MICA1_MOUSE
ID MICA1_MOUSE Reviewed; 1048 AA.
AC Q8VDP3; D3Z4C6; E9PXR1; Q3TB77; Q3TBH9; Q3TX89;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=[F-actin]-monooxygenase MICAL1 {ECO:0000305};
DE EC=1.14.13.225 {ECO:0000269|PubMed:23911929, ECO:0000269|PubMed:26935886};
DE EC=1.6.3.1 {ECO:0000250|UniProtKB:Q8TDZ2};
DE AltName: Full=Molecule interacting with CasL protein 1;
DE Short=MICAL-1;
DE Short=mMical1;
DE AltName: Full=NEDD9-interacting protein with calponin homology and LIM domains;
GN Name=Mical1; Synonyms=Mical, Nical;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary tumor;
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 [4]
RP INTERACTION WITH RAB8A.
RX PubMed=18094055; DOI=10.1091/mbc.e07-06-0551;
RA Yamamura R., Nishimura N., Nakatsuji H., Arase S., Sasaki T.;
RT "The interaction of JRAB/MICAL-L2 with Rab8 and Rab13 coordinates the
RT assembly of tight junctions and adherens junctions.";
RL Mol. Biol. Cell 19:971-983(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-777 AND SER-781, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, AND INTERACTION WITH STK38 AND STK38L.
RX PubMed=21730291; DOI=10.1128/mcb.01389-10;
RA Zhou Y., Adolfs Y., Pijnappel W.W., Fuller S.J., Van der Schors R.C.,
RA Li K.W., Sugden P.H., Smit A.B., Hergovich A., Pasterkamp R.J.;
RT "MICAL-1 is a negative regulator of MST-NDR kinase signaling and
RT apoptosis.";
RL Mol. Cell. Biol. 31:3603-3615(2011).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND CAUTION.
RX PubMed=23911929; DOI=10.1016/j.molcel.2013.06.019;
RA Lee B.C., Peterfi Z., Hoffmann F.W., Moore R.E., Kaya A., Avanesov A.,
RA Tarrago L., Zhou Y., Weerapana E., Fomenko D.E., Hoffmann P.R.,
RA Gladyshev V.N.;
RT "MsrB1 and MICALs regulate actin assembly and macrophage function via
RT reversible stereoselective methionine oxidation.";
RL Mol. Cell 51:397-404(2013).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=25007825; DOI=10.1038/ncomms5317;
RA Van Battum E.Y., Gunput R.A., Lemstra S., Groen E.J., Yu K.L., Adolfs Y.,
RA Zhou Y., Hoogenraad C.C., Yoshida Y., Schachner M., Akhmanova A.,
RA Pasterkamp R.J.;
RT "The intracellular redox protein MICAL-1 regulates the development of
RT hippocampal mossy fibre connections.";
RL Nat. Commun. 5:4317-4317(2014).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 1-489 IN COMPLEX WITH FAD, AND
RP COFACTOR.
RX PubMed=16275925; DOI=10.1073/pnas.0504997102;
RA Siebold C., Berrow N., Walter T.S., Harlos K., Owens R.J., Stuart D.I.,
RA Terman J.R., Kolodkin A.L., Pasterkamp R.J., Jones E.Y.;
RT "High-resolution structure of the catalytic region of MICAL (molecule
RT interacting with CasL), a multidomain flavoenzyme-signaling molecule.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:16836-16841(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 2-615 IN COMPLEX WITH FAD,
RP COFACTOR, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP CAUTION.
RX PubMed=26935886; DOI=10.1038/srep22176;
RA Alqassim S.S., Urquiza M., Borgnia E., Nagib M., Amzel L.M., Bianchet M.A.;
RT "Modulation of MICAL monooxygenase activity by its calponin homology
RT domain: structural and mechanistic insights.";
RL Sci. Rep. 6:22176-22176(2016).
CC -!- FUNCTION: Monooxygenase that promotes depolymerization of F-actin by
CC mediating oxidation of specific methionine residues on actin to form
CC methionine-sulfoxide, resulting in actin filament disassembly and
CC preventing repolymerization. In the absence of actin, it also functions
CC as a NADPH oxidase producing H(2)O(2) (By similarity). Acts as a
CC cytoskeletal regulator that connects NEDD9 to intermediate filaments.
