MICA3_BOVIN
ID MICA3_BOVIN Reviewed; 1960 AA.
AC G3MWR8;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=[F-actin]-monooxygenase MICAL3;
DE EC=1.14.13.225 {ECO:0000250|UniProtKB:Q7RTP6};
DE AltName: Full=Molecule interacting with CasL protein 3;
DE Short=MICAL-3;
GN Name=MICAL3;
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).
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). Seems to act as Rab effector
CC protein and play a role in vesicle trafficking. Involved in exocytic
CC vesicles tethering and fusion: the monooxygenase activity is required
CC for this process and implicates RAB8A associated with exocytotic
CC vesicles. Required for cytokinesis. Contributes to stabilization and/or
CC maturation of the intercellular bridge independently of its
CC monooxygenase activity. Promotes recruitment of Rab8 and ERC1 to the
CC intercellular bridge, and together these proteins are proposed to
CC function in timely abscission. {ECO:0000250|UniProtKB:Q7RTP6}.
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 -!- SUBUNIT: Interacts with RAB1B, RAB8A, RAB10, RAB13 and RAB15 (in their
CC GTP-bound forms); binding to RAB1B is of low affinity compared to other
CC Rab proteins; at least in case of RAB8A can bind 2 molecules of RAB8A
CC simultaneously through a high and a low affinity binding site,
CC respectively. Interacts with ERC1 and RAB8A; may bridge ERC1 with
CC RAB8A. Interacts with KIF23 and ERC1; enhances the interaction between
CC KIF23 and ERC1. Interacts with NINL. {ECO:0000250|UniProtKB:Q7RTP6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7RTP6}.
CC Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q7RTP6}. Cytoplasm,
CC cytoskeleton {ECO:0000250|UniProtKB:Q7RTP6}. Nucleus
CC {ECO:0000250|UniProtKB:Q7RTP6}. Midbody {ECO:0000250|UniProtKB:Q7RTP6}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q7RTP6}.
CC Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000250|UniProtKB:Q7RTP6}. Note=Mainly localizes in the nucleus.
CC {ECO:0000250|UniProtKB:Q7RTP6}.
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:Q7RTP6}.
CC -!- SIMILARITY: Belongs to the Mical family. {ECO:0000305}.
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DR EMBL; DAAA02014628; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02014629; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002687965.2; XM_002687919.5.
DR RefSeq; XP_015319081.1; XM_015463595.1.
DR AlphaFoldDB; G3MWR8; -.
DR SMR; G3MWR8; -.
DR STRING; 9913.ENSBTAP00000053971; -.
DR SwissPalm; G3MWR8; -.
DR PaxDb; G3MWR8; -.
DR PRIDE; G3MWR8; -.
DR eggNOG; KOG1700; Eukaryota.
DR HOGENOM; CLU_000329_1_1_1; -.
DR InParanoid; G3MWR8; -.
DR OrthoDB; 430978at2759; -.
DR TreeFam; TF333408; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
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: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; 1.
DR PANTHER; PTHR24206:SF66; PTHR24206:SF66; 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; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Exocytosis; FAD; Flavoprotein; LIM domain; Metal-binding; Monooxygenase;
KW NADP; Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..1960
FT /note="[F-actin]-monooxygenase MICAL3"
FT /id="PRO_0000416304"
FT DOMAIN 518..624
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 762..824
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 1799..1948
FT /note="bMERB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01195"
FT REGION 2..494
FT /note="Monooxygenase domain"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT REGION 658..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..1295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1316..1550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1564..1782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1779..1952
FT /evidence="ECO:0000255"
FT COMPBIAS 662..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..982
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1013
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1051
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1249
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1250..1284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1395..1424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1472..1487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1489..1504
