Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Membrane primary amine oxidase

Gene

Aoc3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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 similarity1 Publication

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)DescriptionActionsGraphical viewLength
Active sitei386Proton acceptorBy similarity1
Active sitei471Schiff-base intermediate with substrate; via topaquinoneBy similarity1
Metal bindingi520Copper; via tele nitrogenBy similarity1
Metal bindingi522Copper; via tele nitrogenBy similarity1
Metal bindingi529Calcium 1By similarity1
Metal bindingi530Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi531Calcium 1By similarity1
Metal bindingi572Calcium 2By similarity1
Metal bindingi663Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi667Calcium 2By similarity1
Metal bindingi673Calcium 1By similarity1
Metal bindingi674Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi684Copper; via pros nitrogenBy similarity1

GO - Molecular functioni

GO - Biological processi

  • aging Source: RGD
  • amine metabolic process Source: UniProtKB
  • cell adhesion Source: UniProtKB
  • eating behavior Source: RGD
  • leukocyte migration involved in inflammatory response Source: RGD
  • positive regulation of acute inflammatory response Source: RGD
  • positive regulation of glucose transport Source: RGD
  • positive regulation of leukocyte migration Source: RGD
  • regulation of blood pressure Source: RGD
  • response to immobilization stress Source: RGD
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. 5301.
ReactomeiR-RNO-211945. Phase 1 - Functionalization of compounds.

Names & Taxonomyi

Protein namesi
Recommended name:
Membrane primary amine oxidase (EC:1.4.3.21By similarity)
Alternative name(s):
Copper amine oxidase
Semicarbazide-sensitive amine oxidase
Short name:
SSAO
VP97
Vascular adhesion protein 1
Short name:
VAP-1
Gene namesi
Name:Aoc3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi62058. Aoc3.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 6CytoplasmicSequence analysis5
Transmembranei7 – 27Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini28 – 763ExtracellularSequence analysisAdd BLAST736

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • extracellular space Source: RGD
  • integral component of membrane Source: UniProtKB
  • intracellular membrane-bounded organelle Source: RGD
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4592.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000641052 – 763Membrane primary amine oxidaseAdd BLAST762

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi137N-linked (GlcNAc...)By similarity1
Disulfide bondi198 ↔ 199By similarity
Glycosylationi212O-linked (GalNAc...)By similarity1
Glycosylationi232N-linked (GlcNAc...)By similarity1
Glycosylationi294N-linked (GlcNAc...)By similarity1
Disulfide bondi404 ↔ 430By similarity
Modified residuei4712',4',5'-topaquinoneBy similarity1
Glycosylationi592N-linked (GlcNAc...) (complex)By similarity1
Glycosylationi666N-linked (GlcNAc...)By similarity1
Disulfide bondi734 ↔ 741By similarity
Disulfide bondi748InterchainBy similarity

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, TPQ

Proteomic databases

PaxDbiO08590.
PRIDEiO08590.

PTM databases

iPTMnetiO08590.
PhosphoSitePlusiO08590.

Expressioni

Tissue specificityi

Highly expressed in adipocytes, aorta and lung. Expressed at lower levels in heart, kidney, large intestine, liver, small intestine and stomach.1 Publication

Gene expression databases

GenevisibleiO08590. RN.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000059889.

Chemistry databases

BindingDBiO08590.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni384 – 394Substrate bindingBy similarityAdd BLAST11
Regioni468 – 473Substrate bindingBy similarity6
Regioni578 – 585Heparin-bindingBy similarity8

Sequence similaritiesi

Belongs to the copper/topaquinone oxidase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1186. Eukaryota.
KOG4470. Eukaryota.
COG3733. LUCA.
GeneTreeiENSGT00510000046461.
HOGENOMiHOG000233919.
HOVERGENiHBG004164.
InParanoidiO08590.
KOiK00276.
OrthoDBiEOG091G02WY.

Family and domain databases

Gene3Di2.70.98.20. 1 hit.
InterProiIPR000269. 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.
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.