CC Also acts as a negative regulator of apoptosis via its interaction with
CC STK38 and STK38L; acts by antagonizing STK38 and STK38L activation by
CC MST1/STK4. Involved in regulation of lamina-specific connectivity in
CC the nervous system such as the development of lamina-restricted
CC hippocampal connections. Through redox regulation of the actin
CC cytoskeleton controls the intracellular distribution of secretory
CC vesicles containing L1/neurofascin/NgCAM family proteins in neurons,
CC thereby regulating their cell surface levels. May act as Rab effector
CC protein and play a role in vesicle trafficking.
CC {ECO:0000250|UniProtKB:Q8TDZ2, ECO:0000269|PubMed:21730291,
CC ECO:0000269|PubMed:23911929, ECO:0000269|PubMed:25007825,
CC ECO:0000269|PubMed:26935886}.
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:23911929,
CC ECO:0000269|PubMed:26935886};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 = H2O2 + NADP(+); Xref=Rhea:RHEA:11260,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.3.1;
CC Evidence={ECO:0000250|UniProtKB:Q8TDZ2};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:16275925};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.3 uM for actin (for a monooxygenase domain construct)
CC {ECO:0000269|PubMed:26935886};
CC KM=28.8 uM for NADPH (for a monooxygenase domain construct)
CC {ECO:0000269|PubMed:26935886};
CC -!- SUBUNIT: Associates with the SH3 domain of NEDD9. Interacts with VIM
CC and PLXNA3. Interacts with RAB1B, RAB8A, RAB10, RAB13 and RAB15 (in
CC their GTP-bound forms); binding to RAB1B is of low affinity compared to
CC other Rab proteins; at least in case of RAB8A and RAB10 can bind 2
CC molecules of the Rab proteins simultaneously (By similarity). Interacts
CC with STK38 and STK38L. {ECO:0000250, ECO:0000250|UniProtKB:Q8TDZ2,
CC ECO:0000269|PubMed:16275925, ECO:0000269|PubMed:18094055,
CC ECO:0000269|PubMed:21730291}.
CC -!- INTERACTION:
CC Q8VDP3; Q91VJ4: Stk38; NbExp=9; IntAct=EBI-4394891, EBI-2527046;
CC Q8VDP3; A4GW50: Stk38l; Xeno; NbExp=2; IntAct=EBI-4394891, EBI-4404035;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TDZ2}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8TDZ2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8VDP3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VDP3-2; Sequence=VSP_042591;
CC Name=3;
CC IsoId=Q8VDP3-3; Sequence=VSP_042592;
CC -!- TISSUE SPECIFICITY: Expressed in the postnatal and adult hippocampus;
CC found in dentate gyrus, the polymorphic layer, cornu ammonis (CA) 1-3
CC and in mossy fibers of the striatum lucidum. In adult hippocampus
CC strongly expressed in CA3 pyramidial neurons.
CC {ECO:0000269|PubMed:25007825}.
CC -!- DOMAIN: The C-terminal coiled coil part contains the plexin-interacting
CC region.
CC -!- DOMAIN: The bivalent Mical/EHBP Rab binding (bMERB) domain, mediates
CC binding to predominantly Rab8, Rab10, Rab10, Rab13 and Rab15 (in their
CC GTP-bound forms). {ECO:0000250|UniProtKB:Q8TDZ2}.
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:Q86BA1,
CC ECO:0000250|UniProtKB:Q8TDZ2, ECO:0000269|PubMed:23911929,
CC ECO:0000269|PubMed:26935886}.
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DR EMBL; AK159369; BAE35027.1; -; mRNA.
DR EMBL; AK170881; BAE42090.1; -; mRNA.
DR EMBL; AK171234; BAE42330.1; -; mRNA.
DR EMBL; AK171411; BAE42437.1; -; mRNA.
DR EMBL; AK171429; BAE42447.1; -; mRNA.
