AOC3_PONAB
ID AOC3_PONAB Reviewed; 763 AA.
AC Q5R9I0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 87.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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. May play a role in
CC adipogenesis (By similarity). {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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR859408; CAH91580.1; -; mRNA.
DR RefSeq; NP_001125929.1; NM_001132457.1.
DR AlphaFoldDB; Q5R9I0; -.
DR SMR; Q5R9I0; -.
DR STRING; 9601.ENSPPYP00000009411; -.
DR GeneID; 100172863; -.
DR KEGG; pon:100172863; -.
DR CTD; 8639; -.
DR eggNOG; KOG1186; Eukaryota.
DR InParanoid; Q5R9I0; -.
DR OrthoDB; 1320015at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
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; IEA:InterPro.
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 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; PS01165; COPPER_AMINE_OXID_2; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Copper; Disulfide bond; Glycoprotein; Membrane;
KW Metal-binding; Oxidoreductase; Reference proteome; Signal-anchor; TPQ;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..763
FT /note="Membrane primary amine oxidase"
FT /id="PRO_0000064104"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..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 592
FT /note="N-linked (GlcNAc...) (complex) 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"
SQ SEQUENCE 763 AA; 84602 MW; AB73B9807646D707 CRC64;
MNQKTILVLL ILAVITIFAL VCVLLVGRGG DGGEPSQLPH CPSISPSAQP WTHPGQSQLF
ADLSREELTA VMRFLTQRLG PGLVDAAQAQ PSDNCIFSVE LQLPPKAAAL AHLDRGSPPP
AREALAIILF GRQPQPNVSE LVVGPLPHPS YMRDVTVEHH GGPLPYHRRP VLFQEYLDID
QMIFDRELPQ ASGLLHHCCF YKRRGRNLVT MTTAPRGLQS GDRATWFGLY YNISGAGFFL
HHVGLELLVN HKALDPAHWT IQKVFYQGRY YDSLAQLEAQ FEAGLVNVVL IPDNGTGGSW
SLKSPVPPGP APPLQFYPQG PRFSVQGSRV ASSLWTFSFG LGAFSGPRIF DVRFQGERLV
YEISLQEALA IYGGNSPAAM TTRYVDGGFG MGKYATPLTR GVDCPYLATY VDWHFLLESR
APKTIRDAFC VFEQNQGLPL RRHHSDLYSH YFGGLAETVQ VIRSMSTLLN YDYVWDMVFH
PSGAIEIRFY ATGYISSAFL FGATGKYGNQ VSEHTLGTVH THSAHFKVDL DIAGLENWVW
AEDMVFVPMA VPWSPEHQLQ RLQVTRKLLE TEEQAAFLMG SATPRYLYLA SNHSNKWGHP
RGYRIQMLSF AGKPLPQNSS MAKGFSWERY QLAVTQRKEE EPSSSSVFNQ NDPWAATVDF
SDFINNETIA GKDLVAWVTA GFLHIPHAED IPNTVTVGNG VGFFLRPYNF FDEDPSFYSA
DSIYFRGDQD AGACEVNPLA CLPQAAACAP DLPAFSHGGF SHN
