MICA1_DANRE
ID MICA1_DANRE Reviewed; 1214 AA.
AC E7F9T0; F1R7H4;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 79.
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 Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
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 prevent repolymerization. {ECO:0000250|UniProtKB:Q8VDP3}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Mical family. {ECO:0000305}.
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DR EMBL; BX548066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001303659.1; NM_001316730.1.
DR RefSeq; XP_003201274.1; XM_003201226.4.
DR RefSeq; XP_009295352.1; XM_009297077.2.
DR AlphaFoldDB; E7F9T0; -.
DR SMR; E7F9T0; -.
DR STRING; 7955.ENSDARP00000121526; -.
DR PaxDb; E7F9T0; -.
DR PeptideAtlas; E7F9T0; -.
DR Ensembl; ENSDART00000184761; ENSDARP00000155850; ENSDARG00000011809.
DR Ensembl; ENSDART00000187222; ENSDARP00000154178; ENSDARG00000011809.
DR GeneID; 568573; -.
DR KEGG; dre:568573; -.
DR CTD; 64780; -.
DR ZFIN; ZDB-GENE-081022-3; mical1.
DR eggNOG; KOG1700; Eukaryota.
DR GeneTree; ENSGT00940000159117; -.
DR InParanoid; E7F9T0; -.
DR OrthoDB; 430978at2759; -.
DR PhylomeDB; E7F9T0; -.
DR PRO; PR:E7F9T0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 23.
DR Bgee; ENSDARG00000011809; Expressed in granulocyte and 19 other tissues.
DR ExpressionAtlas; E7F9T0; baseline.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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:0030042; P:actin filament depolymerization; ISS:UniProtKB.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
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 3: Inferred from homology;
KW Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton; FAD; Flavoprotein;
KW LIM domain; Metal-binding; Monooxygenase; NADP; Oxidoreductase;
KW Reference proteome; Zinc.
FT CHAIN 1..1214
FT /note="[F-actin]-monooxygenase mical1"
FT /id="PRO_0000416300"
FT DOMAIN 508..614
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 686..748
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 1053..1199
FT /note="bMERB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01195"
FT REGION 1..488
FT /note="Monooxygenase domain"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT REGION 484..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1194..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1061..1131
FT /evidence="ECO:0000255"
FT COMPBIAS 747..768
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1019
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 96
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 115..117
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 122..124
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 182
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 292
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 392
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 688
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 691
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 709
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 712
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 715
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 718
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 738
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 741
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
SQ SEQUENCE 1214 AA; 138021 MW; E9C4B901C4518CA1 CRC64;
MVNPLDSVNP SHALFEGFVQ AQTCKETQQN FTELCRHLQV DPKDYKHFYS KLKDRLNYWK
AKDLWQKIDK RAAHPDYDQG KACHQNKCLV LGAGPCGLRT AIELALLGAQ VVVLEKRSSF
TRNNVLHLWP FTIKDLLNLG AKKFYGRFCS GSIHHISIRQ LQLILLKVAL FLGVEVHTGV
AFEGLNEPSG SAGWRANVSP KSHPVADFQF DVFISAGGGK YVPDGFKIKE LRGKLAIGIT
ANFVNRHTKQ EAQVQEISGV ARIYNQQFFQ ALQSEIGVDL ENIVYYKDDT HYFVMTAKKA
SLLKKGVIKQ DFSDADKLLA PSNVNQEALQ DYAFEACDFS TEHLLPNLEF AKNHKGQADV
AMFDFTCMQR AESASLVKER NGKRLLIGLV GDSLVEPFWP LGTGIARGFL GAFDAAWMVR
SWGKGVQPME VLAERESVYQ LLSQTTPENT SKNYMAYSID PSTRYPNINL SSIKPRQVKR
LYEAEEQESK PNKLKKPDIK AKPRKDSMKR LEELLSWCQK NTVGYEHVKV KDLSESWRSG
LALCALIHSF RPELVDMSAL DEYNIIKNNK LAFDLMEKEF GITPIMRPGD MMTCGKIDQL
SMVVYLTQIR NALTEKDTPA AQSNTLSLSR KRSAVAFLNT LKRNSLQRHK DRLASVKGPR
QQNMKEKEEK KDVKEESLSS ETSACEPCYF CKKHLYVVER ESAEGKFFHR SCFNCFQCGS
TLRQGGYSFH SDNGRFYCEL HSLAEEEEGD EGHGGAQNHT ENGSKEDKNG ETTAASSPPA
HLSIKRKGSY KISVDPDFDE STEFPAPDQD EPPDLEESHQ PPKPSELSAE NTNMENQQHN
INPVPAPRGS RAPLPKPRTV HNVVHEPCNI PEEAEQIPEE PKPKPSLRKL QQSEEEKVDL
LSQDSDSETR GSSSAASTSS SSKQHEEEGY WSGGTTWGKS HREQRNRPCI RRKSEPPLPL
TGHSQHGKMR SKFSPWNLSS PRLQQRFSVH RVPAGQSQPD QYVSEDDNED DEDEDEEDLQ
AEHYLDCEGA DFEFSDSEKR NLKRMKTLER KAKMTEIQRF HKAQSIQRRL EEIEVTFKEL
EEKGVELERA LRGETGTGDP EIIDQWIELV QEKNNLLSEE SDLMVASRQL ELEDKQSMLE
MELRRYMEMD DSEKSPEQQK HEAEILQEML DVVDMRDSLV AFLEEKRLKE VNDQFNSSLD
AKRRSTTASQ VHWE
