AOC3_BOVIN
ID AOC3_BOVIN Reviewed; 763 AA.
AC Q9TTK6; A5D7R7; Q58D95;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Membrane primary amine oxidase;
DE EC=1.4.3.21 {ECO:0000250|UniProtKB:P19801};
DE AltName: Full=Copper amine oxidase;
DE AltName: Full=Semicarbazide-sensitive amine oxidase;
DE Short=SSAO;
DE AltName: Full=Vascular adhesion protein 1;
DE Short=VAP-1;
GN Name=AOC3;
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] (ISOFORM 1).
RA Iwabuki H., Matsumura K., Mure M., Kuroda S., Tanizawa K.;
RT "Molecular cloning of semicarbazide-sensitive amine oxidase gene from
RT Bovine aorta.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell adhesion protein that participates in lymphocyte
CC recirculation by mediating the binding of lymphocytes to peripheral
CC lymph node vascular endothelial cells in an L-selectin-independent
CC fashion. Has a monoamine oxidase activity (By similarity).
CC {ECO:0000250}.
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:0000250|UniProtKB:P19801};
CC Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:P19801};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P19801};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:P19801};
CC -!- COFACTOR:
CC Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC Evidence={ECO:0000250|UniProtKB:P19801};
CC Note=Contains 1 topaquinone per subunit.
CC {ECO:0000250|UniProtKB:P19801};
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Forms a
CC heterodimer with AOC2 (By similarity). {ECO:0000250|UniProtKB:P19801,
CC ECO:0000250|UniProtKB:Q16853}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9TTK6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9TTK6-2; Sequence=VSP_016603;
CC -!- PTM: N- and O-glycosylated. {ECO:0000250}.
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000250|UniProtKB:P12807}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000305}.
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DR EMBL; AB019242; BAA88896.1; -; mRNA.
DR EMBL; BT021702; AAX46549.1; -; mRNA.
DR EMBL; BC140657; AAI40658.1; -; mRNA.
DR RefSeq; NP_851345.1; NM_181002.3. [Q9TTK6-1]
DR AlphaFoldDB; Q9TTK6; -.
DR SMR; Q9TTK6; -.
DR STRING; 9913.ENSBTAP00000047520; -.
DR BindingDB; Q9TTK6; -.
DR ChEMBL; CHEMBL3265; -.
DR PaxDb; Q9TTK6; -.
DR PeptideAtlas; Q9TTK6; -.
DR PRIDE; Q9TTK6; -.
DR Ensembl; ENSBTAT00000042831; ENSBTAP00000040442; ENSBTAG00000030333. [Q9TTK6-1]
DR GeneID; 281002; -.
DR KEGG; bta:281002; -.
DR CTD; 8639; -.
DR VEuPathDB; HostDB:ENSBTAG00000030333; -.
DR eggNOG; KOG1186; Eukaryota.
DR GeneTree; ENSGT00950000183207; -.
DR InParanoid; Q9TTK6; -.
DR OMA; CMFEIDK; -.
DR OrthoDB; 1320015at2759; -.
DR Reactome; R-BTA-211945; Phase I - Functionalization of compounds.
DR SABIO-RK; Q9TTK6; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000030333; Expressed in mammary gland fat and 101 other tissues.
DR ExpressionAtlas; Q9TTK6; baseline and differential.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0048038; F:quinone binding; ISS:UniProtKB.
DR GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0009308; P:amine metabolic process; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Cell adhesion; Copper; Disulfide bond;
KW Glycoprotein; Membrane; Metal-binding; Oxidoreductase; Reference proteome;
KW Signal-anchor; TPQ; Transmembrane; Transmembrane helix.
FT CHAIN 1..763
FT /note="Membrane primary amine oxidase"
FT /id="PRO_0000064101"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..763
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 386
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT ACT_SITE 471
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 384..394
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 468..473
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 520
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 522
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 529
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 530
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 531
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 572
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 578..585
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT BINDING 663
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 665
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 667
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 673
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 674
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 684
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT MOD_RES 471
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT CARBOHYD 212
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q16853"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q16853"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q16853"
FT CARBOHYD 618
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q16853"
FT CARBOHYD 666
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q16853"
FT DISULFID 198..199
FT /evidence="ECO:0000250|UniProtKB:Q16853"
FT DISULFID 404..430
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT DISULFID 734..741
FT /evidence="ECO:0000250|UniProtKB:Q16853"
FT DISULFID 748
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT VAR_SEQ 734..763
FT /note="CEVNSLACLPKDPACAPDLPAFSHGGFFTN -> SMLPESGASQLCAPQLAG
FT FLSQRRGTVSQEAGVMVTRFYKTPRCIFRRHG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_016603"
FT CONFLICT 178
FT /note="D -> H (in Ref. 2; AAX46549)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 763 AA; 84500 MW; DB61ED9A89E71E90 CRC64;
MNQKTTLVLL ALAVITIFAL VCVLIAGRGG DGGEASQPHY CPSGTPSVQP WTHPGQNQLF
ADLSREELTA VMSFLTQKLG PDLVDAAQAR PSDNCIFSVE LQLPPKAAAL AHLDRRSPPP
AREALAIVFF GGQPQPNVTE LVVGPLPQPS YMRDVTVERH GGPLPYYRRP VLLREYLDID
QMIFNRELPQ AAGVLHHCCS YKQGGGNLVT MTTAPRGLQS GDRATWFGLY YNISGAGYYL
HPVGLELLVD HKALDPAQWT IQKVFFQGRY YESLAQLEEQ FEAGRVNVVV IPNNGTGGSW
SLKSQVPPGP TPPLQFHPQG TRFSVQGSRV TSSLWTFSFG LGAFSGPRIF DIRFQGERLA
YEISLQEAVA IYGGNTPAAM LTRYMDGCFG MGKFATPLTR GVDCPYLATY VDWHFLLESQ
APRTLHDAFC VFEQNKGLPL RRHHSDFISQ YFGGVVETVL VFRSVSTLLN YDYVWDMVFH
PNGAIEVKFH ATGYISSAFF FGTAQKYGNQ VRENTLGTVH THSAHYKVDL DVGGLENWVW
AEDMAFVPTT VPWSPEHQIQ RLQVTRKQLE TEEQAAFPLG GASPRYLYLA SKQSNKWGHP
RGYRIQTVSF AGRPLPQNSS TERAISWGRY QLAVTQRKET EPSSSSVFNQ NDPWTPTVDF
ADFINNETIA GKDLVAWVTA GFLHIPHAED IPNTVTVGNG VGFFLRPYNF FDEDPSINSA
DSIYFQKHQD AGSCEVNSLA CLPKDPACAP DLPAFSHGGF FTN
