AOFA_HUMAN
ID AOFA_HUMAN Reviewed; 527 AA.
AC P21397; B4DF46; Q16426;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 228.
DE RecName: Full=Amine oxidase [flavin-containing] A {ECO:0000305};
DE EC=1.4.3.21 {ECO:0000269|PubMed:18391214, ECO:0000269|PubMed:20493079, ECO:0000269|PubMed:24169519, ECO:0000269|PubMed:8316221};
DE EC=1.4.3.4 {ECO:0000269|PubMed:20493079};
DE AltName: Full=Monoamine oxidase type A;
DE Short=MAO-A;
GN Name=MAOA {ECO:0000312|HGNC:HGNC:6833};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3418353; DOI=10.1111/j.1471-4159.1988.tb03105.x;
RA Hsu Y.-P.P., Weyler W., Chen S., Sims K.B., Rinehart W.B., Utterback M.C.,
RA Powell J.F., Breakefield X.O.;
RT "Structural features of human monoamine oxidase A elucidated from cDNA and
RT peptide sequences.";
RL J. Neurochem. 51:1321-1324(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=3387449; DOI=10.1073/pnas.85.13.4934;
RA Bach A.W.J., Lan N.C., Johnson D.L., Abell C.W., Bembenek M.E., Kwan S.W.,
RA Seeburg P.H., Shih J.C.;
RT "cDNA cloning of human liver monoamine oxidase A and B: molecular basis of
RT differences in enzymatic properties.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:4934-4938(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1886775; DOI=10.1093/nar/19.16.4537;
RA Chen Z.-Y., Hotamisligil G.S., Huang J.-K., Wen L., Ezzeddine D.,
RA Aydin-Muderrisoglu N., Powell J.F., Huang R.H., Breakefield X.O., Craig I.,
RA Hsu Y.-P.P.;
RT "Structure of the human gene for monoamine oxidase type A.";
RL Nucleic Acids Res. 19:4537-4541(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2023912; DOI=10.1073/pnas.88.9.3637;
RA Grimsby J., Chen K., Wang L.J., Lan N.C., Shih J.C.;
RT "Human monoamine oxidase A and B genes exhibit identical exon-intron
RT organization.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:3637-3641(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
RX PubMed=1432104; DOI=10.1523/jneurosci.12-11-04437.1992;
RA Zhu Q.S., Grimsby J.S., Chen K., Shih J.C.;
RT "Promoter organization and activity of human monoamine oxidase (MAO) A and
RT B genes.";
RL J. Neurosci. 12:4437-4446(1992).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RX PubMed=8584674; DOI=10.1016/s0079-6123(08)61202-9;
RA Denney R.M.;
RT "The promoter of the human monoamine oxidase A gene.";
RL Prog. Brain Res. 106:57-66(1995).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
RX PubMed=7519662; DOI=10.1046/j.1471-4159.1994.63030843.x;
RA Denney R.M., Sharma A., Dave S.K., Waguespack A.;
RT "A new look at the promoter of the human monoamine oxidase A gene: mapping
RT transcription initiation sites and capacity to drive luciferase
RT expression.";
RL J. Neurochem. 63:843-856(1994).
RN [11]
RP PROTEIN SEQUENCE OF 31-45; 62-78; 109-129; 268-288; 298-315; 318-332;
RP 336-352; 372-412; 430-440 AND 458-493.
RC TISSUE=Placenta;
RX PubMed=3178846; DOI=10.1016/s0006-291x(88)80861-1;
RA Chen S.-Y., Weyler W.;
RT "Partial amino acid sequence analysis of human placenta monoamine oxidase A
RT and bovine liver monoamine oxidase B.";
RL Biochem. Biophys. Res. Commun. 156:445-450(1988).
