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Protein

Amiloride-sensitive amine oxidase [copper-containing]

Gene

AOC1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the degradation of compounds such as putrescine, histamine, spermine, and spermidine, substances involved in allergic and immune responses, cell proliferation, tissue differentiation, tumor formation, and possibly apoptosis.By similarity

Catalytic activityi

Histamine + H2O + O2 = (imidazol-4-yl)acetaldehyde + NH3 + H2O2.2 Publications

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

Enzyme regulationi

Inhibited by amiloride in a competitive manner.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei376Proton acceptorBy similarity1
Active sitei464Schiff-base intermediate with substrate; via topaquinone1 Publication1
Metal bindingi513Copper; via tele nitrogenBy similarity1
Metal bindingi515Copper; via tele nitrogenBy similarity1
Metal bindingi522Calcium 1By similarity1
Metal bindingi523Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi524Calcium 1By similarity1
Metal bindingi565Calcium 2By similarity1
Metal bindingi656Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi659Calcium 2By similarity1
Metal bindingi661Calcium 2By similarity1
Metal bindingi667Calcium 1By similarity1
Metal bindingi668Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi678Copper; via pros nitrogenBy similarity1

GO - Molecular functioni

GO - Biological processi

  • amine metabolic process Source: InterPro
  • cellular response to azide Source: UniProtKB
  • cellular response to copper ion Source: UniProtKB
  • cellular response to copper ion starvation Source: UniProtKB
  • cellular response to histamine Source: UniProtKB
  • oxidation-reduction process Source: UniProtKB
  • response to antibiotic Source: UniProtKB
  • response to drug Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Calcium, Copper, Heparin-binding, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14652.
BRENDAi1.4.3.22. 6170.
ReactomeiR-SSC-211945. Phase 1 - Functionalization of compounds.
R-SSC-6798695. Neutrophil degranulation.
SABIO-RKQ9TRC7.

Names & Taxonomyi

Protein namesi
Recommended name:
Amiloride-sensitive amine oxidase [copper-containing]Curated (EC:1.4.3.222 Publications)
Short name:
DAO1 Publication
Short name:
Diamine oxidase1 Publication
Alternative name(s):
Amiloride-binding protein 11 Publication
Amine oxidase copper domain-containing protein 1Curated
HistaminaseCurated
Gene namesi
Name:AOC1
Synonyms:ABP1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 18

Subcellular locationi

GO - Cellular componenti

  • bicellular tight junction Source: UniProtKB
  • extracellular exosome Source: Ensembl
  • extracellular space Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3108636.
DrugBankiDB00594. Amiloride.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
ChainiPRO_000006410025 – 755Amiloride-sensitive amine oxidase [copper-containing]Sequence analysisAdd BLAST731

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi115N-linked (GlcNAc...)By similarity1
Disulfide bondi182 ↔ 186By similarity
Disulfide bondi394 ↔ 420By similarity
Modified residuei4642',4',5'-topaquinone1 Publication1
Glycosylationi541N-linked (GlcNAc...)By similarity1
Disulfide bondi740InterchainBy similarity
Glycosylationi749N-linked (GlcNAc...)By similarity1

Post-translational modificationi

N-glycosylated; the glycans are primarily linear, di-, or tribranched fucosylated complex type.1 Publication
Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, TPQ

Proteomic databases

PaxDbiQ9TRC7.
PeptideAtlasiQ9TRC7.

PTM databases

UniCarbKBiQ9TRC7.

Expressioni

Gene expression databases

BgeeiENSSSCG00000016442.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000017422.

Chemistry databases

BindingDBiQ9TRC7.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni374 – 384Substrate bindingBy similarityAdd BLAST11
Regioni461 – 466Substrate bindingBy similarity6
Regioni571 – 578Heparin-bindingBy similarity8

Sequence similaritiesi

Belongs to the copper/topaquinone oxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1186. Eukaryota.
COG3733. LUCA.
GeneTreeiENSGT00510000046461.
InParanoidiQ9TRC7.
KOiK11182.
OMAiFNSNFKG.
OrthoDBiEOG091G0C1O.

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.

