FHL2_RAT
ID FHL2_RAT Reviewed; 279 AA.
AC O35115;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Four and a half LIM domains protein 2;
DE Short=FHL-2;
DE AltName: Full=LIM domain protein DRAL;
DE AltName: Full=Skeletal muscle LIM-protein 3;
DE Short=SLIM-3;
GN Name=Fhl2; Synonyms=Dral, Slim3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=11001931; DOI=10.1093/oxfordjournals.hmg.a018919;
RA Tanahashi H., Tabira T.;
RT "Alzheimer's disease-associated presenilin 2 interacts with DRAL, an LIM-
RT domain protein.";
RL Hum. Mol. Genet. 9:2281-2289(2000).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=11813260; DOI=10.1002/jcb.10041.abs;
RA Ng E.K.O., Chan K.K., Wong C.H., Tsui S.K.W., Ngai S.M., Lee S.M.Y.,
RA Kotaka M., Lee C.Y., Waye M.M.Y., Fung K.P.;
RT "Interaction of the heart-specific LIM domain protein, FHL2, with DNA-
RT binding nuclear protein, hNP220.";
RL J. Cell. Biochem. 84:556-566(2002).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22851699; DOI=10.1128/mcb.05948-11;
RA Hojayev B., Rothermel B.A., Gillette T.G., Hill J.A.;
RT "FHL2 binds calcineurin and represses pathological cardiac growth.";
RL Mol. Cell. Biol. 32:4025-4034(2012).
CC -!- FUNCTION: May function as a molecular transmitter linking various
CC signaling pathways to transcriptional regulation. Negatively regulates
CC the transcriptional repressor E4F1 and may function in cell growth.
CC Inhibits the transcriptional activity of FOXO1 and its apoptotic
CC function by enhancing the interaction of FOXO1 with SIRT1 and FOXO1
CC deacetylation (By similarity). Negatively regulates the
CC calcineurin/NFAT signaling pathway in cardiomyocytes (PubMed:22851699).
CC {ECO:0000250|UniProtKB:Q14192, ECO:0000269|PubMed:22851699}.
CC -!- SUBUNIT: Interacts with ZNF638 and TTN/titin. Interacts with E4F1.
CC Interacts with GRB7. Interacts with SIRT1 and FOXO1. Interacts with
CC CEFIP and calcineurin. Interacts with FOXK1.
CC {ECO:0000250|UniProtKB:O70433, ECO:0000250|UniProtKB:Q14192}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14192}. Nucleus
CC {ECO:0000250|UniProtKB:Q14192}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000269|PubMed:22851699}.
CC -!- TISSUE SPECIFICITY: Expressed in heart only (at protein level).
CC {ECO:0000269|PubMed:11813260}.
CC -!- DOMAIN: The third LIM zinc-binding mediates interaction with E4F1.
CC {ECO:0000250|UniProtKB:Q14192}.
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DR EMBL; AB008571; BAA23357.1; -; mRNA.
DR RefSeq; NP_113865.1; NM_031677.1.
DR RefSeq; XP_006244911.1; XM_006244849.3.
DR RefSeq; XP_017452106.1; XM_017596617.1.
DR AlphaFoldDB; O35115; -.
DR SMR; O35115; -.
DR BioGRID; 248898; 1.
DR IntAct; O35115; 1.
DR STRING; 10116.ENSRNOP00000023014; -.
DR iPTMnet; O35115; -.
DR PhosphoSitePlus; O35115; -.
DR PaxDb; O35115; -.
DR PRIDE; O35115; -.
DR Ensembl; ENSRNOT00000023014; ENSRNOP00000023014; ENSRNOG00000016866.
DR GeneID; 63839; -.
DR KEGG; rno:63839; -.
DR UCSC; RGD:61963; rat.
DR CTD; 2274; -.
DR RGD; 61963; Fhl2.
DR eggNOG; KOG1704; Eukaryota.
DR GeneTree; ENSGT00950000183028; -.
DR HOGENOM; CLU_001357_2_0_1; -.
DR InParanoid; O35115; -.
DR OMA; KXTRKME; -.
DR OrthoDB; 642235at2759; -.
DR PhylomeDB; O35115; -.
DR TreeFam; TF321684; -.
DR PRO; PR:O35115; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000016866; Expressed in heart and 19 other tissues.
DR Genevisible; O35115; RN.
DR GO; GO:0031430; C:M band; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0043425; F:bHLH transcription factor binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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:0003714; F:transcription corepressor activity; ISO:RGD.
DR GO; GO:0008134; F:transcription factor binding; ISS:UniProtKB.
DR GO; GO:0055014; P:atrial cardiac muscle cell development; ISO:RGD.
DR GO; GO:0060347; P:heart trabecula formation; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0001649; P:osteoblast differentiation; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0009725; P:response to hormone; ISO:RGD.
DR GO; GO:0055015; P:ventricular cardiac muscle cell development; ISO:RGD.
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; 4.
DR PROSITE; PS50023; LIM_DOMAIN_2; 4.
PE 1: Evidence at protein level;
KW Cytoplasm; Isopeptide bond; LIM domain; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..279
FT /note="Four and a half LIM domains protein 2"
FT /id="PRO_0000075739"
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 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14192"
FT CROSSLNK 78
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14192"
FT CROSSLNK 167
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14192"
FT CROSSLNK 220
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14192"
SQ SEQUENCE 279 AA; 32087 MW; 9A9D8E5935034173 CRC64;
MTERFDCHHC NESLYGKKYI LKEENPHCVA CFEELYANTC EECGTPIGCD CKDLSYKDRH
WHEGCFHCSR CGSSLVDKPF AAKEEQLLCT DCYSNEYSSK CQECKKTIMP GTRKMEYKGS
SWHETCFTCQ RCQQPIGTKS FIPKENQNFC VPCYEKQYAL QCVQCKKPIT TGGVTYRDQP
WHRECFVCTA CKKQLSGQRF TARDEFPYCL TCFCDLYAKK CAGCTNPISG LGGTKYISFE
ERQWHNDCFN CKKCSLSLVG RGFLTERDDI LCPDCGKDI
