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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)DescriptionActionsGraphical viewLength
Active sitei385Proton acceptorBy similarity1
Active sitei470Schiff-base intermediate with substrate; via topaquinoneCombined sources1
Metal bindingi519Copper; via tele nitrogenCombined sources1 Publication1
Metal bindingi521Copper; via tele nitrogenCombined sources1 Publication1
Metal bindingi528Calcium 1Combined sources1
Metal bindingi529Calcium 1; via carbonyl oxygenCombined sources1
Metal bindingi530Calcium 1Combined sources1
Metal bindingi571Calcium 2Combined sources1
Metal bindingi662Calcium 2; via carbonyl oxygenCombined sources1
Metal bindingi664Calcium 2Combined sources1
Metal bindingi666Calcium 2Combined sources1
Metal bindingi672Calcium 1Combined sources1
Metal bindingi673Calcium 1; via amide nitrogen and carbonyl oxygenCombined sources1
Metal bindingi683Copper; via pros nitrogenCombined sources1 Publication1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 16Sequence analysisAdd BLAST16
ChainiPRO_000003566917 – 762Primary amine oxidase, liver isozymeAdd BLAST746

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi136N-linked (GlcNAc...)Combined sources1 Publication1
Disulfide bondi197 ↔ 198By similarity
Glycosylationi231N-linked (GlcNAc...)Combined sources1 Publication1
Disulfide bondi403 ↔ 429By similarity
Modified residuei4702',4',5'-topaquinoneCombined sources1
Glycosylationi665N-linked (GlcNAc...)Combined sources1 Publication1
Disulfide bondi733 ↔ 740By similarity
Disulfide bondi747InterchainBy 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.
PeptideAtlasiQ29437.
PRIDEiQ29437.

Expressioni

Tissue specificityi

Liver.

Gene expression databases

BgeeiENSBTAG00000001041.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.1 Publication

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000001383.

Structurei

Secondary structure

1762
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi64 – 78Combined sources15
Turni85 – 87Combined sources3
Beta strandi92 – 101Combined sources10
Helixi105 – 114Combined sources10
Beta strandi122 – 129Combined sources8
Beta strandi131 – 134Combined sources4
Beta strandi136 – 147Combined sources12
Beta strandi150 – 153Combined sources4
Helixi155 – 159Combined sources5
Helixi165 – 167Combined sources3
Helixi172 – 184Combined sources13
Helixi187 – 190Combined sources4
Helixi191 – 198Combined sources8
Turni200 – 203Combined sources4
Beta strandi207 – 210Combined sources4
Beta strandi216 – 218Combined sources3
Beta strandi223 – 230Combined sources8
Beta strandi233 – 235Combined sources3
Helixi237 – 239Combined sources3
Beta strandi240 – 249Combined sources10
Beta strandi252 – 254Combined sources3
Helixi255 – 257Combined sources3
Beta strandi259 – 265Combined sources7
Beta strandi268 – 272Combined sources5
Helixi273 – 281Combined sources9
Beta strandi322 – 325Combined sources4
Beta strandi328 – 341Combined sources14
Turni342 – 344Combined sources3
Beta strandi345 – 353Combined sources9
Beta strandi356 – 371Combined sources16
Helixi376 – 380Combined sources5
Beta strandi382 – 384Combined sources3
Helixi385 – 387Combined sources3
Turni390 – 393Combined sources4
Turni399 – 401Combined sources3
Beta strandi407 – 420Combined sources14
Beta strandi422 – 441Combined sources20
Beta strandi453 – 467Combined sources15
Beta strandi470 – 478Combined sources9
Beta strandi484 – 492Combined sources9
Helixi503 – 506Combined sources4
Beta strandi507 – 511Combined sources5
Beta strandi514 – 517Combined sources4
Beta strandi519 – 529Combined sources11
Beta strandi533 – 550Combined sources18
Beta strandi553 – 567Combined sources15
Helixi571 – 574Combined sources4
Beta strandi575 – 577Combined sources3
Beta strandi584 – 593Combined sources10
Beta strandi599 – 607Combined sources9
Helixi621 – 628Combined sources8
Beta strandi629 – 635Combined sources7
Turni646 – 650Combined sources5
Helixi659 – 662Combined sources4
Beta strandi669 – 683Combined sources15
Helixi687 – 689Combined sources3
Beta strandi700 – 713Combined sources14

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ29437.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni383 – 393Substrate bindingCombined sourcesAdd BLAST11
Regioni467 – 472Substrate bindingCombined sources6

Sequence similaritiesi

Belongs to the copper/topaquinone oxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1186. Eukaryota.
COG3733. LUCA.
GeneTreeiENSGT00510000046461.
HOGENOMiHOG000233919.
HOVERGENiHBG004164.
InParanoidiQ29437.
KOiK00276.
OMAiPYLHPVG.
OrthoDBiEOG091G02WY.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TU5X-ray2.37A/B17-762[»]
2PNCX-ray2.40A/B17-762[»]
ProteinModelPortaliQ29437.
SMRiQ29437.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000001383.

Proteomic databases

PaxDbiQ29437.
PeptideAtlasiQ29437.
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.
OMAiPYLHPVG.
OrthoDBiEOG091G02WY.
TreeFamiTF314750.

Miscellaneous databases

EvolutionaryTraceiQ29437.

Gene expression databases

BgeeiENSBTAG00000001041.

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 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: November 30, 2016
This is version 129 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.