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Membrane primary amine oxidase (EC 1.4.3.21) (Copper amine oxidase) (Semicarbazide-sensitive amine oxidase) (SSAO) (Vascular adhesion protein 1) (VAP-1)

 AOC3_MOUSE              Reviewed;         765 AA.
O70423; A2A4I7; Q66JM4; Q9R055;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
20-JUN-2018, entry version 153.
RecName: Full=Membrane primary amine oxidase;
EC=1.4.3.21 {ECO:0000250|UniProtKB:P19801};
AltName: Full=Copper amine oxidase;
AltName: Full=Semicarbazide-sensitive amine oxidase;
Short=SSAO;
AltName: Full=Vascular adhesion protein 1;
Short=VAP-1;
Name=Aoc3; Synonyms=Vap1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
STRAIN=129/SvJ, and BALB/cJ;
PubMed=9743358;
Bono P., Salmi M., Smith D.J., Leppanen I., Horelli-Kuitunen N.,
Palotie A., Jalkanen S.;
"Isolation, structural characterization, and chromosomal mapping of
the mouse vascular adhesion protein-1 gene and promoter.";
J. Immunol. 161:2953-2960(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10092636; DOI=10.1074/jbc.274.14.9515;
Moldes M., Feve B., Pairault J.;
"Molecular cloning of a major mRNA species in murine 3T3 adipocyte
lineage. differentiation-dependent expression, regulation, and
identification as semicarbazide-sensitive amine oxidase.";
J. Biol. Chem. 274:9515-9523(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Cell adhesion protein that participates in lymphocyte
recirculation by mediating the binding of lymphocytes to
peripheral lymph node vascular endothelial cells in an L-selectin-
independent fashion. Has a monoamine oxidase activity. May play a
role in adipogenesis (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: RCH(2)NH(2) + H(2)O + O(2) = RCHO + NH(3) +
H(2)O(2). {ECO:0000250|UniProtKB:P19801}.
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378;
Evidence={ECO:0000250|UniProtKB:P19801};
Note=Binds 1 copper ion per subunit.
{ECO:0000250|UniProtKB:P19801};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000250|UniProtKB:P19801};
Note=Binds 2 calcium ions per subunit.
{ECO:0000250|UniProtKB:P19801};
-!- COFACTOR:
Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
Evidence={ECO:0000250|UniProtKB:P19801};
Note=Contains 1 topaquinone per subunit.
{ECO:0000250|UniProtKB:P19801};
-!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Forms a
heterodimer with AOC2 (By similarity).
{ECO:0000250|UniProtKB:P19801, ECO:0000250|UniProtKB:Q16853}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O70423-1; Sequence=Displayed;
Name=2;
IsoId=O70423-2; Sequence=VSP_016604;
Note=No experimental confirmation available.;
-!- PTM: N- and O-glycosylated. {ECO:0000250}.
-!- PTM: Topaquinone (TPQ) is generated by copper-dependent
autoxidation of a specific tyrosyl residue.
{ECO:0000250|UniProtKB:P12807}.
-!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF054831; AAC23747.1; -; mRNA.
EMBL; AF078705; AAC35839.1; -; Genomic_DNA.
EMBL; AF115411; AAD09199.1; -; mRNA.
EMBL; AL590969; CAM19551.1; -; Genomic_DNA.
EMBL; BC080857; AAH80857.1; -; mRNA.
CCDS; CCDS25465.1; -. [O70423-1]
RefSeq; NP_033805.1; NM_009675.2. [O70423-1]
UniGene; Mm.67281; -.
ProteinModelPortal; O70423; -.
SMR; O70423; -.
BioGrid; 198116; 1.
IntAct; O70423; 4.
MINT; O70423; -.
STRING; 10090.ENSMUSP00000099394; -.
BindingDB; O70423; -.
ChEMBL; CHEMBL4727; -.
iPTMnet; O70423; -.
PhosphoSitePlus; O70423; -.
MaxQB; O70423; -.
PaxDb; O70423; -.
PeptideAtlas; O70423; -.
PRIDE; O70423; -.
