FHL3_MOUSE
ID FHL3_MOUSE Reviewed; 289 AA.
AC Q9R059; A6H6N4; Q9JLP5; Q9WUH3;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Four and a half LIM domains protein 3;
DE Short=FHL-3;
DE AltName: Full=Skeletal muscle LIM-protein 2;
DE Short=SLIM-2;
GN Name=Fhl3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10049693; DOI=10.1006/bbrc.1999.0179;
RA Morgan M.J., Madgwick A.J.A.;
RT "The LIM proteins FHL1 and FHL3 are expressed differently in skeletal
RT muscle.";
RL Biochem. Biophys. Res. Commun. 255:245-250(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10906474; DOI=10.1016/s0925-4773(00)00341-5;
RA Chu P.-H., Ruiz-Lozano P., Zhou Q., Cai C., Chen J.;
RT "Expression patterns of FHL/SLIM family members suggest important
RT functional roles in skeletal muscle and cardiovascular system.";
RL Mech. Dev. 95:259-265(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-228.
RA Li H.Y., Lee S.M.Y., Tsui S.K.W., Chan K.K., Kotaka M., Chim S.S.C.,
RA Lee C.Y., Fung K.P., Waye M.M.Y.;
RT "The cloning, sequencing and characterization of a mouse FHL3, which
RT contains four and a half LIM domains.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, INTERACTION WITH SOX15, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=17363903; DOI=10.1038/sj.emboj.7601635;
RA Meeson A.P., Shi X., Alexander M.S., Williams R.S., Allen R.E., Jiang N.,
RA Adham I.M., Goetsch S.C., Hammer R.E., Garry D.J.;
RT "Sox15 and Fhl3 transcriptionally coactivate Foxk1 and regulate myogenic
RT progenitor cells.";
RL EMBO J. 26:1902-1912(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-157 AND LYS-244, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Recruited by SOX15 to FOXK1 promoters where it acts as a
CC transcriptional coactivator of FOXK1. {ECO:0000269|PubMed:17363903}.
CC -!- SUBUNIT: Interacts with SOX15; the interaction recruits FHL3 to FOXK1
CC promoters where it acts as a transcriptional coactivator of FOXK1.
CC {ECO:0000269|PubMed:17363903}.
CC -!- INTERACTION:
CC Q9R059; P43267: Sox15; NbExp=7; IntAct=EBI-7332617, EBI-7332587;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17363903}. Cytoplasm
CC {ECO:0000269|PubMed:17363903}.
CC -!- TISSUE SPECIFICITY: Expressed in myogenic progenitor cells (at protein
CC level) (PubMed:17363903). Expressed in skeletal striated muscle and the
CC heart (PubMed:10906474, PubMed:17363903). Expressed to a lesser extent,
CC in lung, and kidney (PubMed:10906474). Expressed in skin and skeletal
CC muscles such as the masseter, tongue, tibialis anterior and plantar
CC muscles (PubMed:10049693). {ECO:0000269|PubMed:10049693,
CC ECO:0000269|PubMed:10906474, ECO:0000269|PubMed:17363903}.
CC -!- DEVELOPMENTAL STAGE: Expressed ubiquitously at low levels during
CC embryonic development. {ECO:0000269|PubMed:10906474}.
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 EMBL; AF134772; AAD32623.1; -; mRNA.
DR EMBL; AF114382; AAD53231.1; -; mRNA.
DR EMBL; AL606907; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC144903; AAI44904.1; -; mRNA.
DR EMBL; BC145939; AAI45940.1; -; mRNA.
DR EMBL; AF149826; AAF73159.1; -; mRNA.
DR CCDS; CCDS38874.1; -.
DR RefSeq; NP_034343.2; NM_010213.3.
DR RefSeq; XP_006502831.1; XM_006502768.3.
DR AlphaFoldDB; Q9R059; -.
DR SMR; Q9R059; -.
DR BioGRID; 199670; 5.
DR IntAct; Q9R059; 1.
DR MINT; Q9R059; -.
DR STRING; 10090.ENSMUSP00000040150; -.
