ID AOC3_HUMAN Reviewed; 763 AA. AC Q16853; B2RCI5; K7ESB3; L0L8N9; Q45F94; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 09-DEC-2015, entry version 163. DE RecName: Full=Membrane primary amine oxidase; DE EC=1.4.3.21; DE AltName: Full=Copper amine oxidase; DE AltName: Full=HPAO; DE AltName: Full=Semicarbazide-sensitive amine oxidase; DE Short=SSAO; DE AltName: Full=Vascular adhesion protein 1; DE Short=VAP-1; GN Name=AOC3; Synonyms=VAP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Placenta; RX PubMed=8972912; DOI=10.1016/S0378-1119(96)00387-3; RA Zhang X., McIntire W.S.; RT "Cloning and sequencing of a copper-containing, topaquinone-containing RT monoamine oxidase from human placenta."; RL Gene 179:279-286(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, RP FUNCTION, SELF-ASSOCIATION, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Lung; RX PubMed=9653080; DOI=10.1084/jem.188.1.17; RA Smith D.J., Salmi M., Bono P., Hellman J., Leu T., Jalkanen S.; RT "Cloning of vascular adhesion protein 1 reveals a novel RT multifunctional adhesion molecule."; RL J. Exp. Med. 188:17-27(1998). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=14585497; DOI=10.1016/S0378-1119(03)00753-4; RA Zhang Q., Mashima Y., Noda S., Imamura Y., Kudoh J., Shimizu N., RA Nishiyama T., Umeda S., Oguchi Y., Tanaka Y., Iwata T.; RT "Characterization of AOC2 gene encoding a copper-binding amine oxidase RT expressed specifically in retina."; RL Gene 318:45-53(2003). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBUNIT, ALTERNATIVE RP SPLICING, AND TISSUE SPECIFICITY. RX PubMed=23349812; DOI=10.1371/journal.pone.0054151; RA Kaitaniemi S., Gron K., Elovaara H., Salmi M., Jalkanen S., Elima K.; RT "Functional modulation of vascular adhesion protein-1 by a novel RT splice variant."; RL PLoS ONE 8:E54151-E54151(2013). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-5; TYR-167; RP THR-371; SER-408; HIS-426; TRP-441; THR-582; SER-700 AND VAL-749. RG NIEHS SNPs program; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in RT the human lineage."; RL Nature 440:1045-1049(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=PNS; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP PROTEIN SEQUENCE OF 79-90 AND 123-132. RC TISSUE=Adipocyte; RX PubMed=15242332; DOI=10.1042/BJ20040647; RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.; RT "Vectorial proteomics reveal targeting, phosphorylation and specific RT fragmentation of polymerase I and transcript release factor (PTRF) at RT the surface of caveolae in human adipocytes."; RL Biochem. J. 383:237-248(2004). RN [10] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-592; ASN-618 AND ASN-666. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [11] RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=17400359; DOI=10.1016/j.biochi.2007.02.013; RA Bour S., Daviaud D., Gres S., Lefort C., Prevot D., Zorzano A., RA Wabitsch M., Saulnier-Blache J.-S., Valet P., Carpene C.; RT "Adipogenesis-related increase of semicarbazide-sensitive amine RT oxidase and monoamine oxidase in human adipocytes."; RL Biochimie 89:916-925(2007). RN [12] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF RP MET-211; TYR-394 AND LEU-469. RX PubMed=19588076; DOI=10.1007/s00018-009-0076-5; RA Kaitaniemi S., Elovaara H., Groen K., Kidron H., Liukkonen J., RA Salminen T., Salmi M., Jalkanen S., Elima K.; RT "The unique substrate specificity of human AOC2, a semicarbazide- RT sensitive amine oxidase."; RL Cell. Mol. Life Sci. 66:2743-2757(2009). RN [13] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-137; ASN-294; ASN-592; RP ASN-618 AND ASN-666. