Q8VDP3

EV
Gene name
Mical1 (Mical, Nical)
Protein name
[F-actin]-monooxygenase MICAL1
Names
Molecule interacting with CasL protein 1, MICAL-1, mMical1, NEDD9-interacting protein with calponin homology and LIM domains
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:171580
EC number
1.6.3.1: With oxygen as acceptor
Protein Class
CALPONIN HOMOLOGY DOMAIN-CONTAINING PROTEIN DDB_G0272472-RELATED (PTHR23167)

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)

761-1048 (C-terminal autoinhibitory region) EV

Target domain

1-489 (FAD-binding domain)

Relief mechanism

Partner binding

Assay

Deletion assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

6 structures for Q8VDP3

Entry ID Method Resolution Chain Position Source
2BRA X-ray 200 A A/B 1-484 PDB
2BRY X-ray 145 A A/B 1-489 PDB
2C4C X-ray 290 A A/B 1-489 PDB
4TXI X-ray 231 A A 2-615 PDB
4TXK X-ray 288 A A 2-615 PDB
AF-Q8VDP3-F1 Predicted AlphaFoldDB

21 variants for Q8VDP3

Variant ID(s) Position Change Description Diseaes Association Provenance
rs46648788 72 S>C No Ensembl
rs241080081 179 V>I No Ensembl
rs223150407 310 R>H No Ensembl
rs219721095 321 G>S No Ensembl
rs49273840 378 V>F No Ensembl
rs1132729107 497 E>K No Ensembl
rs242358119 504 T>I No Ensembl
rs244935615 562 M>L No Ensembl
rs243625568 620 V>A No Ensembl
rs215602919 624 S>P No Ensembl
rs49597497 648 D>G No Ensembl
rs226530831 677 A>T No Ensembl
rs257967767 758 T>P No Ensembl
rs220515960 773 V>A No Ensembl
rs586195609 774 T>M No Ensembl
rs46048980 840 V>I No Ensembl
rs253351979 842 A>V No Ensembl
rs258733996 843 P>S No Ensembl
rs583952271 854 D>E No Ensembl
rs258028096 893 Y>C No Ensembl
rs251946918 956 L>F No Ensembl

No associated diseases with Q8VDP3

4 regional properties for Q8VDP3

Type Name Position InterPro Accession
domain Calponin homology domain 507 - 611 IPR001715
domain Zinc finger, LIM-type 681 - 743 IPR001781
domain FAD-binding domain 85 - 121 IPR002938
domain bMERB domain 905 - 1048 IPR022735

Functions

Description
EC Number 1.6.3.1 With oxygen as acceptor
Subcellular Localization
  • Cytoplasm
  • Cytoplasm, cytoskeleton
  • Endosome membrane
  • Midbody
PANTHER Family PTHR23167 CALPONIN HOMOLOGY DOMAIN-CONTAINING PROTEIN DDB_G0272472-RELATED
PANTHER Subfamily PTHR23167:SF35 [F-ACTIN]-MONOOXYGENASE MICAL1
PANTHER Protein Class scaffold/adaptor protein
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytoskeleton A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles.
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.

9 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.
monooxygenase activity Catalysis of the incorporation of one atom from molecular oxygen into a compound and the reduction of the other atom of oxygen to water.
NAD(P)H oxidase H2O2-forming activity Catalysis of the reaction: NAD(P)H + H+ + O2 = NAD(P)+ + hydrogen peroxide.
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.

6 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 cysteine-type endopeptidase activity involved in apoptotic process Any process that stops, prevents, or reduces the frequency, rate or extent of a cysteine-type endopeptidase activity involved in the 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
F1MH07 MICAL1 [F-actin]-monooxygenase MICAL1 Bos taurus (Bovine) SS
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
D3ZBP4 Mical1 [F-actin]-monooxygenase MICAL1 Rattus norvegicus (Rat) SS
10 20 30 40 50 60
MASPASTNPA HDHFETFVQA QLCQDVLSSF QGLCRALGVE SGGGLSQYHK IKAQLNYWSA
70 80 90 100 110 120
KSLWAKLDKR ASQPVYQQGQ ACTNTKCLVV GAGPCGLRAA VELALLGARV VLVEKRIKFS
130 140 150 160 170 180
RHNVLHLWPF TIHDLRALGA KKFYGRFCTG TLDHISIRQL QLLLLKVALL LGVEIHWGVK
190 200 210 220 230 240
FTGLQPPPRK GSGWRAQLQP NPPAQLASYE FDVLISAAGG KFVPEGFTIR EMRGKLAIGI
250 260 270 280 290 300
TANFVNGRTV EETQVPEISG VARIYNQKFF QSLLKATGID LENIVYYKDE THYFVMTAKK
310 320 330 340 350 360
QCLLRLGVLR QDLSETDQLL GKANVVPEAL QRFARAAADF ATHGKLGKLE FAQDARGRPD
370 380 390 400 410 420
VAAFDFTSMM RAESSARVQE KHGARLLLGL VGDCLVEPFW PLGTGVARGF LAAFDAAWMV
430 440 450 460 470 480
KRWAEGAGPL EVLAERESLY QLLSQTSPEN MHRNVAQYGL DPATRYPNLN LRAVTPNQVQ
490 500 510 520 530 540
DLYDMMDKEH AQRKSDEPDS RKTTTGSAGT EELLHWCQEQ TAGFPGVHVT DFSSSWADGL
550 560 570 580 590 600
ALCALVHHLQ PGLLEPSELQ GMGALEATTW ALRVAEHELG ITPVLSAQAV MAGSDPLGLI
610 620 630 640 650 660
AYLSHFHSAF KNTSHSSGLV SQPSGTPSAI LFLGKLQRSL QRTRAKVDEE TPSTEEPPVS
670 680 690 700 710 720
EPSMSPNTPE LSEHQEAGAE ELCELCGKHL YILERFCVDG HFFHRSCFCC HTCEATLWPG
730 740 750 760 770 780
GYGQHPGDGH FYCLQHLPQE DQKEADNNGS LESQELPTPG DSNMQPDPSS PPVTRVSPVP
790 800 810 820 830 840
SPSQPARRLI RLSSLERLRL SSLNIIPDSG AEPPPKPPRS CSDLARESLK SSFVGWGVPV
850 860 870 880 890 900
QAPQVPEAIE KGDDEEEEEE EEEEEEEPLP PLEPELEQTL LTLAKNPGAM TKYPTWRRTL
910 920 930 940 950 960
MRRAKEEEMK RFCKAQAIQR RLNEIEATMR ELEAEGTKLE LALRKESSSP EQQKKLWLDQ
970 980 990 1000 1010 1020
LLRLIQKKNS LVTEEAELMI TVQELDLEEK QRQLDHELRG YMNREETMKT EADLQSENQV
1030 1040
LRKLLEVVNQ RDALIQFQEE RRLREMPA