ID I3JF91_ORENI Unreviewed; 888 AA.
AC I3JF91;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 69.
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:ENSONIP00000007532.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000007532.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000007532.2}
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 {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the Mical family.
CC {ECO:0000256|ARBA:ARBA00008223}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; I3JF91; -.
DR STRING; 8128.ENSONIP00000042020; -.
DR Ensembl; ENSONIT00000007537.2; ENSONIP00000007532.2; ENSONIG00000005981.2.
DR GeneTree; ENSGT00940000158780; -.
DR Proteomes; UP000005207; Linkage group LG1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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 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 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 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:UP000005207};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 512..618
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 693..755
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT REGION 758..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 888 AA; 100253 MW; 95F8262D9F44A3A8 CRC64;
MGETEEERDN VGKLFENFIQ ASTCKGALQA FNVLCRCHNL DPAEHSTFYN SLKAKVTSWK
AKALWSKLDK RMSHKEYRKG QACVGTKCLI IGGGPCGLRT AIELALLGAK VVVIEKRDSF
SRNNVLHLWP YTIHDLRGLG AKKFYGKFCA GAIDHISIQQ LQLILLKVAL IVAVEFHINV
EFVNLLEPQE NEGVGWRAAI QPADHPVANF EFDVVVGADG RRNTLEGFKR KEFRGKLAIA
ITANFINRNT TAEAKVEEIS GVAFIFNQKF FLDLKEETGI DLENIVYYKD NTHYFVMTAK
KQSLLDKGVV INDYSDTEML LSGENVNQEA LLCYAREAAD FGTNYQLPTL DFAMNHCGQP
DVAMFDFTNM YASENAALVR ERFGHQLLVA LVGDSLLEPF WPMGTGCARG FLAAFDTAWM
VKSWARGQPV LEVLAERESI YRLLPQTTPE NIAKNFEQYT LDPATRYPNL NSSCVRPHQV
RHLYISGQLN PCSLERAATI RRPVNLSRRD SEVRPARLLT WCQKQTEGYR NVIITDLTSS
WKNGIALCAL IHRFKPQLID FDSLNEEDHV ANLQLAFDIS EREFGIRPFT SAKELSEEEQ
LDKNKMINYL SKFYELFRGT PLPASGTLLY YSVLLATNLA SNGSTVRDRP DPKENKVRSM
ATQLLAKFEN KPNYTIRKTQ GGSVRRAFPP SGDKCHSCQK RVYMVERICT EGLYFHRECF
RCSTCSSVLR QGAHAFHSEE GKLYCKLHFD QRNNGTSIRR TFSLPSNRDS IQERRPADED
ITPSSSPADL QSEPAAGTFS SFMRKQLSWP LSVTRAVCNA PRYLSQRACH AARAFAGHLR
DNAQDYTLLY ELLSMSLPLL FVLQEVLLQM YTEMCGCAGC APAKEDTL
//
