ID A0A1S3MJW8_SALSA Unreviewed; 1782 AA.
AC A0A1S3MJW8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=F-actin monooxygenase {ECO:0000256|ARBA:ARBA00012709};
DE EC=1.14.13.225 {ECO:0000256|ARBA:ARBA00012709};
GN Name=LOC106573205 {ECO:0000313|RefSeq:XP_014003492.1};
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_014003492.1};
RN [1] {ECO:0000313|RefSeq:XP_014003492.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014003492.1};
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the Mical family.
CC {ECO:0000256|ARBA:ARBA00008223}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_014003492.1; XM_014148017.1.
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: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: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:SF39; [F-ACTIN]-MONOOXYGENASE MICAL2; 1.
DR PANTHER; PTHR23167; CALPONIN HOMOLOGY DOMAIN-CONTAINING PROTEIN DDB_G0272472-RELATED; 1.
DR Pfam; PF12130; bMERB_dom; 2.
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 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
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 513..619
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1045..1107
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 1572..1770
FT /note="BMERB"
FT /evidence="ECO:0000259|PROSITE:PS51848"
FT REGION 652..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1260..1306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1323..1364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1389..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1427..1449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1521..1575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1634..1661
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 655..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..771
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1389..1408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1554..1575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1782 AA; 200428 MW; 7119949ED0DAEDE2 CRC64;
MEDERSAQAG QLFENFVQAS TCKGTLQAFS ILCRQMDLDP LDYRNFYSNL KATVTNWKAK
ALWTKLDKRA GHKEYKRAKA CEGTRSLIIG GGPCGLRTAI ELALLGAKVV VIEKRDTFSR
NNVLHLWPYT IHDLRGLGAK KFYGKFCAGA IDHISIRQLQ LMLLKVSLIV GVEVHVNVEF
VKLLEPPDNQ ENEGPGWRAE IRPSNHPLTD FEFDVVIGAD GRRNTLDGFK RKEFRGKLAI
AITANFVNRN TTAEAKVEEI SGVAFIFNQK FFLELKEETG IDLENIVYYR DNTHYFVMTA
KKQSLLDKGV IIHDYIETEK LLGQDNVNQE ALLSYAREAA DFGTNYQLPS LDYAINHCNQ
PDVAMFDFTC MYASENAALF REKCGHQLLV ALVGDSLLEP FWPTGTGCAR GFLAAFDTVW
MVRGWAQGKA HLEILAEREG LYRLLPQTTT ENISKNFDQY TIDPVTRYPN LNSSCVKPHQ
VRHLFIDGQQ DSCPLERGGP TRRSVNLSRR ESDIRPSRLL TWCQKQTQGY RGVDVTNLTS
SWKSGLALCA LIHRLRPDLI DFDSLNEKDS AKNNQLAFDI AEHEFGIQPV TTGNEMALDQ
DPDKLMMVLY ISKLYEMFRN SPASITGTRE TEENNEAYSS ESAYSVYNLM NRTQPKKRIP
KDNGKLEEND PMNKRRRKGS TYLEELSCQS APPAGDGGEQ NKVRSMATQL LAKFEENASP
GSSLRNKSDL NSDSDSSHPS SPSLDMMENP RFAKPKEQPP PSPPPPRPKW QPSIYMRLLE
EPATVAQPTP LHVPTRSWSP PPHDDQTQAS PRADLVQQRV WIPHTETPDD VDYPEQPSPD
PTGMGQCLEK LEDKMSQKKV QTVTTGEFNR KSIKERAVLL RSMFPESETP LMKEYKTDRS
AFVPKITSIR PVSEPSALSC FSSLTPTSPV HHYKCNGSAA SSRLNQTPIE CPVSYQAEPF
KPDMSAEQCN GSAAPSVMIK KTIDQSESCP VEPSKPAKQR TVGKVSSHIG ARAETLAILY
ETDHRPNALP CIVRKEFPQN LGGSDTCHFC SKRVYVMERL SAEGHFFHRE CFRCDVCSST
LRLGGHAYDS QHGKFYCKPH YSQRRSSLQS SSKFLRRTED QGRLTSSPDR SDPYSATDSL
QSQPSGRHYR YTGLLNGLYT RMVPEVAEEA MDTMDLDTNR TADSKKQDHS NTSLQPQDSA
QEKKEPSDSN SSLLSGNSRW KRKIRATLPL ILVRHFSHEN ATEKEEPTIE EDNFDFNVIE
TPQVSDDGPK LPPDSPNQNP SMGKEAPPVT KVPQLQEAVG PKKRLTLSLS EKQKLLDWNL
VTPEEARSPG GGDPSKHYKP GDQILQKDPL PQVDPETEPV PAQPQPAPSM FQIWANAFRK
SFGVPGTTTD SNTVVTRRNN NGPTKSRPLS DGAFSFISLF GATAQSQEAE PVGVGQKSQP
TPHPCKASMG DRPADLPTLL DQVSLGSNKS VGSFTTDDMA SLPPRKHNFF SYLRLKKREG
PVSMGAGVLE KDIGTILSNI RNKASSEQQK DESNSSSDDE LVPAKPLSQP KTHGSSERQR
RRQEKTVIQQ DKREKLKRLH RAQVIQRQLE EVGEKQKDLE ERGVTIEKVL RGESPDKGDG
LSDEHELLQM WFKLVLEKNR LARYEEELVI FAQELELEDR QSQLQMDLRC RMSIDGIGHT
LCNCSVVLCN CSTQQLHILY LPLLQLLYVC TAALCPLWPF ADSRKSSSEL AEEQEMLTEI
MKVVERRDTL VSLLEEQRLQ ERAEDRDPES LVLSRGYQFH WT
//