RN [12]
RP PARTIAL PROTEIN SEQUENCE, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=11812236; DOI=10.1006/prep.2001.1546;
RA Li M., Hubalek F., Newton-Vinson P., Edmondson D.E.;
RT "High-level expression of human liver monoamine oxidase A in Pichia
RT pastoris: comparison with the enzyme expressed in Saccharomyces
RT cerevisiae.";
RL Protein Expr. Purif. 24:152-162(2002).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20493079; DOI=10.1016/0197-0186(86)90182-8;
RA O'Carroll A.M., Bardsley M.E., Tipton K.F.;
RT "The oxidation of adrenaline and noradrenaline by the two forms of
RT monoamine oxidase from human and rat brain.";
RL Neurochem. Int. 8:493-500(1986).
RN [14]
RP DETERMINATION OF PROTEIN-FAD RATIO.
RC TISSUE=Placenta;
RX PubMed=2764901; DOI=10.1042/bj2600725;
RA Weyler W.;
RT "Monoamine oxidase A from human placenta and monoamine oxidase B from
RT bovine liver both have one FAD per subunit.";
RL Biochem. J. 260:725-729(1989).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF CYS-165; CYS-266; CYS-306; CYS-321; CYS-323; CYS-374;
RP CYS-398 AND CYS-406.
RX PubMed=8316221;
RA Wu H.F., Chen K., Shih J.C.;
RT "Site-directed mutagenesis of monoamine oxidase A and B: role of
RT cysteines.";
RL Mol. Pharmacol. 43:888-893(1993).
RN [16]
RP INVOLVEMENT IN BRNRS.
RX PubMed=8211186; DOI=10.1126/science.8211186;
RA Brunner H.G., Nelen M., Breakefield X.O., Ropers H.-H., van Oost B.A.;
RT "Abnormal behavior associated with a point mutation in the structural gene
RT for monoamine oxidase A.";
RL Science 262:578-580(1993).
RN [17]
RP POLYMORPHISM IN THE PROMOTER REGION.
RX PubMed=9799080; DOI=10.1007/s004390050816;
RA Sabol S.Z., Hu S., Hamer D.;
RT "A functional polymorphism in the monoamine oxidase A gene promoter.";
RL Hum. Genet. 103:273-279(1998).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), COFACTOR, AND SUBUNIT.
RX PubMed=16129825; DOI=10.1073/pnas.0505975102;
RA De Colibus L., Li M., Binda C., Lustig A., Edmondson D.E., Mattevi A.;
RT "Three-dimensional structure of human monoamine oxidase A (MAO A): relation
RT to the structures of rat MAO A and human MAO B.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12684-12689(2005).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF 12-524 IN COMPLEX WITH FAD AND
RP THE INHIBITOR HARMINE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TOPOLOGY.
RX PubMed=18391214; DOI=10.1073/pnas.0710626105;
RA Son S.-Y., Ma J., Kondou Y., Yoshimura M., Yamashita E., Tsukihara T.;
RT "Structure of human monoamine oxidase A at 2.2-A resolution: the control of
RT opening the entry for substrates/inhibitors.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:5739-5744(2008).
RN [21]
RP VARIANT [LARGE SCALE ANALYSIS] GLU-15.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [22]
RP VARIANT LYS-188.
RX PubMed=21179162; DOI=10.1038/nature09629;
RA Bevilacqua L., Doly S., Kaprio J., Yuan Q., Tikkanen R., Paunio T.,
RA Zhou Z., Wedenoja J., Maroteaux L., Diaz S., Belmer A., Hodgkinson C.A.,
RA Dell'osso L., Suvisaari J., Coccaro E., Rose R.J., Peltonen L.,
RA Virkkunen M., Goldman D.;
RT "A population-specific HTR2B stop codon predisposes to severe
RT impulsivity.";
RL Nature 468:1061-1066(2010).
RN [23]
RP VARIANT PHE-266, FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION OF
RP VARIANT PHE-266.
