MICAL_DROME
ID MICAL_DROME Reviewed; 4723 AA.
AC Q86BA1; B7Z0U5; F2FB99; Q86BA2; Q86BA3; Q8MTA1; Q8MUJ8; Q8MUJ9; Q8MUK0;
AC Q9VH41;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=[F-actin]-monooxygenase Mical;
DE EC=1.14.13.225 {ECO:0000269|PubMed:22116028};
DE AltName: Full=Molecule interacting with CasL protein homolog;
GN Name=Mical; ORFNames=CG33208;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B; C AND E), FUNCTION, COFACTOR,
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION
RP WITH PLEXA, AND MUTAGENESIS OF 134-GLY--GLY-139.
RX PubMed=12110185; DOI=10.1016/s0092-8674(02)00794-8;
RA Terman J.R., Mao T., Pasterkamp R.J., Yu H.-H., Kolodkin A.L.;
RT "MICALs, a family of conserved flavoprotein oxidoreductases, function in
RT plexin-mediated axonal repulsion.";
RL Cell 109:887-900(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Testis;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
RC STRAIN=Berkeley; TISSUE=Head;
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1049; SER-1194; SER-1199;
RP SER-1212; SER-4349; SER-4353 AND SER-4426, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [7]
RP INDUCTION.
RX PubMed=19881505; DOI=10.1038/nn.2415;
RA Kirilly D., Gu Y., Huang Y., Wu Z., Bashirullah A., Low B.C.,
RA Kolodkin A.L., Wang H., Yu F.;
RT "A genetic pathway composed of Sox14 and Mical governs severing of
RT dendrites during pruning.";
RL Nat. Neurosci. 12:1497-1505(2009).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20148037; DOI=10.1038/nature08724;
RA Hung R.J., Yazdani U., Yoon J., Wu H., Yang T., Gupta N., Huang Z.,
RA van Berkel W.J., Terman J.R.;
RT "Mical links semaphorins to F-actin disassembly.";
RL Nature 463:823-827(2010).
RN [9]
RP FUNCTION, COFACTOR, CATALYTIC ACTIVITY, AND CAUTION.
RX PubMed=22116028; DOI=10.1126/science.1211956;
RA Hung R.J., Pak C.W., Terman J.R.;
RT "Direct redox regulation of F-actin assembly and disassembly by Mical.";
RL Science 334:1710-1713(2011).
RN [10]
RP FUNCTION.
RX PubMed=24212093; DOI=10.1038/ncb2871;
RA Hung R.J., Spaeth C.S., Yesilyurt H.G., Terman J.R.;
RT "SelR reverses Mical-mediated oxidation of actin to regulate F-actin
RT dynamics.";
RL Nat. Cell Biol. 15:1445-1454(2013).
CC -!- FUNCTION: Monooxygenase that promotes depolymerization of F-actin by
CC mediating oxidation of specific methionine residues on actin. Acts by
CC modifying actin subunits at 'Met-44' and 'Met-47' through the addition
CC of oxygen to form methionine-sulfoxide, leading to promote actin
CC filament disassembly and prevent repolymerization. Plays a key role in
CC semaphorin-plexin repulsive axon guidance and cell morphological
CC changes, probably via its ability to modify and regulate actin.
CC {ECO:0000269|PubMed:12110185, ECO:0000269|PubMed:20148037,
CC ECO:0000269|PubMed:22116028}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-methionyl-[F-actin] + NADPH + O2 = H2O + L-methionyl-
CC (R)-S-oxide-[F-actin] + NADP(+); Xref=Rhea:RHEA:51308, Rhea:RHEA-
CC COMP:12953, Rhea:RHEA-COMP:12956, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16044,
CC ChEBI:CHEBI:45764, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.14.13.225; Evidence={ECO:0000269|PubMed:22116028};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:12110185, ECO:0000269|PubMed:22116028};
CC -!- SUBUNIT: Interacts with plexA. {ECO:0000269|PubMed:12110185}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=C; Synonyms=D, F, G, H;
CC IsoId=Q86BA1-1; Sequence=Displayed;
CC Name=E;
CC IsoId=Q86BA1-2; Sequence=VSP_042614, VSP_042617;
CC Name=B;
CC IsoId=Q86BA1-3; Sequence=VSP_042617;
CC Name=I;
CC IsoId=Q86BA1-4; Sequence=VSP_042612, VSP_042613;
CC Name=A;
CC IsoId=Q86BA1-5; Sequence=VSP_042615, VSP_042616;
CC -!- TISSUE SPECIFICITY: Present in neuronal cell bodies, along axons, and
CC in growth cones. Appears in the nervous system at stage 13 and labels
CC motor and CNS projections, and at later embryonic stages, it is present
CC on axons that make up all motor axon pathways: the intersegmental nerve
CC (ISN), the intersegmental nerves b and d (ISNb and ISNd), and the
CC segmental nerves a and c (SNa and SNc). Also present in segment
CC boundaries at the position of muscle attachment sites and at low levels
CC in the lateral cluster of chordotonal organs (at protein level).