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [14] RP GLYCOSYLATION AT ASN-592. RX PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200; RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.; RT "A strategy for precise and large scale identification of core RT fucosylated glycoproteins."; RL Mol. Cell. Proteomics 8:913-923(2009). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH COPPER AND RP CALCIUM IONS, DISULFIDE BONDS, TOPAQUINONE AT TYR-471, AND RP GLYCOSYLATION AT ASN-137; THR-212; ASN-232; ASN-294; ASN-592; ASN-618 RP AND ASN-666. RX PubMed=16046623; DOI=10.1110/ps.051438105; RA Airenne T.T., Nymalm Y., Kidron H., Smith D.J., Pihlavisto M., RA Salmi M., Jalkanen S., Johnson M.S., Salminen T.A.; RT "Crystal structure of the human vascular adhesion protein-1: unique RT structural features with functional implications."; RL Protein Sci. 14:1964-1974(2005). CC -!- FUNCTION: Cell adhesion protein that participates in lymphocyte CC extravasation and recirculation by mediating the binding of CC lymphocytes to peripheral lymph node vascular endothelial cells in CC an L-selectin-independent fashion. Has semicarbazide-sensitive CC (SSAO) monoamine oxidase activity. May play a role in CC adipogenesis. {ECO:0000269|PubMed:17400359, CC ECO:0000269|PubMed:19588076, ECO:0000269|PubMed:23349812, CC ECO:0000269|PubMed:9653080}. CC -!- CATALYTIC ACTIVITY: RCH(2)NH(2) + H(2)O + O(2) = RCHO + NH(3) + CC H(2)O(2). CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Note=Binds 1 copper ion per subunit.; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Note=Binds 2 calcium ions per subunit.; CC -!- COFACTOR: CC Name=L-topaquinone; Xref=ChEBI:CHEBI:79027; CC Note=Contains 1 topaquinone per subunit.; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.94 mM for 2-phenylethylamine {ECO:0000269|PubMed:19588076}; CC KM=0.67 mM for methylamine {ECO:0000269|PubMed:19588076}; CC -!- SUBUNIT: Homodimer; disulfide-linked. Can heterodimerize with CC isoform 2 leading to reduced surface expression. Forms a CC heterodimer with AOC2. {ECO:0000269|PubMed:16046623, CC ECO:0000269|PubMed:19588076, ECO:0000269|PubMed:23349812}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9653080}; CC Single-pass type II membrane protein {ECO:0000269|PubMed:9653080}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q16853-1; Sequence=Displayed; CC Name=2; Synonyms=VAP-1Delta3; CC IsoId=Q16853-2; Sequence=VSP_053751, VSP_053752; CC Note=Devoid of the semicarbazide-sensitive amine oxidase (SSAO) CC activity.; CC Name=3; CC IsoId=Q16853-3; Sequence=VSP_055201; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Strongly expressed on the high endothelial CC venules of peripheral lymph nodes and on hepatic endothelia. Also CC highly expressed in appendix, lung and small intestine. Expressed CC also in adipose tissue, in bone marrow, colon, heart, kidney, CC ovary, pancreas, placenta, prostate, skeletal muscle, spleen and CC testis. Isoform 2 seems to be the predominant transcript in fetal CC kidneys, fetal cartilage and fetal tonsils. The highest relative CC expression of isoform 2 occurs in skeletal muscle, heart, CC pancreas, kidney, and lung. {ECO:0000269|PubMed:17400359, CC ECO:0000269|PubMed:23349812, ECO:0000269|PubMed:9653080}. CC -!