AOCX_BOVIN
ID AOCX_BOVIN Reviewed; 762 AA.
AC Q29437;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Primary amine oxidase, liver isozyme;
DE EC=1.4.3.21 {ECO:0000250|UniProtKB:P19801};
DE AltName: Full=Amine oxidase [copper-containing];
DE AltName: Full=Copper amine oxidase;
DE AltName: Full=Serum amine oxidase;
DE Short=SAO;
DE Flags: Precursor;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=8144587; DOI=10.1016/s0021-9258(17)36971-5;
RA Mu D., Medzihradszky K.F., Adams G.W., Mayer P., Hines W.M.,
RA Burlingame A.L., Smith A.J., Cai D., Klinman J.P.;
RT "Primary structures for a mammalian cellular and serum copper amine
RT oxidase.";
RL J. Biol. Chem. 269:9926-9932(1994).
RN [2]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=1457410; DOI=10.1021/bi00163a025;
RA Janes S.M., Palcic M.M., Scaman C.H., Smith A.J., Brown D.E., Dooley D.M.,
RA Mure M., Klinman J.P.;
RT "Identification of topaquinone and its consensus sequence in copper amine
RT oxidases.";
RL Biochemistry 31:12147-12154(1992).
RN [3] {ECO:0007744|PDB:1TU5}
RP X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF 17-762 IN COMPLEX WITH CALCIUM;
RP COPPER AND SUBSTRATE, TOPAQUINONE AT TYR-470, GLYCOSYLATION AT ASN-136;
RP ASN-231 AND ASN-665, AND SUBUNIT.
RX PubMed=15701511; DOI=10.1016/j.jmb.2004.12.038;
RA Lunelli M., Di Paolo M.L., Biadene M., Calderone V., Battistutta R.,
RA Scarpa M., Rigo A., Zanotti G.;
RT "Crystal structure of amine oxidase from bovine serum.";
RL J. Mol. Biol. 346:991-1004(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58001; EC=1.4.3.21;
CC Evidence={ECO:0000250|UniProtKB:P19801};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:15701511};
CC Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:15701511};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:15701511};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000269|PubMed:15701511};
CC -!- COFACTOR:
CC Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC Evidence={ECO:0000269|PubMed:15701511};
CC Note=Contains 1 topaquinone per subunit. {ECO:0000269|PubMed:15701511};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:15701511}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Liver.
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000269|PubMed:15701511}.
CC -!- MISCELLANEOUS: Inhibited by amiloride in a competitive manner.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000305}.
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DR EMBL; S69583; AAB30397.1; -; mRNA.
DR EMBL; L27218; AAA30525.1; -; mRNA.
DR PIR; A54411; A54411.
DR RefSeq; NP_001124236.1; NM_001130764.1.
DR PDB; 1TU5; X-ray; 2.37 A; A/B=17-762.
DR PDB; 2PNC; X-ray; 2.40 A; A/B=17-762.
DR PDBsum; 1TU5; -.
DR PDBsum; 2PNC; -.
DR AlphaFoldDB; Q29437; -.
DR SMR; Q29437; -.
DR iPTMnet; Q29437; -.
DR PaxDb; Q29437; -.
DR PeptideAtlas; Q29437; -.
DR PRIDE; Q29437; -.
DR Ensembl; ENSBTAT00000081083; ENSBTAP00000058891; ENSBTAG00000039321.
DR GeneID; 789307; -.
DR KEGG; bta:789307; -.
DR CTD; 789307; -.
DR VEuPathDB; HostDB:ENSBTAG00000039321; -.
DR eggNOG; KOG1186; Eukaryota.
DR GeneTree; ENSGT00950000183207; -.
DR HOGENOM; CLU_015739_1_0_1; -.
DR InParanoid; Q29437; -.
DR OMA; PQPYSEF; -.
DR OrthoDB; 1320015at2759; -.
DR TreeFam; TF314750; -.
DR Reactome; R-BTA-211945; Phase I - Functionalization of compounds.
DR EvolutionaryTrace; Q29437; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000039321; Expressed in liver and 33 other tissues.
DR ExpressionAtlas; Q29437; baseline.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0052594; F:aminoacetone:oxygen oxidoreductase(deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0008131; F:primary amine oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0009308; P:amine metabolic process; IBA:GO_Central.
DR GO; GO:1902283; P:negative regulation of primary amine oxidase activity; IBA:GO_Central.
DR GO; GO:0046677; P:response to antibiotic; IBA:GO_Central.
DR Gene3D; 2.70.98.20; -; 1.
DR InterPro; IPR000269; Cu_amine_oxidase.
DR InterPro; IPR015798; Cu_amine_oxidase_C.
DR InterPro; IPR036460; Cu_amine_oxidase_C_sf.
DR InterPro; IPR016182; Cu_amine_oxidase_N-reg.
DR InterPro; IPR015800; Cu_amine_oxidase_N2.
DR InterPro; IPR015802; Cu_amine_oxidase_N3.
DR PANTHER; PTHR10638; PTHR10638; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR Pfam; PF02727; Cu_amine_oxidN2; 1.
DR Pfam; PF02728; Cu_amine_oxidN3; 1.
DR PRINTS; PR00766; CUDAOXIDASE.
DR SUPFAM; SSF49998; SSF49998; 1.
DR SUPFAM; SSF54416; SSF54416; 2.
DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
DR PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Copper; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Metal-binding; Oxidoreductase; Reference proteome; Secreted;
KW Signal; TPQ.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..762
FT /note="Primary amine oxidase, liver isozyme"
FT /id="PRO_0000035669"
FT REGION 23..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 385
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT ACT_SITE 470
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0007744|PDB:2PNC"
FT BINDING 383..393
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:2PNC"
FT BINDING 467..472
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:2PNC"
FT BINDING 519
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:15701511,
FT ECO:0007744|PDB:1TU5, ECO:0007744|PDB:2PNC"
FT BINDING 521
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:15701511,
FT ECO:0007744|PDB:1TU5, ECO:0007744|PDB:2PNC"
FT BINDING 528
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:1TU5, ECO:0007744|PDB:2PNC"
FT BINDING 529
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:1TU5, ECO:0007744|PDB:2PNC"
FT BINDING 530
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:1TU5, ECO:0007744|PDB:2PNC"
FT BINDING 571
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:1TU5, ECO:0007744|PDB:2PNC"
FT BINDING 662
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:1TU5, ECO:0007744|PDB:2PNC"
FT BINDING 664
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:1TU5, ECO:0007744|PDB:2PNC"
FT BINDING 666
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:1TU5, ECO:0007744|PDB:2PNC"
FT BINDING 672
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:1TU5, ECO:0007744|PDB:2PNC"
FT BINDING 673
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:1TU5, ECO:0007744|PDB:2PNC"
FT BINDING 683
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:15701511,
FT ECO:0007744|PDB:1TU5, ECO:0007744|PDB:2PNC"
FT MOD_RES 470
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0007744|PDB:1TU5"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15701511,
FT ECO:0007744|PDB:1TU5, ECO:0007744|PDB:2PNC"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15701511,
FT ECO:0007744|PDB:1TU5"
FT CARBOHYD 665
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15701511,
FT ECO:0007744|PDB:1TU5"
FT DISULFID 197..198
FT /evidence="ECO:0000250|UniProtKB:Q16853"
FT DISULFID 403..429
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT DISULFID 733..740
FT /evidence="ECO:0000250|UniProtKB:Q16853"
FT DISULFID 747
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT HELIX 64..78
FT /evidence="ECO:0007829|PDB:1TU5"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 92..101
FT /evidence="ECO:0007829|PDB:1TU5"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 122..129
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 136..147
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:1TU5"
FT HELIX 155..159
FT /evidence="ECO:0007829|PDB:1TU5"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:1TU5"
FT HELIX 172..184
FT /evidence="ECO:0007829|PDB:1TU5"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:1TU5"
FT HELIX 191..198
FT /evidence="ECO:0007829|PDB:1TU5"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:1TU5"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 240..249
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:1TU5"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:1TU5"
FT HELIX 273..281
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 328..341
FT /evidence="ECO:0007829|PDB:1TU5"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 345..353
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 356..371
FT /evidence="ECO:0007829|PDB:1TU5"
FT HELIX 376..380
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:1TU5"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:1TU5"
FT TURN 390..393
FT /evidence="ECO:0007829|PDB:1TU5"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 407..420
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 422..441
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 453..467
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 470..478
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 484..492
FT /evidence="ECO:0007829|PDB:1TU5"
FT HELIX 503..506
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 507..511
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 514..517
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 519..529
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 533..550
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 553..567
FT /evidence="ECO:0007829|PDB:1TU5"
FT HELIX 571..574
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 575..577
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 584..593
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 599..607
FT /evidence="ECO:0007829|PDB:1TU5"
FT HELIX 621..628
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 629..635
FT /evidence="ECO:0007829|PDB:1TU5"
FT TURN 646..650
FT /evidence="ECO:0007829|PDB:1TU5"
FT HELIX 659..662
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 669..683
FT /evidence="ECO:0007829|PDB:1TU5"
FT HELIX 687..689
FT /evidence="ECO:0007829|PDB:1TU5"
FT STRAND 700..713
FT /evidence="ECO:0007829|PDB:1TU5"
SQ SEQUENCE 762 AA; 84757 MW; AA959771360295FE CRC64;
MFIFIFLSLW TLLVMGREEG GVGSEEGVGK QCHPSLPPRC PSRSPSDQPW THPDQSQLFA
DLSREELTTV MSFLTQQLGP DLVDAAQARP SDNCVFSVEL QLPPKAAALA HLDRGSPPPA
REALAIVFFG GQPQPNVTEL VVGPLPQPSY MRDVTVERHG GPLPYYRRPV LLREYLDIDQ
MIFNRELPQA AGVLHHCCSY KQGGQKLLTM NSAPRGVQSG DRSTWFGIYY NITKGGPYLH
PVGLELLVDH KALDPADWTV QKVFFQGRYY ENLAQLEEQF EAGQVNVVVI PDDGTGGFWS
LKSQVPPGPT PPLQFHPQGP RFSVQGNRVA SSLWTFSFGL GAFSGPRVFD VRFQGERLAY
EISLQEAGAV YGGNTPAAML TRYMDSGFGM GYFATPLIRG VDCPYLATYM DWHFVVESQT
PKTLHDAFCV FEQNKGLPLR RHHSDFLSHY FGGVAQTVLV FRSVSTMLNY DYVWDMVFYP
NGAIEVKLHA TGYISSAFLF GAARRYGNQV GEHTLGPVHT HSAHYKVDLD VGGLENWVWA
EDMAFVPTAI PWSPEHQIQR LQVTRKQLET EEQAAFPLGG ASPRYLYLAS KQSNKWGHPR
GYRIQTVSFA GGPMPQNSPM ERAFSWGRYQ LAITQRKETE PSSSSVFNQN DPWTPTVDFS
DFINNETIAG KDLVAWVTAG FLHIPHAEDI PNTVTVGNGV GFFLRPYNFF DQEPSMDSAD
SIYFREGQDA GSCEINPLAC LPQAATCAPD LPVFSHGGYP EY
