ID A0A2K5LZH0_CERAT Unreviewed; 1055 AA.
AC A0A2K5LZH0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
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:ENSCATP00000018339.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000018339.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000018339.1}
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 -!- 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; A0A2K5LZH0; -.
DR Ensembl; ENSCATT00000042514.1; ENSCATP00000018339.1; ENSCATG00000032923.1.
DR GeneTree; ENSGT00940000159117; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000032923; Expressed in lung 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; 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:UP000233060};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 511..615
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 684..746
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 906..1055
FT /note="BMERB"
FT /evidence="ECO:0000259|PROSITE:PS51848"
FT REGION 648..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 916..943
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 765..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..874
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1055 AA; 116388 MW; BB6F9B6E355E940F CRC64;
MASPTSTNPA HAHFESFLQA QLCQDVLSSF QELCGALGLE PGGGLPQYHK IKDQLNYWSA
KSLWTKLDKR AGQPVYQQGR ACTSTKCLVV GAGPCGLRVA VELALLGARV VLVEKRTKFS
RHNVLHLWPF TIHDLRALGA KKFYGRFCTG TLDHISIRQL QLLLLKVVLL LGVEIHWGVT
FTGLQPPPRK GSGWRAQLQP NPLAQLANYE FDVLISAAGG KFVPEGFKVR EMRGKLAIGI
TANFVNGRTV EETQVPEISG VARIYNQSFF QSLLKATGID LENIVYYKDD THYFVMTAKK
QCLLRLGVLR QDWPDTDRLL GSANVVPEAL QRFARAAADF ATHGKLGKLE FAQDAHRQPD
VSAFDFTSMM RAESSARVQE KHGARLLLGL VGDCLVEPFW PLGTGVARGF LAAFDAAWMV
KRWAEGAEPL EVLAERESLY QLLSQTSPEN MHRNVAQYGL DPATRYPNLN LRAVTPNQVR
DLYDVLTKEP VQRNDKTDAG MPTTGSAGGS AGTQEELLRW CQEQTAGYPG VHVSDLSSSW
TDGLALCALV HRLQPGLLEP SELQGLGALE ATAWALKVAE HELGITPVVS AQAVVAGSDP
LGLIAYLSHF HSAFKSTAHS PGPVSQASPG TSSAVLFLGK LQRTLQRSRA KMDAETPSTE
VPPDPEPGVP LTPPSQHQEA GAGDLCALCG EHLYVLERLC VDGHFFHRSC FRCHTCEATL
WPGGYEQHPG DGHFYCLQHL PQPDHKEEGS DGGPESPELP TPSENSMPPG LSTPTASQEG
VGPVPDPSQP TRRRIHLSSL ERQRLSSLNL TPDPEMEPPP KPPRSCSALA RHALESSFVG
WGLPAQSPQA LAAMEKEEEE SSSSSEEEED VPLDSDVEQA LQTFAKTSGT MNDYPTWRRT
LLRRAKEEEM KRFRKAQTIQ RRLNEIEGAL RELEAEGVKL ELALRRQSSS PEQQKKLWVG
QLLQLVDKKN SLVAEEAELM ITVQELNLEE KQWQLDQELR GYMNREETLK TAADRQAEDQ
VLRKLVDLVN QRDALIRLQE ERRLSELALG IGAQG
//
