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

Primary amine oxidase, lung isozyme

Gene
N/A
Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei385 – 3851Proton acceptorBy similarity
Active sitei470 – 4701Schiff-base intermediate with substrate; via topaquinoneBy similarity
Metal bindingi519 – 5191Copper; via tele nitrogenBy similarity
Metal bindingi521 – 5211Copper; via tele nitrogenBy similarity
Metal bindingi528 – 5281Calcium 1By similarity
Metal bindingi529 – 5291Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi530 – 5301Calcium 1By similarity
Metal bindingi571 – 5711Calcium 2By similarity
Metal bindingi662 – 6621Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi664 – 6641Calcium 2By similarity
Metal bindingi666 – 6661Calcium 2By similarity
Metal bindingi672 – 6721Calcium 1By similarity
Metal bindingi673 – 6731Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi683 – 6831Copper; via pros nitrogenBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Calcium, Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Primary amine oxidase, lung isozyme (EC:1.4.3.21By similarity)
Alternative name(s):
Amine oxidase [copper-containing]
BOLAO
Copper amine oxidase
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence analysisAdd
BLAST
Chaini17 – 762746Primary amine oxidase, lung isozymePRO_0000035670Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi136 – 1361N-linked (GlcNAc...)By similarity
Disulfide bondi197 ↔ 198By similarity
Glycosylationi211 – 2111O-linked (GalNAc...)By similarity
Glycosylationi231 – 2311N-linked (GlcNAc...)By similarity
Glycosylationi293 – 2931N-linked (GlcNAc...)By similarity
Disulfide bondi403 ↔ 429By similarity
Modified residuei470 – 47012',4',5'-topaquinoneBy similarity
Glycosylationi617 – 6171N-linked (GlcNAc...)By similarity
Glycosylationi665 – 6651N-linked (GlcNAc...)By similarity
Disulfide bondi733 ↔ 740By similarity
Disulfide bondi747 – 747InterchainBy 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

PRIDEiO46406.

Expressioni

Tissue specificityi

Expressed in lung, spleen, heart and kidney.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.By similarity

Structurei

3D structure databases

ProteinModelPortaliO46406.
SMRiO46406. Positions 57-717.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni383 – 39311Substrate bindingBy similarityAdd
BLAST
Regioni467 – 4726Substrate bindingBy similarity
Regioni577 – 5848Heparin-bindingBy similarity

Sequence similaritiesi

Belongs to the copper/topaquinone oxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG004164.

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.

O46406-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFIFIFLSLW TLLVMGREEG GVGSEEGVGK QCHPSLPPRC PSRSPSDQPW
60 70 80 90 100
THPDQSQLFA DLSREELTAV MSFLTQKLGP DLVDAAQARP SDNCIFSVEL
110 120 130 140 150
QLPPKAAALA HLDRRSPPPA REALAIVFFG GQPQPNVTEL VVGPLPQPSY
160 170 180 190 200
MRDVTVERHG GPLPYYRHTV LLREYLDIDQ MIFNRELPQA AGVLHHCCSY
210 220 230 240 250
KQGGGNLVTM TTAPPGLQSG DRATWFGLYY NISKAGYYLH PVGLELLVDH
260 270 280 290 300
KALDPAQWTI QKVFFQGRYY ESLVQLEEQF EAGRVNVVVI PNNGTGGSWS
310 320 330 340 350
LKSQVPPGPT PPLQFHPQGT RFSVQGSRVT SSLWTFSFGL GAFSGPRIFD
360 370 380 390 400
IRFQGERLAY EISLQEAVAI YGGNTPAAML TRYMDACFGM GKFATPLTRG
410 420 430 440 450
VDCPYLATYV DWHFLLESQA PKTLHDAFCV FEQNKGLPLR RHHSDFISQY
460 470 480 490 500
FGGVVETVLV FRSVSTLLNY DYVWDMVFHP NGAIEVKFHV TGYISSAFFF
510 520 530 540 550
GTAQKYGNQV RENTLGTVHT HSAHYKVDLD VGGLENWVWA EDMAFVPTTV
560 570 580 590 600
PWSPEHQIQR LQVIRKQLET EEQAAFPLGG GSPRYLYLAS KQSNKWGHPR
610 620 630 640 650
GYRIQTVSFA GRPLPQNSST ERAISWGRYQ LAVTQRKETE PSSSSVFNQN
660 670 680 690 700
DPWTPTVDFA DFINNETIAG KDLVAWVTAG FLHIPHAEDI PNTVTVGNGV
710 720 730 740 750
GFFLRPYNFF DQEPSMDSAD SIYFREGQDA GSCEINPLAC LPQAATCAPD
760
LPVFSHGGYP EY
Length:762
Mass (Da):84,883
Last modified:June 1, 1998 - v1
Checksum:iBB43D04776744AF2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y15774 mRNA. Translation: CAA75776.1.
UniGeneiBt.105258.
Bt.105260.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y15774 mRNA. Translation: CAA75776.1.
UniGeneiBt.105258.
Bt.105260.

3D structure databases

ProteinModelPortaliO46406.
SMRiO46406. Positions 57-717.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO46406.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG004164.

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. "Structure and tissue-specific expression of genes encoding bovine copper amine oxidases."
    Hogdall E.V.S., Houen G., Borre M., Bundgaard J.R., Larsson L.-I., Vuust J.
    Eur. J. Biochem. 251:320-328(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.

Entry informationi

Entry nameiAOCY_BOVIN
AccessioniPrimary (citable) accession number: O46406
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: January 20, 2016
This is version 100 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.