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Database: UniProt
Entry: A0A1S3MJW8_SALSA
LinkDB: A0A1S3MJW8_SALSA
Original site: A0A1S3MJW8_SALSA 
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}.
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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
//
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