CC Localizes to growing bristle tips in close proximity to the bristle
CC cell membrane and at sites of bristle branching and actin localization.
CC Localizes to growth cones. {ECO:0000269|PubMed:12110185}.
CC -!- DEVELOPMENTAL STAGE: During early development (stages 7-8), expressed
CC in the ventral neurogenic region and in many nonneuronal tissues
CC (including developing mesoderm, cells surrounding the cephalic furrow
CC and amnioproctodeal invagination, and in gut primordia). This
CC nonneuronal expression is also seen later in embryonic development
CC (stages 11-17), where it is expressed within the anterior and posterior
CC midgut primordia, the visceral musculature, and weakly in somatic
CC musculature. During axonal pathfinding (stage 13 onward), expressed
CC within the developing brain and ventral nerve cord in most, if not all,
CC CNS neurons. Not highly expressed in peripheral sensory neurons.
CC {ECO:0000269|PubMed:12110185}.
CC -!- INDUCTION: Directly regulated by Sox14 during pruning.
CC {ECO:0000269|PubMed:19881505}.
CC -!- DISRUPTION PHENOTYPE: Defects in motor neuron guidance, myofilament
CC organization and bristle formation. Surviving adult flies show
CC abnormally shaped bristle cell processes that are variously straight,
CC thick, bent, twisted and/or had abnormal 'club-like' or blunt tips.
CC {ECO:0000269|PubMed:12110185, ECO:0000269|PubMed:20148037}.
CC -!- SIMILARITY: Belongs to the Mical family. {ECO:0000305}.
CC -!- CAUTION: The reaction mechanism is subject to discussion. Some work
CC suggest MICAL enzymes directly oxidize actin methionine residues to
CC produce methionine-(R)-S-oxide. Other publications suggest that the
CC enzyme functions as a NADPH oxidase producing H(2)O(2) (EC 1.6.3.1) and
CC that it is the produced H(2)O(2) that is responsible for the
CC methionine-(R)-S-oxide production. {ECO:0000250|UniProtKB:Q8TDZ2,
CC ECO:0000250|UniProtKB:Q8VDP3, ECO:0000269|PubMed:22116028,
CC ECO:0000269|PubMed:24212093}.
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DR EMBL; AF520713; AAM55242.1; -; mRNA.
DR EMBL; AF520714; AAM55243.1; -; mRNA.
DR EMBL; AF520715; AAM55244.1; -; mRNA.
DR EMBL; AE014297; AAF54478.2; -; Genomic_DNA.
DR EMBL; AE014297; AAO41531.1; -; Genomic_DNA.
DR EMBL; AE014297; AAO41532.1; -; Genomic_DNA.
DR EMBL; AE014297; AAO41533.1; -; Genomic_DNA.
DR EMBL; AE014297; AAO41534.1; -; Genomic_DNA.
DR EMBL; AE014297; AAO41535.1; -; Genomic_DNA.
DR EMBL; AE014297; AAO41536.1; -; Genomic_DNA.
DR EMBL; AE014297; AAO41537.1; -; Genomic_DNA.
DR EMBL; AE014297; ACL83491.1; -; Genomic_DNA.
DR EMBL; AY118290; AAM48319.1; -; mRNA.
DR EMBL; BT126186; AEA30989.1; -; mRNA.
DR RefSeq; NP_001138032.1; NM_001144560.3. [Q86BA1-4]
DR RefSeq; NP_788620.1; NM_176443.2. [Q86BA1-2]
DR RefSeq; NP_788621.1; NM_176444.2. [Q86BA1-3]
DR RefSeq; NP_788622.1; NM_176445.2. [Q86BA1-1]
DR RefSeq; NP_788623.1; NM_176446.2. [Q86BA1-1]
DR RefSeq; NP_788624.1; NM_176447.2. [Q86BA1-1]
DR RefSeq; NP_788625.1; NM_176448.2. [Q86BA1-1]
DR RefSeq; NP_788626.2; NM_176449.3.