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1631..1658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1746..1782
FT /note="Basic and acidic 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 298
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 398
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8VDP3"
FT BINDING 764
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 767
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 785
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 788
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 791
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 794
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 814
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 817
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CJ19"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CJ19"
FT MOD_RES 887
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 971
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CJ19"
FT MOD_RES 1129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 1139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 1156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 1188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CJ19"
FT MOD_RES 1250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 1252
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 1254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 1286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 1313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 1317
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 1404
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 1425
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 1660
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 1663
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7RTP6"
FT MOD_RES 1870
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CJ19"
SQ SEQUENCE 1960 AA; 217545 MW; 780A13287CAC8CE1 CRC64;
MEESKNEATN RAHVLFDRFV QATTCKGTLK AFQELCDHLE LKPKDHRSFY HKLKSKLNYW
KAKALWAKLD KRGSHKDYKK GKVCTNTKCL IIGAGPCGLR TAIDLSLLGA KVVVIEKRDA
FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC AGAIDHISIR QLQLILLKVA LILGIEIHVN
VEFRGLVEPP EDQENERIGW RALVHPKTHP VSEYEFEVII GGDGRRNTLE GFRRKEFRGK
LAIAITANFI NRNTTAEAKV EEISGVAFIF NQKFFQELRE ATGIDLENIV YYKDDTHYFV
MTAKKQSLLD KGVILHDYAD TELLLSRENV DQEALLSYAR EAADFSTQQQ LPSLDFAINH
YGQPDVAMFD FTCMYASENA ALVREHNGHQ LLVALVGDSL LEPFWPMGTG IARGFLAAMD
SAWMVRSWSL GTSPLEVLAE RESIYRLLPQ TTPENVSKNF SQYSIDPVTR YPNVNVNFLR
PSQVRHLYDT GDTKDVHLEM ENLVNSRTTP KLARNESVAR SSKLLGWCQR QTDGYAGVNV
TDLTMSWKSG LALCAIIHRY RPDLIDFDSL DEQNVEKNNQ LAFDIAEKEL GISPIMTGRE
MASVGEPDKL SMVMYLTQFY EMFKDSLPSR DASDLNAEER AVLIASTKSP ISFLSKLGQT
ISRKRSPKDK KEKDLDGAGK RRKTSQSEEE DTPRGHRGAR PTLVSTLTDR RMDVALGNQN
KVKYMATQLL AKFEENAPPQ SVGVRRQGSI KKEFPQNLGG SDTCYFCQKR VYVMERLSAE
GKFFHRSCFK CEHCATTLRL SAYAYALEDG KFYCKPHYCY RLSGPAQRKR PAGVPLSGKE
ARGPLQDSPA ADASGRPSTS ASPAERSPGP SVNGLEEPSV AKRLRGTPER IELENYRLSV
RQAEGLEEVP EETQAEHNLS SVLDTGTEED AASSSSESEM EEEEPPLPTS DLGGVPWKEA
VRIHALLRGK SEEELEASRS FGAGEEEEED EEDEEEEEEE EDEEDEEEDE DESSEVGSPR
RLQQLLNPAD PLEIQADVHW THIRESQEER AALAPKSPLP GVPFDEDDLE RDVDSEPAEI
KGEAAENGDA GDTGAELDDD QHWSDDVPSE ANTELHLPAV GAELELRVSD GEEEPPPASV
GHPERGPSRV SSPTRSPEEP TGLSSPARSP GAQSAHPPLA AVATGVRSPA ESPLPEPSTP
PAEPEAHPPI RSQPEARTPP SPASPQRPSP PTQLPICSQP QPSPEATVPS PTLSPIRSQP
VPARTSTPLA PLPVKNQGVT KDTLGSSLPG DEALKRSDLV AEFWMKSAEI RRSLGLTPVH
RSPGSELAFQ SPPLKACPAE KAPQSEGLRL LKPPPVPRKL GLPAAEGAQP CPPTPVSPPD
REPKGPREEH RDLSSSSGLG LQGSSSRTRT PGSQSFNTSD STMLTPPSSP PPPPPDEEPA
TLHRKPALAG QLVASAPPPP AVCVRPPREP TQPPQEEARK SFVESVDEIP FADDVEDTYD
DNTCDDRTED SSLQETFFTP PSHWPHPKQP LAPENGRGPE SAVPLQKRGL PLVSAEAKEL
AAERMRAREK SVRSQALRDA MARQLSRMKE MDIAAAAPRT PRTPAPRRAT AVPPKGPEEP
APRHEATSEE LLSPPSDSGG PDGSVTSSEG SSGKSKKRSS LFSPRRSKKE KKPKGEGRPL
ERPSPGTLEE AAAKPRSLWK SVFSGYRKDK KKSDGRSCPS TPSSGTTVDA GKPRASPVSR
AELRTRRQLS CSEDSDLSSD DVLERTSQKS RKEPRTYTEE ELNAKLTRRV QKAARRQAKQ
EELKRLHRAQ IIQRQLEQVE EKQRQLEERG VAVEKALRGE AGMGKKDDPK LMQEWFKLVQ
EKNAMVRYES ELMIFARELE LEDRQSRLQQ ELRERMAVED HLKTEEELAE EKRILNEMLE
VVEQRDALVA LLEEQRLREK EEDKDLEAAM LSKGFSLHWS
