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[F-actin]-L-methionine + NADH + O2 + H+
[F-actin]-L-methionine-(R)-S-oxide + NAD+ + H2O
-
-
-
?
[F-actin]-L-methionine + NADPH + O2 + H+
[F-actin]-L-methionine-(R)-S-oxide + NADP+ + H2O
additional information
?
-
[F-actin]-L-methionine + NADPH + O2 + H+
[F-actin]-L-methionine-(R)-S-oxide + NADP+ + H2O
-
Mical post-translationally oxidizes the methionine 44 residue within the D-loop of actin, simultaneously severing filaments and decreasing polymerization
-
?
[F-actin]-L-methionine + NADPH + O2 + H+
[F-actin]-L-methionine-(R)-S-oxide + NADP+ + H2O
-
-
-
?
[F-actin]-L-methionine + NADPH + O2 + H+
[F-actin]-L-methionine-(R)-S-oxide + NADP+ + H2O
-
-
-
?
[F-actin]-L-methionine + NADPH + O2 + H+
[F-actin]-L-methionine-(R)-S-oxide + NADP+ + H2O
-
only 2-3 residues are oxidized in each actin monomer. Several residues, including Met44 and Met47, are modified with similar probability
-
?
[F-actin]-L-methionine + NADPH + O2 + H+
[F-actin]-L-methionine-(R)-S-oxide + NADP+ + H2O
usage of F-actin from rabbit skeletal muscle purified from G-actin by ultracentrifugation
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-
?
[F-actin]-L-methionine + NADPH + O2 + H+
[F-actin]-L-methionine-(R)-S-oxide + NADP+ + H2O
-
-
-
?
[F-actin]-L-methionine + NADPH + O2 + H+
[F-actin]-L-methionine-(R)-S-oxide + NADP+ + H2O
-
-
-
?
additional information
?
-
the Km for NADPH of the NADPH oxidase reaction is sensitive to ionic strength and type of ions. The apparent kcat (pH 7) is limited by enzyme reduction by NADPH, which occurs without detectable intermediates. The reaction is also sensitive to solvent viscosity
-
-
?
additional information
?
-
-
the Km for NADPH of the NADPH oxidase reaction is sensitive to ionic strength and type of ions. The apparent kcat (pH 7) is limited by enzyme reduction by NADPH, which occurs without detectable intermediates. The reaction is also sensitive to solvent viscosity
-
-
?
additional information
?
-
MICAL has additionally NADPH oxidase activity that underlies F-actin disassembly simultaneously with the oxidation of NADPH. For MICAL3 containing the FMO and CH domains, the kcat/Km ratio for NADPH oxidase activity increases dramatically on adding F-actin, while the kcat/Km value for MICAL3 lacking the CH domain changes little
-
-
-
additional information
?
-
-
MICAL has additionally NADPH oxidase activity that underlies F-actin disassembly simultaneously with the oxidation of NADPH. For MICAL3 containing the FMO and CH domains, the kcat/Km ratio for NADPH oxidase activity increases dramatically on adding F-actin, while the kcat/Km value for MICAL3 lacking the CH domain changes little
-
-
-
additional information
?
-
the reductive half-reaction of the mical2 hydroxylase domain is stimulated by F-actin. In the absence of actin, NADPH reduces the flavin relatively slowly. Actin speeds that reaction significantly. The separate monooxygenase domain has the classic regulatory behavior of flavin-dependent aromatic hydroxylases (Class A monooxygenases) with slow reduction of the flavin when the substrate to be oxygenated is absent
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-
?
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Adenocarcinoma of Lung
MICAL2 is a novel nucleocytoplasmic shuttling protein promoting cancer invasion and growth of lung adenocarcinoma.
Anthracosilicosis
[Cellular metabolism in nasal lining and buccal epithelium in coal miners]
Arrhythmias, Cardiac
MICAL1 constrains cardiac stress responses and protects against disease by oxidizing CaMKII.
Breast Neoplasms
MICAL1 controls cell invasive phenotype via regulating oxidative stress in breast cancer cells.
Breast Neoplasms
MICAL1 facilitates breast cancer cell proliferation via ROS-sensitive ERK/cyclin D pathway.