RX PubMed=24169519; DOI=10.1038/ejhg.2013.243;
RA Piton A., Poquet H., Redin C., Masurel A., Lauer J., Muller J.,
RA Thevenon J., Herenger Y., Chancenotte S., Bonnet M., Pinoit J.M., Huet F.,
RA Thauvin-Robinet C., Jaeger A.S., Le Gras S., Jost B., Gerard B., Peoc'h K.,
RA Launay J.M., Faivre L., Mandel J.L.;
RT "20 ans apres: a second mutation in MAOA identified by targeted high-
RT throughput sequencing in a family with altered behavior and cognition.";
RL Eur. J. Hum. Genet. 22:776-783(2014).
CC -!- FUNCTION: Catalyzes the oxidative deamination of primary and some
CC secondary amine such as neurotransmitters, with concomitant reduction
CC of oxygen to hydrogen peroxide and has important functions in the
CC metabolism of neuroactive and vasoactive amines in the central nervous
CC system and peripheral tissues (PubMed:20493079, PubMed:8316221,
CC PubMed:18391214, PubMed:24169519). Preferentially oxidizes serotonin
CC (PubMed:20493079, PubMed:24169519). Also catalyzes the oxidative
CC deamination of kynuramine to 3-(2-aminophenyl)-3-oxopropanal that can
CC spontaneously condense to 4-hydroxyquinoline (By similarity).
CC {ECO:0000250|UniProtKB:P21396, ECO:0000269|PubMed:18391214,
CC ECO:0000269|PubMed:20493079, ECO:0000269|PubMed:24169519,
CC ECO:0000269|PubMed:8316221}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary aliphatic amine + H2O + O2 = a primary amine + an
CC aldehyde + H2O2; Xref=Rhea:RHEA:26414, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478,
CC ChEBI:CHEBI:58855, ChEBI:CHEBI:65296; EC=1.4.3.4;
CC Evidence={ECO:0000269|PubMed:20493079};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-adrenaline + H2O + O2 = (R)-3,4-dihydroxymandelaldehyde +
CC H2O2 + methylamine; Xref=Rhea:RHEA:51168, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:59338,
CC ChEBI:CHEBI:71406, ChEBI:CHEBI:180943;
CC Evidence={ECO:0000269|PubMed:20493079};
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:0000269|PubMed:18391214, ECO:0000269|PubMed:20493079,
CC ECO:0000269|PubMed:24169519, ECO:0000269|PubMed:8316221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dopamine + H2O + O2 = 3,4-dihydroxyphenylacetaldehyde + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:27946, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:27978, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:59905; Evidence={ECO:0000269|PubMed:20493079};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + tyramine = (4-hydroxyphenyl)acetaldehyde + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:30591, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15621, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:327995; Evidence={ECO:0000269|PubMed:20493079};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-noradrenaline + H2O + O2 = (R)-3,4-dihydroxymandelaldehyde
CC + H2O2 + NH4(+); Xref=Rhea:RHEA:69076, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:72587, ChEBI:CHEBI:180943;
CC Evidence={ECO:0000269|PubMed:20493079};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + serotonin = (5-hydroxyindol-3-yl)acetaldehyde +
CC H2O2 + NH4(+); Xref=Rhea:RHEA:69072, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:50157, ChEBI:CHEBI:350546;
CC Evidence={ECO:0000269|PubMed:20493079, ECO:0000269|PubMed:24169519,
CC ECO:0000269|PubMed:8316221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + kynuramine + O2 = 3-(2-aminophenyl)-3-oxopropanal + H2O2
CC + NH4(+); Xref=Rhea:RHEA:59596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:180898,
CC ChEBI:CHEBI:180899; Evidence={ECO:0000269|PubMed:18391214};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59597;
CC Evidence={ECO:0000305|PubMed:18391214};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + tryptamine = H2O2 + indole-3-acetaldehyde + NH4(+);
CC Xref=Rhea:RHEA:59416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:18086, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57887; Evidence={ECO:0000250|UniProtKB:P21396};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-phenylethylamine + H2O + O2 = 2-phenylacetaldehyde + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:25265, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16424, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:225237; Evidence={ECO:0000250|UniProtKB:P21396};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:16129825, ECO:0000269|PubMed:18391214};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=208 uM for (R)-adrenaline {ECO:0000269|PubMed:20493079};