DR RefSeq; NP_788627.1; NM_176450.1. [Q86BA1-5]
DR SMR; Q86BA1; -.
DR BioGRID; 66380; 14.
DR DIP; DIP-61753N; -.
DR IntAct; Q86BA1; 23.
DR STRING; 7227.FBpp0297564; -.
DR iPTMnet; Q86BA1; -.
DR PaxDb; Q86BA1; -.
DR PRIDE; Q86BA1; -.
DR DNASU; 41225; -.
DR EnsemblMetazoa; FBtr0082206; FBpp0081684; FBgn0053208. [Q86BA1-5]
DR EnsemblMetazoa; FBtr0082207; FBpp0081685; FBgn0053208. [Q86BA1-3]
DR EnsemblMetazoa; FBtr0082208; FBpp0081686; FBgn0053208. [Q86BA1-2]
DR EnsemblMetazoa; FBtr0082209; FBpp0081687; FBgn0053208. [Q86BA1-1]
DR EnsemblMetazoa; FBtr0082210; FBpp0081688; FBgn0053208. [Q86BA1-1]
DR EnsemblMetazoa; FBtr0082212; FBpp0081690; FBgn0053208. [Q86BA1-1]
DR EnsemblMetazoa; FBtr0082213; FBpp0081691; FBgn0053208. [Q86BA1-1]
DR EnsemblMetazoa; FBtr0273185; FBpp0271693; FBgn0053208. [Q86BA1-4]
DR GeneID; 41225; -.
DR KEGG; dme:Dmel_CG33208; -.
DR UCSC; CG33208-RA; d. melanogaster.
DR UCSC; CG33208-RB; d. melanogaster.
DR UCSC; CG33208-RC; d. melanogaster. [Q86BA1-1]
DR UCSC; CG33208-RE; d. melanogaster.
DR CTD; 41225; -.
DR FlyBase; FBgn0053208; Mical.
DR VEuPathDB; VectorBase:FBgn0053208; -.
DR eggNOG; KOG1700; Eukaryota.
DR InParanoid; Q86BA1; -.
DR BRENDA; 1.14.13.225; 1994.
DR SignaLink; Q86BA1; -.
DR BioGRID-ORCS; 41225; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Mical; fly.
DR GenomeRNAi; 41225; -.
DR PRO; PR:Q86BA1; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0053208; Expressed in cleaving embryo and 28 other tissues.
DR ExpressionAtlas; Q86BA1; baseline and differential.
DR Genevisible; Q86BA1; DM.
DR GO; GO:0005829; C:cytosol; NAS:FlyBase.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; IDA:FlyBase.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0030042; P:actin filament depolymerization; IDA:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
DR GO; GO:0030047; P:actin modification; IDA:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IMP:UniProtKB.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0016322; P:neuron remodeling; IMP:FlyBase.
DR GO; GO:1904799; P:regulation of neuron remodeling; IMP:FlyBase.
DR GO; GO:0045214; P:sarcomere organization; IMP:FlyBase.
DR GO; GO:0030240; P:skeletal muscle thin filament assembly; IMP:FlyBase.
DR GO; GO:0060386; P:synapse assembly involved in innervation; IMP:FlyBase.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR022735; bMERB_dom.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF12130; DUF3585; 1.
DR Pfam; PF00412; LIM; 1.
DR SMART; SM00132; LIM; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS51848; BMERB; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cytoplasm; FAD; Flavoprotein;
KW Leucine-rich repeat; LIM domain; Metal-binding; Monooxygenase; NADP;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Repeat; Zinc.