Breast Neoplasms
MICAL1 regulates actin cytoskeleton organization, directional cell migration and the growth of human breast cancer cells as orthotopic xenograft tumours.
Breast Neoplasms
MICAL2 is expressed in cancer associated neo-angiogenic capillary endothelia and it is required for endothelial cell viability, motility and VEGF response.
Breast Neoplasms
MICAL2 promotes breast cancer cell migration by maintaining epidermal growth factor receptor (EGFR) stability and EGFR/P38 signalling activation.
Breast Neoplasms
Semaphorin signaling via MICAL3 induces symmetric cell division to expand breast cancer stem-like cells.
Carcinogenesis
MICAL2 Mediates p53 Ubiquitin Degradation through Oxidating p53 Methionine 40 and 160 and Promotes Colorectal Cancer Malignance.
Colorectal Neoplasms
MICAL2 Mediates p53 Ubiquitin Degradation through Oxidating p53 Methionine 40 and 160 and Promotes Colorectal Cancer Malignance.
Epilepsy
Expression pattern of Mical-1 in the temporal neocortex of patients with intractable temporal epilepsy and pilocarpine-induced rat model.
Epilepsy, Temporal Lobe
Expression pattern of Mical-1 in the temporal neocortex of patients with intractable temporal epilepsy and pilocarpine-induced rat model.
Glioblastoma
MICAL2 is expressed in cancer associated neo-angiogenic capillary endothelia and it is required for endothelial cell viability, motility and VEGF response.
Latent Infection
Identification potential biomarkers in pulmonary tuberculosis and latent infection based on bioinformatics analysis.
Lentivirus Infections
MICAL2 regulates myofibroblasts differentiation in epidural fibrosis via SRF/MRTF-A signaling pathway.
Liver Cirrhosis
LncRNA Mical2/miR-203a-3p sponge participates in epithelial-mesenchymal transition by targeting p66Shc in liver fibrosis.
Lymphatic Metastasis
MICAL2 is a novel nucleocytoplasmic shuttling protein promoting cancer invasion and growth of lung adenocarcinoma.
Melanoma
Sema6A and Mical1 control cell growth and survival of BRAFV600E human melanoma cells.
Myxoma
MICAL2 is expressed in cancer associated neo-angiogenic capillary endothelia and it is required for endothelial cell viability, motility and VEGF response.
Neoplasm Metastasis
Identification and expression analysis of mical family genes in zebrafish.
Neoplasm Metastasis
MICAL2 is a novel human cancer gene controlling mesenchymal to epithelial transition involved in cancer growth and invasion.
Neoplasm Metastasis
MICAL2 promotes breast cancer cell migration by maintaining epidermal growth factor receptor (EGFR) stability and EGFR/P38 signalling activation.
Neoplasm Metastasis
Overexpression of MICAL2, a novel tumor-promoting factor, accelerates tumor progression through regulating cell proliferation and EMT.
Neoplasms
Amplification of F-Actin Disassembly and Cellular Repulsion by Growth Factor Signaling.
Neoplasms
Deregulation of Rab and Rab effector genes in bladder cancer.
Neoplasms
Development and clinical validation of a novel 9-gene prognostic model based on multi-omics in pancreatic adenocarcinoma.
Neoplasms
Identification and expression analysis of mical family genes in zebrafish.
Neoplasms
Identification of novel TGF-? regulated genes with pro-migratory roles.
Neoplasms
MICAL redox enzymes and actin remodeling: New links to classical tumorigenic and cancer pathways.
Neoplasms
MICAL1 regulates actin cytoskeleton organization, directional cell migration and the growth of human breast cancer cells as orthotopic xenograft tumours.
Neoplasms
MICAL2 Facilitates Gastric Cancer Cell Migration via MRTF-A-Mediated CDC42 Activation.
Neoplasms
MICAL2 is a novel human cancer gene controlling mesenchymal to epithelial transition involved in cancer growth and invasion.
Neoplasms
MICAL2 is a novel nucleocytoplasmic shuttling protein promoting cancer invasion and growth of lung adenocarcinoma.