CC KM=212 uM for dopamine {ECO:0000269|PubMed:20493079};
CC KM=137 uM for serotonin {ECO:0000269|PubMed:20493079};
CC KM=284 uM for (R)-noradrenaline {ECO:0000269|PubMed:20493079};
CC KM=140 uM for 2-phenylethylamine {ECO:0000269|PubMed:20493079};
CC KM=127 uM for tyramine {ECO:0000269|PubMed:20493079};
CC KM=127 uM for serotonin {ECO:0000269|PubMed:8316221};
CC KM=0.117 mM for kynuramine (with the detergent-solubilized form)
CC {ECO:0000269|PubMed:18391214};
CC KM=0.044 mM for kynuramine (with the membrane-bound form)
CC {ECO:0000269|PubMed:18391214};
CC Vmax=379 pmol/min/mg enzyme toward (R)-adrenaline
CC {ECO:0000269|PubMed:20493079};
CC Vmax=680 pmol/min/mg enzyme toward dopamine
CC {ECO:0000269|PubMed:20493079};
CC Vmax=228 pmol/min/mg enzyme toward serotonin
CC {ECO:0000269|PubMed:20493079};
CC Vmax=561 pmol/min/mg enzyme toward (R)-noradrenaline
CC {ECO:0000269|PubMed:20493079};
CC Vmax=20 pmol/min/mg enzyme toward 2-phenylethylamine
CC {ECO:0000269|PubMed:20493079};
CC Vmax=182 pmol/min/mg enzyme toward tyramine
CC {ECO:0000269|PubMed:20493079};
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. {ECO:0000269|PubMed:16129825,
CC ECO:0000269|PubMed:18391214}.
CC -!- INTERACTION:
CC P21397; P27338: MAOB; NbExp=2; IntAct=EBI-1190845, EBI-3911344;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:P21396}; Single-pass type IV membrane protein
CC {ECO:0000250|UniProtKB:P21396}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P21396}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P21397-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P21397-2; Sequence=VSP_045173;
CC -!- TISSUE SPECIFICITY: Heart, liver, duodenum, blood vessels and kidney.
CC -!- MASS SPECTROMETRY: Mass=60512; Mass_error=6; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11812236};
CC -!- POLYMORPHISM: A polymorphism 1.2 kb upstream of the MAOA coding
CC sequences consists of a 30-bp repeated sequence present in 3, 3.5, 4,
CC or 5 copies. The polymorphism affect transcriptional activity of the
CC MAOA gene promoter. Alleles with 3.5 or 4 copies of the repeat sequence
CC are transcribed 2 to 10 times more efficiently than those with 3 or 5
CC copies of the repeat.
CC -!- DISEASE: Brunner syndrome (BRNRS) [MIM:300615]: A form of X-linked non-
CC dysmorphic mild intellectual disability. Male patients are affected by
CC borderline intellectual deficit and exhibit abnormal behavior,
CC including disturbed regulation of impulsive aggression. Obligate female
CC carriers have normal intelligence and behavior.
CC {ECO:0000269|PubMed:8211186}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Monoamine oxidase entry;
CC URL="https://en.wikipedia.org/wiki/Monoamine_oxidase";
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Approaching happiness
CC - Issue 172 of August 2015;
CC URL="https://web.expasy.org/spotlight/back_issues/172/";
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DR EMBL; M69226; AAA59549.1; -; mRNA.
DR EMBL; M68840; AAA59548.1; -; mRNA.
DR EMBL; X60806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X60807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X60808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X60809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X60810; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X60811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X60812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X60813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X60814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X60815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X60816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X60817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X60818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X60819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M68857; AAA59547.1; -; Genomic_DNA.
