneIDi11754.
KEGGimmu:11754.
UCSCiuc007lop.2. mouse. [O70423-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF054831 mRNA. Translation: AAC23747.1 .
AF078705 Genomic DNA. Translation: AAC35839.1 .
AF115411 mRNA. Translation: AAD09199.1 .
AL590969 Genomic DNA. Translation: CAM19551.1 .
BC080857 mRNA. Translation: AAH80857.1 .
CCDSi CCDS25465.1. [O70423-1 ]
RefSeqi NP_033805.1. NM_009675.2. [O70423-1 ]
UniGenei Mm.67281.

3D structure databases

ProteinModelPortali O70423.
SMRi O70423. Positions 58-761.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198116. 1 interaction.
IntActi O70423. 4 interactions.
MINTi MINT-4087892.
STRINGi 10090.ENSMUSP00000099394.

Chemistry

BindingDBi O70423.
ChEMBLi CHEMBL4727.

Proteomic databases

MaxQBi O70423.
PaxDbi O70423.
PRIDEi O70423.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000103105 ; ENSMUSP00000099394 ; ENSMUSG00000019326 . [O70423-1 ]
GeneIDi 11754.
KEGGi mmu:11754.
UCSCi uc007lop.2. mouse. [O70423-1 ]

Organism-specific databases

CTDi 8639.
MGIi MGI:1306797. Aoc3.

Phylogenomic databases

eggNOGi COG3733.
GeneTreei ENSGT00510000046461.
HOGENOMi HOG000233919.
HOVERGENi HBG004164.
InParanoidi O70423.
KOi K00276.
OMAi SWERYQL.
OrthoDBi EOG7353W8.
PhylomeDBi O70423.
TreeFami TF314750.

Miscellaneous databases

NextBioi 279503.
PROi O70423.
SOURCEi Search...

Gene expression databases

Bgeei O70423.
CleanExi MM_AOC3.
ExpressionAtlasi O70423. baseline and differential.
Genevestigatori O70423.

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. "Isolation, structural characterization, and chromosomal mapping of the mouse vascular adhesion protein-1 gene and promoter."
    Bono P., Salmi M., Smith D.J., Leppanen I., Horelli-Kuitunen N., Palotie A., Jalkanen S.
    J. Immunol. 161:2953-2960(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    Strain: 129/SvJ and BALB/c.
  2. "Molecular cloning of a major mRNA species in murine 3T3 adipocyte lineage. differentiation-dependent expression, regulation, and identification as semicarbazide-sensitive amine oxidase."
    Moldes M., Feve B., Pairault J.
    J. Biol. Chem. 274:9515-9523(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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 2).
    Strain: C57BL/6.
    Tissue: Brain.

Entry informationi

Entry nameiAOC3_MOUSE
AccessioniPrimary (citable) accession number: O70423
Secondary accession number(s): A2A4I7, Q66JM4, Q9R055
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 128 of the entry and version 3 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

External Data

Dasty 3