- INDUCTION: Up-regulated during in vitro adipocyte differentiation. CC {ECO:0000269|PubMed:17400359}. CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent CC autoxidation of a specific tyrosyl residue. CC -!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:16046623, CC ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, CC ECO:0000269|PubMed:19159218}. CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/aoc3/"; 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; U39447; AAC50919.1; -; mRNA. DR EMBL; AF067406; AAC25170.1; -; mRNA. DR EMBL; AB050502; BAB18866.1; -; Genomic_DNA. DR EMBL; JX020506; AGB67480.1; -; mRNA. DR EMBL; AK025727; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK315129; BAG37582.1; -; mRNA. DR EMBL; DQ143944; AAZ38716.1; -; Genomic_DNA. DR EMBL; AC016889; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC050549; AAH50549.1; -; mRNA. DR CCDS; CCDS11444.1; -. [Q16853-1] DR CCDS; CCDS62198.1; -. [Q16853-3] DR CCDS; CCDS74071.1; -. [Q16853-2] DR PIR; JC5234; JC5234. DR RefSeq; NP_001264660.1; NM_001277731.1. [Q16853-2] DR RefSeq; NP_001264661.1; NM_001277732.1. [Q16853-3] DR RefSeq; NP_003725.1; NM_003734.3. [Q16853-1] DR UniGene; Hs.198241; -. DR PDB; 1PU4; X-ray; 3.20 A; A/B=1-763. DR PDB; 1US1; X-ray; 2.90 A; A/B=1-763. DR PDB; 2C10; X-ray; 2.50 A; A/B/C/D=29-763. DR PDB; 2C11; X-ray; 2.90 A; A/B/C/D=29-763. DR PDB; 2Y73; X-ray; 2.60 A; A/B=1-763. DR PDB; 2Y74; X-ray; 2.95 A; A/B=1-763. DR PDB; 3ALA; X-ray; 2.90 A; A/B/C/D/E/F/G=33-763. DR PDB; 4BTW; X-ray; 2.80 A; A/B=27-763. DR PDB; 4BTX; X-ray; 2.78 A; A/B=27-763. DR PDB; 4BTY; X-ray; 3.10 A; A/B=27-763. DR PDBsum; 1PU4; -. DR PDBsum; 1US1; -. DR PDBsum; 2C10; -. DR PDBsum; 2C11; -. DR PDBsum; 2Y73; -. DR PDBsum; 2Y74; -. DR PDBsum; 3ALA; -. DR PDBsum; 4BTW; -. DR PDBsum; 4BTX; -. DR PDBsum; 4BTY; -. DR ProteinModelPortal; Q16853; -. DR SMR; Q16853; 58-761. DR BioGrid; 114192; 8. DR IntAct; Q16853; 2. DR STRING; 9606.ENSP00000312326; -. DR BindingDB; Q16853; -. DR ChEMBL; CHEMBL3437; -. DR DrugBank; DB01275; Hydralazine. DR DrugBank; DB00780; Phenelzine. DR GuidetoPHARMACOLOGY; 2767; -. DR DMDM; 2501336; -. DR PaxDb; Q16853; -. DR PeptideAtlas; Q16853; -. DR PRIDE; Q16853; -. DR Ensembl; ENST00000308423; ENSP00000312326; ENSG00000131471. [Q16853-1] DR Ensembl; ENST00000591562; ENSP00000468632; ENSG00000131471. [Q16853-3] DR Ensembl; ENST00000613571; ENSP00000484312; ENSG00000131471. [Q16853-2] DR Ensembl; ENST00000617500; ENSP00000477686; ENSG00000131471. [Q16853-3] DR GeneID; 8639; -. DR KEGG; hsa:8639; -. DR UCSC; uc002ibv.4; human. [Q16853-1] DR CTD; 8639; -. DR GeneCards; AOC3; -. DR HGNC; HGNC:550; AOC3. DR HPA; CAB025797; -. DR HPA; HPA000980; -. DR MIM; 603735; gene. DR neXtProt; NX_Q16853; -. DR PharmGKB; PA24840; -. DR eggNOG; KOG1186; Eukaryota. DR eggNOG; COG3733; LUCA. DR GeneTree; ENSGT00510000046461; -. DR HOGENOM; HOG000233919; -. DR HOVERGEN; HBG004164; -. DR InParanoid; Q16853; -. DR KO; K00276; -. DR OMA; DEGRFNW; -. DR OrthoDB; EOG7353W8; -. DR PhylomeDB; Q16853; -. DR TreeFam; TF314750; -. DR BRENDA; 1.4.3.21; 2681. DR Reactome; R-HSA-211945; Phase 1 - Functionalization of compounds. DR SABIO-RK; Q16853; -. DR EvolutionaryTrace; Q16853; -. DR GeneWiki; AOC3; -. DR GenomeRNAi; 8639; -. DR NextBio; 32389; -. DR PRO; PR:Q16853; -. DR Proteomes; UP000005640; Chromosome 17. DR Bgee; Q16853; -. DR CleanEx; HS_AOC3; -. DR ExpressionAtlas; Q16853; baseline and differential. DR Genevisible; Q16853; HS. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005769; C:early endosome; IDA:CACAO. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:CACAO. DR GO; GO:0005794; C:Golgi apparatus; IDA:CACAO. DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB. DR GO; GO:0005902; C:microvillus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA: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; IDA:UniProtKB. DR GO; GO:0005261; F:cation channel activity; IDA:UniProtKB. DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB. DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC. DR GO; GO:0008131; F:primary amine oxidase activity; IDA:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; TAS:UniProtKB. DR GO; GO:0048038; F:quinone binding; IDA:UniProtKB. DR GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC. DR GO; GO:0009308; P:amine metabolic process; IDA:UniProtKB. DR GO; GO:0098655; P:cation transmembrane transport; IDA:GOC. DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB. DR GO; GO:0006954; P:inflammatory response; TAS:UniProtKB. DR GO; GO:0046677; P:response to antibiotic; IDA:UniProtKB. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome. DR Gene3D; 2.70.98.20; -; 1. DR InterPro; IPR000269; Cu_amine_oxidase. DR InterPro; IPR015798; Cu_amine_oxidase_C. 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; Alternative splicing; Calcium; Cell adhesion; KW Cell membrane; Complete proteome; Copper; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Membrane; Metal-binding; Oxidoreductase; KW Polymorphism; Reference proteome; Signal-anchor; TPQ; Transmembrane; KW Transmembrane helix. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O08590}. FT CHAIN 2 763 Membrane primary amine oxidase. FT /FTId=PRO_0000064102. FT TOPO_DOM 2 5 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 6 26 Helical; Signal-anchor for type II FT membrane protein. {ECO:0000255}. FT TOPO_DOM 27 763 Extracellular. {ECO:0000255}. FT ACT_SITE 386 386 Proton acceptor. {ECO:0000250}. FT ACT_SITE 471 471 Schiff-base intermediate with substrate; FT via topaquinone. {ECO:0000250}. FT METAL 520 520 Copper. {ECO:0000269|PubMed:16046623}. FT METAL 522 522 Copper. {ECO:0000269|PubMed:16046623}. FT METAL 529 529 Calcium 1. FT METAL 530 530 Calcium 1; via carbonyl oxygen. FT METAL 531 531 Calcium 1. FT METAL 572 572 Calcium 2. FT METAL 638 638 Calcium 2. FT METAL 663 663 Calcium 2; via carbonyl oxygen. FT METAL 665 665 Calcium 2. FT METAL 667 667 Calcium 2. FT METAL 673 673 Calcium 1. FT METAL 674 674 Calcium 1; via carbonyl oxygen. FT METAL 684 684 Copper. {ECO:0000269|PubMed:16046623}. FT MOD_RES 471 471 2',4',5'-topaquinone. FT CARBOHYD 137 137 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:16046623, FT ECO:0000269|PubMed:19159218}. FT CARBOHYD 212 212 O-linked (GalNAc...). FT {ECO:0000305|PubMed:16046623}. FT CARBOHYD 232 232 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:16046623}. FT CARBOHYD 294 294 