DR EMBL; M68843; AAA59547.1; JOINED; Genomic_DNA.
DR EMBL; M68844; AAA59547.1; JOINED; Genomic_DNA.
DR EMBL; M68845; AAA59547.1; JOINED; Genomic_DNA.
DR EMBL; M68846; AAA59547.1; JOINED; Genomic_DNA.
DR EMBL; M68847; AAA59547.1; JOINED; Genomic_DNA.
DR EMBL; M68848; AAA59547.1; JOINED; Genomic_DNA.
DR EMBL; M68849; AAA59547.1; JOINED; Genomic_DNA.
DR EMBL; M68850; AAA59547.1; JOINED; Genomic_DNA.
DR EMBL; M68851; AAA59547.1; JOINED; Genomic_DNA.
DR EMBL; M68852; AAA59547.1; JOINED; Genomic_DNA.
DR EMBL; M68853; AAA59547.1; JOINED; Genomic_DNA.
DR EMBL; M68854; AAA59547.1; JOINED; Genomic_DNA.
DR EMBL; M68855; AAA59547.1; JOINED; Genomic_DNA.
DR EMBL; M68856; AAA59547.1; JOINED; Genomic_DNA.
DR EMBL; AK293926; BAG57307.1; -; mRNA.
DR EMBL; AL109855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX530072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX537147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX537148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008064; AAH08064.1; -; mRNA.
DR EMBL; M89636; AAB46385.1; -; Genomic_DNA.
DR EMBL; S81371; AAD14361.1; -; Genomic_DNA.
DR EMBL; S72704; AAD14113.1; -; Genomic_DNA.
DR CCDS; CCDS14260.1; -. [P21397-1]
DR CCDS; CCDS59163.1; -. [P21397-2]
DR PIR; A36175; A36175.
DR RefSeq; NP_000231.1; NM_000240.3. [P21397-1]
DR RefSeq; NP_001257387.1; NM_001270458.1. [P21397-2]
DR PDB; 2BXR; X-ray; 3.00 A; A/B=1-527.
DR PDB; 2BXS; X-ray; 3.15 A; A/B=1-527.
DR PDB; 2Z5X; X-ray; 2.20 A; A=12-524.
DR PDB; 2Z5Y; X-ray; 2.17 A; A=12-524.
DR PDBsum; 2BXR; -.
DR PDBsum; 2BXS; -.
DR PDBsum; 2Z5X; -.
DR PDBsum; 2Z5Y; -.
DR AlphaFoldDB; P21397; -.
DR SMR; P21397; -.
DR BioGRID; 110301; 12.
DR IntAct; P21397; 6.
DR MINT; P21397; -.
DR STRING; 9606.ENSP00000340684; -.
DR BindingDB; P21397; -.
DR ChEMBL; CHEMBL1951; -.
DR DrugBank; DB01472; 4-Methoxyamphetamine.
DR DrugBank; DB00918; Almotriptan.
DR DrugBank; DB00182; Amphetamine.
DR DrugBank; DB06698; Betahistine.
DR DrugBank; DB04889; Bicifadine.
DR DrugBank; DB13876; Brofaromine.
DR DrugBank; DB01445; Bufotenine.
DR DrugBank; DB06774; Capsaicin.
DR DrugBank; DB04017; Clorgiline.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB05205; CX157.
DR DrugBank; DB07641; Decyl(dimethyl)phosphine oxide.
DR DrugBank; DB00988; Dopamine.
DR DrugBank; DB01363; Ephedra sinica root.
DR DrugBank; DB00668; Epinephrine.
DR DrugBank; DB12329; Eravacycline.
DR DrugBank; DB01175; Escitalopram.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR DrugBank; DB14914; Flortaucipir F-18.
DR DrugBank; DB00614; Furazolidone.
DR DrugBank; DB01381; Ginkgo biloba.