FT CHAIN 1..4723
FT /note="[F-actin]-monooxygenase Mical"
FT /id="PRO_0000416307"
FT DOMAIN 562..669
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 1072..1136
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REPEAT 1297..1320
FT /note="LRR 1"
FT REPEAT 1579..1601
FT /note="LRR 2"
FT REPEAT 1730..1754
FT /note="LRR 3"
FT REPEAT 1931..1956
FT /note="LRR 4"
FT REPEAT 2548..2574
FT /note="LRR 5"
FT REPEAT 2680..2704
FT /note="LRR 6"
FT REPEAT 2934..2957
FT /note="LRR 7"
FT REPEAT 3545..3568
FT /note="LRR 8"
FT REPEAT 3642..3665
FT /note="LRR 9"
FT DOMAIN 4550..4705
FT /note="bMERB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01195"
FT REPEAT 4646..4668
FT /note="LRR 10"
FT REGION 1..520
FT /note="Monooxygenase domain"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1130..1182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1434..1591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1614..1648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1684..1781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1797..1825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1992..2013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2028..2092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2145..2172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2329..2379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2418..2549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2604..2676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2699..2866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3411..3456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3468..3488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3655..3694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3809..3830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3888..3909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3922..3962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3983..4037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4072..4150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4260..4284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4317..4347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4360..4414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4449..4492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4505..4544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4704..4723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1246
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1282..1308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1511..1564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1694..1724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1765..1781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1992..2006
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2051..2075
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2150..2172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2344..2359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2418..2448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2457..2479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2608..2622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2633..2652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2779..2813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2814..2866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3430..3451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3469..3488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3924..3962
