ID A0A2K5VYK7_MACFA Unreviewed; 1101 AA.
AC A0A2K5VYK7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Molecule interacting with CasL protein 1 {ECO:0000256|ARBA:ARBA00044245};
DE EC=1.14.13.225 {ECO:0000256|ARBA:ARBA00012709};
DE EC=1.6.3.1 {ECO:0000256|ARBA:ARBA00012698};
GN Name=MICAL1 {ECO:0000313|Ensembl:ENSMFAP00000029887.2};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000029887.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000029887.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000029887.2}
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 -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 = H2O2 + NADP(+); Xref=Rhea:RHEA:11260,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000547};
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}. Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004608}. Midbody
CC {ECO:0000256|ARBA:ARBA00004214}.
CC -!- SIMILARITY: Belongs to the Mical family.
CC {ECO:0000256|ARBA:ARBA00008223}.
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DR AlphaFoldDB; A0A2K5VYK7; -.
DR Ensembl; ENSMFAT00000004090.2; ENSMFAP00000029887.2; ENSMFAG00000042065.2.
DR VEuPathDB; HostDB:ENSMFAG00000042065; -.
DR GeneTree; ENSGT00940000159117; -.
DR Proteomes; UP000233100; Chromosome 4.
DR Bgee; ENSMFAG00000042065; Expressed in bone marrow and 12 other cell types or tissues.
DR GO; GO:0005884; C:actin filament; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0010008; C:endosome membrane; IEA:Ensembl.
DR GO; GO:1990026; C:hippocampal mossy fiber expansion; IEA:Ensembl.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0030042; P:actin filament depolymerization; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:1903305; P:regulation of regulated secretory pathway; IEA:Ensembl.
DR GO; GO:0019417; P:sulfur oxidation; IEA:Ensembl.
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 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:UP000233100};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 543..647
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 730..792
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 952..1101
FT /note="BMERB"
FT /evidence="ECO:0000259|PROSITE:PS51848"
FT REGION 680..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 962..989
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 680..700
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..920
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1101 AA; 121157 MW; BD2285F218811BED CRC64;
MEGDGAGYVR RSWGPTCLCP AAALPGSPRE 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 EPVQRNDKTD AGMPTTGSAG
GSAGTQEELL RWCQEQTAGY PGVHVSDLSS SWTDGLALCA LVHRLQPGLL EPSELQGLGA
LEATAWALKV AEHELGITPV VSAQAVVAGS DPLGLIAYLS HFHSAFKSTA HSPGPVSQAS
PGTSSAVLFL GKLQRTLQRS RAKENAEDAG GKKLRLEMDA ETPSTEVPPD PEPGVPLTPP
SQHQEAGAGD LCALCGEHLY VLERLCVDGH FFHRSCFRCH TCEATLWPGG YEQHPGDGHF
YCLQHLPQPD HKEEGSDGGP ESPELPTPSE NSMPPGLSTP TASQEGVGPV PDPSQPTRRR
IHLSSLERQR LSSLNLTPDP EMEPPPKPPR SCSALARHAL ESSFVGWGLP VQSPQALAAM
EKEEEESSSS SEEEEDVPLD SDVEQALQTF AKTSGTMNDY PTWRRTLLRR AKEEEMKRFR
KAQTIQRRLN EIEGALRELE AEGVKLELAL RRQSSSPEQQ KKLWVGQLLQ LVDKKNSLVA
EEAELMITVQ ELNLEEKQWQ LDQELRGYMN REETLKTAAD RQAEDQVLRK LVDLVNQRDA
LIRLQEERRL SELALGIGAQ G
//