DR EMBL; AK171479; BAE42481.1; -; mRNA.
DR EMBL; AC153360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021477; AAH21477.1; -; mRNA.
DR EMBL; BC034682; AAH34682.1; -; mRNA.
DR CCDS; CCDS35888.1; -. [Q8VDP3-1]
DR CCDS; CCDS48547.1; -. [Q8VDP3-2]
DR RefSeq; NP_001157905.1; NM_001164433.1. [Q8VDP3-2]
DR RefSeq; NP_612188.1; NM_138315.2. [Q8VDP3-1]
DR RefSeq; XP_011241439.1; XM_011243137.2. [Q8VDP3-1]
DR PDB; 2BRA; X-ray; 2.00 A; A/B=1-484.
DR PDB; 2BRY; X-ray; 1.45 A; A/B=1-489.
DR PDB; 2C4C; X-ray; 2.90 A; A/B=1-489.
DR PDB; 4TXI; X-ray; 2.31 A; A=2-615.
DR PDB; 4TXK; X-ray; 2.88 A; A=2-615.
DR PDBsum; 2BRA; -.
DR PDBsum; 2BRY; -.
DR PDBsum; 2C4C; -.
DR PDBsum; 4TXI; -.
DR PDBsum; 4TXK; -.
DR AlphaFoldDB; Q8VDP3; -.
DR SMR; Q8VDP3; -.
DR BioGRID; 228624; 10.
DR IntAct; Q8VDP3; 4.
DR STRING; 10090.ENSMUSP00000097519; -.
DR iPTMnet; Q8VDP3; -.
DR PhosphoSitePlus; Q8VDP3; -.
DR EPD; Q8VDP3; -.
DR jPOST; Q8VDP3; -.
DR MaxQB; Q8VDP3; -.
DR PaxDb; Q8VDP3; -.
DR PeptideAtlas; Q8VDP3; -.
DR PRIDE; Q8VDP3; -.
DR ProteomicsDB; 295663; -. [Q8VDP3-1]
DR ProteomicsDB; 295664; -. [Q8VDP3-2]
DR ProteomicsDB; 295665; -. [Q8VDP3-3]
DR Antibodypedia; 32258; 289 antibodies from 24 providers.
DR DNASU; 171580; -.
DR Ensembl; ENSMUST00000019967; ENSMUSP00000019967; ENSMUSG00000019823. [Q8VDP3-1]
DR Ensembl; ENSMUST00000099934; ENSMUSP00000097519; ENSMUSG00000019823. [Q8VDP3-2]
DR Ensembl; ENSMUST00000119962; ENSMUSP00000113783; ENSMUSG00000019823. [Q8VDP3-3]
DR GeneID; 171580; -.
DR KEGG; mmu:171580; -.
DR UCSC; uc007exn.2; mouse. [Q8VDP3-1]
DR UCSC; uc007exp.2; mouse. [Q8VDP3-2]
DR CTD; 64780; -.
DR MGI; MGI:2385847; Mical1.
DR VEuPathDB; HostDB:ENSMUSG00000019823; -.
DR eggNOG; KOG1700; Eukaryota.
DR GeneTree; ENSGT00940000159117; -.
DR HOGENOM; CLU_000329_0_0_1; -.
DR InParanoid; Q8VDP3; -.
DR OMA; CKAQSIQ; -.
DR OrthoDB; 430978at2759; -.
DR TreeFam; TF324129; -.
DR BRENDA; 1.14.13.225; 3474.
DR SABIO-RK; Q8VDP3; -.
DR BioGRID-ORCS; 171580; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Mical1; mouse.
DR EvolutionaryTrace; Q8VDP3; -.
DR PRO; PR:Q8VDP3; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8VDP3; protein.
DR Bgee; ENSMUSG00000019823; Expressed in granulocyte and 234 other tissues.
DR ExpressionAtlas; Q8VDP3; baseline and differential.
DR Genevisible; Q8VDP3; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:1990026; C:hippocampal mossy fiber expansion; IMP:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISO:MGI.
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:0004497; F:monooxygenase activity; IMP:MGI.
