MICA1_BOVIN
ID MICA1_BOVIN Reviewed; 1070 AA.
AC F1MH07; A2VDL7;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=[F-actin]-monooxygenase MICAL1;
DE EC=1.14.13.225 {ECO:0000250|UniProtKB:Q8TDZ2};
DE EC=1.6.3.1 {ECO:0000250|UniProtKB:Q8TDZ2};
DE AltName: Full=Molecule interacting with CasL protein 1;
DE Short=MICAL-1;
GN Name=MICAL1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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). Acts as a cytoskeletal regulator
CC that connects NEDD9 to intermediate filaments. Also acts as a negative
CC regulator of apoptosis via its interaction with STK38 and STK38L; acts
CC by antagonizing STK38 and STK38L activation by MST1/STK4. Involved in
CC regulation of lamina-specific connectivity in the nervous system such
CC as the development of lamina-restricted hippocampal connections.
CC Through redox regulation of the actin cytoskeleton controls the
CC intracellular distribution of secretory vesicles containing
CC L1/neurofascin/NgCAM family proteins in neurons, thereby regulating
CC their cell surface levels. May act as Rab effector protein and play a
CC role in vesicle trafficking. {ECO:0000250|UniProtKB:Q8TDZ2}.
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:0000250|UniProtKB:Q8TDZ2};
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:0000250|UniProtKB:Q8TDZ2};
CC -!- SUBUNIT: Interacts with STK38 and STK38L. Associates with the SH3
CC domain of NEDD9. Interacts with VIM and PLXNA3. Interacts with RAB1B,
CC RAB8A, RAB10, RAB13 and RAB15 (in their GTP-bound forms); binding to
CC RAB1B is of low affinity compared to other Rab proteins; at least in
CC case of RAB8A and RAB10 can bind 2 molecules of the Rab proteins
CC simultaneously. {ECO:0000250|UniProtKB:Q8TDZ2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TDZ2}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8TDZ2}.
CC -!- DOMAIN: The bivalent Mical/EHBP Rab binding (bMERB) domain, mediates
CC binding to predominantly Rab8, Rab10, Rab10, Rab13 and Rab15 (in their
CC GTP-bound forms). {ECO:0000250|UniProtKB:Q8TDZ2}.
CC -!- DOMAIN: The C-terminal coiled coil part contains the plexin-interacting
CC region. {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:0000250|UniProtKB:Q8VDP3}.
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DR EMBL; DAAA02025917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC133298; AAI33299.1; -; mRNA.
DR RefSeq; NP_001075051.1; NM_001081582.1.
DR RefSeq; XP_005210830.1; XM_005210773.3.
DR RefSeq; XP_010806727.1; XM_010808425.2.
DR AlphaFoldDB; F1MH07; -.
DR SMR; F1MH07; -.
DR STRING; 9913.ENSBTAP00000010714; -.
DR PaxDb; F1MH07; -.
DR PRIDE; F1MH07; -.
DR Ensembl; ENSBTAT00000010714; ENSBTAP00000010714; ENSBTAG00000008147.
DR GeneID; 508306; -.
DR KEGG; bta:508306; -.
DR CTD; 64780; -.
DR VEuPathDB; HostDB:ENSBTAG00000008147; -.
DR VGNC; VGNC:31457; MICAL1.
DR eggNOG; KOG1700; Eukaryota.
DR GeneTree; ENSGT00940000159117; -.
DR HOGENOM; CLU_000329_0_0_1; -.
DR InParanoid; F1MH07; -.
DR OMA; CKAQSIQ; -.
DR OrthoDB; 430978at2759; -.
DR TreeFam; TF324129; -.
DR Proteomes; UP000009136; Chromosome 9.
DR Bgee; ENSBTAG00000008147; Expressed in nasopharynx and 107 other tissues.
DR ExpressionAtlas; F1MH07; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:1990026; C:hippocampal mossy fiber expansion; IEA:Ensembl.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0030042; P:actin filament depolymerization; ISS:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:1903305; P:regulation of regulated secretory pathway; IEA:Ensembl.
