MCA3A_DANRE
ID MCA3A_DANRE Reviewed; 1994 AA.
AC F1QH17; Q1LWQ6; Q6PBR2;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Protein-methionine sulfoxide oxidase mical3a;
DE EC=1.14.13.225 {ECO:0000250|UniProtKB:Q7RTP6};
DE AltName: Full=Molecule interacting with CasL protein 3A;
DE Short=MICAL-3A;
GN Name=mical3a; ORFNames=si:dkeyp-122e2.1;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-677.
RC TISSUE=Eye;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2003) 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. 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=AAH59615.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=CAK04976.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAK11321.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL929264; CAK04976.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BX537323; CAK04976.1; JOINED; Genomic_DNA.
DR EMBL; BX537323; CAK11321.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL929264; CAK11321.1; JOINED; Genomic_DNA.
DR EMBL; BC059615; AAH59615.1; ALT_SEQ; mRNA.
DR AlphaFoldDB; F1QH17; -.
DR SMR; F1QH17; -.
DR STRING; 7955.ENSDARP00000037651; -.
DR PaxDb; F1QH17; -.
DR PRIDE; F1QH17; -.
DR Ensembl; ENSDART00000161990; ENSDARP00000136331; ENSDARG00000097017.
DR ZFIN; ZDB-GENE-050126-2; mical3a.
DR eggNOG; KOG1700; Eukaryota.
DR GeneTree; ENSGT00940000155580; -.
DR HOGENOM; CLU_000329_1_1_1; -.
DR InParanoid; F1QH17; -.
DR OMA; CREIRIE; -.
DR PRO; PR:F1QH17; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 18.
DR Bgee; ENSDARG00000097017; Expressed in muscle tissue and 30 other tissues.
DR ExpressionAtlas; F1QH17; 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:0051015; F:actin filament binding; IEA:InterPro.
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; IPR045268; LIMA-like.
DR InterPro; IPR029941; MICAL3.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24206; PTHR24206; 2.
DR PANTHER; PTHR24206:SF66; PTHR24206:SF66; 2.
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; Exocytosis; FAD;
KW Flavoprotein; LIM domain; Metal-binding; Monooxygenase; NADP; Nucleus;
KW Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..1994
FT /note="Protein-methionine sulfoxide oxidase mical3a"
FT /id="PRO_0000416305"
FT DOMAIN 521..627
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 772..834
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 1816..1982
FT /note="bMERB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01195"
FT REGION 2..498
FT /note="Monooxygenase domain"
FT /evidence="ECO:0000250"
FT REGION 666..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1176..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1281..1476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1493..1555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1598..1747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1796..1855
FT /evidence="ECO:0000255"
FT COILED 1894..1960
FT /evidence="ECO:0000255"
FT COMPBIAS 668..709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..888
