ID   AOFB_MOUSE              Reviewed;         520 AA.
AC   Q8BW75; Q8C0B2;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 48.
DE   RecName: Full=Amine oxidase [flavin-containing] B;
DE            EC=1.4.3.4;
DE   AltName: Full=Monoamine oxidase type B;
DE            Short=MAO-B;
GN   Name=Maob;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata, and Oviduct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- FUNCTION: Catalyzes the oxidative deamination of biogenic and
CC       xenobiotic amines and has important functions in the metabolism of
CC       neuroactive and vasoactive amines in the central nervous system
CC       and peripheral tissues. MAOB preferentially degrades benzylamine
CC       and phenylethylamine (By similarity).
CC   -!- CATALYTIC ACTIVITY: RCH(2)NHR' + H(2)O + O(2) = RCHO + R'NH(2) +
CC       H(2)O(2).
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- SUBUNIT: Monomer, homo- or heterodimer (containing two subunits of
CC       similar size). Each subunit contains a covalently bound flavin.
CC       Enzymatically active as monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
CC       type IV membrane protein; Cytoplasmic side (By similarity).
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
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DR   EMBL; AK031833; BAC27571.1; -; mRNA.
DR   EMBL; AK054050; BAC35634.1; -; mRNA.
DR   IPI; IPI00226140; -.
DR   RefSeq; NP_766366.1; -.
DR   UniGene; Mm.241656; -.
DR   HSSP; P27338; 1GOS.
DR   SMR; Q8BW75; 2-500, 3-501.
DR   PhosphoSite; Q8BW75; -.
DR   PRIDE; Q8BW75; -.
DR   Ensembl; ENSMUSG00000040147; Mus musculus.
DR   GeneID; 109731; -.
DR   KEGG; mmu:109731; -.
DR   MGI; MGI:96916; Maob.
DR   HOGENOM; Q8BW75; -.
DR   HOVERGEN; Q8BW75; -.
DR   BRENDA; 1.4.3.4; 244.
DR   NextBio; 362651; -.
DR   ArrayExpress; Q8BW75; -.
DR   Bgee; Q8BW75; -.
DR   CleanEx; MM_MAOB; -.
DR   GermOnline; ENSMUSG00000040147; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008131; F:amine oxidase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001613; Amineoxid_fl.
DR   InterPro; IPR002937; Amino_oxidase.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   PRINTS; PR00757; AMINEOXDASEF.
PE   1: Evidence at protein level;
KW   Acetylation; FAD; Flavoprotein; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Oxidoreductase; Transmembrane.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    520       Amine oxidase [flavin-containing] B.
FT                                /FTId=PRO_0000099860.
FT   TOPO_DOM      2    489       Cytoplasmic (By similarity).
FT   TRANSMEM    490    516       Anchor for type IV membrane protein (By
FT                                similarity).
FT   TOPO_DOM    517    520       Mitochondrial intermembrane (By
FT                                similarity).
FT   COMPBIAS     36     52       Arg/Lys-rich (basic).
FT   SITE        156    156       Important for catalytic activity (By
FT                                similarity).
FT   SITE        365    365       Important for catalytic activity (By
FT                                similarity).
FT   SITE        382    382       Important for catalytic activity (By
FT                                similarity).
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES      52     52       N6-acetyllysine.
FT   MOD_RES     397    397       S-8alpha-FAD cysteine (By similarity).
FT   CONFLICT    408    408       S -> T (in Ref. 1; BAC27571).
FT   CONFLICT    482    482       L -> M (in Ref. 1; BAC27571).
SQ   SEQUENCE   520 AA;  58544 MW;  D7CD7EBBF5C4B837 CRC64;
     MSNKSDVIVV GGGISGMAAA KLLHDCGLSV VVLEARDRVG GRTYTIRNKN VKYVDLGGSY
     VGPTQNRILR LAKELGLETY KVNEVERLIH FVKGKSYAFR GPFPPVWNPI TYLDNNNLWR
     TMDEMGQEIP SDAPWKAPLA EEWDYMTMKE LLDKICWTKS TKQIATLFVN LCVTAETHEV
     SALWFLWYVK QCGGTTRIIS TTNGGQERKF IGGSGQVSER IKDILGDRVK LERPVIHIDQ
     TGENVIVKTL NHEIYEAKYV ISAIPPALGM KIHYSPPLPM LRNQLISRVP LGSVIKCMVY
     YKEPFWRKKD FCGTMVIEGE EAPIAYTLDD TKPDGTYAAI MGFILAHKAR KLVRLTKEER
     LRKLCELYAK VLNSQEALQP VHYEEKNWCE EQYSGGCYTT YFPPGILSQY GRVLRQPVGK
     IFFAGTETAS HWSGYMEGAV EAGERAAREI LHAIGKIPED EIWQPEPESL DVPARPITST
     FLERHLPSVP GLLKLFGLTT ILSATALGFL AHKRGLFVHF
//