Neoplasms
MICAL2 is expressed in cancer associated neo-angiogenic capillary endothelia and it is required for endothelial cell viability, motility and VEGF response.
Neoplasms
MICAL2 promotes breast cancer cell migration by maintaining epidermal growth factor receptor (EGFR) stability and EGFR/P38 signalling activation.
Neoplasms
ORN: Inferring patient-specific dysregulation status of pathway modules in cancer with OR-gate Network.
Neoplasms
Overexpression of MICAL2, a novel tumor-promoting factor, accelerates tumor progression through regulating cell proliferation and EMT.
Neoplasms
Semaphorin signaling via MICAL3 induces symmetric cell division to expand breast cancer stem-like cells.
Osteoarthritis
Allelic expression analysis of the osteoarthritis susceptibility locus that maps to MICAL3.
Prostatic Neoplasms
Actin Stimulates Reduction of the MICAL-2 Monooxygenase Domain.
Prostatic Neoplasms
Expression of novel molecules, MICAL2-PV (MICAL2 prostate cancer variants), increases with high Gleason score and prostate cancer progression.
Seizures
Expression pattern of Mical-1 in the temporal neocortex of patients with intractable temporal epilepsy and pilocarpine-induced rat model.
Spinal Cord Injuries
MICAL flavoprotein monooxygenases: expression during neural development and following spinal cord injuries in the rat.
Spinal Cord Injuries
MICAL1 (molecule interacting with CasL 1) protects oligodendrocyte cells from oxidative injury through regulating apoptosis, autophagy in spinal cord injury.
Stomach Neoplasms
MICAL2 Facilitates Gastric Cancer Cell Migration via MRTF-A-Mediated CDC42 Activation.
Stomach Neoplasms
NEDD9 Facilitates Hypoxia-Induced Gastric Cancer Cell Migration via MICAL1 Related Rac1 Activation.
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0.03 - 1.438
[F-actin]-L-methionine
-
additional information
additional information
-
0.019
NADPH
isolated monooxygenase-like domain, pH 7.0, 25°C
0.093
NADPH
pH 7.0, 25°C, presence of 10% glycerol
0.134
NADPH
truncated form comprising the MO and CH domains, pH 7.0, 25°C
0.23
NADPH
truncated form comprising the MO, CH and LIM domains, pH 7.0, 25°C
0.375
NADPH
wild-type, pH 7.0, 25°C
0.499
NADPH
pH 7.0, 25°C, presence of 0.1 M NaCl
0.03
[F-actin]-L-methionine
wild-type, pH 7.0, 25°C
-
0.2669
[F-actin]-L-methionine
pH 8.0, 25°C, recombinant hMICAL3FMOCH
-
0.5438
[F-actin]-L-methionine
recombinant MICAL3 containing the FMO and CH domains, pH 7.5, 25°C
-
0.8172
[F-actin]-L-methionine
recombinant MICAL3 lacking the CH domain, pH 7.5, 25°C
-
1.264
[F-actin]-L-methionine
pH 8.0, 25°C, recombinant hMICAL3FMO
-
1.438
[F-actin]-L-methionine
pH 8.0, 25°C, recombinant hMICAL3FMOCHDELTA213,530
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
NADPH
the Km for NADPH of the NADPH oxidase reaction is sensitive to ionic strength and type of ions. pH 7.0, 25°C
additional information
NADPH
-
the Km for NADPH of the NADPH oxidase reaction is sensitive to ionic strength and type of ions. pH 7.0, 25°C
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0.0006 - 0.0169
[F-actin]-L-methionine
-
0.28
NADPH
wild-type, pH 7.0, 25°C
2.5
NADPH
truncated form comprising the MO and CH domains, pH 7.0, 25°C
2.6
NADPH
pH 7.0, 25°C, presence of 0.1 M NaCl
2.9
NADPH
pH 7.0, 25°C, presence of 10% glycerol
3.1
NADPH
isolated monooxygenase-like domain, pH 7.0, 25°C
3.5
NADPH
truncated form comprising the MO, CH and LIM domains, pH 7.0, 25°C
0.0006
[F-actin]-L-methionine
pH 8.0, 25°C, recombinant hMICAL3FMOCH
-
0.0024
[F-actin]-L-methionine
recombinant MICAL3 lacking the CH domain, pH 7.5, 25°C
-
0.0031
[F-actin]-L-methionine
pH 8.0, 25°C, recombinant hMICAL3FMO
-
0.0033
[F-actin]-L-methionine
pH 8.0, 25°C, recombinant hMICAL3FMOCHDELTA213,530
-
0.0169
[F-actin]-L-methionine
recombinant MICAL3 containing the FMO and CH domains, pH 7.5, 25°C
-
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0.00225 - 0.031
[F-actin]-L-methionine
-
0.75
