ID A0A1S3MJI6_SALSA Unreviewed; 2459 AA.
AC A0A1S3MJI6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=F-actin monooxygenase {ECO:0000256|ARBA:ARBA00012709};
DE EC=1.14.13.225 {ECO:0000256|ARBA:ARBA00012709};
GN Name=LOC106573174 {ECO:0000313|RefSeq:XP_014003388.1};
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_014003388.1};
RN [1] {ECO:0000313|RefSeq:XP_014003388.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014003388.1};
RG RefSeq;
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the Mical family.
CC {ECO:0000256|ARBA:ARBA00008223}.
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DR RefSeq; XP_014003388.1; XM_014147913.1.
DR OrthoDB; 5399346at2759; -.
DR Proteomes; UP000087266; Chromosome ssa16.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
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); 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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: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 1078..1140
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 2298..2447
FT /note="BMERB"
FT /evidence="ECO:0000259|PROSITE:PS51848"
FT REGION 672..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1223..1356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1389..1517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1564..1694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1715..1944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1961..1991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2010..2043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2074..2256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2282..2335
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 675..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1275
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1352
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1415..1434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1481..1503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1569..1590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1646..1693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1718..1732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1798..1834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1835..1849
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1850..1866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1884..1898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2024..2043
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2074..2098
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2109..2140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2151..2175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2183..2199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2200..2217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2218..2251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2459 AA; 274843 MW; 9A94A8F33FFDADE0 CRC64;
MGTMGDLGGF TTTGERVNPA HILFDRFVQA STCKVTLKAF QELCDHLELK PCEYRVFYHK
LKSRLNYWKA KALWAKLDKR AGQKEYKKGR ACTNSKCLII GAGPCGLRTA IELGFLGAKV
VLLEKRDAFS RNNVLHLWPF TIQDLRGLGA KKFYGKFCAG AIDHISIRQL QLMLLKVALL
LGIEIHVNTE FKGLIEPPED QENERIGWRA EVLPRTHPVN ELEFDVIIGA DGRRNTLAGF
RRKEFRGKLA IAITANFINR NTTAEAKVEE ISGVAFIFNQ KFFQDLREAT GIDLENIVYY
KDDTHYFVMT AKKQSLLEKG VILHDYADTE MLLSRANVDQ AALLSYAREA ADFSTNHQLP
TLDFAINHYG QPDVAMFDFT CMYASENAAL VRQRNGRQLL VSLVGDSLLE PFWPMGTGIA
RGFLAAMDSG WMVKSWAQGN PSLDVLAERE SIYRLLPQTT PENINKNFSH YSVDPTTRYP
NISLHFLRPN QVRHLIDTGD SSREMLIEME NVVNSSTPKL TRNESIARSS KLLNWCQRQT
EGYRKVSVTD LTMSWKSGMA LCALIHRYRP DLIDFDSLDE RDQQKNNQLG FDVAEREFGI
SPCMTGKEMS QVSEPDKLSM VMYLSQFYEM FKDTVPPGAG GDQNMSPEEK AALINSTKSP
ISFLSKLGQS IAISRKRNPK DKKEKEVDGL GKRRKTSQAD NSEDEEVLRG NRDDRPSNST
ALTERKMKEE SAAVGNHNKV KSMATQLLAK FEENAPAESK GLKRQGDSLP SLGLVLALPP
PPASLDPPRE PVRLAPVPAW RQKRTQQQEQ LSFRYKEKVK CQTLPIRGEQ PRSGTEWCSG
SRSCPKKTIL LSSTSSLSLH SQHCDREGLE EEETTQNQTP QAHRKWEPMQ LEEPEPIHIP
SIQERSAWLI AKFKGKPEKP KLKKKPSRFF IEQWHLSART LSQNTQNLLS SPEALGQEIE
PLRSDDQMPL HVLSVQERAE QLASQFQGKL ANSQSMKKAL HFCVQKRHLS HSQKPESPLS
SPETLRPRYL KMYTGEVSLL AEQIANQLQP QEEPKPLLDK WELGSLRKEF PQNIGGSDVC
FFCQKRVYVM ERLSAEGKFF HRSCFKCDYC GTTLRLSSYA FDVEDGKFYC KPHYCYRSSG
QAQRKRPAPT PALLNAKDNQ ASLPAAVTVD SPGRGAMASP SPTERRSSVP EVNGLQEPSL
AKRLRGTPER IELENYRLSL QREEDLEEVP EETLAEHNLS SVLDKDAHAD LGSSSSESDM
EEEDQEEEEQ HEEEEQQDPP SPSDLGGVPW KEAVELHAKL KTDSDPGAEG EDGEGEDETH
GHIARDLEVE EEEDDEEEEE DDEAESTDEG EYCPWELELQ SGIWLENLQD EEDTCRFKAR
NLQIQQVLQP VDPTGIKNLR RVSVLSEGDK EEPPASASQP STMLTQSPST APAHTSARHE
AVRVWLESVS GEPCEDDDPE AEVGSHDFEP GTEMDQEDIP SDAEAEARLH QSELSDALPE
EDKKSQSQGI AYSIEQTSVS PVKLVGEVAL SPVKPLTPQP DLQMSHTSPP YLVKSPGMRF
FPDPFASENI TIPQRTVQTP NAKSPQYATP APSPIHSPLQ SPIRSQPIPL PETVTPKSPV
NSPPCSCPST GNPLSPICAQ PLPCHEPSSP LTSDSPVRTQ PVPAITSTPL AKPDSSDRTT
PEPQKSLNLT DETPVKKTDI IEEFWLKSAE IRKSLGLTPL DRSSSSSSKA PEKCPVTVGK
VPTPDSPSTK SYTPEDLSEE LRPSPSPFTG RSVIRRLNIT VEGQVISPAE PKSNGSDRRD
LSSSSGLGLN GSTATNQTSQ AASDSYHTSD STMLTPPSSP PPPPPNEEPA TLRQQQKHQV
SWDNGIDGPT TPEPAKAAPT KTNSPVPAPR TQISPVSMPV SAPKPAPRTT PVTSPVTSPV
TAPVTPLVVM RREKSSKPRR EEVRKSFVEC VAEIPFADDV EDTYDERTPD TTMDRFYTPP
SSKPNREREK RPLHLALAME NGKPIFPVNQ QASKSQKAQQ FSPEAKEIAE ERMRAREKSI
KSQALKEAMA KQLNKMKETD TAKGAAAAAK VVWNVASSET SGKSTKKSSG SPKTSAVKSL
ESKKAETLPE RFFSSQGNKS LDSSTVSSDG SASGGKSKKR SSLFSPRKNK KEKKAKNESQ
LSVKHGTDET PSPPKHKSLW KVVFSGYKKD KKKNKDDKSC PSTPSSSNTN DSGKKRLSPL
GRSSDLKSRR NLSFSEDSDL SCDDVLERSS QKSRTDSVYV PHALAFKRAY ATKKTYTEEE
LNAKLTRRVQ KAARRQAKQE ELKRLHRAQT IQRQLEQVEE KQRQLEERGV AVEKALRGEA
GMGKKDDPKL MQEWFKLVQE KNALVRYESE LMIFARELEL EDRQSRLQQD LRERMAIEDH
LKTEVELAQE KRILNEMLEV VEQRDSLVAL LEEQRLREKE EDKDLESVML SKGFNLNWA
//