DR iPTMnet; Q9R059; -.
DR PhosphoSitePlus; Q9R059; -.
DR EPD; Q9R059; -.
DR MaxQB; Q9R059; -.
DR PaxDb; Q9R059; -.
DR PeptideAtlas; Q9R059; -.
DR PRIDE; Q9R059; -.
DR ProteomicsDB; 270989; -.
DR Antibodypedia; 31823; 178 antibodies from 32 providers.
DR DNASU; 14201; -.
DR Ensembl; ENSMUST00000038684; ENSMUSP00000040150; ENSMUSG00000032643.
DR GeneID; 14201; -.
DR KEGG; mmu:14201; -.
DR UCSC; uc008uqv.2; mouse.
DR CTD; 2275; -.
DR MGI; MGI:1341092; Fhl3.
DR VEuPathDB; HostDB:ENSMUSG00000032643; -.
DR eggNOG; KOG1704; Eukaryota.
DR GeneTree; ENSGT00950000183028; -.
DR InParanoid; Q9R059; -.
DR OrthoDB; 642235at2759; -.
DR PhylomeDB; Q9R059; -.
DR TreeFam; TF314113; -.
DR BioGRID-ORCS; 14201; 3 hits in 57 CRISPR screens.
DR ChiTaRS; Fhl3; mouse.
DR PRO; PR:Q9R059; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9R059; protein.
DR Bgee; ENSMUSG00000032643; Expressed in hindlimb stylopod muscle and 62 other tissues.
DR ExpressionAtlas; Q9R059; baseline and differential.
DR Genevisible; Q9R059; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0001725; C:stress fiber; IDA:MGI.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0003779; F:actin binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:MGI.
DR InterPro; IPR037987; FHL2/3/5.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24205; PTHR24205; 1.
DR Pfam; PF00412; LIM; 4.
DR SMART; SM00132; LIM; 4.
DR PROSITE; PS00478; LIM_DOMAIN_1; 3.
DR PROSITE; PS50023; LIM_DOMAIN_2; 4.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Cytoplasm; LIM domain; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13643"
FT CHAIN 2..289
FT /note="Four and a half LIM domains protein 3"
FT /id="PRO_0000075741"
FT DOMAIN 40..92
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 101..153
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 162..212
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 221..275
FT /note="LIM zinc-binding 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT ZN_FING 7..31
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q13643"
FT MOD_RES 157
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 244
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 77
FT /note="D -> G (in Ref. 1; AAD32623)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="E -> D (in Ref. 1; AAD32623)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="T -> S (in Ref. 1; AAD32623)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="G -> A (in Ref. 2; AAD53231)"
FT /evidence="ECO:0000305"
FT CONFLICT 157..159
FT /note="KFA -> NLT (in Ref. 5; AAF73159)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="K -> Q (in Ref. 1; AAD32623)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="Q -> H (in Ref. 2; AAD53231)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="D -> E (in Ref. 1; AAD32623)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="K -> N (in Ref. 2; AAD53231)"
FT /evidence="ECO:0000305"
FT CONFLICT 229..238
FT /note="TGGSGGGEGA -> V (in Ref. 1; AAD32623)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="G -> A (in Ref. 2; AAD53231)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="S -> N (in Ref. 1; AAD32623)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 31795 MW; 38168919F5303237 CRC64;
MSEAFDCAKC NESLYGRKYI QTDSGPYCVP CYDNTFANTC AECQQLIGHD SRELFYEDRH
FHEGCFRCCR CQRSLADEPF TCQDSELLCN ECYCTAFSSQ CSACGETVMP GSRKLEYGGQ
TWHEHCFLCS GCEQPLGSRS FVPDKGAHYC VPCYENKFAP RCARCSKTLT QGGVTYRDQP
WHRECLVCTG CKTPLAGQQF TSRDDDPYCV ACFGELFAPK CSSCKRPITG GSGGGEGAGL
GGGKYVSFED RHWHHSCFSC ARCSTSLVGQ GFVPDGDQVL CQGCSQAGP
