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 27-MAR-2024, entry version 175. 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. Promotes endosomal CC tubule extension by associating with RAB8 (RAB8A or RAB8B), RAB10 and CC GRAF (GRAF1/ARHGAP26 or GRAF2/ARHGAP10) on the endosomal membrane which CC may connect GRAFs to Rabs, thereby participating in neosynthesized CC Rab8-Rab10-Rab11-dependent protein export (By similarity). 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. Interacts with GRAF1/ARHGAP26, GRAF2/ARHGAP10, CC RAB8A, RAB8B and RAB10; may bind simultaneously to GRAFs and Rabs and CC connects GRAFs to Rabs (By similarity). Does not interact with RAB1 and CC RAB11A (By similarity). {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}. Endosome CC membrane {ECO:0000250|UniProtKB:Q8TDZ2}. Midbody CC {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, Rab13 and Rab15 (in their GTP- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 11. DR IntAct; Q8VDP3; 4. DR STRING; 10090.ENSMUSP00000019967; -. DR iPTMnet; Q8VDP3; -. DR PhosphoSitePlus; Q8VDP3; -. DR EPD; Q8VDP3; -. DR jPOST; Q8VDP3; -. DR MaxQB; Q8VDP3; -. DR PaxDb; 10090-ENSMUSP00000097519; -. DR PeptideAtlas; Q8VDP3; -. DR ProteomicsDB; 295663; -. [Q8VDP3-1] DR ProteomicsDB; 295664; -. [Q8VDP3-2] DR ProteomicsDB; 295665; -. [Q8VDP3-3] DR Pumba; Q8VDP3; -. DR Antibodypedia; 32258; 334 antibodies from 24 providers. DR DNASU; 171580; -. DR Ensembl; ENSMUST00000019967.16; ENSMUSP00000019967.10; ENSMUSG00000019823.18. [Q8VDP3-1] DR Ensembl; ENSMUST00000099934.11; ENSMUSP00000097519.5; ENSMUSG00000019823.18. [Q8VDP3-2] DR Ensembl; ENSMUST00000119962.8; ENSMUSP00000113783.2; ENSMUSG00000019823.18. [Q8VDP3-3] DR GeneID; 171580; -. DR KEGG; mmu:171580; -. DR UCSC; uc007exn.2; mouse. [Q8VDP3-1] DR UCSC; uc007exp.2; mouse. [Q8VDP3-2] DR AGR; MGI:2385847; -. 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; DTIEQWI; -. DR OrthoDB; 5399346at2759; -. DR TreeFam; TF324129; -. DR BRENDA; 1.14.13.225; 3474. DR SABIO-RK; Q8VDP3; -. DR BioGRID-ORCS; 171580; 1 hit in 76 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 236 other cell types or tissues. DR ExpressionAtlas; Q8VDP3; baseline and differential. DR GO; GO:0005884; C:actin filament; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB. 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; cd21196; CH_MICAL1; 1. DR CDD; cd09358; LIM_Mical_like; 1. DR DisProt; DP02723; -. DR Gene3D; 1.10.418.10; Calponin-like domain; 1. DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 1. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1. DR InterPro; IPR022735; bMERB_dom. DR InterPro; IPR001715; CH_dom. DR InterPro; IPR036872; CH_dom_sf. DR InterPro; IPR002938; FAD-bd. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR001781; Znf_LIM. DR PANTHER; PTHR23167:SF35; [F-ACTIN]-MONOOXYGENASE MICAL1; 1. DR PANTHER; PTHR23167; CALPONIN HOMOLOGY DOMAIN-CONTAINING PROTEIN DDB_G0272472-RELATED; 1. DR Pfam; PF12130; bMERB_dom; 1. DR Pfam; PF00307; CH; 1. DR Pfam; PF01494; FAD_binding_3; 1. DR SMART; SM00033; CH; 1. DR SMART; SM01203; DUF3585; 1. DR SMART; SM00132; LIM; 1. DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2. DR PROSITE; PS51848; BMERB; 1. DR PROSITE; PS50021; CH; 1. DR PROSITE; PS00478; LIM_DOMAIN_1; 1. DR PROSITE; PS50023; LIM_DOMAIN_2; 1. DR Genevisible; Q8VDP3; MM. PE 1: Evidence at protein level; KW 3D-structure; Actin-binding; Alternative splicing; Coiled coil; Cytoplasm; KW Cytoskeleton; Endosome; FAD; Flavoprotein; LIM domain; Membrane; KW Metal-binding; Monooxygenase; NADP; Oxidoreductase; Phosphoprotein; KW 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 SITE 816 FT /note="Important for interaction with ARHGAP26 AND FT ARHGAP10" 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 //