ID A0A2Y9ND48_DELLE Unreviewed; 2012 AA.
AC A0A2Y9ND48;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 2.
DT 27-MAR-2024, entry version 25.
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|RefSeq:XP_022432839.2};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022432839.2};
RN [1] {ECO:0000313|RefSeq:XP_022432839.2}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022432839.2};
RG RefSeq;
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 RefSeq; XP_022432839.2; XM_022577131.2.
DR Proteomes; UP000248483; 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; 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; 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:SF51; [F-ACTIN]-MONOOXYGENASE MICAL3; 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 PRINTS; PR00420; RNGMNOXGNASE.
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); 1.
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:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Exocytosis {ECO:0000256|ARBA:ARBA00022483};
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
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 762..824
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 1790..2000
FT /note="BMERB"
FT /evidence="ECO:0000259|PROSITE:PS51848"
FT REGION 658..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1312..1772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1800..1827
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1940..2001
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 662..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..986
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1007
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1079
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1224
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1350..1375
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1390..1419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1435
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1549..1566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1629..1648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1693..1708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1737..1772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2012 AA; 223125 MW; 135184135831043D CRC64;
MEERKNEATN RAHILFDRFV QATTCKGTLK AFQELCDHLE LKPKDHRSFY HKLKSKLNYW
RAKALWAKLD KRGSHKDYKK GKACTNTKCL IIGAGPCGLR TAIDLSLLGA KVVVIEKRDA
FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC AGAIDHISIR QLQLILLKVA LILGIEIHVN
VEFQGLVEPP EDQENERIGW RALVHPKTHP VSEYEFEVII GGDGRRNTLE GFRRKEFRGK
LAIAITANFI NRNTTAEAKV EEISGVAFIF NQKFFQELRE ATGIDLENIV YYKDDTHYFV
MTAKKQSLLD KGVILHDYAD TELLLSRENV DQEALLSYAR EAADFSTQQQ LPSLDFAINH
YGQPDVAMFD FTCMYASENA ALVREHGGHQ LLVALVGDSL LEPFWPMGTG IARGFLAAMD
SAWMVRSWSL GRSPLEVLAE RESIYRLLPQ TTPENVSKNF SQYSIDPVTR YPNMNVNFLR
PSQVRHLYDT GETKDIHLEM ENLVNSRTTP KLARNESVAR SSKLLGWCQR QTDGYAGVNV
TDLTMSWKSG LALCAIIHRY RPDLIDFDSL DEQNVEKNNQ LAFDIAEKEL GISPIMTGRE
MASVGEPDKL SMVMYLTQFY EMFRDSLPSR DALDLNAEER AVLVASTKSP ISFLSKLGQT
ISRKRSPKDK KEKDLDGAGK RRKTSQSEEE DAPRGYRGGR PTLVSTLSDR RVDVALGNQN
KVKYMATQLL AKFEENAPAQ STGMRRQGSM KKEFPQNLGG SDTCYFCRKR VYVMERLSAE
GKFFHRSCFK CEYCATTLRL SAYAYALEDG KFYCKPHYCY RLSGPVQRKR PAVAPLSGKE
ARGPLQDSPA ADTNGQPSTS ASPAERTPGP SMNGLEEPSI AKRLRGTPER IELENYRLSV
RQAEGLEEVP EETQAEHNLS SVLDTGTEED AASSSSESEM EEEEPPLPPS DLGGVPWKEA
VRIHALLKGR SEEELEASRS FVAGEEDAED AGDEEDEEDE EDEEDASSEA GSPRLQQLVN
PADPLEIQAD VHWTHIRESQ EEQVSPASES PPSRVPFDED DLEEDVDSEP AEIEGEAAEN
GDTGDTGAEL GDGQHWSDDV PSETNTELQQ VAAGVGLELR VSEGEEEPPA ALARRPERGR
SQVSSPSRSP EEHSVLSSPA HSPRAQGTRA PRASAAAMRG LPAESPVPEP EPELAHGEPT
AGTPVQSQPE ARTPPSPASP QRRSPLAPLP ICSQPQPSAE ATVPSPTVSP IRFQPVPART
STPLAPLPVK SQGVTKDTLG SPLPGDEALR RSDLVAEFWM KSAEIRRSLG LMPVRRGPGP
EPAFQPAPLQ ACRAEKLPQG EGPWLLKPTP VPGRLGPPAA RGTQPSPPTP GSPPGREPKG
ARAEHRDLSS SSGLGLQGSS SRTRTPGSQS FSTSDSTMLT PPSSPPPPPP DEEPATLHGK
PALAGQLTAS ESRAPAACVR TPREPTRPPP EEAPKPFVES VDEIPFADDV EDTYDDRTED
SSLQEPFFTP PSRWPCPEQP LAQERGQGPE SGLPPQKRGL PLVSAEAKEL AAERMRAREK
SVRSPALRDA MARQLSRMKE MDTVATAPRA PRTPAPRRAT AVPPKGPEEP TPTYKAMSEE
VPSPPSDSGG LDGSVTSSEG SSGKSKKRSS LFSPRRNKKE KKPKGDGRPP ERPSPSALEE
AAAKPRSLWK SVFSGYRKDK KKKGDGRSRP STPSSGTTVD AGKPGASPVT RAELRPRRQL
SCSEDSDISS DDVLERTSQK SRREPRTYTE EELNTKLTRR VQKAARRQAK QEELKRLHRA
QIIQRQLEQV EEKQRQLEER GVAVEKALRG EADYWGESYY TDLIDLRLGG PIKGQRQRPP
CPAISLAALD QVEPSGGTPR RRPLSFCPCC VQEGMGKKDD PKLMQEWFKL VQEKNAVVRY
ESELMIFARE LELEDRQSRL QQELRERMAM EDHLKTEEEL SEEKRILNEM LEVVEQRDAL
VALLEEQRLR EKEEDKDLEA AMLSKGFSLN WS
//
