AOFA_RAT
ID AOFA_RAT Reviewed; 526 AA.
AC P21396; Q63817;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Amine oxidase [flavin-containing] A {ECO:0000305};
DE EC=1.4.3.21 {ECO:0000269|PubMed:18391214, ECO:0000269|PubMed:20493079};
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|RGD:61898};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1368522; DOI=10.1271/bbb1961.54.253;
RA Kuwahara T., Takamoto S., Ito A.;
RT "Primary structure of rat monoamine oxidase A deduced from cDNA and its
RT expression in rat tissues.";
RL Agric. Biol. Chem. 54:253-257(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-526.
RC TISSUE=Liver;
RX PubMed=1526120; DOI=10.1016/0305-0491(92)90286-z;
RA Kwan S.W., Abell C.W.;
RT "cDNA cloning and sequencing of rat monoamine oxidase A: comparison with
RT the human and bovine enzymes.";
RL Comp. Biochem. Physiol. 102B:143-147(1992).
RN [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF PHE-208.
RX PubMed=9162023; DOI=10.1074/jbc.272.22.14033;
RA Tsugeno Y., Ito A.;
RT "A key amino acid responsible for substrate selectivity of monoamine
RT oxidase A and B.";
RL J. Biol. Chem. 272:14033-14036(1997).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH INHIBITOR, SUBUNIT,
RP COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=15050826; DOI=10.1016/j.jmb.2004.02.032;
RA Ma J., Yoshimura M., Yamashita E., Nakagawa A., Ito A., Tsukihara T.;
RT "Structure of rat monoamine oxidase A and its specific recognitions for
RT substrates and inhibitors.";
RL J. Mol. Biol. 338:103-114(2004).
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:18391214, PubMed:9162023).
CC Preferentially oxidizes serotonin (PubMed:20493079). Also catalyzes the
CC oxidative deamination of kynuramine to 3-(2-aminophenyl)-3-oxopropanal
CC that can spontaneously condense to 4-hydroxyquinoline
CC (PubMed:18391214). {ECO:0000269|PubMed:18391214,
CC ECO:0000269|PubMed:20493079, ECO:0000269|PubMed:9162023}.
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=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:9162023};
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=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 ECO:0000269|PubMed:9162023};
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:9162023};
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:0000269|PubMed:9162023};
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:0000269|PubMed:20493079,
CC ECO:0000269|PubMed:9162023};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:15050826};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=610 uM for (R)-adrenaline {ECO:0000269|PubMed:20493079};
CC KM=150 uM for dopamine {ECO:0000269|PubMed:20493079};
CC KM=340 uM for serotonin {ECO:0000269|PubMed:20493079};
CC KM=582 uM for (R)-noradrenaline {ECO:0000269|PubMed:20493079};
CC KM=327 uM for 2-phenylethylamine {ECO:0000269|PubMed:20493079};
CC KM=116 uM for tyramine {ECO:0000269|PubMed:20493079};
CC KM=0.096 mM for kynuramine (with the detergent-solubilized form)
CC {ECO:0000269|PubMed:18391214};
CC KM=0.026 mM for kynuramine (with the membrane-bound form)
CC {ECO:0000269|PubMed:18391214};
CC KM=0.31 mM for serotonin {ECO:0000269|PubMed:9162023};
CC KM=0.40 mM for tyramine {ECO:0000269|PubMed:9162023};
CC KM=0.23 mM for tryptamine {ECO:0000269|PubMed:20493079};
CC KM=0.24 mM for 2-phenylethylamine {ECO:0000269|PubMed:20493079};
CC Vmax=558 pmol/min/mg enzyme toward (R)-adrenaline
CC {ECO:0000269|PubMed:20493079};
CC Vmax=889 pmol/min/mg enzyme toward dopamine
CC {ECO:0000269|PubMed:20493079};
CC Vmax=997 pmol/min/mg enzyme toward serotonin
CC {ECO:0000269|PubMed:20493079};
CC Vmax=1213 pmol/min/mg enzyme toward (R)-noradrenaline
CC {ECO:0000269|PubMed:20493079};
CC Vmax=53 pmol/min/mg enzyme toward 2-phenylethylamine
CC {ECO:0000269|PubMed:20493079};
CC Vmax=258 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 (By similarity).