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..963
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..996
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1040
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1389..1403
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1434..1458
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1604..1633
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1634..1665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1680..1718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1732..1747
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 101..129
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 120
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 127
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1994 AA; 222811 MW; 7ABC1319AC1905BA CRC64;
MGDGGVNAVG EGVNQSHMLF DRFVQATTCK GTLKAFQELC DFLELKPNEY RVFYHKLKSK
LNYWKAKALW AKLDKRASHK EYKKGRACAN TKCLIIGAGP CGLRTAIELG FLGAKVVLLE
KRDAFSRNNV LHLWPFTIQD LRGLGAKKFY GKFCAGAIDH ISIRQLQLML LKVALLLGIE
IHVNVEFKGL IEPPEDQENE RIGWRAEVHP RTHPVNELEF DVIIGADGRR NTLSGFRRKE
FRGKLAIAIT ANFINRNTTA EAKVEEISGV AFIFNQKFFQ DLREATGIDL ENIVYYKDDT
HYFVMTAKKQ SLLEKGVILH DYADTEMLLS RANVDQKALL SYAREAADFS TNHQLPKLDF
AINHYGQPDV AMFDFTCMYA SENAALVRQR NGHKLLVALV GDSLLEPFWP MGTGIARGFL
AAMDSAWMVR SWAHGSSPLE VLAERESIYR LLPQTTPENV SKNFSQYSVD PTTRYPNISL
HQVRPNQVRH LLDTGETRDL RVDLENVVNS STPKLTRNES IVRSSKLLNW CQRQTEGYRG
VSVSDLTTSW KSGLALCALI HRYRPDLIDF ESLDEKDVEK NNQLAFDVAE REFGISPIMT
GKEMSVVVEP DKLSMVMYLS QFYEMFKDTV PPGENQNLSP EEKAALIAST KSPISFLSKL
GQSIAISRKR NPKDKKEKEL DGLGKRRKTS QAGQSEDEEL QRANRDDRPS IATALAERKI
DSAAAANNNN KVKSMATQLL AKFEENAPTQ STGLKRQGSF RKEFPQNIGG SDVCFFCRKR
VYVMERLSAE GKFFHRSCFK CDYCGTTLRL SSYAFDVEDG KFYCKPHYCY RLSGVAQRKR
PAPAAAPANA KEPQVLAVSP NTVDAPGQAI TTQTPAERRP SETEVNGVTE PSVAKRLKGT
PERIELENYR LSMMREEELE EVPEETLAEH NLSSVLDKAT DIEEGSSSSE SDMEEEDEDA
EAAGPSDLGG VPWKEAVELH AKLKGESDPG ADDDGLHDGD GEMDEDEEEE EDEEDEDEEE
EEESSEEPCE EDDDPEAEAG SPDFEPGTEI DQEDIPSDAE AEARSRCIDE VVTLPVDNDK
TESQGQVFNT AEKTSANPRE LIVDVVLSPI QKPALPIEEV HEVSPVVLVK SPGARFFPEP
YLPDKVKQNI PPPQSPDVKT PHSPVAQIIA LSPICSQPVP QPGTASPKSP VQPQPCACSP
TGNPLSPICT QSQPCNEPPS PLSTSSPVRT QPVPAVTSTP LAKPASENRT NEHLKDSTPE
LKKTDLIEEF WLKSAEIRKS LGLTPLERSK TAVEKSIVKT PTPESSSPKS YTPEDLSEEQ
KPTFTGRSII RRINITLEGQ VISPVEPKSN GSEKKDLSSS SGLGLNGSVT TSQTAASDSY
NNSDSTMLTP PSSPPPPPPR EEPACLQNKK SQVSWDNLLE GTEEPKSETM PIKPRTPVSP
PQPKQKPVTA PVPTPRTNPP VVMRVKEPNK PRREEVRKSF VECVDEIPFA DDVEDTYDDR
TPDASGLEKF YTPPTSKVNR DKPPLHLALA MENGKPNIPG VSRTAKGSQH FSPEAKEIAE
ERMRAREKSV KSQALKDAMA KQLTKMKDSE VAKGAVAKVA WDIPETKGKS KKQSKAQKDS
AVKALESKKQ ADTLPDRFFS TPSSKALDSS VTSSESSTGG KSKKRSSLFS PRKNKKEKKA
KNERLSSTEE TPPKHKSLWK AVFSGYKKDK KKKDDKSCPS TPSSSTTGDS GKKKDSPLDR
SSDLRLRRNL SFSEDSDLSC DDVLERSSQK SKGDSVYVPH ALAFKRSYAT KKTYTEEELN
AKLTRRVQKA ARRQAKQEEL KRLHRAQMIQ RQLEQVEEKQ RQLEERGVAV EKALRGEADY
WGESNYSEIL DLHLGGMGKK DDPKLMQEWF KLVQEKNALV RYESELMIFA RELELEDRQS
RLQQELRERM AIDDHLKTEE ELAEEKQILN EMLEVVEQRD SLVALLEEQR LREKEEDKDL
EAVMLSKGFN LNWA