Ensembl; ENSMUST00000103105; ENSMUSP00000099394; ENSMUSG00000019326. [O70423-1]
GeneID; 11754; -.
KEGG; mmu:11754; -.
UCSC; uc007lop.2; mouse. [O70423-1]
CTD; 8639; -.
MGI; MGI:1306797; Aoc3.
eggNOG; KOG1186; Eukaryota.
eggNOG; COG3733; LUCA.
GeneTree; ENSGT00510000046461; -.
HOGENOM; HOG000233919; -.
HOVERGEN; HBG004164; -.
InParanoid; O70423; -.
KO; K00276; -.
OMA; ISWGRYQ; -.
OrthoDB; EOG091G02WY; -.
PhylomeDB; O70423; -.
TreeFam; TF314750; -.
Reactome; R-MMU-211945; Phase I - Functionalization of compounds.
PRO; PR:O70423; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000019326; -.
CleanEx; MM_AOC3; -.
ExpressionAtlas; O70423; baseline and differential.
Genevisible; O70423; MM.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005769; C:early endosome; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005902; C:microvillus; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:UniProtKB-EC.
GO; GO:0052594; F:aminoacetone:oxygen oxidoreductase(deaminating) activity; IEA:UniProtKB-EC.
GO; GO:0005509; F:calcium ion binding; ISO:MGI.
GO; GO:0005507; F:copper ion binding; ISO:MGI.
GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
GO; GO:0008131; F:primary amine oxidase activity; ISS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0048038; F:quinone binding; ISS:UniProtKB.
GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
GO; GO:0009308; P:amine metabolic process; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
GO; GO:0042755; P:eating behavior; ISO:MGI.
GO; GO:0002523; P:leukocyte migration involved in inflammatory response; ISO:MGI.
GO; GO:1902283; P:negative regulation of primary amine oxidase activity; ISO:MGI.
GO; GO:0002675; P:positive regulation of acute inflammatory response; ISO:MGI.
GO; GO:0010828; P:positive regulation of glucose transmembrane transport; ISO:MGI.
GO; GO:0002687; P:positive regulation of leukocyte migration; ISO:MGI.
GO; GO:0008217; P:regulation of blood pressure; ISO:MGI.
GO; GO:0046677; P:response to antibiotic; ISO:MGI.
GO; GO:0035902; P:response to immobilization stress; ISO:MGI.
Gene3D; 2.70.98.20; -; 1.
InterPro; IPR000269; Cu_amine_oxidase.
InterPro; IPR015798; Cu_amine_oxidase_C.
InterPro; IPR036460; Cu_amine_oxidase_C_sf.
InterPro; IPR016182; Cu_amine_oxidase_N-reg.
InterPro; IPR015800; Cu_amine_oxidase_N2.
InterPro; IPR015802; Cu_amine_oxidase_N3.
PANTHER; PTHR10638; PTHR10638; 1.
Pfam; PF01179; Cu_amine_oxid; 1.
Pfam; PF02727; Cu_amine_oxidN2; 1.
Pfam; PF02728; Cu_amine_oxidN3; 1.
PRINTS; PR00766; CUDAOXIDASE.
SUPFAM; SSF49998; SSF49998; 1.
SUPFAM; SSF54416; SSF54416; 2.
PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Cell adhesion; Complete proteome;
Copper; Disulfide bond; Glycoprotein; Membrane; Metal-binding;
Oxidoreductase; Reference proteome; Signal-anchor; TPQ; Transmembrane;
Transmembrane helix.
CHAIN 1 765 Membrane primary amine oxidase.
/FTId=PRO_0000064103.
TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.
TRANSMEM 7 27 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 28 765 Extracellular. {ECO:0000255}.
REGION 384 394 Substrate binding.
{ECO:0000250|UniProtKB:P19801}.
REGION 468 473 Substrate binding.
{ECO:0000250|UniProtKB:P19801}.
REGION 578 585 Heparin-binding. {ECO:0000250}.
ACT_SITE 386 386 Proton acceptor.
{ECO:0000250|UniProtKB:P19801}.
ACT_SITE 471 471 Schiff-base intermediate with substrate;
via topaquinone.