CC {ECO:0000250|UniProtKB:P21397}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:15050826}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:15050826}; Cytoplasmic side
CC {ECO:0000269|PubMed:15050826}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
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; D00688; BAA00592.1; -; mRNA.
DR EMBL; S45812; AAB23355.2; -; mRNA.
DR PIR; JT0528; JT0528.
DR PDB; 1O5W; X-ray; 3.20 A; A/B/C/D=1-526.
DR PDBsum; 1O5W; -.
DR AlphaFoldDB; P21396; -.
DR SMR; P21396; -.
DR IntAct; P21396; 1.
DR MINT; P21396; -.
DR STRING; 10116.ENSRNOP00000063784; -.
DR BindingDB; P21396; -.
DR ChEMBL; CHEMBL3358; -.
DR DrugCentral; P21396; -.
DR iPTMnet; P21396; -.
DR PhosphoSitePlus; P21396; -.
DR jPOST; P21396; -.
DR PaxDb; P21396; -.
DR PRIDE; P21396; -.
DR UCSC; RGD:61898; rat.
DR RGD; 61898; Maoa.
DR eggNOG; KOG0029; Eukaryota.
DR InParanoid; P21396; -.
DR PhylomeDB; P21396; -.
DR BioCyc; MetaCyc:MON-14994; -.
DR BRENDA; 1.4.3.4; 5301.
DR Reactome; R-RNO-141333; Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.
DR Reactome; R-RNO-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-379397; Enzymatic degradation of dopamine by COMT.
DR Reactome; R-RNO-379398; Enzymatic degradation of Dopamine by monoamine oxidase.
DR Reactome; R-RNO-380612; Metabolism of serotonin.
DR SABIO-RK; P21396; -.
DR EvolutionaryTrace; P21396; -.
DR PRO; PR:P21396; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:RHEA.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:RGD.
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:0051378; F:serotonin binding; IDA:RGD.
DR GO; GO:0042424; P:catecholamine catabolic process; NAS:RGD.
DR GO; GO:0042420; P:dopamine catabolic process; ISO:RGD.
DR GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042443; P:phenylethylamine metabolic process; IDA:RGD.
DR GO; GO:0009967; P:positive regulation of signal transduction; ISO:RGD.
DR GO; GO:0042428; P:serotonin metabolic process; IDA:RGD.
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; Catecholamine metabolism; FAD; Flavoprotein;
KW Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Neurotransmitter degradation; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..526
FT /note="Amine oxidase [flavin-containing] A"
FT /id="PRO_0000099854"
FT TOPO_DOM 1..497
FT /note="Cytoplasmic"
FT TRANSMEM 498..518
FT /note="Helical; Anchor for type IV membrane protein"
FT TOPO_DOM 519..526
FT /note="Mitochondrial intermembrane"
FT REGION 520..522
FT /note="Interaction with membrane phospholipid headgroups"
FT /evidence="ECO:0000250"
FT SITE 335
FT /note="Important for substrate specificity"
FT SITE 374
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P21397"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 406
FT /note="S-8alpha-FAD cysteine"
FT MUTAGEN 208
FT /note="F->A: Lower affinity for serotonin and tyramine; no
FT change for tryptamine."
FT /evidence="ECO:0000269|PubMed:9162023"
FT MUTAGEN 208
FT /note="F->I: Lower affinity for serotonin and tyramine; no
FT change for tryptamine."
FT /evidence="ECO:0000269|PubMed:9162023"
FT MUTAGEN 208
FT /note="F->V: Lower affinity for serotonin and tyramine; no
FT change for tryptamine."
FT /evidence="ECO:0000269|PubMed:9162023"
FT MUTAGEN 208
FT /note="F->Y: No change in substrate affinity."