DR GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; ISO:MGI.
DR GO; GO:0106294; F:NADPH oxidase H202-forming activity; IEA:RHEA.
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:0019901; F:protein kinase binding; IDA:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0030042; P:actin filament depolymerization; IDA:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:1903305; P:regulation of regulated secretory pathway; IMP:UniProtKB.
DR GO; GO:0019417; P:sulfur oxidation; IDA:UniProtKB.
DR CDD; cd00014; CH; 1.
DR DisProt; DP02723; -.
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; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF12130; DUF3585; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SMART; SM00033; CH; 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; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Coiled coil; Cytoplasm;
KW Cytoskeleton; FAD; Flavoprotein; LIM domain; Metal-binding; Monooxygenase;
KW NADP; Oxidoreductase; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..1048
FT /note="[F-actin]-monooxygenase MICAL1"
FT /id="PRO_0000075843"
FT DOMAIN 507..611
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 681..743
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 905..1048
FT /note="bMERB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01195"
FT REGION 1..489
FT /note="Monooxygenase domain"
FT REGION 488..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 847..867
FT /evidence="ECO:0000255"
FT COILED 906..949
FT /evidence="ECO:0000255"
FT COILED 974..1031
FT /evidence="ECO:0000255"
FT COMPBIAS 656..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..872
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 95
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16275925,
FT ECO:0007744|PDB:4TXI, ECO:0007744|PDB:4TXK"
FT BINDING 114..116
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16275925,
FT ECO:0007744|PDB:4TXI, ECO:0007744|PDB:4TXK"
FT BINDING 121..123
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16275925,
FT ECO:0007744|PDB:4TXI, ECO:0007744|PDB:4TXK"
FT BINDING 181
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16275925,
FT ECO:0007744|PDB:4TXI, ECO:0007744|PDB:4TXK"
FT BINDING 293
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16275925,
FT ECO:0007744|PDB:4TXI, ECO:0007744|PDB:4TXK"
FT BINDING 393
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16275925,
FT ECO:0007744|PDB:4TXI, ECO:0007744|PDB:4TXK"
FT BINDING 683
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 686
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 704
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 707
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 710
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 713
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 733
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 736
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT MOD_RES 475
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:D3ZBP4"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 87..159
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_042591"
FT VAR_SEQ 192
FT /note="S -> D (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_042592"
FT CONFLICT 871
FT /note="P -> H (in Ref. 1; BAE35027)"
FT /evidence="ECO:0000305"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:2BRY"
FT HELIX 23..37
FT /evidence="ECO:0007829|PDB:2BRY"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:2BRY"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:2BRY"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:2BRY"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:2BRY"
FT TURN 80..84
FT /evidence="ECO:0007829|PDB:2BRY"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:2BRY"
FT HELIX 94..105
FT /evidence="ECO:0007829|PDB:2BRY"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:2BRY"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:2BRY"
