MICAL1

Microtubule associated monooxygenase, calponin and LIM domain containing 1

PDB rendering based on 1wyl.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1WYL, 2CO8, 2DK9

Identifiers

MICAL1 ; MICAL; MICAL-1; NICAL

External IDs

OMIM: 607129 MGI: 2385847 HomoloGene: 11246 GeneCards: MICAL1 Gene

Gene ontology
Molecular function	• actin binding • protein binding • zinc ion binding • 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 • SH3 domain binding • Rab GTPase binding • FAD binding
Cellular component	• cytoplasm • intermediate filament
Biological process	• negative regulation of protein phosphorylation • cytoskeleton organization • signal transduction • sulfur oxidation • actin filament depolymerization • negative regulation of apoptotic process • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process • oxidation-reduction process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

ENSG00000135596

ENSMUSG00000019823

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 6:
109.77 – 109.79 Mb

Chr 10:
41.48 – 41.49 Mb

PubMed search

NEDD9-interacting protein with calponin homology and LIM domains is a protein that in humans is encoded by the MICAL1 gene.^[1]^[2]

Interactions

MICAL1 has been shown to interact with NEDD9^[1] and RAB1A.^[3]

References

↑ 1.0 1.1 Suzuki T, Nakamoto T, Ogawa S, Seo S, Matsumura T, Tachibana K, Morimoto C, Hirai H (Apr 2002). "MICAL, a novel CasL interacting molecule, associates with vimentin". J Biol Chem 277 (17): 14933–41. doi:10.1074/jbc.M111842200. PMID 11827972.
↑ "Entrez Gene: MICAL1 microtubule associated monoxygenase, calponin and LIM domain containing 1".
↑ Weide, Thomas; Teuber Julia; Bayer Michael; Barnekow Angelika (Jun 2003). "MICAL-1 isoforms, novel rab1 interacting proteins". Biochem. Biophys. Res. Commun. (United States) 306 (1): 79–86. doi:10.1016/S0006-291X(03)00918-5. ISSN 0006-291X. PMID 12788069.

Further reading

Iwata S, Ohashi Y, Kamiguchi K, Morimoto C (2000). "Beta 1-integrin-mediated cell signaling in T lymphocytes.". J. Dermatol. Sci. 23 (2): 75–86. doi:10.1016/S0923-1811(99)00096-1. PMID 10808124.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Hattori A, Okumura K, Nagase T et al. (2001). "Characterization of long cDNA clones from human adult spleen". DNA Res. 7 (6): 357–66. doi:10.1093/dnares/7.6.357. PMID 11214971.
Terman JR, Mao T, Pasterkamp RJ et al. (2002). "MICALs, a family of conserved flavoprotein oxidoreductases, function in plexin-mediated axonal repulsion". Cell 109 (7): 887–900. doi:10.1016/S0092-8674(02)00794-8. PMID 12110185.
Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Weide T, Teuber J, Bayer M, Barnekow A (2003). "MICAL-1 isoforms, novel rab1 interacting proteins". Biochem. Biophys. Res. Commun. 306 (1): 79–86. doi:10.1016/S0006-291X(03)00918-5. PMID 12788069.
Mungall AJ, Palmer SA, Sims SK et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
Ota T, Suzuki Y, Nishikawa T et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Gerhard DS, Wagner L, Feingold EA et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Fischer J, Weide T, Barnekow A (2005). "The MICAL proteins and rab1: a possible link to the cytoskeleton?". Biochem. Biophys. Res. Commun. 328 (2): 415–23. doi:10.1016/j.bbrc.2004.12.182. PMID 15694364.
Bayer M, Fischer J, Kremerskothen J et al. (2006). "Identification and characterization of Iporin as a novel interaction partner for rab1". BMC Cell Biol. 6: 15. doi:10.1186/1471-2121-6-15. PMC 1079803. PMID 15796781.
Olsen JV, Blagoev B, Gnad F et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
Jin X, Zhang J, Dai H et al. (2007). "Investigation of the four cooperative unfolding units existing in the MICAL-1 CH domain". Biophys. Chem. 129 (2–3): 269–78. doi:10.1016/j.bpc.2007.06.008. PMID 17662518.

PDB gallery

1wyl: Solution structure of the CH domain of human NEDD9 interacting protein with calponin homology and LIM domains

2bra: STRUCTURE OF N-TERMINAL FAD BINDING MOTIF OF MOUSE MICAL

2bry: CRYSTAL STRUCTURE OF THE NATIVE MONOOXYGENASE DOMAIN OF MICAL AT 1.45 A RESOLUTION

2c4c: CRYSTAL STRUCTURE OF THE NADPH-TREATED MONOOXYGENASE DOMAIN OF MICAL

2co8: Solution structures of the LIM domain of human NEDD9 interacting protein with calponin homology and LIM domains

2dk9: Solution structure of Calponin Homology domain of Human MICAL-1