DR GO; GO:0019417; P:sulfur oxidation; ISS:UniProtKB.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR022735; bMERB_dom.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF12130; DUF3585; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF00412; LIM; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00132; LIM; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS51848; BMERB; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton; FAD; Flavoprotein;
KW LIM domain; Metal-binding; Monooxygenase; NADP; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..1070
FT /note="[F-actin]-monooxygenase MICAL1"
FT /id="PRO_0000416298"
FT DOMAIN 508..612
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 695..757
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 921..1070
FT /note="bMERB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01195"
FT REGION 1..489
FT /note="Monooxygenase domain"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT REGION 643..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 928..1030
FT /evidence="ECO:0000255"
FT COMPBIAS 646..667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..887
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:0000250|UniProtKB:Q8VDP3"
FT BINDING 114..116
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 121..123
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 181
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 293
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 393
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 697
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 700
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 718
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 721
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 724
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 727
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 747
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 750
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT MOD_RES 475
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:D3ZBP4"
FT MOD_RES 793
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT MOD_RES 876
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT MOD_RES 1060
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT CONFLICT 553
FT /note="A -> G (in Ref. 2; AAI33299)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1070 AA; 118696 MW; 1D4063C4C925AA86 CRC64;
MASTISTNPA HAHFESFLQA QLCQDVLSSF QGLCGALGVE PGGGLSQYHK VKAQLNYWNA
KSLWAKLDKR ASQPVYQQGR ACTGTKCLVV GAGPCGLRAA VELAMLGARV VLVEKRTKFS
RHNVLHLWPF TIHDLRALGA KKFYGRFCTG SLDHISIRQL QLLLLKVALL LGVEIHWGIT
FTGLQPPPKK GSGWRAQLQP SPPAQLAKYE FDVLISAAGG KFVPEGFTVR EMRGKLAIGI
TANFVNGRTV EETQVPEISG VARIYNQSFF QSLLKATGID LENIVYYKDD THYFVMTAKK
QCLLRLGVLH KDWPDTERLL GSANVVPEAL QRFARAAADF ATHGKLGKLE FARDAHGRPD
VSAFDFTSMM RAESSARVQE RHGTRLLLGL VGDCLVEPFW PLGTGVARGF LAAFDAAWMV
KRWAEGAGPL EVLAERESLY QLLSQTSPEN MHRNVAQYGL DPATRYPNLN LRAVTPSQVR
DLYDMEAKEP VQRMSDETDS GKAATGAVGS QEELLRWCQE QTAGYPGVHV TDLSSSWADG
LALCALVHRL RPALLEPSEL QGMGALEATS WALKMAEHEL GITPVLSAQA MVAGSDPLGL
IAYLSHFHSA FKSVPHNPGS VSQGSPGTAS AVLFLGKLQR TLQRTRTQEN GEDAGGKKPR
LEVKAETPST EEPPVPKPDE PMTPPSQQQD ASAEDLCALC GQHLYILERL CADGRFFHRS
CFRCHICEAT LWPGGYRQHP GDGYLYCLQH LPQTGHEEDS SDRGPESQDL PMSSENNTPS
GPATPVDLHQ GTSPVPNPIQ PTRRLIRLSS PERQRLSSLH LTPDPEMEPP PKPPRSCSTL
AHQALEASFK GWGMPVQSPQ VLEAMEMGEE ERSSSSEEET EEEEDVPLDS DMEHFLRNLA
ENSGTMNNYP TWRRTLLRRA KEEEMKRFCK AQAIQRRLNE IEAALRELEA RGTELELALR
SQSSSPEKQK ALWVEQLLQL VQKKNSLVAE EAELMITVQE LNLEEKQWQL DQELRTYMNR
EETLKTAADR QAEDQVLRKL LDVVNQRDAL IRLQEERRLS ELASEPGVQG
