ID A0A1S3KR33_SALSA Unreviewed; 2279 AA.
AC A0A1S3KR33;
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_013980779.1};
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_013980779.1};
RN [1] {ECO:0000313|RefSeq:XP_013980779.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013980779.1};
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_013980779.1; XM_014125304.1.
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 886..948
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 2079..2267
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 978..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1407..1486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1508..1700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1742..1771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1811..1882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1900..2020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2063..2116
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 988..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1063
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1083
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1151
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1434..1466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1530..1561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1575..1622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1623..1637
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1678..1700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1811..1825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1852..1873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1900..1921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1932..1956
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1964..1980
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1981..1998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1999..2020
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2279 AA; 253961 MW; DB5AF488F7857CB2 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 EQRYLKIYTG
GVSLLADQIA NQLQPQEEPK PLLDQRELVE LGSLRKEFPQ NIGGSDVCFF CQKRVYVMER
LSAEGKFFHR SCFKCDYCGT TLRLSSYAFD VEDGKFYCKP HYCYRLSGQA QRKRPAPTPA
LLNAKDNQAS LPAVVTVDSP GRGEMASLSP TECQTSVPEV NGLQEPSLPK RLRGTPERIE
LENYRLSLQR EEDLEEVPEE TLAEHNLSSV LDKDKHAELG SSSSESDMEE EDQEDEDHEE
EQQEPPSPSD LGGVPWKEAV ELHAKLKTDS DPGAEGEDGA QAQIVRDLKV EEKEEDDEEE
DDEEESSDEG EYCPWERELQ SGVWLENLKD EEDTGTFKAR YLQIQQVLQP VDPSIIKNIR
GVSVLSEGPP ASASQPSSTA PANTSARHEA VRVWLESVSG ETCEDDDPEA EVGSHDFEPG
TEMDQEDIPS DAEAEARLHQ SEINEAFPEE AKKSESQGLA SSIEQSSVSP VKLVGEVVLL
PVKPPTPQPD SQMSHPSPCL VKSPGMHFFP EPFPLEDITT PQRTAQTPNA KIPPYPAPTM
SPIPSPVCSP VHSPICSQPV PLLETVTTKS PVNSPSCSCP PTGNPLSPIC AQPLPCQEPS
SSLTSDSPVR TQPVPAVTST SLVKPASPDR ATPEPQKSLD LSDLETPVKK TDIIEEFWLK
SAEIRKSLGL TPMERSSSKS PEKSHVTVGR VPTPDSSSPK SYTPEDLSEE LSPSPFTGRS
VIRRLNITVE GQVISPVEPK SNGTDQRDLS SSSGLGLNGS TTTSQTSQAA SDSYNTSDST
MLTPPSSPPP PPPNEEPATL RQQQKHHVSW NNGIDGPTTP EPAKAAPTKI KSPVPAPRTQ
LSPVSMPVSV PKSAPRTTLV TSPVTAPVVI MRREKSSKPR QEEVRKSFVE CVAEIPFADD
VEDMYDERTP DTTMDRFFTP PTSRPNGERE KPPLHLALAM VNGTANFPGN QRASKHHKAQ
HISPEAKEIA EERMRAREKS IKSQALKDAM AKQLSKMKET DMAKGSAASA KVVWNVASSE
TSGKSTKKSP GSPKTSAVKA LESKKAETLP ELFFSSQVNK SLDGSTVSSD GSASGGKSKK
RSSLFSPRKN KKEKKAKNES QLFDKHGADE TPSPPKHKSL WKAVFSGYKK DKKKNKDDKS
CPSTPSSSTT NDSGKKRSSP LGRSSDLKSR RNRSFSEDSD LSCDDVLERS SLKSKADSVY
VPHALAFKRA YATKKTYTEE ELNAKLTRRV QKAARRQAKQ EELKRLHRAQ IIQRQLEQVE
EKQRQLEERG VAVEKALRGE ADYWGESNYT EIMDLHLGVE PFVGTPRRRP ISFCPCCSSE
GMGKKDDPKL MQEWFKLVQE KNALVRYESE LMIFARELEL EDRQSRLQQD LRERMAIEDH
LKTEVELAQE KHILNEMLEV VEQRDSLVAL LEEQRLSEKE EDKDLESVML SKGFNLNWA
//
