MICA2_BOVIN
ID MICA2_BOVIN Reviewed; 1865 AA.
AC F1MF74; A0A3Q1LSU4;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 74.
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 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: Methionine monooxygenase that promotes depolymerization of F-
CC actin by mediating oxidation of residues 'Met-44' and 'Met-47' on actin
CC to form methionine-sulfoxide, resulting in actin filament disassembly
CC and preventing repolymerization (By similarity). Regulates the
CC disassembly of branched actin networks also by oxidizing ARP3B-
CC containing ARP2/3 complexes leading to ARP3B dissociation from the
CC network. Acts as a key regulator of the SRF signaling pathway elicited
CC by nerve growth factor and serum: mediates oxidation and subsequent
CC depolymerization of nuclear actin, leading to increase MKL1/MRTF-A
CC presence in the nucleus and promote SRF:MKL1/MRTF-A-dependent gene
CC transcription. Does not activate SRF:MKL1/MRTF-A through RhoA (By
CC similarity). {ECO:0000250|UniProtKB:O94851,
CC ECO:0000250|UniProtKB:Q8TDZ2}.
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 -!- SUBUNIT: Interacts with PLXNA4 (By similarity). Interacts with RAB1B
CC (By similarity). Interacts with MAPK1/ERK2 (By similarity). Interacts
CC with RAB35, RAB8A, RAB10, RAB13 and RAB15 (in their GTP-bound forms);
CC binding to RAB35 is of low affinity compared to other Rab proteins; at
CC least in case of RAB8A may bind 2 molecules of RAB8A simultaneously
CC through a high and a low affinity binding site, respectively (By
CC similarity). May interact with MAPK1/ERK2 (By similarity).
CC {ECO:0000250|UniProtKB:O94851, ECO:0000250|UniProtKB:Q8BML1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O94851}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8BML1}.
CC -!- DOMAIN: The C-terminal RAB-binding domain (RBD) (1796-1945), also
CC described as bivalent Mical/EHBP Rab binding (bMERB) domain, mediates
CC binding to predominantly RAB8A, RAB10, RAB13 and RAB15 (in their GTP-
CC bound forms). {ECO:0000250|UniProtKB:O94851}.
CC -!- SIMILARITY: Belongs to the Mical family. {ECO:0000305}.
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DR EMBL; DAAA02040675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02040676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02040677; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02040678; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02040679; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005216149.1; XM_005216092.3.
DR RefSeq; XP_015321996.1; XM_015466510.1.
DR AlphaFoldDB; F1MF74; -.
DR STRING; 9913.ENSBTAP00000043575; -.
DR PaxDb; F1MF74; -.
DR PRIDE; F1MF74; -.
DR Ensembl; ENSBTAT00000074119; ENSBTAP00000058159; ENSBTAG00000014855.
DR GeneID; 534041; -.
DR KEGG; bta:534041; -.
DR CTD; 9645; -.
DR VEuPathDB; HostDB:ENSBTAG00000014855; -.
DR VGNC; VGNC:31458; MICAL2.
DR eggNOG; KOG1700; Eukaryota.
DR GeneTree; ENSGT00940000158780; -.
DR HOGENOM; CLU_000329_0_1_1; -.
DR InParanoid; F1MF74; -.
DR OMA; RRIVPKS; -.
DR OrthoDB; 430978at2759; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000014855; Expressed in occipital lobe and 105 other tissues.
DR ExpressionAtlas; F1MF74; baseline and differential.
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; 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; IPR029939; MICAL2.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR23167:SF39; PTHR23167:SF39; 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; Cytoplasm; FAD; Flavoprotein; LIM domain; Metal-binding;
KW Monooxygenase; NADP; Nucleus; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Zinc.