NADPH
wild-type, pH 7.0, 25°C
5.2
NADPH
pH 7.0, 25°C, presence of 0.1 M NaCl
15.3
NADPH
truncated form comprising the MO, CH and LIM domains, pH 7.0, 25°C
18.5
NADPH
truncated form comprising the MO and CH domains, pH 7.0, 25°C
31.2
NADPH
pH 7.0, 25°C, presence of 10% glycerol
163
NADPH
isolated monooxygenase-like domain, pH 7.0, 25°C
0.00225
[F-actin]-L-methionine
pH 8.0, 25°C, recombinant hMICAL3FMOCH
-
0.0023
[F-actin]-L-methionine
pH 8.0, 25°C, recombinant hMICAL3FMOCHDELTA213,530
-
0.00245
[F-actin]-L-methionine
pH 8.0, 25°C, recombinant hMICAL3FMO
-
0.0029
[F-actin]-L-methionine
recombinant MICAL3 lacking the CH domain, pH 7.5, 25°C
-
0.031
[F-actin]-L-methionine
recombinant MICAL3 containing the FMO and CH domains, pH 7.5, 25°C
-
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malfunction
the catalytic efficiency of MICAL3 increases on adding F-actin only when the CH domain is available. But this does not occur when two residues, Glu213 and Arg530, are mutated in the FMO and CH domains, respectively
physiological function
F-actin is a direct and specific substrate for Mical. The reaction alters actin at a specific amino acid residue disrupting actin-actin associations and fragmenting filaments. The modified actin no longer polymerizes normally. Mical modifies the pointed-end of actin proteins, and not the fast-growing, membrane-proximal barbed-end. Therefore actin reassembly and branching follows Semaphorin/Plexin/Mical-mediated F-actin collapse
physiological function
F-actin is efficiently dismantled through a post-translational-mediated synergism between cofilin and the actin-oxidizing enzyme Mical. Mical-mediated oxidation of actin improves cofilin binding to filaments, where their combined effect dramatically accelerates F-actin disassembly compared with either effector alone. This synergism is also necessary and sufficient for F-actin disassembly in vivo, magnifying the effects of both Mical and cofilin on cellular remodelling, axon guidance and Semaphorin-Plexin repulsion
physiological function
Mical is both necessary and sufficient for semaphorin-plexin mediated F-actin reorganization in vivo. Mical directly binds F-actin and disassembles both individual and bundled actin filaments. Mical utilizes its redox activity to alter F-actin dynamics in vivo and in vitro
physiological function
Mical oxidizes actin stereo-specifically to generate actin Met-44-R-sulfoxide. Methionine sulfoxide reductase enzyme SelR opposes Mical redox activity and Semaphorin/Plexin repulsion to direct multiple actin-dependent cellular behaviors in vivo
physiological function
MICAL1 gene disruption in MDA-MB-231 cells knocks out protein expression, which affects F-actin organization, cell size and motility. MICAL1 deletion significantly affects the expression of over 700 genes, with the majority being reduced in their expression levels. Receptor regulator activity is the most significant negatively enriched molecular function gene set. MICAL1 deletion on is also associated with changes in the expression of several serum-response factor regulated genes. MICAL1 disruption attenuates breast cancer tumour growth in vivo
physiological function
MICAL isozymes are involved in actin cytoskeleton reorganization through methionine oxidation. The enzyme functions in F-actin disassembly
physiological function
MICAL2 is essential for skeletal muscle homeostasis and functionality. Lack of MICAL2 results in muscle actin defects. MICAL2 upregulation shows a positive impact on skeletal and cardiac muscle commitments
physiological function
splicing isoform MICAL2PV is a tunneling nanotubes (TNT) regulator that suppresses TNT formation and modulates mitochondrial distribution. MICAL2PV interacts with mitochondrial Rho GTPase Miro2 and regulates subcellular mitochondrial trafficking. Downregulation of MICAL2PV enhances survival of cells treated with chemotherapeutical drugs. The monooxygenase domain of MICAL2PV is required for its activity to inhibit TNT formation by depolymerizing F-actin
