AOC3_RAT
ID AOC3_RAT Reviewed; 763 AA.
AC O08590; Q497D2; Q5R1T5;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 159.
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=VP97;
DE AltName: Full=Vascular adhesion protein 1;
DE Short=VAP-1;
GN Name=Aoc3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Aorta;
RX PubMed=15744061; DOI=10.1248/bpb.28.413;
RA Ochiai Y., Itoh K., Sakurai E., Tanaka Y.;
RT "Molecular cloning and characterization of rat semicarbazide-sensitive
RT amine oxidase.";
RL Biol. Pharm. Bull. 28:413-418(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-322, PARTIAL PROTEIN SEQUENCE, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley; TISSUE=Adipocyte;
RX PubMed=9083076; DOI=10.1074/jbc.272.14.9388;
RA Morris N.J., Ducret A., Aebersold R., Ross S.A., Keller S.R.,
RA Lienhard G.E.;
RT "Membrane amine oxidase cloning and identification as a major protein in
RT the adipocyte plasma membrane.";
RL J. Biol. Chem. 272:9388-9392(1997).
RN [4]
RP PROTEIN SEQUENCE OF 2-20, AND SUBCELLULAR LOCATION.
RC TISSUE=Adipocyte;
RX PubMed=8520629; DOI=10.3109/09687689509072428;
RA Jochen A., Guven S., Hays J.;
RT "The major integral membrane glycoprotein in adipocytes is a novel 200-kDa
RT heterodimer.";
RL Mol. Membr. Biol. 12:277-281(1995).
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 ECO:0000269|PubMed:15744061}.
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:0000269|PubMed:8520629,
CC ECO:0000269|PubMed:9083076}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:8520629, ECO:0000269|PubMed:9083076}.
CC -!- TISSUE SPECIFICITY: Highly expressed in adipocytes, aorta and lung.
CC Expressed at lower levels in heart, kidney, large intestine, liver,
CC small intestine and stomach. {ECO:0000269|PubMed:15744061}.
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; AB195675; BAD74047.1; -; mRNA.
DR EMBL; BC100613; AAI00614.1; -; mRNA.
DR EMBL; U72632; AAC53189.1; -; mRNA.
DR RefSeq; NP_113770.2; NM_031582.2.
DR AlphaFoldDB; O08590; -.
DR SMR; O08590; -.
DR BioGRID; 248115; 1.
DR STRING; 10116.ENSRNOP00000068449; -.
DR BindingDB; O08590; -.
DR ChEMBL; CHEMBL4592; -.
DR DrugCentral; O08590; -.
DR GlyGen; O08590; 6 sites.
DR iPTMnet; O08590; -.
DR PhosphoSitePlus; O08590; -.
DR PaxDb; O08590; -.
DR PRIDE; O08590; -.
DR GeneID; 29473; -.
DR KEGG; rno:29473; -.
DR UCSC; RGD:62058; rat.
DR CTD; 8639; -.
DR RGD; 62058; Aoc3.
DR VEuPathDB; HostDB:ENSRNOG00000053448; -.
DR eggNOG; KOG1186; Eukaryota.
DR HOGENOM; CLU_015739_1_0_1; -.
DR InParanoid; O08590; -.
DR OrthoDB; 1320015at2759; -.
DR BRENDA; 1.4.3.21; 5301.
DR Reactome; R-RNO-211945; Phase I - Functionalization of compounds.
DR PRO; PR:O08590; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000051307; Expressed in lung and 19 other tissues.
DR Genevisible; O08590; RN.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005902; C:microvillus; ISO:RGD.
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:0005509; F:calcium ion binding; ISO:RGD.
DR GO; GO:0005507; F:copper ion binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0008131; F:primary amine oxidase activity; IDA:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
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:0007568; P:aging; IEP:RGD.
DR GO; GO:0009308; P:amine metabolic process; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0042755; P:eating behavior; IMP:RGD.
DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IMP:RGD.
DR GO; GO:1902283; P:negative regulation of primary amine oxidase activity; ISO:RGD.
DR GO; GO:0002675; P:positive regulation of acute inflammatory response; IMP:RGD.
DR GO; GO:0010828; P:positive regulation of glucose transmembrane transport; IDA:RGD.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; IMP:RGD.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:RGD.
DR GO; GO:0046677; P:response to antibiotic; ISO:RGD.
DR GO; GO:0035902; P:response to immobilization stress; IMP:RGD.
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 Calcium; Cell adhesion; Copper; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Membrane; Metal-binding; Oxidoreductase; Reference proteome;
KW Signal-anchor; TPQ; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8520629"
FT CHAIN 2..763
FT /note="Membrane primary amine oxidase"
FT /id="PRO_0000064105"
FT TOPO_DOM 2..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 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 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 CONFLICT 54
FT /note="P -> S (in Ref. 3; AAC53189)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="Q -> R (in Ref. 1; BAD74047)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="S -> F (in Ref. 1; BAD74047)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 763 AA; 84981 MW; 5FD739AF43F39039 CRC64;
MTQKTTLVLL ALAVITIFAL VCVLLAGRSG DGGRLSQPLH CPSVLPSVQP QTHPGQSQPF
ADLSPEELTA VMSFLIKHLG PGLVDAAQAR PSDNCVFSVE LQLPAKAAAL AHLDRGGPPP
VREALAIIFF GGQPKPNVSE LVVGPLPHPS YMRDVTVERH GGPLPYYRRP VLTREYQDIQ
EMIFHRELPQ ASGLLHHCCF YKRQGHNLLK MTTAPRGLQS GDRATWFGIY YNLSGAGFYP
HPIGLELLVD HKALDPALWT IQKVFYQGRY YESLTQLEDM FEAGLVNVVL VPDNGTGGSW
SLKSSVPPGR APPLQFHPEG PRFSVQGSQV RSSLWAFSFG LGAFSGPRIF DIRFQGERVA
YEISVQEAIA LYGGNSPASM STCYMDGSFG IGKYSTPLTR GVDCPYLATY VDWHFLLESQ
TPKTLRDAFC VFEQNQGLPL RRHHSDFYSH YFGGVVETVL VVRSVATLLN YDYVWDMVFH
SNGAIEVKFH ATGYITSAFF FGAGEKFGNR VAEHTLGTVH THNAHFKVDL DVAGLKNWAW
AEDLAFVPMN VPWQPEFQMQ RLQVTRKLLE TEEEAAFPLG NATPRYLYLA SNHSNKWGHR
RGYRIQILSF AGKPLPQESP IEKAFTWGRY HLAVTQRKEE EPSSSSIYNQ NDPWTPTVDF
TDFISNETIA GEDLVAWVTA GFLHIPHAED IPNTVTVGNG VGFFLRPYNF FDEDPSFYSP
DSIYFRKDQD VTDCEVNSLA CLSQTANCVP DLPAFSHGGF TYK
