MICA2_XENTR
ID MICA2_XENTR Reviewed; 1126 AA.
AC F6QZ15;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=[F-actin]-monooxygenase mical2 {ECO:0000250|UniProtKB:O94851};
DE EC=1.14.13.225 {ECO:0000250|UniProtKB:O94851};
DE AltName: Full=Molecule interacting with CasL protein 2;
DE Short=MICAL-2;
GN Name=mical2 {ECO:0000250|UniProtKB:O94851};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
CC -!- FUNCTION: Nuclear monooxygenase that promotes depolymerization of F-
CC actin by mediating oxidation of specific methionine residues on actin
CC and regulates the srf signaling. Acts by modifying nuclear actin
CC subunits through the addition of oxygen to form methionine-sulfoxide,
CC leading to promote actin filament severing and prevent repolymerization
CC (By similarity). Acts as a key regulator of the srf signaling pathway
CC elicited by nerve growth factor and serum: mediates oxidation and
CC subsequent depolymerization of nuclear actin, leading to increase
CC mkl1/mrtf-a presence in the nucleus and promote srf:mkl1/mrtf-a-
CC dependent gene transcription (By similarity).
CC {ECO:0000250|UniProtKB:F1RA39, ECO:0000250|UniProtKB:O94851}.
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:O94851};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q8TDZ2};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O94851}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8BML1}.
CC -!- SIMILARITY: Belongs to the Mical family. {ECO:0000305}.
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DR EMBL; AAMC01118102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118106; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118107; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118109; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118110; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118112; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118113; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118118; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01118127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F6QZ15; -.
DR SMR; F6QZ15; -.
DR STRING; 8364.ENSXETP00000029978; -.
DR PaxDb; F6QZ15; -.
DR eggNOG; KOG1700; Eukaryota.
DR HOGENOM; CLU_000329_0_1_1; -.
DR InParanoid; F6QZ15; -.
DR OMA; RSAICFM; -.
DR TreeFam; TF324129; -.
DR Proteomes; UP000008143; Genome assembly.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0043914; F:NADPH:sulfur oxidoreductase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB.
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:0030042; P:actin filament depolymerization; ISS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0001947; P:heart looping; ISS:UniProtKB.
DR GO; GO:0010735; P:positive regulation of transcription via serum response element binding; ISS:UniProtKB.
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; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR029939; MICAL2.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR23167:SF39; PTHR23167:SF39; 1.
DR Pfam; PF00307; CH; 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; PS50021; CH; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 3: Inferred from homology;
KW Actin-binding; Cytoplasm; FAD; Flavoprotein; LIM domain; Metal-binding;
KW Monooxygenase; NADP; Nucleus; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..1126
FT /note="[F-actin]-monooxygenase mical2"
FT /id="PRO_0000416303"
FT DOMAIN 516..619
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 1001..1063
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 2..494
FT /note="Monooxygenase domain"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT REGION 748..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 659..680
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 754..773
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..821
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..921
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 116..118
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 123..125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 183
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 299
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 399
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 1003
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1006
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1024
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1027
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1030
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1033
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1053
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1056
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
SQ SEQUENCE 1126 AA; 125940 MW; 357FFD6F8C2F8E53 CRC64;
MGENGDDKHG RSGQLFENFI QATTCKGTLQ AFNILTRQLE LDPQDHRHFY AKLKSKVTSW
KAKALWNKLD KKHGQKEYKK GKACIGTKCL IIGGGPCGLR TAIELSCLGA KVVVVEKRDT
FSRNNVLHLW PYTIHDLRCL GAKKFYGKFC AGAIDHISIW QLQLMLFKIA LLHGIEIHVN
VEFMKLLEPL EDQENQNIIA LFCTESESPD NSECKTRLSA PVVFRCIVGI GGDHSFPNTL
AFAFIYIYMN RNKEAVGPSP VWALAGRPRP LHTALLQPGR QQNRIDLENI VYYKDSTHYF
VMTAKKQSLL DKGVIINDYA DAEMLLCAEN VDQDNLQSYA REAADFATNY QLPSLDFAIN
HYGQPDVAMF DFTSMYASEN AALVRERHGH QLLVALVGDS LLEPFWPMGT GCARGFLAAF
DTAWMVRSWA QGALPLELLA ERISLLIFLN HRLTWQFLNP KKGLQTCHPN VWIPSHALRL
SHHVKHLFIT NELQTCSLER ASSIRRSVGV SRHESDVRPN KLLIWCQKQT EGYGNVTVTN
LTSSWKSGLA LCALIHRFRP ELVDFGSLKE DDVVGNNQLA FDIAEREFGI SPMTTGKEMA
ATEEPDKLSM VLYLSKFYEL FRGAPLRPVD TASKDNGDAR SAKPSNLIVN NYLNLTLPRK
RVPKDEKTSD DSDLNKRRKT VFRCFEEPAN VPSRNVNSGN ECNDTKEVIN QNKVKSMATQ
LLAKFEENAP NTSLRRQESL TLSEADQAVT APLTDPPPVN PRFAKPQEPT PSPPQAETKR
QFQAVSRTQP VVRPPVQPRP GPAKPTRELR VVERAQSHPD DLGRSESLSS ACPSALVLSN
ILERLQDLEE KAQQKRAQNL ANRDFHKKNI KEKAAHLASL FGSVDLPKNK LPSLGFSHHS
PQIPYSSSRT PDPPPPSSSS DSSPSSAPSR KSGMSWKGST FFSKHSLNVW ILMTVGKVSS
GIGAVAEVLV NLYMCDHKPK PKSSHLGSLR KEFPANIGGS DTCYFCKRRV YVVERLSAEG
HFFHRECFKC AFCSTSIRLG NYVFNVEDGN FYCQPHFMHS VTKNKHRKRR TESKAQLEED
KTWRSGEAEA AEVATDSAYS ACSSSGDSSP VPLVPFNIPV LDPLIG