Q9TRC7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRGTLALGW AGAALLLLQM LAAAERSPRT PGGKAGVFAD LSAQELKAVH
60 70 80 90 100
SFLWSQKELK LEPSGTLTMA KNSVFLIEML LPKKQHVLKF LDKGHRRPVR
110 120 130 140 150
EARAVIFFGA QEQPNVTEFA VGPLPTPRYM RDLPPRPGHQ VSWASRPISK
160 170 180 190 200
AEYALLSHKL QEATQPLRQF FRRTTGSSFG DCHEQCLTFT DVAPRGLASG
210 220 230 240 250
QRRTWFILQR QMPGYFLHPT GLELLVDHGS TNAQDWTVEQ VWYNGKFYRS
260 270 280 290 300
PEELAQKYND GEVDVVILED PLAKGKDGES LPEPALFSFY QPRGDFAVTM
310 320 330 340 350
HGPHVVQPQG PRYSLEGNRV MYGGWSFAFR LRSSSGLQIL DVHFGGERIA
360 370 380 390 400
YEVSVQEAVA LYGGHTPAGM QTKYIDVGWG LGSVTHELAP DIDCPETATF
410 420 430 440 450
LDALHHYDAD GPVLYPRALC LFEMPTGVPL RRHFNSNFSG GFNFYAGLKG
460 470 480 490 500
QVLVLRTTST VYNYDYIWDF IFYPNGVMEA KMHATGYVHA TFYTPEGLRY
510 520 530 540 550
GTRLHTHLIG NMHTHLVNYR VDLDVAGTTN SFQTLQMELE NITNPWSPRH
560 570 580 590 600
RLVQPTLKQT RYSRERQAAF RFGQPLPKYL LITSPKENPW GHTRSYRLQL
610 620 630 640 650
HSMADQVLPP GWQEERAVTW ARYPLAVTRY RESELSSSSI YNQNDPWDPP
660 670 680 690 700
VVFEEFLRNN ENIEDEDLVA WVTVGFLHIP HSEDIPNTAT PGNSVGFLLR
710 720 730 740 750
PFNFFPEDPA LASRDLVVVW PLENGSTYAQ RWIPEEDQSC LKPPPFSYNG

SYRPV
Length:755
Mass (Da):85,475
Last modified:February 4, 2015 - v3
Checksum:i3859049D87819255
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti33G → P AA sequence (PubMed:8144586).Curated1
Sequence conflicti40 – 42DLS → AGV AA sequence (PubMed:8144586).Curated3
Sequence conflicti44 – 45QE → ED AA sequence (PubMed:8144586).Curated2
Sequence conflicti474P → Y AA sequence (PubMed:1457410).Curated1
Sequence conflicti593Missing in CAA23203 (PubMed:8672129).Curated1
Sequence conflicti595 – 597SYR → AVP in CAA23203 (PubMed:8672129).Curated3
Sequence conflicti602S → F in CAA23203 (PubMed:8672129).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU928555 Genomic DNA. No translation available.
F14708 mRNA. Translation: CAA23203.1.
PIRiB54410.
RefSeqiXP_003134601.1. XM_003134553.3.
UniGeneiSsc.21957.

Genome annotation databases

EnsembliENSSSCT00000017903; ENSSSCP00000017422; ENSSSCG00000016442.
GeneIDi100517436.
KEGGissc:100517436.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU928555 Genomic DNA. No translation available.
F14708 mRNA. Translation: CAA23203.1.
PIRiB54410.
RefSeqiXP_003134601.1. XM_003134553.3.
UniGeneiSsc.21957.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000017422.

Chemistry databases

BindingDBiQ9TRC7.
ChEMBLiCHEMBL3108636.
DrugBankiDB00594. Amiloride.

PTM databases

UniCarbKBiQ9TRC7.

Proteomic databases

PaxDbiQ9TRC7.
PeptideAtlasiQ9TRC7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000017903; ENSSSCP00000017422; ENSSSCG00000016442.
GeneIDi100517436.
KEGGissc:100517436.

Organism-specific databases

CTDi26.

Phylogenomic databases

eggNOGiKOG1186. Eukaryota.
COG3733. LUCA.
GeneTreeiENSGT00510000046461.
InParanoidiQ9TRC7.
KOiK11182.
OMAiFNSNFKG.
OrthoDBiEOG091G0C1O.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14652.
BRENDAi1.4.3.22. 6170.
ReactomeiR-SSC-211945. Phase 1 - Functionalization of compounds.
R-SSC-6798695. Neutrophil degranulation.
SABIO-RKQ9TRC7.

Gene expression databases

BgeeiENSSSCG00000016442.

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 nameiAOC1_PIG
AccessioniPrimary (citable) accession number: Q9TRC7
Secondary accession number(s): F1SSL3, Q29317
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: February 4, 2015
Last modified: November 30, 2016
This is version 89 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, 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.