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3983..4005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4084..4122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4333..4347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4383..4398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4530..4544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 138
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 157..159
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 164..166
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 224
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 334
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 434
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 1074
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1077
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1095
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1098
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT MOD_RES 1049
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1194
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1199
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1212
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 4349
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 4353
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 4426
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 770..789
FT /note="QNDTPRRSKKRRQVDKTANI -> LLKITILHHSLMENKFRSGC (in
FT isoform I)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_042612"
FT VAR_SEQ 790..4723
FT /note="Missing (in isoform I)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_042613"
FT VAR_SEQ 790..1057
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000303|PubMed:12110185"
FT /id="VSP_042614"
FT VAR_SEQ 790..810
FT /note="EERQQRLQEIEENRQERMSKR -> VSKCWHYFISWIGSYANVQKV (in
FT isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_042615"
FT VAR_SEQ 811..4723
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_042616"
FT VAR_SEQ 1325..3045
FT /note="Missing (in isoform E and isoform B)"
FT /evidence="ECO:0000303|PubMed:12110185"
FT /id="VSP_042617"
FT MUTAGEN 134..139
FT /note="GAGPCG->WAWPCW: Abolishes Monooxygenase activity and
FT impairs axon guidance functions."
FT /evidence="ECO:0000269|PubMed:12110185"
FT CONFLICT 518
FT /note="S -> N (in Ref. 5; AEA30989)"
FT /evidence="ECO:0000305"
FT CONFLICT 770
FT /note="Q -> L (in Ref. 5; AEA30989)"
FT /evidence="ECO:0000305"
FT CONFLICT 815
FT /note="Y -> C (in Ref. 1; AAM55243/AAM55244)"
FT /evidence="ECO:0000305"
FT CONFLICT 1083
FT /note="L -> P (in Ref. 1; AAM55244)"
FT /evidence="ECO:0000305"
FT CONFLICT 1124
FT /note="F -> L (in Ref. 1; AAM55244)"
FT /evidence="ECO:0000305"
FT CONFLICT 1187
FT /note="E -> Q (in Ref. 1; AAM55244)"
FT /evidence="ECO:0000305"
FT CONFLICT 1283..1285
FT /note="Missing (in Ref. 1; AAM55244)"
FT /evidence="ECO:0000305"
FT CONFLICT 1339
FT /note="R -> G (in Ref. 1; AAM55244)"
FT /evidence="ECO:0000305"
FT CONFLICT 1373
FT /note="N -> D (in Ref. 1; AAM55244)"
FT /evidence="ECO:0000305"
FT CONFLICT 1414
FT /note="D -> G (in Ref. 1; AAM55244)"
FT /evidence="ECO:0000305"
FT CONFLICT 1543
FT /note="I -> V (in Ref. 1; AAM55244)"