FT /evidence="ECO:0000269|PubMed:9162023"
FT CONFLICT 17..18
FT /note="GL -> VV (in Ref. 2; AAB23355)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="Q -> L (in Ref. 2; AAB23355)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="C -> S (in Ref. 2; AAB23355)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="A -> R (in Ref. 2; AAB23355)"
FT /evidence="ECO:0000305"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:1O5W"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:1O5W"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1O5W"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:1O5W"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:1O5W"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1O5W"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:1O5W"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1O5W"
FT STRAND 94..103
FT /evidence="ECO:0007829|PDB:1O5W"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:1O5W"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1O5W"
FT HELIX 118..136
FT /evidence="ECO:0007829|PDB:1O5W"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1O5W"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:1O5W"
FT HELIX 157..164
FT /evidence="ECO:0007829|PDB:1O5W"
FT HELIX 168..182
FT /evidence="ECO:0007829|PDB:1O5W"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:1O5W"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:1O5W"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:1O5W"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:1O5W"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:1O5W"
FT HELIX 225..232
FT /evidence="ECO:0007829|PDB:1O5W"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:1O5W"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:1O5W"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:1O5W"
FT STRAND 250..261
FT /evidence="ECO:0007829|PDB:1O5W"
FT STRAND 263..271
FT /evidence="ECO:0007829|PDB:1O5W"
FT HELIX 275..280
FT /evidence="ECO:0007829|PDB:1O5W"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:1O5W"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:1O5W"
FT STRAND 303..309
FT /evidence="ECO:0007829|PDB:1O5W"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:1O5W"
FT STRAND 320..327
FT /evidence="ECO:0007829|PDB:1O5W"
FT STRAND 334..338
FT /evidence="ECO:0007829|PDB:1O5W"
FT STRAND 348..354
FT /evidence="ECO:0007829|PDB:1O5W"
FT HELIX 355..362
FT /evidence="ECO:0007829|PDB:1O5W"
FT HELIX 366..381
FT /evidence="ECO:0007829|PDB:1O5W"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:1O5W"
FT STRAND 390..396
FT /evidence="ECO:0007829|PDB:1O5W"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:1O5W"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:1O5W"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:1O5W"
FT TURN 413..415
FT /evidence="ECO:0007829|PDB:1O5W"
FT HELIX 416..419
FT /evidence="ECO:0007829|PDB:1O5W"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:1O5W"
FT STRAND 428..432
FT /evidence="ECO:0007829|PDB:1O5W"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:1O5W"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:1O5W"
FT HELIX 445..461
FT /evidence="ECO:0007829|PDB:1O5W"
FT TURN 462..464
FT /evidence="ECO:0007829|PDB:1O5W"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:1O5W"
FT HELIX 490..494
FT /evidence="ECO:0007829|PDB:1O5W"
FT HELIX 498..519
FT /evidence="ECO:0007829|PDB:1O5W"
SQ SEQUENCE 526 AA; 59508 MW; 381AE35D5A73E25B CRC64;
MTDLEKPNLA GHMFDVGLIG GGISGLAAAK LLSEYKINVL VLEARDRVGG RTYTVRNEHV
KWVDVGGAYV GPTQNRILRL SKELGIETYK VNVNERLVQY VKGKTYPFRG AFPPVWNPLA
YLDYNNLWRT MDEMGKEIPV DAPWQARHAQ EWDKMTMKDL IDKICWTKTA REFAYLFVNI
NVTSEPHEVS ALWFLWYVRQ CGGTARIFSV TNGGQERKFV GGSGQVSEQI MGLLGDKVKL
SSPVTYIDQT DDNIIVETLN HEHYECKYVI SAIPPILTAK IHFKPELPPE RNQLIQRLPM
GAVIKCMVYY KEAFWKKKDY CGCMIIEDEE APIAITLDDT KPDGSLPAIM GFILARKADR
QAKLHKDIRK RKICELYAKV LGSQEALYPV HYEEKNWCEE QYSGGCYTAY FPPGIMTQYG
RVIRQPVGRI YFAGTETATQ WSGYMEGAVE AGERAAREVL NALGKVAKKD IWVEEPESKD
VPAIEITHTF LERNLPSVPG LLKITGVSTS VALLCFVLYK IKKLPC
