FHL1_MOUSE
ID FHL1_MOUSE Reviewed; 280 AA.
AC P97447; O55181; Q8K318;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-NOV-2002, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Four and a half LIM domains protein 1;
DE Short=FHL-1;
DE AltName: Full=KyoT;
DE AltName: Full=RBP-associated molecule 14-1;
DE Short=RAM14-1;
DE AltName: Full=Skeletal muscle LIM-protein 1;
DE Short=SLIM;
DE Short=SLIM-1;
GN Name=Fhl1;
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] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
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], SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING.
RX PubMed=9418910; DOI=10.1128/mcb.18.1.644;
RA Taniguchi Y., Furukawa T., Tun T., Han H., Honjo T.;
RT "LIM protein KyoT2 negatively regulates transcription by association with
RT the RBP-J DNA-binding protein.";
RL Mol. Cell. Biol. 18:644-654(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND LYS-4, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP 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: May have an involvement in muscle development or hypertrophy.
CC Isoform 2 binds to RBP-J and plays a negative regulatory role in the
CC RBP-J-mediated transcription in mammalian systems.
CC -!- INTERACTION:
CC P97447-2; P31266: Rbpj; NbExp=4; IntAct=EBI-16082627, EBI-1392666;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=KyoT1;
CC IsoId=P97447-1; Sequence=Displayed;
CC Name=2; Synonyms=KyoT2;
CC IsoId=P97447-2; Sequence=VSP_003120, VSP_003121;
CC -!- TISSUE SPECIFICITY: Isoform 1 seems to be most abundant in each tissue
CC and isoform 2 much less abundant. Isoform 1 is highly expressed in
CC skeletal muscle and lung, and to a lesser extent in heart, brain and
CC kidney. Isoform 2 was found in brain, lung kidney and genital organs.
CC {ECO:0000269|PubMed:10906474}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH29024.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U77039; AAC02727.1; -; mRNA.
DR EMBL; U41739; AAC02805.1; -; mRNA.
DR EMBL; AF114380; AAD53229.1; -; mRNA.
DR EMBL; BC031120; AAH31120.1; -; mRNA.
DR EMBL; BC029024; AAH29024.1; ALT_INIT; mRNA.
DR CCDS; CCDS30148.1; -. [P97447-1]
DR RefSeq; NP_001070830.1; NM_001077362.2.
DR RefSeq; NP_001274729.1; NM_001287800.1. [P97447-1]
DR RefSeq; NP_034341.2; NM_010211.3. [P97447-1]
DR RefSeq; XP_006527871.2; XM_006527808.2. [P97447-2]
DR RefSeq; XP_017173870.1; XM_017318381.1. [P97447-1]
DR RefSeq; XP_017173871.1; XM_017318382.1. [P97447-2]
DR PDB; 4J2X; X-ray; 2.85 A; B/D=168-194.
DR PDBsum; 4J2X; -.
DR AlphaFoldDB; P97447; -.
DR SMR; P97447; -.
DR BioGRID; 199668; 18.
DR CORUM; P97447; -.
DR DIP; DIP-42041N; -.
DR IntAct; P97447; 3.
DR MINT; P97447; -.
DR iPTMnet; P97447; -.
DR PhosphoSitePlus; P97447; -.
DR SwissPalm; P97447; -.
DR jPOST; P97447; -.
DR MaxQB; P97447; -.
DR PRIDE; P97447; -.
DR ProteomicsDB; 266841; -. [P97447-1]
DR ProteomicsDB; 266842; -. [P97447-2]
DR Antibodypedia; 16643; 503 antibodies from 37 providers.
DR DNASU; 14199; -.
DR Ensembl; ENSMUST00000023854; ENSMUSP00000023854; ENSMUSG00000023092. [P97447-1]
DR Ensembl; ENSMUST00000116596; ENSMUSP00000112295; ENSMUSG00000023092. [P97447-1]
DR GeneID; 14199; -.
DR KEGG; mmu:14199; -.
DR UCSC; uc009tgm.2; mouse. [P97447-1]
DR CTD; 2273; -.
DR MGI; MGI:1298387; Fhl1.
DR VEuPathDB; HostDB:ENSMUSG00000023092; -.
DR GeneTree; ENSGT00940000154833; -.
DR InParanoid; P97447; -.
DR OrthoDB; 642235at2759; -.
DR BioGRID-ORCS; 14199; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Fhl1; mouse.
DR PRO; PR:P97447; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P97447; protein.
DR Bgee; ENSMUSG00000023092; Expressed in plantaris and 273 other tissues.
DR ExpressionAtlas; P97447; baseline and differential.
DR Genevisible; P97447; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007517; P:muscle organ development; IEA:InterPro.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0043268; P:positive regulation of potassium ion transport; ISO:MGI.
DR GO; GO:0003254; P:regulation of membrane depolarization; ISO:MGI.
DR GO; GO:1901016; P:regulation of potassium ion transmembrane transporter activity; ISO:MGI.
DR InterPro; IPR042997; Fhl1.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR47029; PTHR47029; 1.
DR Pfam; PF00412; LIM; 4.
DR SMART; SM00132; LIM; 4.
DR PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR PROSITE; PS50023; LIM_DOMAIN_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Developmental protein; Differentiation; Isopeptide bond; LIM domain;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Ubl conjugation; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CHAIN 2..280
FT /note="Four and a half LIM domains protein 1"
FT /id="PRO_0000075736"
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..276
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:0007744|PubMed:23806337"
FT MOD_RES 4
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CROSSLNK 86
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13642"
FT VAR_SEQ 168..194
FT /note="AITSGGITYQDQPWHAECFVCVTCSKK -> GLVKAPVWWPMKDNPGTTTAS
FT TAKNAP (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_003120"
FT VAR_SEQ 195..280
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_003121"
FT CONFLICT 98
FT /note="S -> F (in Ref. 1; AAC02727)"
FT /evidence="ECO:0000305"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:4J2X"
SQ SEQUENCE 280 AA; 31889 MW; 76C64FB8087BA36D CRC64;
MSEKFDCHYC RDPLQGKKYV QKDGRHCCLK CFDKFCANTC VDCRKPISAD AKEVHYKNRY
WHDNCFRCAK CLHPLASETF VSKDGKILCN KCATREDSPR CKGCFKAIVA GDQNVEYKGT
VWHKDCFTCS NCKQVIGTGS FFPKGEDFYC VTCHETKFAK HCVKCNKAIT SGGITYQDQP
WHAECFVCVT CSKKLAGQRF TAVEDQYYCV DCYKNFVAKK CAGCKNPITG FGKGSSVVAY
EGQSWHDYCF HCKKCSVNLA NKRFVFHNEQ VYCPDCAKKL