FT /evidence="ECO:0000305"
FT CONFLICT 1556
FT /note="G -> D (in Ref. 1; AAM55244)"
FT /evidence="ECO:0000305"
FT CONFLICT 1782
FT /note="K -> E (in Ref. 1; AAM55244)"
FT /evidence="ECO:0000305"
FT CONFLICT 1870
FT /note="G -> E (in Ref. 1; AAM55244)"
FT /evidence="ECO:0000305"
FT CONFLICT 1931
FT /note="A -> G (in Ref. 1; AAM55244)"
FT /evidence="ECO:0000305"
FT CONFLICT 2001
FT /note="S -> A (in Ref. 1; AAM55244)"
FT /evidence="ECO:0000305"
FT CONFLICT 2366
FT /note="K -> E (in Ref. 1; AAM55244)"
FT /evidence="ECO:0000305"
FT CONFLICT 2485
FT /note="T -> A (in Ref. 1; AAM55244)"
FT /evidence="ECO:0000305"
FT CONFLICT 2500
FT /note="M -> R (in Ref. 1; AAM55244)"
FT /evidence="ECO:0000305"
FT CONFLICT 2802
FT /note="L -> P (in Ref. 1; AAM55244)"
FT /evidence="ECO:0000305"
FT CONFLICT 3022
FT /note="C -> CVIS (in Ref. 1; AAM55244)"
FT /evidence="ECO:0000305"
FT CONFLICT 3138
FT /note="P -> S (in Ref. 1; AAM55242/AAM55243)"
FT /evidence="ECO:0000305"
FT CONFLICT 3141
FT /note="K -> R (in Ref. 1; AAM55244)"
FT /evidence="ECO:0000305"
FT CONFLICT 3185
FT /note="E -> G (in Ref. 1; AAM55244)"
FT /evidence="ECO:0000305"
FT CONFLICT 3199
FT /note="N -> D (in Ref. 1; AAM55242/AAM55243)"
FT /evidence="ECO:0000305"
FT CONFLICT 3283
FT /note="G -> D (in Ref. 1; AAM55242/AAM55243)"
FT /evidence="ECO:0000305"
FT CONFLICT 3789
FT /note="S -> P (in Ref. 1; AAM55242/AAM55243/AAM55244)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4723 AA; 525047 MW; C96ECC28393C7E9F CRC64;
MSRQHQRHHQ QHHHLPPHQQ PQQQMPQQQQ QLTAQQQQQQ QLLMAEHAAA AEAAELFDLL
CVATTMRQIL ALHRAMCEAV GLRPSPLNDF YPRLKAKVRS WKAQALWKKF DARAAHRVYG
KGAACTGTRV LVIGAGPCGL RTAIEAQLLG AKVVVLEKRD RITRNNVLHL WPFVITDLRN
LGAKKFYGKF CAGSIDHISI RQLQCMLLKV ALLLGVEIHE GVSFDHAVEP SGDGGGWRAA
VTPADHPVSH YEFDVLIGAD GKRNMLDFRR KEFRGKLAIA ITANFINKKT EAEAKVEEIS
GVAFIFNQAF FKELYGKTGI DLENIVYYKD ETHYFVMTAK KHSLIDKGVI IEDMADPGEL
LAPANVDTQK LHDYAREAAE FSTQYQMPNL EFAVNHYGKP DVAMFDFTSM FAAEMSCRVI
VRKGARLMQC LVGDSLLEPF WPTGSGCARG FLSSMDAAYA IKLWSNPQNS TLGVLAQRES
IYRLLNQTTP DTLQRDISAY TVDPATRYPN LNRESVNSWQ VKHLVDTDDP SILEQTFMDT
HALQTPHLDT PGRRKRRSGD LLPQGATLLR WISAQLHSYQ FIPELKEASD VFRNGRVLCA
LINRYRPDLI DYAATKDMSP VECNELSFAV LERELHIDRV MSAKQSLDLT ELESRIWLNY
LDQICDLFRG EIPHIKHPKM DFSDLRQKYR INHTHAQPDF SKLLATKPKA KSPMQDAVDI
PTTVQRRSVL EEERAKRQRR HEQLLNIGGG AAGAAAGVAG SGTGTTTQGQ NDTPRRSKKR
RQVDKTANIE ERQQRLQEIE ENRQERMSKR RQQRYHQTQN FYKSLQLLQA GKLLREGGEA
GVAEDGTPFE DYSIFLYRQQ APVFNDRVKD LERKLLFPDR ERGDIPSALP RTADEQFSDR
IKNMEQRMTG RGGLGGDKKP KDLMRAIGKI DSNDWNVREI EKKIELSKKT EIHGPKGREK
VPKWSKEQFQ ARQHKMSKPQ RQDSREAEKF KDIDQTIRNL DKQLKEGHNL DVGERGRNKV
ASIAGQFGKK DEANSDEKNA GSSNATTNTN NTVIPKSSSK VALAFKKQAA SEKCRFCKQT
VYLMEKTTVE GLVLHRNCLK CHHCHTNLRL GGYAFDRDDP QGRFYCTQHF RLPPKPLPQR
TNKARKSAAA QPASPAVPPT AGSVPTAAAT SEHMDTTPPR DQVDLLETSR ANASADAMSD
DEANVIDEHE WSGRNFLPES NNDSQSELSS SDESDTESDS EMFEEADDSP FGAQTLQLAS
DWIGKQYCED SDDSDDFYDS SEGIADDGKD DTEGEEFKKA RELRRQEVRL QPLPANLPTD
TETEKLKLNV DNKENMADRS SLKSGNSFES ARSQPSTPLS TPTRVEMEQL ERNAPRKFSS
EIEAISEKLY HMNNMVKMNK DLEVLAKENL VKSDILRKLT LKEKWLAENA AIAAGQKVTP
TPSATAPGLQ PKSKFDEKFE KVVSPPQPVV EPKPKPVIDF NLDELKPRKP NFEERPKEQL
PRPESLKKPP QQKPKGSSTN VSRSNSLKSN ASNGSPKVKK APISNNSKMQ IEGILGTLRK
IQSQNSSDQD EDMDVDEDVE RKPNKELNSK LKEIQASSFA GTMDHIKSQL TMPTVSAQAP
PSMDLSKYFP NQKQEKSSTS STNKNQVTLK DVNLAKYFPS SPAPQRRTVE TVADRLKKSQ
