ID A0A1S3KQ07_SALSA Unreviewed; 2406 AA.
AC A0A1S3KQ07;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=F-actin monooxygenase {ECO:0000256|ARBA:ARBA00012709};
DE EC=1.14.13.225 {ECO:0000256|ARBA:ARBA00012709};
GN Name=LOC106561386 {ECO:0000313|RefSeq:XP_013980773.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013980773.1};
RN [1] {ECO:0000313|RefSeq:XP_013980773.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013980773.1};
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_013980773.1; XM_014125298.1.
DR OrthoDB; 5399346at2759; -.
DR Proteomes; UP000087266; Chromosome ssa10.
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 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:UP000087266};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 526..632
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1013..1075
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 2206..2394
FT /note="BMERB"
FT /evidence="ECO:0000259|PROSITE:PS51848"
FT REGION 672..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1332..1434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1448..1505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1534..1613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1635..1827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1869..1898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1938..2009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2027..2147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2190..2243
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 675..725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1210
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1259..1278
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1534..1552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1561..1593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1657..1688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1702..1749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1750..1764
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1805..1827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1938..1952
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1979..2000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2027..2048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2059..2083
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2091..2107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2108..2125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2126..2147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2406 AA; 268253 MW; 4C87218A3A946CB4 CRC64;
MGTMGDPGGF TTTGERVNPA HVMFDRFTQA STCKGTLKAF QELCDHLDLK PCEYRIFYHK
LKSRLNYWKA KALWVKLDKR AGQKEYKKGR ACANSKCLII GAGPCGLRTA IELGFLGAKV
VLLEKRDAFS RNNVLHLWPF SIQDLRGLGA KKFHGKFCAG AIDHISIRQL QLMLLKVALL
LGIEIHVNVE FKGLIEPPED QENERIGWRA EVHPRTHPVN ELEFDVIIGA DGRRNTLAGF
RRKEFRGKLA IAITANFINR NTTAEAKVEE ISGVAFIFNQ KFFQDLREAT GIDLENIVYY
KDDTHYFVMT AKKQSLLEKG VILHDYADTE MLLSRANVDQ EALLSYAREA ADFSTNHQLP
TLDFAINHYG QPDVAMFDFT CMYASENAAL VRQRNGRQLL VSLVGDSLLE PFWPMGTGIA
RGFLAAMDSG WMVKSWAQGN TPLDVLAERE SIYRLLPQTT PENISKNFSH YSVDPTTRYP
NISLHFLRPN QVQHLIDTGD SNSEMRIEME NVVTSSTPKL TRNESIARSS KLLNWCQRQT
EGYRKVSVTD LTMSWKSGMA LCSLIHRYRP DLIDFDSLDE RDQQKNNQLG FDVAEREFGI
SPCMTGKEMS QVSEPDKLSM VMYLSQFYEM FKDTVPPGAG DNQNMSPEEK VALINSTKSP
ISFLSKLGQS IAISRKRNPK DKKEKDVDGL GKRRKTSQAG HSEEEEVLRG NHDDRPSNST
ALTERKMKEE TAAVGNHNKV KSMATQLLAK FEENAPAESK GLKRQGDSLP NLDLLVAQPP
PPPPAPLDPP RESVRLALVP AWRQKQTQQQ EQLSFGYKEK FKCQTLPNRG EQPRSSTESI
CGSRSCPKKT ILLSSSSTTS SLSLHSQHCD GGVMEEEDTT QDQTLLTYRK WKPVQLDEPE
PIHIPSIQER SARLVAKFKG KPEKPKPKKK PSRFFIEQWH RSGSHSPESP LSSPETLRQR
YLKIYTGGVS LLADQIANQL QPQEEPKPLL DQRELVELGS LRKEFPQNIG GSDVCFFCQK
RVYVMERLSA EGKFFHRSCF KCDYCGTTLR LSSYAFDVED GKFYCKPHYC YRLSGQAQRK
RPAPTPALLN AKDNQASLPA VVTVDSPGRG EMASLSPTEC QTSVPEVNGL QEPSLPKRLR
GTPERIELEN YRLSLQREED LEEVPEETLA EHNLSSVLDK DKHAELGSSS SESDMEEEDQ
EDEDHEEEQQ EPPSPSDLGG VPWKEAVELH AKLKTDSDPG AEGEDGAQAQ IVRDLKVEEK
EEDDEEEDDE EESSDEGEYC PWERELQSGV WLENLKDEED TGTFKARYLQ IQQVLQPVDP
SIIKNIRGVS VLSEGPPASA SQPSSTAPAN TSARHEAVRV WLESVSGETC EDDDPEAEVG
SHDFEPGTEM DQEDIPSDAE AEARLHQSEI NEAFPEEAKK SESQGLASSI EQSSVSPVKL
VGEVVLLPVK PPTPQPDSQM SHPSPCLVKS PGMHFFPEPF PLEDITTPQR TAQTPNAKIP
PYPAPTMSPI PSPVCSPVHS PICSQPVPLL ETVTTKSPVN SPSCSCPPTG NPLSPICAQP
LPCQEPSSSL TSDSPVRTQP VPAVTSTSLV KPASPDRATP EPQKSLDLSD LETPVKKTDI
IEEFWLKSAE IRKSLGLTPM ERSSSKSPEK SHVTVGRVPT PDSSSPKSYT PEDLSEELSP
SPFTGRSVIR RLNITVEGQV ISPVEPKSNG TDQRDLSSSS GLGLNGSTTT SQTSQAASDS
YNTSDSTMLT PPSSPPPPPP NEEPATLRQQ QKHHVSWNNG IDGPTTPEPA KAAPTKIKSP
VPAPRTQLSP VSMPVSVPKS APRTTLVTSP VTAPVVIMRR EKSSKPRQEE VRKSFVECVA
EIPFADDVED MYDERTPDTT MDRFFTPPTS RPNGEREKPP LHLALAMVNG TANFPGNQRA
SKHHKAQHIS PEAKEIAEER MRAREKSIKS QALKDAMAKQ LSKMKETDMA KGSAASAKVV
WNVASSETSG KSTKKSPGSP KTSAVKALES KKAETLPELF FSSQVNKSLD GSTVSSDGSA
SGGKSKKRSS LFSPRKNKKE KKAKNESQLF DKHGADETPS PPKHKSLWKA VFSGYKKDKK
KNKDDKSCPS TPSSSTTNDS GKKRSSPLGR SSDLKSRRNR SFSEDSDLSC DDVLERSSLK
SKADSVYVPH ALAFKRAYAT KKTYTEEELN AKLTRRVQKA ARRQAKQEEL KRLHRAQIIQ
RQLEQVEEKQ RQLEERGVAV EKALRGEADY WGESNYTEIM DLHLGVEPFV GTPRRRPISF
CPCCSSEGMG KKDDPKLMQE WFKLVQEKNA LVRYESELMI FARELELEDR QSRLQQDLRE
RMAIEDHLKT EVELAQEKHI LNEMLEVVEQ RDSLVALLEE QRLSEKEEDK DLESVMLSKG
FNLNWA
//