additional information
the catalytic efficiency of MICAL3 increases on adding F-actin only when the CH domain is available. MICAL3 is structurally highly similar to isozyme MICAL1, which suggests that they may adopt the same catalytic mechanism, but the difference in the relative position of the CH domain produces a difference in F-actin substrate specificity. Interaction analysis of the binding site between the CH domain and the FMO domain in human MICAL3, modeling, overview. The FMO-CH interaction in hMICAL3 is required to increase the catalytic efficiency by conferring specific binding to F-actin. The FMO domain that exhibits monooxygenase activity is localized at the N-terminus of MICAL and is highly conserved among species. The CH domain that is usually found in actin binding proteins is adjacent to the FMO domain and is also highly conserved. CH domains are classified into three types: types 1, 2, and 3. Whereas type 3 CH domains are mainly found in regulatory proteins associated with muscle contraction and signaling proteins, type 1 and 2 CH domains are usually found in cytoskeletal proteins. MICALs have a typical type 2 CH domain
additional information
-
the catalytic efficiency of MICAL3 increases on adding F-actin only when the CH domain is available. MICAL3 is structurally highly similar to isozyme MICAL1, which suggests that they may adopt the same catalytic mechanism, but the difference in the relative position of the CH domain produces a difference in F-actin substrate specificity. Interaction analysis of the binding site between the CH domain and the FMO domain in human MICAL3, modeling, overview. The FMO-CH interaction in hMICAL3 is required to increase the catalytic efficiency by conferring specific binding to F-actin. The FMO domain that exhibits monooxygenase activity is localized at the N-terminus of MICAL and is highly conserved among species. The CH domain that is usually found in actin binding proteins is adjacent to the FMO domain and is also highly conserved. CH domains are classified into three types: types 1, 2, and 3. Whereas type 3 CH domains are mainly found in regulatory proteins associated with muscle contraction and signaling proteins, type 1 and 2 CH domains are usually found in cytoskeletal proteins. MICALs have a typical type 2 CH domain
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MICAL3 has an FAD/NADP-binding Rossmann-fold domain for monooxygenase activity. The flavin-containing monooxygenase (FMO) and calponin-homology (CH) domains of both MICAL3 and MICAL1 are highly similar in structure, but a different relative position of the calponin-homology domain in the asymmetric unit
purified recombinant His-tagged wild-type and mutant MICAL3 variants, sitting drop vapor diffusion method, method optimization, mixing of 500 nl of 25 mg/ml protein in 50 mM Tris, pH 8.5, 100 mM NaCl, 1 mM 1,4-dithiothreitol, 1% glycerol, with 500 nl of crystallization solution containing 0.1 M bicine-NaOH, pH 9.2, 7% v/v MPD, one day, X-ray diffraction structure determination and analysis at 1.9-2.3 A resolution
structure of a fragment of MICAL-1 containing the monooxygenase and the calponin homology domains. The calponin homology domain, loosely connected to the monooxygenase domain by a flexible linker and is far away from the catalytic site, couples F-actin to the enhancement of redox activity of MICALMO-CH by a cooperative mechanism involving a trans interaction between adjacently bound molecules
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Zucchini, D.; Caprini, G.; Pasterkamp, R.J.; Tedeschi, G.; Vanoni, M.A.
Kinetic and spectroscopic characterization of the putative monooxygenase domain of human MICAL-1
Arch. Biochem. Biophys.
515
1-13
2011
Homo sapiens (Q8TDZ2), Homo sapiens
brenda
Vitali, T.; Maffioli, E.; Tedeschi, G.; Vanoni, M.A.