TEAALAKTKL LEDQANNQAE KTKKEVEKEG ESKKITKKVA DSKAVPPKRQ ASLDTFSLRE
HQMDGALDLT KKKGPTKASA GVKKPAKSGS TTSVTKATAT SKGKTIKIVK KIVPKGTKAK
KAAEAAQESA VVEAPPEKKP PKDEAERILD EILGDGEYRS PSSEYQRLFQ DEKSPSDLSD
NIDRILEESG LDVELGLPKR SSKKLVKTKS LGEGDFDMKP SKERLTGVQN ILKRFESMSS
VTSQNSDEQA AFKLRRMEST TSNLSSLTRS RESLVSVSDS MSDLEKTMDY LRNEWRNEAT
NFLQKKRDKF YAKKEEQEKE SKILAKPDPL DNLPVQYRDS KLAKFFGLAA SKSPENRKSP
IKKKKSPSKT PKVTKANNSL EELAKISNVR QTKKAQPKTL KPVEVKPLKP ASPVPDDFEI
LDLLEKATEA KELERSKTKS PAVESISQTP KEAIVEISLP VEDIKNLPKT GCDKSSNSSR
RGSQSSLIMS RRHSEISLNE KLNQDALAAL NQIEKEREAE QVDELFQSMV EEMEQEPQPT
AIVEPPEEDI DADSLCTTIS KSPSAQPVTV VKRGSSEDQS IEKLFSHFSD EMLVNVEFDS
NDELVGITPR ATLVSRNTED RDYLDKLESL ERDEETFQPV VGEKFIQENV QDEVDGLHFP
SRPQRRPKSS SSSSEPSLPV APQRLKKKLS KLDPEDMPPS VQDLLQQVYQ KNIQPELVEV
IPVEGKQTLR FPSMLAEEDV DEVDHSKEGI KKIETAPEEV RKVTEPEDVA RVIPSPIKPS
ISQSNSLKSE NSSGSSLVEI PKIITPPKSS SKENSSDWDM EKLPASPMPR RRLLPNQTPY
KAPSVASKES SLEWDMEKLP NSPMLPRRNK MRAISPSTNP VQLLNNLPSD VDDEAAQRRL
IEDFEQERRQ ALIKRDENFE AIAAEQRRRD SLQSSSNSSS KRSLPPPTPP MMASRRGTTQ
DTNRTQDTAS RHEGTPPMFK KLDVDGSGTS MDSTSCSTRR SSFAFIELQD NKPVIVPMPK
KLKLPKPEPP RFVPEPVATD EPVPEVFQGR AWPKTQLEGE VDLGDSDNED ETEKLKKQLP
EYARSDSPPS AAFKNRKWPD GKTVFDKRAE SLEEEDIFEG LLSPRKRGSQ RFMDKPRSQS
PQPFKPLANS SRKSSKSFSD LKKGPSLQSL SAQSSQDTDT LSTTTTVATA RPASYANYED
PMDASTQALL DRSKRLHNRK RDFVNERVVE RNPYMRDVLR STDRRDYDDV DEDLTSYRPR
HYASSTLNRF PNTTIRKSNN YDYLSPSSDY LSRRSYIPSA SATSSYYPST TRSSHLSDLF
RRRSPASGTV SALSGYGNKE SCIGLALDRV GHLIESKCTW VRSTKVQTES ESTSPDEVEL
NSATEISTDS EFDNDEIIRQ APKIFIDDTH LRKPTKVQIK STMIGPNAAS AGLHQKQLAA
REKGGSYLQK YQPQPPLPQF KPLVQVDPTL LIGSQRAPLQ NPRPGDYLLN KTASTEGIAS
KKSLELKKRY LLGEPANGNK IQKSGSTSVL DSRIRSFQSN ISECQKLLNP SSDISAGMRT
FLDRTKLGEG SQTTPGQTNE LIRSATSNVI NDLRVELRIQ KTGSSHSTDN EKENVFVNCK
NELNKGMEYT DAVNATLLDQ LARKSSPTTP TNKTVVEVID LVTPEKPIDI IDLTALETPK
KQLVDGSAMD VDERLTPDSN KISELQQEVK EEPKPDVSRD VKECIPDILG HIKEGTGSKE
PGGEDQQSLL EQSDEEKRDS PEKDVAEHEL YEPDSVQIQV PNIPWEKSKP EVMSTTGSSG
SICSSSDSSS IEDIQHYILE STTSPDTQTV GGKHNVPRLE VHDTSGALMQ VDSLMIVNGK
YIGDPEDVKF LDMPANVIVP PAPALKTNEL DMEDDQEAEA EPVTATPEPV ECTVIEAERR
VTAPPPLPEM GPPKLKFDSK NENKIESLKN LPLIVESNVE HSQAVKPITL NLSNLARTPD
TPTTPTAHDS DKTPTGEILS RGSDSETEHT GTGQVLTETE LSDWTADDCI SENFVDLEFA
LNSNKGTIKR RKDRRRSGAS KLPSGNEVIH ELARQAPVVQ MDGILSAIDI DDIEFMDTGS
EGSCAEAYSA TNTALIQNRG YMEYIEAEPK KTTRKAAPPS SYPGNLPPLM TKRDEKLGVD
YIEQGAYIMH DDAKTPVNEV APAMTQSLTD SITLNELDDD SMIISQTQPT TTEESEALTV
VTSPLDTSSP RVLDQFASML AAGKGDSTPS SSEQQPKTST VTSSSTGPNS STTGNVSKEP
QEEDLQIQFE YVRALQQRIS QISTQRRKSS KGEAPNLQLN SSAPVIESAE DPAKPAEEPL
VSMRPRTTSI SGKVPEIPTL SSKLEEITKE RTKQKDLIHD LVMDKLQSKK QLNAEKRLHR
SRQRSLLTSG YASGSSLSPT PKLAAACSPQ DSNCSSQAHY HASTAEEAPK PPAERPLQKS
ATSTYVSPYR TVQAPTRSAD LYKPRPFSEH IDSNALAGYK LGKTASFNGG KLGDFAKPIA
PARVNRGGGV ATADIANISA STENLRSEAR ARARLKSNTE LGLSPEEKMQ LIRSRLHYDQ
NRSLKPKQLE EMPSGDLAAR ARKMSASKSV NDLAYMVGQQ QQQQVEKDAV LQAKAADFTS
DPNLASGGQE KAGKTKSGRR PKDPERRKSL IQSLSSFFQK GSGSAASSSK EQGGAVAAVH
SEQSERPGTS SSGTPTISDA AGGGGGGGGV FSRFRISPKS KEKSKSCFDL RNFGFGDKDM
LVCNAASPAG ATSASQKNHS QEYLNTTNNS RYRKQTNTAK PKPESFSSSS PQLYIHKPHH
LAAAHPSALD DQTPPPIPPL PLNYQRSDDE SYANETREHK KQRAISKASR QAELKRLRIA
QEIQREQEEI EVQLKDLEAR GVLIEKALRG EAQNIENLDA TKDNDEKLLK ELLEIWRNIT
ALKKRDEELT IRQQELQLEY RHAQLKEELN LRLSCNKLDK SSADVAAEGA ILNEMLEIVA
KRAALRPTAS QLDLTAAGSA STSAEATGIK LTGQPHDHEE SII