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:16046623, FT ECO:0000269|PubMed:19159218}. FT CARBOHYD 592 592 N-linked (GlcNAc...) (complex). FT {ECO:0000269|PubMed:16046623, FT ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19139490, FT ECO:0000269|PubMed:19159218}. FT CARBOHYD 618 618 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:16046623, FT ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218}. FT CARBOHYD 666 666 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:16046623, FT ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218}. FT DISULFID 198 199 {ECO:0000269|PubMed:16046623}. FT DISULFID 734 741 {ECO:0000269|PubMed:16046623}. FT DISULFID 748 748 Interchain. FT {ECO:0000269|PubMed:16046623}. FT VAR_SEQ 1 543 Missing (in isoform 3). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_055201. FT VAR_SEQ 630 634 YQLAV -> IWWPG (in isoform 2). FT {ECO:0000303|PubMed:23349812}. FT /FTId=VSP_053751. FT VAR_SEQ 635 763 Missing (in isoform 2). FT {ECO:0000303|PubMed:23349812}. FT /FTId=VSP_053752. FT VARIANT 5 5 T -> R (in dbSNP:rs33954211). FT {ECO:0000269|Ref.6}. FT /FTId=VAR_025035. FT VARIANT 78 78 R -> Q (in dbSNP:rs402680). FT /FTId=VAR_052603. FT VARIANT 167 167 H -> Y (in dbSNP:rs2228470). FT {ECO:0000269|Ref.6}. FT /FTId=VAR_025027. FT VARIANT 171 171 V -> M (in dbSNP:rs408038). FT /FTId=VAR_052604. FT VARIANT 203 203 H -> R (in dbSNP:rs630079). FT /FTId=VAR_052605. FT VARIANT 317 317 Y -> H (in dbSNP:rs438287). FT /FTId=VAR_012064. FT VARIANT 329 329 R -> Q (in dbSNP:rs2229595). FT /FTId=VAR_024343. FT VARIANT 371 371 I -> T (in dbSNP:rs35097308). FT {ECO:0000269|Ref.6}. FT /FTId=VAR_025028. FT VARIANT 408 408 A -> S (in dbSNP:rs35643019). FT {ECO:0000269|Ref.6}. FT /FTId=VAR_025029. FT VARIANT 426 426 R -> H (in dbSNP:rs33986943). FT {ECO:0000269|Ref.6}. FT /FTId=VAR_025030. FT VARIANT 441 441 R -> W (in dbSNP:rs2229596). FT {ECO:0000269|Ref.6}. FT /FTId=VAR_025031. FT VARIANT 582 582 A -> T (in dbSNP:rs34987927). FT {ECO:0000269|Ref.6}. FT /FTId=VAR_025032. FT VARIANT 700 700 G -> S (in dbSNP:rs477207). FT {ECO:0000269|Ref.6}. FT /FTId=VAR_025033. FT VARIANT 749 749 A -> V (in dbSNP:rs34012919). FT {ECO:0000269|Ref.6}. FT /FTId=VAR_025034. FT MUTAGEN 211 211 M->V: Increased activity towards 2- FT phenylethylamine, and decreased activity FT towards methylamine; when associated with FT N-394 and G-469. FT {ECO:0000269|PubMed:19588076}. FT MUTAGEN 394 394 Y->N: Increased activity towards 2- FT phenylethylamine, and decreased activity FT towards methylamine; when associated with FT V-211 and G-469. FT {ECO:0000269|PubMed:19588076}. FT MUTAGEN 469 469 L->G: Increased activity towards 2- FT phenylethylamine, and decreased activity FT towards methylamine; when associated with FT V-211 and N-394. FT {ECO:0000269|PubMed:19588076}. FT HELIX 65 78 {ECO:0000244|PDB:2C10}. FT STRAND 83 85 {ECO:0000244|PDB:3ALA}. FT HELIX 86 88 {ECO:0000244|PDB:2C10}. FT STRAND 93 102 {ECO:0000244|PDB:2C10}. FT HELIX 106 115 {ECO:0000244|PDB:2C10}. FT STRAND 123 130 {ECO:0000244|PDB:2C10}. FT STRAND 132 135 {ECO:0000244|PDB:2C10}. FT STRAND 137 144 {ECO:0000244|PDB:2C10}. FT STRAND 146 148 {ECO:0000244|PDB:2C10}. FT STRAND 151 154 {ECO:0000244|PDB:2C10}. FT HELIX 156 160 {ECO:0000244|PDB:2C10}. FT HELIX 166 168 {ECO:0000244|PDB:2C10}. FT HELIX 173 185 {ECO:0000244|PDB:2C10}. FT