DR DrugBank; DB07919; Harmine.
DR DrugBank; DB04818; Iproniazid.
DR DrugBank; DB01247; Isocarboxazid.
DR DrugBank; DB00601; Linezolid.
DR DrugBank; DB01577; Metamfetamine.
DR DrugBank; DB00805; Minaprine.
DR DrugBank; DB01442; MMDA.
DR DrugBank; DB01171; Moclobemide.
DR DrugBank; DB08804; Nandrolone decanoate.
DR DrugBank; DB00952; Naratriptan.
DR DrugBank; DB04820; Nialamide.
DR DrugBank; DB00184; Nicotine.
DR DrugBank; DB04821; Nomifensine.
DR DrugBank; DB06412; Oxymetholone.
DR DrugBank; DB01626; Pargyline.
DR DrugBank; DB00780; Phenelzine.
DR DrugBank; DB00191; Phentermine.
DR DrugBank; DB00388; Phenylephrine.
DR DrugBank; DB00397; Phenylpropanolamine.
DR DrugBank; DB09244; Pirlindole.
DR DrugBank; DB04850; Posizolid.
DR DrugBank; DB00721; Procaine.
DR DrugBank; DB01168; Procarbazine.
DR DrugBank; DB00571; Propranolol.
DR DrugBank; DB00852; Pseudoephedrine.
DR DrugBank; DB09363; Rauwolfia serpentina root.
DR DrugBank; DB00140; Riboflavin.
DR DrugBank; DB00953; Rizatriptan.
DR DrugBank; DB06654; Safinamide.
DR DrugBank; DB01037; Selegiline.
DR DrugBank; DB01104; Sertraline.
DR DrugBank; DB00669; Sumatriptan.
DR DrugBank; DB14569; Tedizolid.
DR DrugBank; DB09042; Tedizolid phosphate.
DR DrugBank; DB00624; Testosterone.
DR DrugBank; DB13943; Testosterone cypionate.
DR DrugBank; DB13944; Testosterone enanthate.
DR DrugBank; DB13946; Testosterone undecanoate.
DR DrugBank; DB09245; Toloxatone.
DR DrugBank; DB00752; Tranylcypromine.
DR DrugBank; DB15328; Ubrogepant.
DR DrugBank; DB04832; Zimelidine.
DR DrugBank; DB00315; Zolmitriptan.
DR DrugBank; DB00909; Zonisamide.
DR DrugCentral; P21397; -.
DR GuidetoPHARMACOLOGY; 2489; -.
DR iPTMnet; P21397; -.
DR PhosphoSitePlus; P21397; -.
DR SwissPalm; P21397; -.
DR BioMuta; MAOA; -.
DR DMDM; 113978; -.
DR EPD; P21397; -.
DR jPOST; P21397; -.
DR MassIVE; P21397; -.
DR MaxQB; P21397; -.
DR PaxDb; P21397; -.
DR PeptideAtlas; P21397; -.
DR PRIDE; P21397; -.
DR ProteomicsDB; 4005; -.
DR ProteomicsDB; 53866; -. [P21397-1]
DR Antibodypedia; 10933; 470 antibodies from 40 providers.
DR DNASU; 4128; -.
DR Ensembl; ENST00000338702.4; ENSP00000340684.3; ENSG00000189221.11. [P21397-1]
DR Ensembl; ENST00000542639.6; ENSP00000440846.1; ENSG00000189221.11. [P21397-2]
DR Ensembl; ENST00000688006.1; ENSP00000510311.1; ENSG00000189221.11. [P21397-2]
DR Ensembl; ENST00000689087.1; ENSP00000508997.1; ENSG00000189221.11. [P21397-2]
DR GeneID; 4128; -.
DR KEGG; hsa:4128; -.
DR MANE-Select; ENST00000338702.4; ENSP00000340684.3; NM_000240.4; NP_000231.1.
DR UCSC; uc011mkw.3; human. [P21397-1]
DR CTD; 4128; -.
