F1MH07

SS
Gene name
MICAL1
Protein name
[F-actin]-monooxygenase MICAL1
Names
EC 1.14.13.225 , EC 1.6.3.1 , Molecule interacting with CasL protein 1 , MICAL-1
Species
Bos taurus (Bovine)
KEGG Pathway
bta:508306
EC number
1.14.13.225: With NADH or NADPH as one donor, and incorporation of one atom of oxygen
Protein Class

Descriptions

MICAL1 (molecule interacting with CasL) is a multidomain cytosolic protein with a putative flavoprotein monooxygenase region required for semaphorin-plexin repulsive axon guidance. The C-terminal domain of MICAL1 inhibits its enzymatic activity. Plexin binding to the C terminus disrupts the interaction of MICAL1 C terminus with the enzymatic domain, releasing autoinhibition and leading to the activation of the monooxygenase activity. Truncation of the C-terminal region (761-1048) relieves autoinhibition of MICAL.

Autoinhibitory domains (AIDs)

775-1070 (C-terminal autoinhibitory region) SS

Target domain

1-489 (FAD-binding domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for F1MH07

Entry ID Method Resolution Chain Position Source
AF-F1MH07-F1 Predicted AlphaFoldDB

No variants for F1MH07

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for F1MH07

No associated diseases with F1MH07

4 regional properties for F1MH07

Type Name Position InterPro Accession
domain Calponin homology domain 508 - 612 IPR001715
domain Zinc finger, LIM-type 695 - 757 IPR001781
domain FAD-binding domain 85 - 122 IPR002938
domain bMERB domain 921 - 1070 IPR022735

Functions

Description
EC Number 1.14.13.225 With NADH or NADPH as one donor, and incorporation of one atom of oxygen
Subcellular Localization
  • Cytoplasm
  • Cytoplasm, cytoskeleton
  • Endosome membrane
  • Midbody
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 GO annotations of cellular component

Name Definition
actin filament A filamentous structure formed of a two-stranded helical polymer of the protein actin and associated proteins. Actin filaments are a major component of the contractile apparatus of skeletal muscle and the microfilaments of the cytoskeleton of eukaryotic cells. The filaments, comprising polymerized globular actin molecules, appear as flexible structures with a diameter of 5-9 nm. They are organized into a variety of linear bundles, two-dimensional networks, and three dimensional gels. In the cytoskeleton they are most highly concentrated in the cortex of the cell just beneath the plasma membrane.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
endosome membrane The lipid bilayer surrounding an endosome.
hippocampal mossy fiber expansion Synaptic expansion of hippocampal mossy fiber axon that makes contact with the thorny excrescences of hippocampal CA3 pyramidal cell dendrites.
intercellular bridge A direct connection between the cytoplasm of two cells that is formed following the completion of cleavage furrow ingression during cell division. They are usually present only briefly prior to completion of cytokinesis. However, in some cases, such as the bridges between germ cells during their development, they become stabilised.
midbody A thin cytoplasmic bridge formed between daughter cells at the end of cytokinesis. The midbody forms where the contractile ring constricts, and may persist for some time before finally breaking to complete cytokinesis.

8 GO annotations of molecular function

Name Definition
actin binding Binding to monomeric or multimeric forms of actin, including actin filaments.
FAD binding Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
metal ion binding Binding to a metal ion.
NADPH oxidase H202-forming activity Catalysis of the reaction
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 Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from NADH or NADPH and one other donor, and one atom of oxygen is incorporated into one donor.
protein kinase binding Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.
SH3 domain binding Binding to a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins.
small GTPase binding Binding to a small monomeric GTPase.

