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Protein

Primary amine oxidase, liver isozyme

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

Functioni

Catalytic activityi

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2.By similarity

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei385 – 3851Proton acceptorBy similarity
Active sitei470 – 4701Schiff-base intermediate with substrate; via topaquinoneCombined sources
Metal bindingi519 – 5191Copper; via tele nitrogenCombined sources1 Publication
Metal bindingi521 – 5211Copper; via tele nitrogenCombined sources1 Publication
Metal bindingi528 – 5281Calcium 1Combined sources
Metal bindingi529 – 5291Calcium 1; via carbonyl oxygenCombined sources
Metal bindingi530 – 5301Calcium 1Combined sources
Metal bindingi571 – 5711Calcium 2Combined sources
Metal bindingi662 – 6621Calcium 2; via carbonyl oxygenCombined sources
Metal bindingi664 – 6641Calcium 2Combined sources
Metal bindingi666 – 6661Calcium 2Combined sources
Metal bindingi672 – 6721Calcium 1Combined sources
Metal bindingi673 – 6731Calcium 1; via amide nitrogen and carbonyl oxygenCombined sources
Metal bindingi683 – 6831Copper; via pros nitrogenCombined sources1 Publication

GO - Molecular functioni

GO - Biological processi

  • amine metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Calcium, Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Primary amine oxidase, liver isozyme (EC:1.4.3.21By similarity)
Alternative name(s):
Amine oxidase [copper-containing]
Copper amine oxidase
Serum amine oxidase
Short name:
SAO
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 19

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, liver isozymePRO_0000035669Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi136 – 1361N-linked (GlcNAc...)Combined sources1 Publication
Disulfide bondi197 ↔ 198By similarity
Glycosylationi231 – 2311N-linked (GlcNAc...)Combined sources1 Publication
Disulfide bondi403 ↔ 429By similarity
Modified residuei470 – 47012',4',5'-topaquinoneCombined sources
Glycosylationi617 – 6171N-linked (GlcNAc...)By similarity
Glycosylationi665 – 6651N-linked (GlcNAc...)Combined sources1 Publication
Disulfide bondi733 ↔ 740By similarity
Disulfide bondi747 – 747InterchainBy similarity

Post-translational modificationi

Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, TPQ

Proteomic databases

PaxDbiQ29437.
PRIDEiQ29437.

Expressioni

Tissue specificityi

Liver.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.1 Publication

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000001383.

Structurei

Secondary structure

1
762
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi64 – 7815Combined sources
Turni85 – 873Combined sources
Beta strandi92 – 10110Combined sources
Helixi105 – 11410Combined sources
Beta strandi122 – 1298Combined sources
Beta strandi131 – 1344Combined sources
Beta strandi136 – 14712Combined sources
Beta strandi150 – 1534Combined sources
Helixi155 – 1595Combined sources
Helixi165 – 1673Combined sources
Helixi172 – 18413Combined sources
Helixi187 – 1904Combined sources
Helixi191 – 1988Combined sources
Turni200 – 2034Combined sources
Beta strandi207 – 2104Combined sources
Beta strandi216 – 2183Combined sources
Beta strandi223 – 2308Combined sources
Beta strandi233 – 2353Combined sources
Helixi237 – 2393Combined sources
Beta strandi240 – 24910Combined sources
Beta strandi252 – 2543Combined sources
Helixi255 – 2573Combined sources
Beta strandi259 – 2657Combined sources
Beta strandi268 – 2725Combined sources
Helixi273 – 2819Combined sources
Beta strandi322 – 3254Combined sources
Beta strandi328 – 34114Combined sources
Turni342 – 3443Combined sources
Beta strandi345 – 3539Combined sources
Beta strandi356 – 37116Combined sources
Helixi376 – 3805Combined sources
Beta strandi382 – 3843Combined sources
Helixi385 – 3873Combined sources
Turni390 – 3934Combined sources
Turni399 – 4013Combined sources
Beta strandi407 – 42014Combined sources
Beta strandi422 – 44120Combined sources
Beta strandi453 – 46715Combined sources
Beta strandi470 – 4789Combined sources
Beta strandi484 – 4929Combined sources
Helixi503 – 5064Combined sources
Beta strandi507 – 5115Combined sources
Beta strandi514 – 5174Combined sources
Beta strandi519 – 52911Combined sources
Beta strandi533 – 55018Combined sources
Beta strandi553 – 56715Combined sources
Helixi571 – 5744Combined sources
Beta strandi575 – 5773Combined sources
Beta strandi584 – 59310Combined sources
Beta strandi599 – 6079Combined sources
Helixi621 – 6288Combined sources
Beta strandi629 – 6357Combined sources
Turni646 – 6505Combined sources
Helixi659 – 6624Combined sources
Beta strandi669 – 68315Combined sources
Helixi687 – 6893Combined sources
Beta strandi700 – 71314Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TU5X-ray2.37A/B17-762[»]
2PNCX-ray2.40A/B17-762[»]
ProteinModelPortaliQ29437.
SMRiQ29437. Positions 57-759.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ29437.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni383 – 39311Substrate bindingCombined sourcesAdd
BLAST
Regioni467 – 4726Substrate bindingCombined sources

Sequence similaritiesi

Belongs to the copper/topaquinone oxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1186. Eukaryota.
COG3733. LUCA.
GeneTreeiENSGT00510000046461.
HOGENOMiHOG000233919.
HOVERGENiHBG004164.
InParanoidiQ29437.
KOiK00276.
OMAiANNDEYG.
OrthoDBiEOG78WKR2.
TreeFamiTF314750.

