ID A0A2K6LU39_RHIBE Unreviewed; 1043 AA.
AC A0A2K6LU39;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=F-actin monooxygenase {ECO:0000256|ARBA:ARBA00012709};
DE EC=1.14.13.225 {ECO:0000256|ARBA:ARBA00012709};
GN Name=MICAL1 {ECO:0000313|Ensembl:ENSRBIP00000027024.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000027024.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000027024.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000027024.1}
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the Mical family.
CC {ECO:0000256|ARBA:ARBA00008223}.
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DR AlphaFoldDB; A0A2K6LU39; -.
DR Ensembl; ENSRBIT00000050950.1; ENSRBIP00000027024.1; ENSRBIG00000037357.1.
DR GeneTree; ENSGT00940000159117; -.
DR Proteomes; UP000233180; Unplaced.
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; cd21196; CH_MICAL1; 1.
DR CDD; cd09358; LIM_Mical_like; 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; IPR022735; bMERB_dom.
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:SF35; [F-ACTIN]-MONOOXYGENASE MICAL1; 1.
DR PANTHER; PTHR23167; CALPONIN HOMOLOGY DOMAIN-CONTAINING PROTEIN DDB_G0272472-RELATED; 1.
DR Pfam; PF12130; bMERB_dom; 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; SM01203; DUF3585; 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; 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 {ECO:0000256|ARBA:ARBA00023203};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000233180};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 521..625
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 672..734
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 894..1043
FT /note="BMERB"
FT /evidence="ECO:0000259|PROSITE:PS51848"
FT REGION 724..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 904..931
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 753..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..862
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1043 AA; 115359 MW; C52E3CF3FF472A13 CRC64;
FHLSSHLPLE ASMASPTSTN PAHAHFESFL QAQLCQDVLS SFQELCGALG LEPGGGLPQY
HKIKDQLNYW SAKSLWTKLD KRAGQPVYQQ GRACTSTKCL VVGAGPCGLR VAVELALLGA
RVVLVEKRTK FSRHNVLHLW PFTIHDLRAL GAKKFYGRFC TGTLDHISIR QLQLLLLKVV
LLLGVEIHWG VTFTGLQPPP RKGSGWRAQL QPNPPAQLAN YEFDVLISAA GGKFVPEGFK
VREMRGKLAI GITANFVNGR TVEETQVPEI SGVARIYNQS FFQSLLKATG IDLENIVYYK
DDTHYFVMTA KKQCLLRLGV LRQDWPDTDR LLGSANVVPE ALQRFARAAA DFATHGKLGK
LEFAQDAHRQ PDVSAFDFTS MMRAESSARV QEKHGARLLL GLVGDCLVEP FWPLGTGVAR
GFLAAFDAAW MVKRWAEGAE PLEVLAERES LYQLLSQTSP ENMHRNVAQY GLDPATRYPN
LNLRAVTPNQ VRDLYDVLTK EPVQRNNDKR DAGMLTTGGS AGTQEELLRW CQEQTAGYPG
VHVSDLSSSW TDGLALCALV HRLQPGVLEP SELQGLGALE ATAWALKVAE HELGITPVVS
AQAVVAGSDP LGLIAYLSHF HSAFKSTAHS PGPVSQASPG TSSAVLFLGK LQRTLQRSRA
KVKSLGRAGA GDLCALCGEH LYVLERLCVD GHFFHRSCFR CHTCEATLWP GGYEQHPGDG
HFYCLQHLPQ PDHQEEGSDG GPESPELPTP SENSMPPGLS TPTASQEGAG PVPDPSQPTR
RRIHLSSLER QRLSSLNLTP DPEMEPPPKP PRSCSALARH ALESSFVGWG LPVQSPQALV
AMEKEEEESS SSSEEEEDVP LDSDVEQALQ TFAKTSGTMK DYPTWRQTLL RRAKEEEMKR
FRKAQTIQRR LNEIEGALRE LEAEGVKLEL ALRRQSSSPE QQKKLWVGQL LQLVDKKNSL
VAEEAELMIT VQELNLEEKQ WQLDQELRGY MNREETLKTA ADRQAEDQVL RKLVDLVNQR
DALIRFQEER RLSELALGTG AQG
//