FT HELIX 129..136
FT /evidence="ECO:0007829|PDB:2BRY"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:2BRY"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:2BRY"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:2BRY"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:2BRY"
FT HELIX 157..170
FT /evidence="ECO:0007829|PDB:2BRY"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:2BRY"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:2BRY"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:2BRY"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:2BRY"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:2BRY"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:2BRY"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:2BRY"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:2BRY"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:4TXK"
FT TURN 263..266
FT /evidence="ECO:0007829|PDB:2BRA"
FT HELIX 269..277
FT /evidence="ECO:0007829|PDB:2BRY"
FT STRAND 281..298
FT /evidence="ECO:0007829|PDB:2BRY"
FT HELIX 300..305
FT /evidence="ECO:0007829|PDB:2BRY"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:2BRY"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:2BRY"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:2BRY"
FT HELIX 327..341
FT /evidence="ECO:0007829|PDB:2BRY"
FT TURN 342..346
FT /evidence="ECO:0007829|PDB:2BRY"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:2BRY"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:2BRY"
FT STRAND 367..373
FT /evidence="ECO:0007829|PDB:2BRY"
FT STRAND 375..381
FT /evidence="ECO:0007829|PDB:2BRY"
FT STRAND 384..390
FT /evidence="ECO:0007829|PDB:2BRY"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:2BRY"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:2BRY"
FT HELIX 405..424
FT /evidence="ECO:0007829|PDB:2BRY"
FT HELIX 429..440
FT /evidence="ECO:0007829|PDB:2BRY"
FT HELIX 441..445
FT /evidence="ECO:0007829|PDB:2BRY"
FT TURN 448..450
FT /evidence="ECO:0007829|PDB:2BRY"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:2BRY"
FT HELIX 462..464
FT /evidence="ECO:0007829|PDB:2BRY"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:2BRY"
FT HELIX 476..482
FT /evidence="ECO:0007829|PDB:2BRY"
FT STRAND 483..485
FT /evidence="ECO:0007829|PDB:2BRY"
FT HELIX 508..520
FT /evidence="ECO:0007829|PDB:4TXI"
FT TURN 521..523
FT /evidence="ECO:0007829|PDB:4TXI"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:4TXI"
FT HELIX 534..536
FT /evidence="ECO:0007829|PDB:4TXI"
FT HELIX 540..549
FT /evidence="ECO:0007829|PDB:4TXI"
FT HELIX 564..579
FT /evidence="ECO:0007829|PDB:4TXI"
FT HELIX 587..592
FT /evidence="ECO:0007829|PDB:4TXI"
FT HELIX 596..610
FT /evidence="ECO:0007829|PDB:4TXI"
SQ SEQUENCE 1048 AA; 116785 MW; C31A392A4AE222FC CRC64;
MASPASTNPA HDHFETFVQA QLCQDVLSSF QGLCRALGVE SGGGLSQYHK IKAQLNYWSA
KSLWAKLDKR ASQPVYQQGQ ACTNTKCLVV GAGPCGLRAA VELALLGARV VLVEKRIKFS
RHNVLHLWPF TIHDLRALGA KKFYGRFCTG TLDHISIRQL QLLLLKVALL LGVEIHWGVK
FTGLQPPPRK GSGWRAQLQP NPPAQLASYE FDVLISAAGG KFVPEGFTIR EMRGKLAIGI
TANFVNGRTV EETQVPEISG VARIYNQKFF QSLLKATGID LENIVYYKDE THYFVMTAKK
QCLLRLGVLR QDLSETDQLL GKANVVPEAL QRFARAAADF ATHGKLGKLE FAQDARGRPD
VAAFDFTSMM RAESSARVQE KHGARLLLGL VGDCLVEPFW PLGTGVARGF LAAFDAAWMV
KRWAEGAGPL EVLAERESLY QLLSQTSPEN MHRNVAQYGL DPATRYPNLN LRAVTPNQVQ
DLYDMMDKEH AQRKSDEPDS RKTTTGSAGT EELLHWCQEQ TAGFPGVHVT DFSSSWADGL
ALCALVHHLQ PGLLEPSELQ GMGALEATTW ALRVAEHELG ITPVLSAQAV MAGSDPLGLI
AYLSHFHSAF KNTSHSSGLV SQPSGTPSAI LFLGKLQRSL QRTRAKVDEE TPSTEEPPVS
EPSMSPNTPE LSEHQEAGAE ELCELCGKHL YILERFCVDG HFFHRSCFCC HTCEATLWPG
GYGQHPGDGH FYCLQHLPQE DQKEADNNGS LESQELPTPG DSNMQPDPSS PPVTRVSPVP
SPSQPARRLI RLSSLERLRL SSLNIIPDSG AEPPPKPPRS CSDLARESLK SSFVGWGVPV
QAPQVPEAIE KGDDEEEEEE EEEEEEEPLP PLEPELEQTL LTLAKNPGAM TKYPTWRRTL
MRRAKEEEMK RFCKAQAIQR RLNEIEATMR ELEAEGTKLE LALRKESSSP EQQKKLWLDQ
LLRLIQKKNS LVTEEAELMI TVQELDLEEK QRQLDHELRG YMNREETMKT EADLQSENQV
LRKLLEVVNQ RDALIQFQEE RRLREMPA