DR DisGeNET; 4128; -.
DR GeneCards; MAOA; -.
DR HGNC; HGNC:6833; MAOA.
DR HPA; ENSG00000189221; Tissue enhanced (intestine).
DR MalaCards; MAOA; -.
DR MIM; 300615; phenotype.
DR MIM; 309850; gene.
DR neXtProt; NX_P21397; -.
DR OpenTargets; ENSG00000189221; -.
DR Orphanet; 3057; Monoamine oxidase A deficiency.
DR PharmGKB; PA236; -.
DR VEuPathDB; HostDB:ENSG00000189221; -.
DR eggNOG; KOG0029; Eukaryota.
DR GeneTree; ENSGT00940000160514; -.
DR HOGENOM; CLU_004498_0_1_1; -.
DR InParanoid; P21397; -.
DR OMA; EWTRGAY; -.
DR PhylomeDB; P21397; -.
DR TreeFam; TF313314; -.
DR BioCyc; MetaCyc:HS01798-MON; -.
DR BRENDA; 1.4.3.4; 2681.
DR PathwayCommons; P21397; -.
DR Reactome; R-HSA-141333; Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.
DR Reactome; R-HSA-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-HSA-379397; Enzymatic degradation of dopamine by COMT.
DR Reactome; R-HSA-379398; Enzymatic degradation of Dopamine by monoamine oxidase.
DR Reactome; R-HSA-380612; Metabolism of serotonin.
DR Reactome; R-HSA-5579012; Defective MAOA causes BRUNS.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR SABIO-RK; P21397; -.
DR SignaLink; P21397; -.
DR SIGNOR; P21397; -.
DR BioGRID-ORCS; 4128; 7 hits in 700 CRISPR screens.
DR ChiTaRS; MAOA; human.
DR EvolutionaryTrace; P21397; -.
DR GeneWiki; Monoamine_oxidase_A; -.
DR GenomeRNAi; 4128; -.
DR Pharos; P21397; Tclin.
DR PRO; PR:P21397; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P21397; protein.
DR Bgee; ENSG00000189221; Expressed in ileal mucosa and 199 other tissues.
DR ExpressionAtlas; P21397; baseline and differential.
DR Genevisible; P21397; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:ParkinsonsUK-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:RHEA.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0097621; F:monoamine oxidase activity; IDA:UniProtKB.
DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:RHEA.
DR GO; GO:0008131; F:primary amine oxidase activity; IDA:UniProtKB.
DR GO; GO:0006576; P:cellular biogenic amine metabolic process; TAS:ProtInc.
DR GO; GO:0042420; P:dopamine catabolic process; TAS:ParkinsonsUK-UCL.
DR GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009967; P:positive regulation of signal transduction; IEA:Ensembl.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Catecholamine metabolism;
KW Direct protein sequencing; Disease variant; FAD; Flavoprotein;
KW Intellectual disability; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Neurotransmitter degradation; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..527
FT /note="Amine oxidase [flavin-containing] A"
FT /id="PRO_0000099850"
FT TOPO_DOM 1..497
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:18391214"
FT TRANSMEM 498..518
FT /note="Helical; Anchor for type IV membrane protein"
FT TOPO_DOM 519..527
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:18391214"
FT REGION 520..522
FT /note="Interaction with membrane phospholipid headgroups"
FT /evidence="ECO:0000305"
FT SITE 335
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000250"
FT SITE 374
FT /note="Important for catalytic activity"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:11812236"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21396"
FT MOD_RES 406
FT /note="S-8alpha-FAD cysteine"
FT /evidence="ECO:0000269|PubMed:18391214,
FT ECO:0007744|PDB:2BXR, ECO:0007744|PDB:2BXS,
FT ECO:0007744|PDB:2Z5X, ECO:0007744|PDB:2Z5Y"
FT VAR_SEQ 1..133
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045173"
FT VARIANT 15
FT /note="D -> E (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036545"
FT VARIANT 188
FT /note="E -> K (in dbSNP:rs77698881)"
FT /evidence="ECO:0000269|PubMed:21179162"
FT /id="VAR_064573"
FT VARIANT 266
FT /note="C -> F (probable disease-associated variant found in
FT a family with Brunner syndrome-like behavioral
FT disturbances; reduced activity; dbSNP:rs587777457)"
FT /evidence="ECO:0000269|PubMed:24169519"
FT /id="VAR_071963"
FT VARIANT 314
FT /note="F -> V (in dbSNP:rs1799835)"
FT /id="VAR_014795"
FT VARIANT 520
FT /note="K -> R (in dbSNP:rs1800466)"
FT /id="VAR_014796"
FT MUTAGEN 165
FT /note="C->S: No loss of activity."