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.

Q29437-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFIFIFLSLW TLLVMGREEG GVGSEEGVGK QCHPSLPPRC PSRSPSDQPW
60 70 80 90 100
THPDQSQLFA DLSREELTTV MSFLTQQLGP DLVDAAQARP SDNCVFSVEL
110 120 130 140 150
QLPPKAAALA HLDRGSPPPA REALAIVFFG GQPQPNVTEL VVGPLPQPSY
160 170 180 190 200
MRDVTVERHG GPLPYYRRPV LLREYLDIDQ MIFNRELPQA AGVLHHCCSY
210 220 230 240 250
KQGGQKLLTM NSAPRGVQSG DRSTWFGIYY NITKGGPYLH PVGLELLVDH
260 270 280 290 300
KALDPADWTV QKVFFQGRYY ENLAQLEEQF EAGQVNVVVI PDDGTGGFWS
310 320 330 340 350
LKSQVPPGPT PPLQFHPQGP RFSVQGNRVA SSLWTFSFGL GAFSGPRVFD
360 370 380 390 400
VRFQGERLAY EISLQEAGAV YGGNTPAAML TRYMDSGFGM GYFATPLIRG
410 420 430 440 450
VDCPYLATYM DWHFVVESQT PKTLHDAFCV FEQNKGLPLR RHHSDFLSHY
460 470 480 490 500
FGGVAQTVLV FRSVSTMLNY DYVWDMVFYP NGAIEVKLHA TGYISSAFLF
510 520 530 540 550
GAARRYGNQV GEHTLGPVHT HSAHYKVDLD VGGLENWVWA EDMAFVPTAI
560 570 580 590 600
PWSPEHQIQR LQVTRKQLET EEQAAFPLGG ASPRYLYLAS KQSNKWGHPR
610 620 630 640 650
GYRIQTVSFA GGPMPQNSPM ERAFSWGRYQ LAITQRKETE PSSSSVFNQN
660 670 680 690 700
DPWTPTVDFS DFINNETIAG KDLVAWVTAG FLHIPHAEDI PNTVTVGNGV
710 720 730 740 750
GFFLRPYNFF DQEPSMDSAD SIYFREGQDA GSCEINPLAC LPQAATCAPD
760
LPVFSHGGYP EY
Length:762
Mass (Da):84,757
Last modified:November 1, 1996 - v1
Checksum:iAA959771360295FE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S69583 mRNA. Translation: AAB30397.1.
L27218 mRNA. Translation: AAA30525.1.
PIRiA54411.
RefSeqiNP_001124236.1. NM_001130764.1.
UniGeneiBt.52514.

Genome annotation databases

EnsembliENSBTAT00000001383; ENSBTAP00000001383; ENSBTAG00000001041.
GeneIDi789307.
KEGGibta:789307.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S69583 mRNA. Translation: AAB30397.1.
L27218 mRNA. Translation: AAA30525.1.
PIRiA54411.
RefSeqiNP_001124236.1. NM_001130764.1.
UniGeneiBt.52514.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TU5X-ray2.37A/B17-762[»]
2PNCX-ray2.40A/B17-762[»]
ProteinModelPortaliQ29437.
SMRiQ29437. Positions 57-759.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000001383.

Proteomic databases

PaxDbiQ29437.
PRIDEiQ29437.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000001383; ENSBTAP00000001383; ENSBTAG00000001041.
GeneIDi789307.
KEGGibta:789307.

Organism-specific databases

CTDi789307.

Phylogenomic databases

eggNOGiKOG1186. Eukaryota.
COG3733. LUCA.
GeneTreeiENSGT00510000046461.
HOGENOMiHOG000233919.
HOVERGENiHBG004164.
InParanoidiQ29437.
KOiK00276.
OMAiANNDEYG.
OrthoDBiEOG78WKR2.
TreeFamiTF314750.

Miscellaneous databases

EvolutionaryTraceiQ29437.

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. "Primary structures for a mammalian cellular and serum copper amine oxidase."
    Mu D., Medzihradszky K.F., Adams G.W., Mayer P., Hines W.M., Burlingame A.L., Smith A.J., Cai D., Klinman J.P.
    J. Biol. Chem. 269:9926-9932(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.
  2. "Identification of topaquinone and its consensus sequence in copper amine oxidases."
    Janes S.M., Palcic M.M., Scaman C.H., Smith A.J., Brown D.E., Dooley D.M., Mure M., Klinman J.P.
    Biochemistry 31:12147-12154(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
  3. Cited for: X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF 17-762 IN COMPLEX WITH CALCIUM; COPPER AND SUBSTRATE, TOPAQUINONE AT TYR-470, GLYCOSYLATION AT ASN-136; ASN-231 AND ASN-665, SUBUNIT.

Entry informationi

Entry nameiAOCX_BOVIN
AccessioniPrimary (citable) accession number: Q29437
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 8, 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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.