{ECO:0000250|UniProtKB:P19801}.
METAL 520 520 Copper; via tele nitrogen.
{ECO:0000250|UniProtKB:P19801}.
METAL 522 522 Copper; via tele nitrogen.
{ECO:0000250|UniProtKB:P19801}.
METAL 529 529 Calcium 1.
{ECO:0000250|UniProtKB:P19801}.
METAL 530 530 Calcium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19801}.
METAL 531 531 Calcium 1.
{ECO:0000250|UniProtKB:P19801}.
METAL 572 572 Calcium 2.
{ECO:0000250|UniProtKB:P19801}.
METAL 663 663 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19801}.
METAL 667 667 Calcium 2.
{ECO:0000250|UniProtKB:P19801}.
METAL 673 673 Calcium 1.
{ECO:0000250|UniProtKB:P19801}.
METAL 674 674 Calcium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19801}.
METAL 684 684 Copper; via pros nitrogen.
{ECO:0000250|UniProtKB:P19801}.
MOD_RES 471 471 2',4',5'-topaquinone.
{ECO:0000250|UniProtKB:P12807}.
CARBOHYD 137 137 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P19801}.
CARBOHYD 212 212 O-linked (GalNAc...) threonine.
{ECO:0000250|UniProtKB:Q16853}.
CARBOHYD 232 232 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q16853}.
CARBOHYD 294 294 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q16853}.
CARBOHYD 592 592 N-linked (GlcNAc...) (complex)
asparagine.
{ECO:0000250|UniProtKB:Q16853}.
CARBOHYD 659 659 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 666 666 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q16853}.
DISULFID 198 199 {ECO:0000250|UniProtKB:Q16853}.
DISULFID 404 430 {ECO:0000250|UniProtKB:P19801}.
DISULFID 734 741 {ECO:0000250|UniProtKB:Q16853}.
DISULFID 748 748 Interchain.
{ECO:0000250|UniProtKB:P19801}.
VAR_SEQ 630 765 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_016604.
CONFLICT 659 659 N -> D (in Ref. 2; AAD09199).
{ECO:0000305}.
SEQUENCE 765 AA; 84534 MW; 7489ED67D3DBB44D CRC64;
MTQKTTLVLL ALAVITIFAL VCVLLAGRSG DGGGLSQPLH CPSVLPSVQP RTHPSQSQPF
ADLSPEELTA VMSFLTKHLG PGLVDAAQAR PSDNCVFSVE LQLPAKAAAL AHLDRGGPPP
VREALAIIFF GGQPKPNVSE LVVGPLPHPS YMRDVTVERH GGPLPYYRRP VLDREYQDIE
EMIFHRELPQ ASGLLHHCCF YKHQGQNLLT MTTAPRGLQS GDRATWFGLY YNLSGAGFYP
HPIGLELLID HKALDPALWT IQKVFYQGRY YESLTQLEDQ FEAGLVNVVL VPNNGTGGSW
SLKSSVPPGP APPLQFHPQG PRFSVQGSQV SSSLWAFSFG LGAFSGPRIF DIRFQGERVA
YEISVQEAIA LYGGNSPASM STCYVDGSFG IGKYSTPLIR GVDCPYLATY VDWHFLLESQ
APKTLRDAFC VFEQNQGLPL RRHHSDFYSH YFGGVVGTVL VVRSVSTLLN YDYIWDMVFH
PNGAIEVKFH ATGYISSAFF FGAGEKFGNR VGAHTLGTVH THSAHFKVDL DVAGLKNWAW
AEDMAFVPTI VPWQPEYQMQ RLQVTRKLLE TEEEAAFPLG GATPRYLYLA SNHSNKWGHR
RGYRIQILSF AGKPLPQESP IEKAFTWGRY HLAVTQRKEE EPSSSSIFNQ NDPWTPTVNF
TDFISNETIA GEDLVAWVTA GFLHIPHAED IPNTVTAGNS VGFFLRPYNF FDEDPSFHSA
DSIYFREGQD ATACEVNPLA CLSQTATCAP EIPAFSHGGF AYRDN


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