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Database: UniProt
Entry: A0A2I3FSS0_NOMLE
LinkDB: A0A2I3FSS0_NOMLE
Original site: A0A2I3FSS0_NOMLE 
ID   A0A2I3FSS0_NOMLE        Unreviewed;      1073 AA.
AC   A0A2I3FSS0;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=F-actin monooxygenase {ECO:0000256|ARBA:ARBA00012709};
DE            EC=1.14.13.225 {ECO:0000256|ARBA:ARBA00012709};
GN   Name=MICAL3 {ECO:0000313|Ensembl:ENSNLEP00000024847.1};
OS   Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC   Nomascus.
OX   NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000024847.1, ECO:0000313|Proteomes:UP000001073};
RN   [1] {ECO:0000313|Ensembl:ENSNLEP00000024847.1, ECO:0000313|Proteomes:UP000001073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Gibbon Genome Sequencing Consortium;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNLEP00000024847.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- SIMILARITY: Belongs to the Mical family.
CC       {ECO:0000256|ARBA:ARBA00008223}.
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DR   EMBL; ADFV01106341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01106342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01106343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01106344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01106345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01106346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01106347; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01106348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01106349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01106350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSNLET00000059959.1; ENSNLEP00000024847.1; ENSNLEG00000007851.3.
DR   GeneTree; ENSGT00940000155580; -.
DR   Proteomes; UP000001073; Chromosome 7b.
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; cd21251; CH_MICAL3; 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:SF51; [F-ACTIN]-MONOOXYGENASE MICAL3; 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); 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 {ECO:0000256|ARBA:ARBA00023203};
KW   Exocytosis {ECO:0000256|ARBA:ARBA00022483};
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023033};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          518..624
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          886..948
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   REGION          658..709
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          757..807
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          960..989
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..706
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        781..807
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        975..989
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1073 AA;  121281 MW;  2DDBA62F31B9B517 CRC64;
     MEERKHETMN PAHVLFDRFV QATTCKGTLK AFQELCDHLE LKPKDYRSFY HKLKSKLNYW
     KAKALWAKLD KRGSHKDYKK GKACTNTKCL IIGAGPCGLR TAIDLSLLGA KVVVIEKRDA
     FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC AGAIDHISIR QLQLILLKVA LILGIEIHVN
     VEFQGLIQPP EDQENERIGW RALVHPKTHP VSEYEFEVII GGDGRRNTLE GFRRKEFRGK
     LAIAITANFI NRNTTAEAKV EEISGVAFIF NQKFFQELRE ATGIDLENIV YYKDDTHYFV
     MTAKKQSLLD KGVILHDYAD TELLLSRENV DQEALLNYAR EAADFSTQQQ LPSLDFAINH
     YGQPDVAMFD FTCMYASENA ALVREQNGHQ LLVALVGDSL LEPFWPMGTG IARGFLAAMD
     SAWMVRSWSL GTSPLEVLAE RESIYRLLPQ TTPENVSKNF SQYSIDPVTR YPNINVNFLR
     PSQVRHLYDT GETKDIHLEM ESLVNSRTTP KLTRNESVAR SSKLLGWCQR QTDGYAGVNV
     TDLTMSWKSG LALCAIIHRY RPDLIDFDSL DEQNVEKNNQ LAFDIAEKEL GISPIMTGKE
     MASVGEPDKL SMVMYLTQFY EMFKDSLPSS DTLDLNAEEK AVLIASTRSP ISFLSKLGQT
     ISRKRSPKDK KEKDLDGAGK RRKTSQSEEE EAPRGHRGER PTLVSTLTDR RMDVAVGNQN
     KVKYMATQLL AKFEENAPAQ SIGIRRQQRE KECSRTCPKK VITLSPPPTP PPCRARGSQQ
     TYRDLDADNR GKQSPHHERP EPEPPRRFFV DQWELSLSLR SSARPASPXX XXXXXKYIKM
     YTGGVSSLAE QIANQLQRKE PPKALLDKKE LGSMKKEFPQ NLGGSDTCYF CQKRVYVMER
     LSAEGKFFHR SCFKCEYCAT TLRLSAYAYD IEDGKFYCKP HYCYRLSGYA QRKRPAVAPL
     SGKEAKGPLQ DGASTDANGR ANTMASSTER TPGSLTSLFG WVARHSLGLC DKAKGMSQHL
     QSNISSFGHQ VAQNPLDSFF MCQLLAFGVP FLYGLSEVLV QIRGEFHWQA VAQ
//
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