HELIX 188 191 {ECO:0000244|PDB:2C10}. FT HELIX 192 199 {ECO:0000244|PDB:2C10}. FT TURN 203 206 {ECO:0000244|PDB:2C11}. FT STRAND 208 211 {ECO:0000244|PDB:2C10}. FT STRAND 217 219 {ECO:0000244|PDB:2C10}. FT STRAND 224 231 {ECO:0000244|PDB:2C10}. FT STRAND 234 236 {ECO:0000244|PDB:2C10}. FT HELIX 238 240 {ECO:0000244|PDB:2C10}. FT STRAND 242 250 {ECO:0000244|PDB:2C10}. FT STRAND 253 255 {ECO:0000244|PDB:2C10}. FT HELIX 256 258 {ECO:0000244|PDB:2C10}. FT STRAND 260 266 {ECO:0000244|PDB:2C10}. FT STRAND 269 272 {ECO:0000244|PDB:2C10}. FT HELIX 274 282 {ECO:0000244|PDB:2C10}. FT TURN 283 285 {ECO:0000244|PDB:4BTW}. FT TURN 298 300 {ECO:0000244|PDB:2C10}. FT STRAND 314 316 {ECO:0000244|PDB:2C10}. FT STRAND 318 320 {ECO:0000244|PDB:4BTW}. FT STRAND 322 326 {ECO:0000244|PDB:2C10}. FT STRAND 329 342 {ECO:0000244|PDB:2C10}. FT TURN 343 345 {ECO:0000244|PDB:2C10}. FT STRAND 346 354 {ECO:0000244|PDB:2C10}. FT STRAND 357 372 {ECO:0000244|PDB:2C10}. FT HELIX 377 380 {ECO:0000244|PDB:2C10}. FT STRAND 383 385 {ECO:0000244|PDB:2C10}. FT HELIX 386 388 {ECO:0000244|PDB:2C10}. FT TURN 391 394 {ECO:0000244|PDB:2C10}. FT TURN 400 402 {ECO:0000244|PDB:2C10}. FT STRAND 408 421 {ECO:0000244|PDB:2C10}. FT STRAND 423 445 {ECO:0000244|PDB:2C10}. FT STRAND 447 449 {ECO:0000244|PDB:2C10}. FT STRAND 451 468 {ECO:0000244|PDB:2C10}. FT STRAND 471 479 {ECO:0000244|PDB:2C10}. FT TURN 481 483 {ECO:0000244|PDB:4BTY}. FT STRAND 485 493 {ECO:0000244|PDB:2C10}. FT STRAND 497 499 {ECO:0000244|PDB:2C10}. FT STRAND 506 512 {ECO:0000244|PDB:2C10}. FT STRAND 515 518 {ECO:0000244|PDB:2C10}. FT STRAND 520 530 {ECO:0000244|PDB:2C10}. FT STRAND 534 551 {ECO:0000244|PDB:2C10}. FT STRAND 554 569 {ECO:0000244|PDB:2C10}. FT HELIX 572 575 {ECO:0000244|PDB:2C10}. FT STRAND 577 581 {ECO:0000244|PDB:4BTW}. FT STRAND 585 594 {ECO:0000244|PDB:2C10}. FT STRAND 600 608 {ECO:0000244|PDB:2C10}. FT STRAND 617 619 {ECO:0000244|PDB:2C11}. FT HELIX 622 629 {ECO:0000244|PDB:2C10}. FT STRAND 630 636 {ECO:0000244|PDB:2C10}. FT TURN 647 651 {ECO:0000244|PDB:2Y73}. FT STRAND 653 655 {ECO:0000244|PDB:1US1}. FT HELIX 660 663 {ECO:0000244|PDB:2C10}. FT STRAND 670 684 {ECO:0000244|PDB:2C10}. FT HELIX 688 690 {ECO:0000244|PDB:2C10}. FT STRAND 700 713 {ECO:0000244|PDB:2C10}. FT HELIX 715 718 {ECO:0000244|PDB:2C10}. FT STRAND 723 729 {ECO:0000244|PDB:2C10}. FT TURN 734 736 {ECO:0000244|PDB:2C10}. FT HELIX 738 741 {ECO:0000244|PDB:2Y73}. FT HELIX 742 745 {ECO:0000244|PDB:2C10}. SQ SEQUENCE 763 AA; 84622 MW; 58AD55605EC9D228 CRC64; MNQKTILVLL ILAVITIFAL VCVLLVGRGG DGGEPSQLPH CPSVSPSAQP WTHPGQSQLF ADLSREELTA VMRFLTQRLG PGLVDAAQAR PSDNCVFSVE LQLPPKAAAL AHLDRGSPPP AREALAIVFF GRQPQPNVSE LVVGPLPHPS YMRDVTVERH GGPLPYHRRP VLFQEYLDID QMIFNRELPQ ASGLLHHCCF YKHRGRNLVT MTTAPRGLQS GDRATWFGLY YNISGAGFFL HHVGLELLVN HKALDPARWT IQKVFYQGRY YDSLAQLEAQ FEAGLVNVVL IPDNGTGGSW SLKSPVPPGP APPLQFYPQG PRFSVQGSRV ASSLWTFSFG LGAFSGPRIF DVRFQGERLV YEISLQEALA IYGGNSPAAM TTRYVDGGFG MGKYTTPLTR GVDCPYLATY VDWHFLLESQ APKTIRDAFC VFEQNQGLPL RRHHSDLYSH YFGGLAETVL VVRSMSTLLN YDYVWDTVFH PSGAIEIRFY ATGYISSAFL FGATGKYGNQ VSEHTLGTVH THSAHFKVDL DVAGLENWVW AEDMVFVPMA VPWSPEHQLQ RLQVTRKLLE MEEQAAFLVG SATPRYLYLA SNHSNKWGHP RGYRIQMLSF AGEPLPQNSS MARGFSWERY QLAVTQRKEE EPSSSSVFNQ NDPWAPTVDF SDFINNETIA GKDLVAWVTA GFLHIPHAED IPNTVTVGNG VGFFLRPYNF FDEDPSFYSA DSIYFRGDQD AGACEVNPLA CLPQAAACAP DLPAFSHGGF SHN //