ID   FHL1_RAT                Reviewed;         280 AA.
AC   Q9WUH4;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Four and a half LIM domains protein 1;
DE            Short=FHL-1;
GN   Name=Fhl1;
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].
RA   Morgan M.J.;
RT   "Rat FHL1 protein sequence is very similar to its mouse and human
RT   counterparts.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; AF134773; AAD32624.1; -; mRNA.
DR   RefSeq; NP_001258128.1; NM_001271199.1.
DR   RefSeq; NP_001258129.1; NM_001271200.1.
DR   AlphaFoldDB; Q9WUH4; -.
DR   SMR; Q9WUH4; -.
DR   BioGRID; 247233; 2.
DR   IntAct; Q9WUH4; 1.
DR   STRING; 10116.ENSRNOP00000049677; -.
DR   iPTMnet; Q9WUH4; -.
DR   PhosphoSitePlus; Q9WUH4; -.
DR   PaxDb; Q9WUH4; -.
DR   PRIDE; Q9WUH4; -.
DR   Ensembl; ENSRNOT00000084594; ENSRNOP00000074052; ENSRNOG00000000875.
DR   GeneID; 25177; -.
DR   KEGG; rno:25177; -.
DR   CTD; 2273; -.
DR   RGD; 2615; Fhl1.
DR   eggNOG; KOG1704; Eukaryota.
DR   GeneTree; ENSGT00940000154833; -.
DR   HOGENOM; CLU_001357_2_0_1; -.
DR   InParanoid; Q9WUH4; -.
DR   PhylomeDB; Q9WUH4; -.
DR   PRO; PR:Q9WUH4; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000000875; Expressed in esophagus and 20 other tissues.
DR   ExpressionAtlas; Q9WUH4; baseline and differential.
DR   Genevisible; Q9WUH4; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
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:RGD.
DR   GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISO:RGD.
DR   GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; ISO:RGD.
DR   GO; GO:0043268; P:positive regulation of potassium ion transport; ISO:RGD.
DR   GO; GO:0003254; P:regulation of membrane depolarization; ISO:RGD.
DR   GO; GO:1901016; P:regulation of potassium ion transmembrane transporter activity; ISO:RGD.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Developmental protein; Differentiation;
KW   Isopeptide bond; LIM domain; Metal-binding; Reference proteome; Repeat;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P97447"
FT   CHAIN           2..280
FT                   /note="Four and a half LIM domains protein 1"
FT                   /id="PRO_0000234933"
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:0000250|UniProtKB:P97447"
FT   MOD_RES         4
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P97447"
FT   CROSSLNK        86
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13642"
SQ   SEQUENCE   280 AA;  31904 MW;  D9738C08B4707027 CRC64;
     MSEKFDCHYC RDPLQGKKYV QKDGRHCCLK CFDKFCANTC VECRKPISAD AKEVHYKNRY
     WHDTCFRCAK CLHPLASETF VSKDGKILCN KCATREDSPR CKGCFKAIVA GDQNVEYKGT
     IWHKDCFTCS NCKQVIGTGS FFPKGEDFYC VTCHETKFAK HCVKCNKAIT SGGITYQDQP
     WHAECFVCVT CSKKLAGQRF TAVEDQYYCV DCYKNFVAKK CAGCKNPITG FGKGSSVVAY
     EGQSWHDYCF HCKKCSVNLA NKRFVFHNEQ VYCPDCAKKL