O08590-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQKTTLVLL ALAVITIFAL VCVLLAGRSG DGGRLSQPLH CPSVLPSVQP
60 70 80 90 100
QTHPGQSQPF ADLSPEELTA VMSFLIKHLG PGLVDAAQAR PSDNCVFSVE
110 120 130 140 150
LQLPAKAAAL AHLDRGGPPP VREALAIIFF GGQPKPNVSE LVVGPLPHPS
160 170 180 190 200
YMRDVTVERH GGPLPYYRRP VLTREYQDIQ EMIFHRELPQ ASGLLHHCCF
210 220 230 240 250
YKRQGHNLLK MTTAPRGLQS GDRATWFGIY YNLSGAGFYP HPIGLELLVD
260 270 280 290 300
HKALDPALWT IQKVFYQGRY YESLTQLEDM FEAGLVNVVL VPDNGTGGSW
310 320 330 340 350
SLKSSVPPGR APPLQFHPEG PRFSVQGSQV RSSLWAFSFG LGAFSGPRIF
360 370 380 390 400
DIRFQGERVA YEISVQEAIA LYGGNSPASM STCYMDGSFG IGKYSTPLTR
410 420 430 440 450
GVDCPYLATY VDWHFLLESQ TPKTLRDAFC VFEQNQGLPL RRHHSDFYSH
460 470 480 490 500
YFGGVVETVL VVRSVATLLN YDYVWDMVFH SNGAIEVKFH ATGYITSAFF
510 520 530 540 550
FGAGEKFGNR VAEHTLGTVH THNAHFKVDL DVAGLKNWAW AEDLAFVPMN
560 570 580 590 600
VPWQPEFQMQ RLQVTRKLLE TEEEAAFPLG NATPRYLYLA SNHSNKWGHR
610 620 630 640 650
RGYRIQILSF AGKPLPQESP IEKAFTWGRY HLAVTQRKEE EPSSSSIYNQ
660 670 680 690 700
NDPWTPTVDF TDFISNETIA GEDLVAWVTA GFLHIPHAED IPNTVTVGNG
710 720 730 740 750
VGFFLRPYNF FDEDPSFYSP DSIYFRKDQD VTDCEVNSLA CLSQTANCVP
760
DLPAFSHGGF TYK
Length:763
Mass (Da):84,981
Last modified:January 23, 2007 - v4
Checksum:i5FD739AF43F39039
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti54P → S in AAC53189 (PubMed:9083076).Curated1
Sequence conflicti329Q → R in BAD74047 (PubMed:15744061).Curated1
Sequence conflicti645S → F in BAD74047 (PubMed:15744061).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB195675 mRNA. Translation: BAD74047.1.
BC100613 mRNA. Translation: AAI00614.1.
U72632 mRNA. Translation: AAC53189.1.
RefSeqiNP_113770.2. NM_031582.2.
UniGeneiRn.198327.

Genome annotation databases

EnsembliENSRNOT00000076820; ENSRNOP00000068449; ENSRNOG00000051307.
GeneIDi29473.
KEGGirno:29473.
UCSCiRGD:62058. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB195675 mRNA. Translation: BAD74047.1.
BC100613 mRNA. Translation: AAI00614.1.
U72632 mRNA. Translation: AAC53189.1.
RefSeqiNP_113770.2. NM_031582.2.
UniGeneiRn.198327.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000059889.

Chemistry databases

BindingDBiO08590.
ChEMBLiCHEMBL4592.

PTM databases

iPTMnetiO08590.
PhosphoSitePlusiO08590.

Proteomic databases

PaxDbiO08590.
PRIDEiO08590.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000076820; ENSRNOP00000068449; ENSRNOG00000051307.
GeneIDi29473.
KEGGirno:29473.
UCSCiRGD:62058. rat.

Organism-specific databases

CTDi8639.
RGDi62058. Aoc3.

Phylogenomic databases

eggNOGiKOG1186. Eukaryota.
KOG4470. Eukaryota.
COG3733. LUCA.
GeneTreeiENSGT00510000046461.
HOGENOMiHOG000233919.
HOVERGENiHBG004164.
InParanoidiO08590.
KOiK00276.
OrthoDBiEOG091G02WY.

Enzyme and pathway databases

BRENDAi1.4.3.21. 5301.
ReactomeiR-RNO-211945. Phase 1 - Functionalization of compounds.

Miscellaneous databases

PROiO08590.

Gene expression databases

GenevisibleiO08590. RN.

Family and domain databases

Gene3Di2.70.98.20. 1 hit.
InterProiIPR000269. 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.
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...

Entry informationi

Entry nameiAOC3_RAT
AccessioniPrimary (citable) accession number: O08590
Secondary accession number(s): Q497D2, Q5R1T5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 133 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.