Properties and catalytic activities of MICAL1, the flavoenzyme involved in cytoskeleton dynamics, and modulation by its CH, LIM and C-terminal domains
Arch. Biochem. Biophys.
593
24-37
2016
Homo sapiens (Q8TDZ2)
brenda
McDonald, C.A.; Liu, Y.Y.; Palfey, B.A.
Actin stimulates reduction of the MICAL-2 monooxygenase domain
Biochemistry
52
6076-6084
2013
Mus musculus (Q8BML1)
brenda
Hung, R.J.; Spaeth, C.S.; Yesilyurt, H.G.; Terman, J.R.
SelR reverses Mical-mediated oxidation of actin to regulate F-actin dynamics
Nat. Cell Biol.
15
1445-1454
2013
Drosophila melanogaster (Q86BA1)
brenda
Grintsevich, E.E.; Yesilyurt, H.G.; Rich, S.K.; Hung, R.J.; Terman, J.R.; Reisler, E.
F-actin dismantling through a redox-driven synergy between Mical and cofilin
Nat. Cell Biol.
18
876-885
2016
Drosophila melanogaster (Q86BA1)
brenda
Hung, R.J.; Yazdani, U.; Yoon, J.; Wu, H.; Yang, T.; Gupta, N.; Huang, Z.; van Berkel, W.J.; Terman, J.R.
Mical links semaphorins to F-actin disassembly
Nature
463
823-827
2010
Drosophila melanogaster (Q86BA1)
brenda
Alqassim, S.S.; Urquiza, M.; Borgnia, E.; Nagib, M.; Amzel, L.M.; Bianchet, M.A.
Modulation of MICAL monooxygenase activity by its calponin homology domain: structural and mechanistic insights
Sci. Rep.
6
22176
2016
Mus musculus (Q8VDP3)
brenda
Hung, R.J.; Pak, C.W.; Terman, J.R.
Direct redox regulation of F-actin assembly and disassembly by Mical
Science
334
1710-1713
2011
Drosophila melanogaster (Q86BA1)
brenda
McGarry, D.J.; Armstrong, G.; Castino, G.; Mason, S.; Clark, W.; Shaw, R.; McGarry, L.; Blyth, K.; Olson, M.F.
MICAL1 regulates actin cytoskeleton organization, directional cell migration and the growth of human breast cancer cells as orthotopic xenograft tumours
Cancer Lett.
519
226-236
2021
Homo sapiens (Q8TDZ2), Homo sapiens
brenda
Giarratana, N.; Conti, F.; La Rovere, R.; Gijsbers, R.; Carai, P.; Duelen, R.; Vervliet, T.; Bultynck, G.; Ronzoni, F.; Piciotti, R.; Costamagna, D.; Fulle, S.; Barravecchia, I.; Angeloni, D.; Torrente, Y.; Sampaolesi, M.
MICAL2 is essential for myogenic lineage commitment
Cell Death Dis.
11
654
2020
Mus musculus (Q8BML1)
brenda
Wang, F.; Chen, X.; Cheng, H.; Song, L.; Liu, J.; Caplan, S.; Zhu, L.; Wu, J.Y.
MICAL2PV suppresses the formation of tunneling nanotubes and modulates mitochondrial trafficking
EMBO Rep.
22
e52006
2021
Homo sapiens (O94851)
brenda
Yoon, J.; Wu, H.; Hung, R.J.; Terman, J.R.
Enhanced production of the Mical redox domain for enzymology and F-actin disassembly assays
Int. J. Mol. Sci.
22
1991
2021
Homo sapiens
brenda
Kim, J.; Lee, H.; Roh, Y.J.; Kim, H.U.; Shin, D.; Kim, S.; Son, J.; Lee, A.; Kim, M.; Park, J.; Hwang, S.Y.; Kim, K.; Lee, Y.K.; Jung, H.S.; Hwang, K.Y.; Lee, B.C.
Structural and kinetic insights into flavin-containing monooxygenase and calponin-homology domains in human MICAL3
IUCrJ
7
90-99
2020
Homo sapiens (Q7RTP6), Homo sapiens
brenda