MCA3B_DANRE
ID MCA3B_DANRE Reviewed; 1673 AA.
AC F1QWK4; Q1LV75;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Protein-methionine sulfoxide oxidase mical3b;
DE EC=1.14.13.225 {ECO:0000250|UniProtKB:Q7RTP6};
DE AltName: Full=Molecule interacting with CasL protein 3B;
DE Short=MICAL-3B;
GN Name=mical3b;
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. Acts by
CC modifying actin subunits through the addition of oxygen to form
CC methionine-sulfoxide, leading to promote actin filament severing and
CC prevent repolymerization. Involved in exocytic vesicles tethering and
CC fusion: the monooxygenase activity is required for this process (By
CC similarity). {ECO:0000250}.
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:Q7RTP6};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Nucleus.
CC Note=Mainly localizes in the nucleus. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Mical family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK05184.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAK11365.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BX901962; CAK05184.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BX649444; CAK05184.1; JOINED; Genomic_DNA.
DR EMBL; BX649444; CAK11365.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BX901962; CAK11365.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; F1QWK4; -.
DR SMR; F1QWK4; -.
DR STRING; 7955.ENSDARP00000122943; -.
DR PaxDb; F1QWK4; -.
DR Ensembl; ENSDART00000147699; ENSDARP00000122943; ENSDARG00000094732.
DR ZFIN; ZDB-GENE-050211-1; mical3b.
DR eggNOG; KOG1700; Eukaryota.
DR GeneTree; ENSGT00940000155580; -.
DR HOGENOM; CLU_000329_3_0_1; -.
DR InParanoid; F1QWK4; -.
DR OMA; FYCKQHY; -.
DR PhylomeDB; F1QWK4; -.
DR TreeFam; TF324129; -.
DR PRO; PR:F1QWK4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 4.
DR Bgee; ENSDARG00000094732; Expressed in brain and 28 other tissues.
DR ExpressionAtlas; F1QWK4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; 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: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:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030042; P:actin filament depolymerization; ISS:UniProtKB.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
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; IPR029941; MICAL3.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR23167:SF51; PTHR23167:SF51; 1.
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; Exocytosis; FAD;
KW Flavoprotein; LIM domain; Metal-binding; Monooxygenase; NADP; Nucleus;
KW Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..1673
FT /note="Protein-methionine sulfoxide oxidase mical3b"
FT /id="PRO_0000416306"
FT DOMAIN 512..618
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 791..853
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 1495..1661
FT /note="bMERB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01195"
FT REGION 2..492
FT /note="Monooxygenase domain"
FT /evidence="ECO:0000250"
FT REGION 647..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1475..1531
FT /evidence="ECO:0000255"
FT COILED 1573..1638
FT /evidence="ECO:0000255"
FT COMPBIAS 654..693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..1012
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1037
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 96..124
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1673 AA; 187262 MW; 342D39D5E7C763C4 CRC64;
MWDGQSEMCQ AHVLFDSFVQ AATCKETLRA FQDLCEELNL NPGGQPQFYH TLRSRLHYWK
AKALWAKLDK RACQKEYMRG HACTSTTCLI IGAGPCGLRT AIELGFLGAR VVLVEKRDAF
SRNNVLHLWP FTIQDLRGLG AKKFYGKFCA GAIDHISIRQ LQLMLLKVAL LLGVEVHVNV
EFKHLLEPPE NQEKRVGWRA EVQPSSHPVR QLEFDVVIGA DGRRNTLPGF RRKEFRGKLA
IAITANFINR NTTAEAKVEE ISGVAFIFNQ RFFQDLRQAT GIDLENIVYY KDDTHYFVMT
AKKQSLLEKG VILRDYADTE MLLSRHNVDQ NALLSYAREA ADFSTNHQLP ALDFAINHYG
QSDVAMFDFT CMYASENAAM VRQRMGHPLL VALVGDSLLE PFWPMGTGIA RGFLAAMDTA
WMVRSWGQGN TPLEVLAERE SVYRLLPQTT PENVSKNYSQ FSVDPASRYP NINMQLINAA
QVRHLIDTGE GPVLGLDAVS SPHPRLTRQE SMARYSKLLS WCQEHTHGYR KVCVTDFTSS
WRSGLALCAL IHTFRPDLID FASLEESEAE FSGQLGLDVA EQEFGICPIM TGKEMSVLEE
SDSLCMVMYL SQLHELLKDT SPPSGSQSSE ERAVLFSSSR SPISLLSKLG QSLSRKRNPK
DKKEKEADSV GKRRRTSQAG QSEEEDALHD GNENKSPAET PGSEPKASEG HSKVRSMASL
LLAKFEENSP SPSTTAIRRQ NYIHMYTGGV SSLALQIANQ IQSQQAQAPK LLHRRESGSQ
KDLPVNVGSS DVCYFCGRRV YVMERLSAEG KFFHRSCFQC DHCSSTIRLS NYTYDQLHGK
FYCKHHFSFR LASVAQRKRP APPVAPRPAQ ASLAASSAST SLSSLGSVGT ATPDSWSSST
HTDMASSLAK RLCGTPERIE LENYKPSPQK QDSPLQEVPE ETLAQHNLSA SLQEKNAEEQ
SSSSESDLEE EELVWKKGEE LHARTNGERK LDLEEELKEE EGGEKLEKQE GEEEGEVSEE
EQDEGDSSDE SYEGCSDDPD IDVSSLSESK LCDQREQEES VPFHQSPAST ESPVSMKPSE
SDLTPDPSTT PESSPAKRSE VVEEFWMKSA EIRKSLGLTP LSRELQPKHI AASTQTSNVK
ESFYTSVTYN TAALDSPNQS ARICDSSTQT HSVTDLQETS PLGPTDGDAG VDLGRCSVVH
RLSITVEGCV MADNQGLDST SFATESVLNP DAGLPTPPYS PSHSPLVGKQ CRALHHSEPI
LDREVMAFSS TCTASVPQRS SFKSDLEQAQ SLPPDEIEIL CGDEAEKLPE RSCRMESGEV
DNRRAEHSRT LPDRVVAPLL AGGPEVRLRR SEMKLWGPDA DGDVKEKKRS SLFSPRKSRK
NGNAAAESGR ETGKHKSLWK TVFSVYKKDK KRKEVAVVAE TLPAANNGSK RKVSGINRTT
DLCFRKNPSF SEDTDMSCHA LLERCPLRAQ RAGTEEELNA RLTRRVQRAA RRQAKQEELR
RLHRAQIIQR QLEQVEVKQR QLEEKGVAVE KALRGEADFW EDSSTSVLLD VHLCGMGKKD
DPSLMHQWFK LVQEKNALVR YESELMIFAR ELELEDRQSR LQQELRERMA VDDHLKGEEE
LAEERRILSE MLDVVEQRDA LVALLEEQRV REKEEDSDLE AVMLSKGFSL HWD