5 GO annotations of biological process

Name Definition
actin filament depolymerization Disassembly of actin filaments by the removal of actin monomers from a filament.
negative regulation of apoptotic process Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
negative regulation of protein phosphorylation Any process that stops, prevents or reduces the rate of addition of phosphate groups to amino acids within a protein.
regulation of regulated secretory pathway Any process that modulates the frequency, rate or extent of regulated secretory pathway.
sulfur oxidation The chemical reactions and pathways resulting the addition of oxygen to elemental sulfur.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9BT23 LIMD2 LIM domain-containing protein 2 Homo sapiens (Human) PR
Q8TDZ2 MICAL1 [F-actin]-monooxygenase MICAL1 Homo sapiens (Human) EV
Q8BGB5 Limd2 LIM domain-containing protein 2 Mus musculus (Mouse) PR
Q9ERG0 Lima1 LIM domain and actin-binding protein 1 Mus musculus (Mouse) PR
Q8VDP3 Mical1 [F-actin]-monooxygenase MICAL1 Mus musculus (Mouse) EV
D3ZBP4 Mical1 [F-actin]-monooxygenase MICAL1 Rattus norvegicus (Rat) SS
10 20 30 40 50 60
MASTISTNPA HAHFESFLQA QLCQDVLSSF QGLCGALGVE PGGGLSQYHK VKAQLNYWNA
70 80 90 100 110 120
KSLWAKLDKR ASQPVYQQGR ACTGTKCLVV GAGPCGLRAA VELAMLGARV VLVEKRTKFS
130 140 150 160 170 180
RHNVLHLWPF TIHDLRALGA KKFYGRFCTG SLDHISIRQL QLLLLKVALL LGVEIHWGIT
190 200 210 220 230 240
FTGLQPPPKK GSGWRAQLQP SPPAQLAKYE FDVLISAAGG KFVPEGFTVR EMRGKLAIGI
250 260 270 280 290 300
TANFVNGRTV EETQVPEISG VARIYNQSFF QSLLKATGID LENIVYYKDD THYFVMTAKK
310 320 330 340 350 360
QCLLRLGVLH KDWPDTERLL GSANVVPEAL QRFARAAADF ATHGKLGKLE FARDAHGRPD
370 380 390 400 410 420
VSAFDFTSMM RAESSARVQE RHGTRLLLGL VGDCLVEPFW PLGTGVARGF LAAFDAAWMV
430 440 450 460 470 480
KRWAEGAGPL EVLAERESLY QLLSQTSPEN MHRNVAQYGL DPATRYPNLN LRAVTPSQVR
490 500 510 520 530 540
DLYDMEAKEP VQRMSDETDS GKAATGAVGS QEELLRWCQE QTAGYPGVHV TDLSSSWADG
550 560 570 580 590 600
LALCALVHRL RPALLEPSEL QGMGALEATS WALKMAEHEL GITPVLSAQA MVAGSDPLGL
610 620 630 640 650 660
IAYLSHFHSA FKSVPHNPGS VSQGSPGTAS AVLFLGKLQR TLQRTRTQEN GEDAGGKKPR
670 680 690 700 710 720
LEVKAETPST EEPPVPKPDE PMTPPSQQQD ASAEDLCALC GQHLYILERL CADGRFFHRS
730 740 750 760 770 780
CFRCHICEAT LWPGGYRQHP GDGYLYCLQH LPQTGHEEDS SDRGPESQDL PMSSENNTPS
790 800 810 820 830 840
GPATPVDLHQ GTSPVPNPIQ PTRRLIRLSS PERQRLSSLH LTPDPEMEPP PKPPRSCSTL
850 860 870 880 890 900
AHQALEASFK GWGMPVQSPQ VLEAMEMGEE ERSSSSEEET EEEEDVPLDS DMEHFLRNLA
910 920 930 940 950 960
ENSGTMNNYP TWRRTLLRRA KEEEMKRFCK AQAIQRRLNE IEAALRELEA RGTELELALR
970 980 990 1000 1010 1020
SQSSSPEKQK ALWVEQLLQL VQKKNSLVAE EAELMITVQE LNLEEKQWQL DQELRTYMNR
1030 1040 1050 1060
EETLKTAADR QAEDQVLRKL LDVVNQRDAL IRLQEERRLS ELASEPGVQG