FT /evidence="ECO:0000269|PubMed:8316221"
FT MUTAGEN 266
FT /note="C->S: No loss of activity."
FT /evidence="ECO:0000269|PubMed:8316221"
FT MUTAGEN 306
FT /note="C->S: No loss of activity."
FT /evidence="ECO:0000269|PubMed:8316221"
FT MUTAGEN 321
FT /note="C->S: No loss of activity."
FT /evidence="ECO:0000269|PubMed:8316221"
FT MUTAGEN 323
FT /note="C->S: No loss of activity."
FT /evidence="ECO:0000269|PubMed:8316221"
FT MUTAGEN 374
FT /note="C->S: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:8316221"
FT MUTAGEN 398
FT /note="C->S: No loss of activity."
FT /evidence="ECO:0000269|PubMed:8316221"
FT MUTAGEN 406
FT /note="C->S: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:8316221"
FT CONFLICT 397
FT /note="W -> M (in Ref. 11; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:2Z5X"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT HELIX 118..136
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT HELIX 157..164
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT HELIX 168..182
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT HELIX 191..199
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT HELIX 204..208
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:2BXS"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT HELIX 224..234
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT STRAND 250..258
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT STRAND 263..271
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT HELIX 289..295
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT STRAND 303..309
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT STRAND 320..327
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT STRAND 334..338
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT STRAND 348..354
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT HELIX 355..361
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT HELIX 366..381
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT STRAND 390..397
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT HELIX 415..418
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT HELIX 445..462
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:2BXS"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT HELIX 490..494
FT /evidence="ECO:0007829|PDB:2Z5Y"
FT HELIX 498..520
FT /evidence="ECO:0007829|PDB:2Z5Y"
SQ SEQUENCE 527 AA; 59682 MW; 4270E346928AE832 CRC64;
MENQEKASIA GHMFDVVVIG GGISGLSAAK LLTEYGVSVL VLEARDRVGG RTYTIRNEHV
DYVDVGGAYV GPTQNRILRL SKELGIETYK VNVSERLVQY VKGKTYPFRG AFPPVWNPIA
YLDYNNLWRT IDNMGKEIPT DAPWEAQHAD KWDKMTMKEL IDKICWTKTA RRFAYLFVNI
NVTSEPHEVS ALWFLWYVKQ CGGTTRIFSV TNGGQERKFV GGSGQVSERI MDLLGDQVKL
NHPVTHVDQS SDNIIIETLN HEHYECKYVI NAIPPTLTAK IHFRPELPAE RNQLIQRLPM
GAVIKCMMYY KEAFWKKKDY CGCMIIEDED APISITLDDT KPDGSLPAIM GFILARKADR
LAKLHKEIRK KKICELYAKV LGSQEALHPV HYEEKNWCEE QYSGGCYTAY FPPGIMTQYG
RVIRQPVGRI FFAGTETATK WSGYMEGAVE AGERAAREVL NGLGKVTEKD IWVQEPESKD
VPAVEITHTF WERNLPSVSG LLKIIGFSTS VTALGFVLYK YKLLPRS
