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Database: UniProt
Entry: A0A2K6CGE1_MACNE
LinkDB: A0A2K6CGE1_MACNE
Original site: A0A2K6CGE1_MACNE 
ID   A0A2K6CGE1_MACNE        Unreviewed;       976 AA.
AC   A0A2K6CGE1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=F-actin monooxygenase {ECO:0000256|ARBA:ARBA00012709};
DE            EC=1.14.13.225 {ECO:0000256|ARBA:ARBA00012709};
GN   Name=MICAL2 {ECO:0000313|Ensembl:ENSMNEP00000022717.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000022717.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000022717.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001591};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the Mical family.
CC       {ECO:0000256|ARBA:ARBA00008223}.
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DR   AlphaFoldDB; A0A2K6CGE1; -.
DR   Ensembl; ENSMNET00000046973.1; ENSMNEP00000022717.1; ENSMNEG00000035003.1.
DR   GeneTree; ENSGT00940000158780; -.
DR   OMA; WAFLEVL; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000035003; Expressed in cerebellum and 11 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030042; P:actin filament depolymerization; IEA:UniProt.
DR   CDD; cd21250; CH_MICAL2; 1.
DR   CDD; cd09439; LIM_Mical; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR23167:SF39; [F-ACTIN]-MONOOXYGENASE MICAL2; 1.
DR   PANTHER; PTHR23167; CALPONIN HOMOLOGY DOMAIN-CONTAINING PROTEIN DDB_G0272472-RELATED; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   Pfam; PF00412; LIM; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00132; LIM; 1.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
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 {ECO:0000256|ARBA:ARBA00023203};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW   ProRule:PRU00125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00125}; Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          516..619
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          774..836
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   REGION          663..714
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          728..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        665..685
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..714
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   976 AA;  111751 MW;  DC804E7290084A16 CRC64;
     MGENEDEKQA QAGQVFENFV QASTCKGTLQ AFNILTRHLD LDPLDHRNFY SKLKSKVTTW
     KAKALWYKLD KRGSHKEYKR GKSCMNTKCL IVGGGPCGLR TAIELAYLGA KVVVVEKRDT
     FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC AGSIDHISIR QLQLILFKVA LMLGVEIHVN
     VEFVKVLEPP EDQENQKIGW RAEFLPADHS LSEFEFDVII GADGRRNTLE GFRRKEFRGK
     LAIAITANFI NRNSTAEAKV EEISGVAFIF NQKFFQDLKE ETGIDLENIV YYKDCTHYFV
     MTAKKQSLLD KGVIINDYID TEMLLCAENV NQDNLLSYAR EAADFATNYQ LPSLDFAMNH
     YGQPDVAMFD FTCMYASENA ALVRERQAHQ LLVALVGDSL LEPFWPMGTG CARGFLAAFD
     TAWMVKNWNQ GTPPLELLAE RESLYRLLPQ TTPENINKNF EQYTLDPGTR YPNLNSHCVR
     PHQVKHLYIT KELEHYPLER LGSVRRSVNL SRRESDIRPS KLLTWCQQQT EGYQHVNVTD
     LTTSWRSGLA LCAIIHRFRP ELINFDSLNE DDAVENNQLA FDVAEREFGI PPVTTGREMV
     SAQEPDELSM VMYLSKFYEL FRGTPLRPVD SWRKNYGENA DLSLAKSSIS NNYLNLTFPR
     KRTPRVDGQI GENDMNKRRR KGFNNLDEPS NFSSRSVGSN QECGSSKEGG NQNKVKSMAN
     QLLAKFEEST RNPSLMKQEK KSPSGFHFHP SHLRTVRPQE SMRKSFPLNL GGSDTCYFCK
     KRVYVMERLS AEGHFFHREC FRCSVCATTL RLAAYTFDCD EGKFYCKPHF IHCKTNSKQR
     KRRAELKQQR EEEATWQEQE APLRDTPTES SCAVAAIGTL EGSPPGISTS FFRKALGWPL
     RLPRDLCNWM QGLLQAVGLH IRDNAYNYCY MYELLSLGLP LLWAFSEVLA AMYRESEGSL
     ESICNWVLRC FPVKLR
//
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