FT CHAIN 1..1865
FT /note="[F-actin]-monooxygenase MICAL2"
FT /id="PRO_0000416301"
FT DOMAIN 516..619
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 977..1039
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 1788..1865
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 660..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1144..1298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1299..1338
FT /note="Interaction with MAPK1"
FT /evidence="ECO:0000250|UniProtKB:Q8BML1"
FT REGION 1334..1409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1478..1612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1669..1782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 660..681
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 662..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..775
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1068
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1263
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1364..1384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1547..1566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1677..1691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1702..1719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1736..1760
FT /note="Polar 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 979
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 982
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1000
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
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="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1009
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1029
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT BINDING 1032
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8TDZ2"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94851"
SQ SEQUENCE 1865 AA; 207144 MW; 7C196B9DA6F62D4D CRC64;
MGENEDEKQT QAGQLFENFV QASTCKGTLQ AFNILTRQLD LDPLDHRNFY SKLKSKVTTW
KAKALWYKLD KRGSHKEYKR GRSCMNTKCL IIGGGPCGLR TAIELAYLGA KVVVVEKRDT
FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC AGSIDHISIR QLQLILFKVA LILGVEIHVN
VEFVKVLEPP EDQENQKIGW RAEFLPVDHS LSEFEFDVII GADGRRNTLE GFRRKEFRGK
LAIAITANFI NRNSTAEAKV EEISGVAFIF NQKFFQDLKK ETGIDLENIV YYKDCTHYFV
MTAKRQSLLD KGVIINDYTD TETLLRAENV NQDNLLSYAR EAADFATNYQ LPSLDFAMNH
YGQPDVAMFD FTSMYASENA ALVRERQSHL LLVALVGDSL LEPFWPMGTG CARGFLAAFD
TAWMVKSWDQ GTSPLELLAE RESLYRLLPQ TTPENINKNF EQYTLDPATR YPNLNSNNIK
PNQVKHLYIT KELHQYPLER LGSVRRSVGL SRRESDVRPS KLLTWCQQQT EGYQHVNVTD
LTTSWRSGLA LCAIIHRFRP DLINFDSLNE DHAVENNQLA FDVAEREFGI APVITGKEMA
SAQEPDKLSM VMYLSKFYEL FRGTPLRPVD SWRKNYEENA DLGLAKSSIP HHYLNLTFPR
KRTPRVDSRT EENDMNKRRR KGFNNLHEPS AFSSQSLGSN QEGIKEGGNQ NKVKSMASQL
LAKFEESSRN PSILRQEHRV SGIGKPILRS SSDPPVNSRC PKPEEPTPSP SPPLKRQFPS
VVVTGHVLRE LKQVSAGGEC PARPWRARAK SDLQLGGPEN LASLPPTCPG ALALSGVLRR
LQQVEEKVLQ KRAQNLANRE FHKKNIKEKA AHLASMFGHG DFPQNKLLSK SLSHTHPPSS
PSCLPSPDSA ATSSPSTVDS VSPARKLTVG KVSSGIGAAA EVLVNLYLND HRPKTQATSP
DLESVRKTFP LNVGGSDTCY FCKKRVYVME RLSAEGRFFH RECFRCSVCA TTLHLATYAF
DVDEGKFFCK PHFIHCKTNS QQRKRRAELK QQKEEEGMWK EQEAARRDPP SESSCAAAAI
ATPEGSPPDE PTSPKKPKSI PEPEPGDVAG GAASPLPSEW TAVRISPGED VVGQDVLAVR
VLVTSDDSSS DAELDRGDSE ASSVEPFDER PQQPELQLPP LLKPFTRHSS LREALPRAVS
PHDLGEPEAE PALQRANSFQ CPTPSEYQSG RRFQSNFMPV NSKMTVSPPK QACPPPPSPS
PPSSSSIGDL NALDSPSLPQ VTVSNTASQI SRGHCSPSTP IFLRRAKAHG PPKDLPLRLP
RGQVLERTEY CLVRPGGNGL QSSRPPSPTE MASDGCQEAV APPRDIRSIH RGPHPVEGKD
RCLPDHPLSP WAGEEPGEGS TRPRRVEDGG LELAEEKSGL KKLVLTPEQK TWLLDWNDSN
LENLYLETGA RLSQKSTRNG SGGHVLKPVH PLLLPLAEKE TLPAQRQSQE KMGAPAERAP
GERSMAPPKS PLRLIANAIR RSLEPLLPNS DSGRKAWAKP ESKTLPTSPP HAYTCSFSFR
KSSSSKDSDQ PSPKRDVASK ASAFFSLGSP TARTAQPSAP SPPAPALCTH SLPSRSSKVF
PALVPPPCGK MEDVPTLLEK VSLQETVPDA SRVPKKRTSL FSSFRLKDKS FESSLQESGP
RKDSQDLFSS PKGKVQPMGN AQPPEKQGQP ISSTCLGQRV HPVSPEKDAS PTHVPIRAQG
TGTVSSTSSS TTSSADEEFH PQPSSRSKER KALRRRRKLE KATKQLVKQE ELKRLHKAQA
IQRQLEEVEE QQRAFEIQGV RLEKALRGEA ADSGTQDEAQ LLQEWLKLVL EKNKLMRYES
ELLIM
