FHL2_BOVIN
ID FHL2_BOVIN Reviewed; 279 AA.
AC Q2KI95;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Four and a half LIM domains protein 2;
DE Short=FHL-2;
GN Name=FHL2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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. Negatively regulates the calcineurin/NFAT signaling
CC pathway in cardiomyocytes (By similarity).
CC {ECO:0000250|UniProtKB:Q14192}.
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:0000250|UniProtKB:O35115}.
CC -!- DOMAIN: The third LIM zinc-binding mediates interaction with E4F1.
CC {ECO:0000250|UniProtKB:Q14192}.
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DR EMBL; BC112720; AAI12721.1; -; mRNA.
DR RefSeq; NP_001039511.1; NM_001046046.2.
DR RefSeq; XP_005212489.1; XM_005212432.1.
DR RefSeq; XP_005212490.1; XM_005212433.3.
DR AlphaFoldDB; Q2KI95; -.
DR SMR; Q2KI95; -.
DR STRING; 9913.ENSBTAP00000001440; -.
DR PaxDb; Q2KI95; -.
DR PRIDE; Q2KI95; -.
DR Ensembl; ENSBTAT00000001440; ENSBTAP00000001440; ENSBTAG00000001086.
DR GeneID; 510008; -.
DR KEGG; bta:510008; -.
DR CTD; 2274; -.
DR VEuPathDB; HostDB:ENSBTAG00000001086; -.
DR VGNC; VGNC:29000; FHL2.
DR eggNOG; KOG1704; Eukaryota.
DR GeneTree; ENSGT00950000183028; -.
DR HOGENOM; CLU_001357_2_0_1; -.
DR InParanoid; Q2KI95; -.
DR OMA; CHYCKET; -.
DR OrthoDB; 642235at2759; -.
DR TreeFam; TF321684; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000001086; Expressed in cardiac ventricle and 108 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; ISS:UniProtKB.
DR GO; GO:0043425; F:bHLH transcription factor binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0008134; F:transcription factor binding; ISS:UniProtKB.
DR GO; GO:0055014; P:atrial cardiac muscle cell development; IEA:Ensembl.
DR GO; GO:0060347; P:heart trabecula formation; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0009725; P:response to hormone; IEA:Ensembl.
DR GO; GO:0055015; P:ventricular cardiac muscle cell development; IEA:Ensembl.
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 2: Evidence at transcript 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_0000265105"
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; 32101 MW; 9103C5D087632F7A CRC64;
MTERFDCHHC EDSLFGRKYV LREEQPYCVA CFEALFASTC EECGKLIGCD CKDLSYKDRH
WHEACFHCSR CRGSLVDKPF AAKEDQLLCT DCYSQEYSSR CQECKKSIMP GTRKMEYKGS
SWHETCFICH RCQQPIGTKS FIPKDSENFC VPCYERQYAL QCVQCKKPIT TGGVTYREQP
WHRECFVCTA CKKPLSGQRF TSRDEFAYCL GCFCDLYAKK CAGCANPISG LGGTKYISFE
ERQWHNDCFN CKKCSLSLVG RGFLTERDDI LCPDCGKDI
