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Protein

Amiloride-sensitive amine oxidase [copper-containing]

Gene

Aoc1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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.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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei368 – 3681Proton acceptorBy similarity
Active sitei456 – 4561Schiff-base intermediate with substrate; via topaquinoneBy similarity
Metal bindingi505 – 5051Copper; via tele nitrogenBy similarity
Metal bindingi507 – 5071Copper; via tele nitrogenBy similarity
Metal bindingi514 – 5141Calcium 1By similarity
Metal bindingi516 – 5161Calcium 1By similarity
Metal bindingi557 – 5571Calcium 2By similarity
Metal bindingi648 – 6481Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi651 – 6511Calcium 2By similarity
Metal bindingi653 – 6531Calcium 2By similarity
Metal bindingi659 – 6591Calcium 1By similarity
Metal bindingi660 – 6601Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi670 – 6701Copper; via pros nitrogenBy similarity

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

BRENDAi1.4.3.22. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Amiloride-sensitive amine oxidase [copper-containing] (EC:1.4.3.22By similarity)
Short name:
DAO
Short name:
Diamine oxidase
Alternative name(s):
Amiloride-binding protein 1
Amine oxidase copper domain-containing protein 1
Histaminase
Gene namesi
Name:Aoc1
Synonyms:Abp1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61296. Aoc1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL4648.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Chaini23 – 746724Amiloride-sensitive amine oxidase [copper-containing]PRO_0000035668Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi110 – 1101N-linked (GlcNAc...)By similarity
Disulfide bondi177 ↔ 181By similarity
Glycosylationi269 – 2691N-linked (GlcNAc...)Sequence analysis
Disulfide bondi386 ↔ 412By similarity
Modified residuei456 – 45612',4',5'-topaquinoneBy similarity
Glycosylationi533 – 5331N-linked (GlcNAc...)By similarity
Glycosylationi652 – 6521N-linked (GlcNAc...)By similarity
Disulfide bondi731 – 731InterchainBy similarity
Glycosylationi740 – 7401N-linked (GlcNAc...)By similarity

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, TPQ

Proteomic databases

PaxDbiP36633.
PRIDEiP36633.

PTM databases

PhosphoSiteiP36633.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000055909.

Chemistry

BindingDBiP36633.

Structurei

3D structure databases

ProteinModelPortaliP36633.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni366 – 37611Substrate bindingBy similarityAdd
BLAST
Regioni453 – 4586Substrate bindingBy similarity
Regioni563 – 5708Heparin-bindingBy similarity

Sequence similaritiesi

Belongs to the copper/topaquinone oxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1186. Eukaryota.
COG3733. LUCA.
HOVERGENiHBG004164.
InParanoidiP36633.

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.

P36633-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCLAFGWAAV ILVLQTVDTA SAVRTPYDKA RVFADLSPQE IKAVHSFLMN
60 70 80 90 100
REELGLQPSK EPTLAKNSVF LIEMLLPKKK HVLKFLDEGR KGPNREARAV
110 120 130 140 150
IFFGAQDYPN VTEFAVGPLP RPYYIRALSP RPGHHLSWSS RPISTAEYDL
160 170 180 190 200
LYHTLKRATM PLHQFFLDTT GFSFLGCDDR CLTFTDVAPR GVASGQRRSW
210 220 230 240 250
FIVQRYVEGY FLHPTGLEIL LDHGSTDVQD WRVEQLWYNG KFYNNPEELA
260 270 280 290 300
RKYAVGEVDT VVLEDPLPNG TEKPPLFSSY KPRGEFHTPV NVAGPHVVQP
310 320 330 340 350
SGPRYKLEGN TVLYGGWSFS YRLRSSSGLQ IFNVLFGGER VAYEVSVQEA
360 370 380 390 400
VALYGGHTPA GMQTKYIDVG WGLGSVTHEL APGIDCPETA TFLDAFHYYD
410 420 430 440 450
SDGPVHYPHA LCLFEMPTGV PLRRHFNSNF KGGFNFYAGL KGYVLVLRTT
460 470 480 490 500
STVYNYDYIW DFIFYSNGVM EAKMHATGYV HATFYTPEGL RHGTRLQTHL
510 520 530 540 550
LGNIHTHLVH YRVDMDVAGT KNSFQTLTMK LENLTNPWSP SHSLVQPTLE
560 570 580 590 600
QTQYSQEHQA AFRFGQTLPK YLLFSSPQKN CWGHRRSYRL QIHSMAEQVL
610 620 630 640 650
PPGWQEERAV TWARYPLAVT KYRESERYSS SLYNQNDPWD PPVVFEEFLR
660 670 680 690 700
NNENIEDEDL VAWVTVGFLH IPHSEDVPNT ATPGNSVGFL LRPFNFFPED
710 720 730 740
PSLASRDTVI VWPQDKGLNR VQRWIPEDRR CLVSPPFSYN GTYKPV
Length:746
Mass (Da):85,021
Last modified:June 1, 1994 - v1
Checksum:i6C564D044D07BCB2
GO

Sequence cautioni

The sequence CAA52117.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti587 – 5871S → T in AAB31157 (PubMed:8023885).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73911 mRNA. Translation: CAA52116.1.
X73912 mRNA. Translation: CAA52117.1. Different initiation.
S70383 mRNA. Translation: AAB31157.1.
PIRiS36847. S34656.
UniGeneiRn.54493.

Genome annotation databases

UCSCiRGD:61296. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73911 mRNA. Translation: CAA52116.1.
X73912 mRNA. Translation: CAA52117.1. Different initiation.
S70383 mRNA. Translation: AAB31157.1.
PIRiS36847. S34656.
UniGeneiRn.54493.

3D structure databases

ProteinModelPortaliP36633.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000055909.

Chemistry

BindingDBiP36633.
ChEMBLiCHEMBL4648.

PTM databases

PhosphoSiteiP36633.

Proteomic databases

PaxDbiP36633.
PRIDEiP36633.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:61296. rat.

Organism-specific databases

RGDi61296. Aoc1.

Phylogenomic databases

eggNOGiKOG1186. Eukaryota.
COG3733. LUCA.
HOVERGENiHBG004164.
InParanoidiP36633.

Enzyme and pathway databases

BRENDAi1.4.3.22. 5301.

Miscellaneous databases

PROiP36633.

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...

Publicationsi

  1. "Molecular cloning and functional expression of different molecular forms of rat amiloride-binding proteins."
    Lingueglia E., Renard S., Voilley N., Waldmann R., Chassande O., Lazdunski M., Barbry P.
    Eur. J. Biochem. 216:679-687(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Colon and Lung.
  2. "Isolation of a rat amiloride-binding protein cDNA clone: tissue distribution and regulation of expression."
    Verity K., Fuller P.J.
    Am. J. Physiol. 266:C1505-C1512(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiAOC1_RAT
AccessioniPrimary (citable) accession number: P36633
Secondary accession number(s): Q63973
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: January 20, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Inhibited by amiloride in a competitive manner.By similarity

Keywords - Technical termi

Complete proteome, 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.