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Membrane primary amine oxidase (EC 1.4.3.21) (Copper amine oxidase) (Semicarbazide-sensitive amine oxidase) (SSAO) (VP97) (Vascular adhesion protein 1) (VAP-1)

 AOC3_RAT                Reviewed;         763 AA.
O08590; Q497D2; Q5R1T5;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
22-NOV-2017, entry version 140.
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=VP97;
AltName: Full=Vascular adhesion protein 1;
Short=VAP-1;
Name=Aoc3;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
STRAIN=Wistar; TISSUE=Aorta;
PubMed=15744061; DOI=10.1248/bpb.28.413;
Ochiai Y., Itoh K., Sakurai E., Tanaka Y.;
"Molecular cloning and characterization of rat semicarbazide-sensitive
amine oxidase.";
Biol. Pharm. Bull. 28:413-418(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-322, PARTIAL PROTEIN SEQUENCE, AND
SUBCELLULAR LOCATION.
STRAIN=Sprague-Dawley; TISSUE=Adipocyte;
PubMed=9083076; DOI=10.1074/jbc.272.14.9388;
Morris N.J., Ducret A., Aebersold R., Ross S.A., Keller S.R.,
Lienhard G.E.;
"Membrane amine oxidase cloning and identification as a major protein
in the adipocyte plasma membrane.";
J. Biol. Chem. 272:9388-9392(1997).
[4]
PROTEIN SEQUENCE OF 2-20, AND SUBCELLULAR LOCATION.
TISSUE=Adipocyte;
PubMed=8520629; DOI=10.3109/09687689509072428;
Jochen A., Guven S., Hays J.;
"The major integral membrane glycoprotein in adipocytes is a novel
200-kDa heterodimer.";
Mol. Membr. Biol. 12:277-281(1995).
-!- 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,
ECO:0000269|PubMed:15744061}.
-!- 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:0000269|PubMed:8520629,
ECO:0000269|PubMed:9083076}; Single-pass type II membrane protein
{ECO:0000269|PubMed:8520629, ECO:0000269|PubMed:9083076}.
-!- TISSUE SPECIFICITY: Highly expressed in adipocytes, aorta and
lung. Expressed at lower levels in heart, kidney, large intestine,
liver, small intestine and stomach. {ECO:0000269|PubMed:15744061}.
-!- 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; AB195675; BAD74047.1; -; mRNA.
EMBL; BC100613; AAI00614.1; -; mRNA.
EMBL; U72632; AAC53189.1; -; mRNA.
RefSeq; NP_113770.2; NM_031582.2.
UniGene; Rn.198327; -.
SMR; O08590; -.
STRING; 10116.ENSRNOP00000059889; -.
BindingDB; O08590; -.
ChEMBL; CHEMBL4592; -.
iPTMnet; O08590; -.
PhosphoSitePlus; O08590; -.
PaxDb; O08590; -.
PRIDE; O08590; -.
Ensembl; ENSRNOT00000076820; ENSRNOP00000068449; ENSRNOG00000051307.
GeneID; 29473; -.
KEGG; rno:29473; -.
UCSC; RGD:62058; rat.
CTD; 8639; -.
RGD; 62058; Aoc3.
eggNOG; KOG1186; Eukaryota.
eggNOG; KOG4470; Eukaryota.
eggNOG; COG3733; LUCA.
GeneTree; ENSGT00510000046461; -.
HOGENOM; HOG000233919; -.
HOVERGEN; HBG004164; -.
InParanoid; O08590; -.
KO; K00276; -.
OrthoDB; EOG091G02WY; -.
BRENDA; 1.4.3.21; 5301.
Reactome; R-RNO-211945; Phase I - Functionalization of compounds.
PRO; PR:O08590; -.
Proteomes; UP000002494; Chromosome 10.
Bgee; ENSRNOG00000051307; -.
Genevisible; O08590; RN.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0005769; C:early endosome; ISO:RGD.
GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0005902; C:microvillus; ISO:RGD.
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:RGD.
GO; GO:0005507; F:copper ion binding; ISO:RGD.
GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
GO; GO:0008131; F:primary amine oxidase activity; IDA:RGD.
GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0048038; F:quinone binding; ISS:UniProtKB.
GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0009308; P:amine metabolic process; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
GO; GO:0042755; P:eating behavior; IMP:RGD.
GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IMP:RGD.
GO; GO:1902283; P:negative regulation of primary amine oxidase activity; ISO:RGD.
GO; GO:0002675; P:positive regulation of acute inflammatory response; IMP:RGD.
GO; GO:0010828; P:positive regulation of glucose transport; IDA:RGD.
GO; GO:0002687; P:positive regulation of leukocyte migration; IMP:RGD.
GO; GO:0008217; P:regulation of blood pressure; IMP:RGD.
GO; GO:0046677; P:response to antibiotic; ISO:RGD.
GO; GO:0035902; P:response to immobilization stress; IMP:RGD.
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;
Calcium; Cell adhesion; Complete proteome; Copper;
Direct protein sequencing; Disulfide bond; Glycoprotein; Membrane;
Metal-binding; Oxidoreductase; Reference proteome; Signal-anchor; TPQ;
Transmembrane; Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:8520629}.
CHAIN 2 763 Membrane primary amine oxidase.
/FTId=PRO_0000064105.
TOPO_DOM 2 6 Cytoplasmic. {ECO:0000255}.
TRANSMEM 7 27 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 28 763 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 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}.
CONFLICT 54 54 P -> S (in Ref. 3; AAC53189).
{ECO:0000305}.
CONFLICT 329 329 Q -> R (in Ref. 1; BAD74047).
{ECO:0000305}.
CONFLICT 645 645 S -> F (in Ref. 1; BAD74047).
{ECO:0000305}.
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


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