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Database: UniProt
Entry: A0A3B1JVF8_ASTMX
LinkDB: A0A3B1JVF8_ASTMX
Original site: A0A3B1JVF8_ASTMX 
ID   A0A3B1JVF8_ASTMX        Unreviewed;      1563 AA.
AC   A0A3B1JVF8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=F-actin monooxygenase {ECO:0000256|ARBA:ARBA00012709};
DE            EC=1.14.13.225 {ECO:0000256|ARBA:ARBA00012709};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000045711.1, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000045711.1}
RP   IDENTIFICATION.
RG   Ensembl;
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 {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   Ensembl; ENSAMXT00000036152.1; ENSAMXP00000045711.1; ENSAMXG00000013076.2.
DR   GeneTree; ENSGT00940000158780; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000013076; Expressed in muscle tissue and 13 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; 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:SF39; [F-ACTIN]-MONOOXYGENASE MICAL2; 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}; 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:UP000018467};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          516..619
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          868..930
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          1402..1551
FT                   /note="BMERB"
FT                   /evidence="ECO:0000259|PROSITE:PS51848"
FT   REGION          626..684
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          728..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1006..1032
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1072..1207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1226..1341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1353..1393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1412..1439
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        627..656
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..684
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..751
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        780..805
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1006..1028
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1082..1114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1123..1207
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1243..1257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1262..1276
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1277..1305
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1563 AA;  175977 MW;  85C3AAA673CE3703 CRC64;
     MGETEDERNS QASQLFENFV QASTCKGTLQ AFSVLCRQLE LDPADHQDFY SSLKAAVTSW
     KAKALWAKLD KRASHKEYKK GNACPDTRCL IIGGGPCGLR TAIELALLGA KVVVIEKRDT
     FSRNNVLHLW PFTIHDLRNL GAKKFYGKFC AGAIDHISIR QLQLILLKVS LIMGVEVHVN
     VEFVNLLEPP EDQGNDGIGW RAEIRPDGHP LADYEFDVLI GADGRRSTLE GFKRKEFRGK
     LAIAITANFV NRNTTAEAKV EEISGVAFIF NQKFFLELKE ETGVDLENIV YYKDNTHYFV
     MTAKKQSLLD KGVIIHDYIE TERLLHSDNV NQEALLSYAR EAADFGTNYQ LPSLDYAINH
     YGQPDVAMFD FTCMYASENA ALIREKNGHQ LLVALVGDSL LEPFWPMGTG CARGFLAAFD
     TVWMVQGWAQ GKSPLEVLCE RESIYRLLPQ TTAENITKNF EQYTIDPATR YPNLNSSCVR
     PHQVRHLFIN GEQNSCMLEH GGPTRRSVNI SRRESEVRPS RLLLWCQKQT QGYRGVDVTD
     LTTSWRSGLA LCALIHRQRP DLIDFDSLNE ADCAKNNQLA FEVAERAFGI QPLITGKEMV
     AEQEPDKLVM VLYLSKFYEK FRNSSLPVTG APRQTDENNE DYSSKSTNSV YNLMNVSQPR
     KRVPKDDKKL DDNDPNKKRR KGYNYLEELS GRDALTAGEG LEQKENKVRS MATQLLAKFE
     ENAPSCALRR QVDGSSPAPP APSPPPKPLS VHSLPACSAL SCLLSPPPPP PPQKQCNEDS
     ESQQNDHQRN TDRSEIKRIE NLDPSKQRTV GKVSSAIGVK AAALAILYET DHRPNNPVTL
     SLTEARRAQD AGSANVRREF APGVGGSDIC HFCKKRVYVM ERLSAEGYFF HRECFRCDVC
     SATLRLGGHA FDSDQGTFYC KLHFAQRKTS HRSRKKELPG GSVSLVDGSD GYSATSSLHS
     QPSDMLGVRS STVTLRSPVQ NSLQNPSIAT EAPAEERLVT ARIVDSTVQD SPAESESLKP
     NSPQLNKVER SYAKGGITNR NISWRKKIRN TLPLILVKTL DRSRIGGQDD ALIEEDSDFE
     EIHAPDSPAK SSKHPEDPHC PLQDKQDQAA KSEIPHYRTH GISSPPKPST SSVEQQNEIS
     YNSTNQQSPK KKLTLSSSER EKLLNWELAN PTQFSQAAVT TDRTEKNGQV CTEDQPKPQN
     DTERSPPLFQ IWANVLRRSF SSSVNNPKVI KRNRPPRARP LSEGSFSFSS LFGASTQFQE
     EEEDDNERKR SRAATEGSQS RLKGRSEITT MLEQVSLTTT KPPGGTKDDM ASLPPRKLNF
     FSSLRLKRNE GTGRGKTDNQ TKDILSILSK FRNKASTQQQ QHEEDDYSSS EEGPESGAPR
     SISDDSERQR KKQEKILIQQ SKREQLKRLH RAQAIQRQLE EVEEKQRVLE EKGVTLEKVL
     RGEMNDPSAD EAELLQTWFK LVLEKNKLAR YESELMIFAQ ELELEDRQSQ LQQELRRRMA
     VEDCEKSAGE LVEEQALLVE VMKAVEERDR LVSLLEEQRL QEKAEDRDLE GLILSKGYLF
     HWA
//
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