LMCD1_MOUSE
ID LMCD1_MOUSE Reviewed; 365 AA.
AC Q8VEE1;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=LIM and cysteine-rich domains protein 1;
GN Name=Lmcd1;
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 [LARGE SCALE MRNA].
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 [2]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GATA1; GATA4 AND GATA6,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DOMAIN.
RX PubMed=16199866; DOI=10.1128/mcb.25.20.8864-8873.2005;
RA Rath N., Wang Z., Lu M.M., Morrisey E.E.;
RT "LMCD1/Dyxin is a novel transcriptional cofactor that restricts GATA6
RT function by inhibiting DNA binding.";
RL Mol. Cell. Biol. 25:8864-8873(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC 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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20026769; DOI=10.1161/hypertensionaha.109.135665;
RA Bian Z.Y., Huang H., Jiang H., Shen D.F., Yan L., Zhu L.H., Wang L.,
RA Cao F., Liu C., Tang Q.Z., Li H.;
RT "LIM and cysteine-rich domains 1 regulates cardiac hypertrophy by targeting
RT calcineurin/nuclear factor of activated T cells signaling.";
RL Hypertension 55:257-263(2010).
CC -!- FUNCTION: Transcriptional cofactor that restricts GATA6 function by
CC inhibiting DNA-binding, resulting in repression of GATA6
CC transcriptional activation of downstream target genes. Represses GATA6-
CC mediated trans activation of lung- and cardiac tissue-specific
CC promoters. Inhibits DNA-binding by GATA4 and GATA1 to the cTNC
CC promoter. Plays a critical role in the development of cardiac
CC hypertrophy via activation of calcineurin/nuclear factor of activated
CC T-cells signaling pathway. {ECO:0000269|PubMed:16199866,
CC ECO:0000269|PubMed:20026769}.
CC -!- SUBUNIT: Interacts with beta-dystroglycan (By similarity). Interacts
CC with GATA1, GATA4 and GATA6. {ECO:0000250,
CC ECO:0000269|PubMed:16199866}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16199866}. Nucleus
CC {ECO:0000269|PubMed:16199866}. Note=May shuttle between the cytoplasm
CC and the nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in distal airway epithelium of the lung,
CC vascular smooth muscle, and myocardium. {ECO:0000269|PubMed:16199866}.
CC -!- DEVELOPMENTAL STAGE: At 9.5 dpc expressed in the myocardium and forming
CC anterior foregut epithelium. By 12.5 dpc, expression is observed in the
CC airways of the developing lung as well as in the myocardium. At 14.5
CC dpc, when proximal-distal differentiation in the lung is proceeding
CC rapidly, expression is observed at high levels in the distal but not
CC proximal airways of the developing lung. By 16.5 dpc, expression
CC decreases in airway epithelium in the lung and expression is also
CC observed in the vascular smooth muscle of pulmonary arteries (at
CC protein level). {ECO:0000269|PubMed:16199866}.
CC -!- DOMAIN: The LIM zinc-binding domains and the Cys-rich region mediate
CC interaction with GATA6. {ECO:0000269|PubMed:16199866}.
CC -!- DISRUPTION PHENOTYPE: Mice display a marked increase in cardiac
CC hypertrophy. {ECO:0000269|PubMed:20026769}.
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DR EMBL; BC019124; AAH19124.1; -; mRNA.
DR CCDS; CCDS20403.1; -.
DR RefSeq; NP_659048.1; NM_144799.2.
DR AlphaFoldDB; Q8VEE1; -.
DR BioGRID; 206014; 2.
DR IntAct; Q8VEE1; 1.
DR STRING; 10090.ENSMUSP00000032376; -.
DR iPTMnet; Q8VEE1; -.
DR PhosphoSitePlus; Q8VEE1; -.
DR MaxQB; Q8VEE1; -.
DR PaxDb; Q8VEE1; -.
DR PRIDE; Q8VEE1; -.
DR ProteomicsDB; 292270; -.
DR Antibodypedia; 10100; 153 antibodies from 18 providers.
DR DNASU; 30937; -.
DR Ensembl; ENSMUST00000032376; ENSMUSP00000032376; ENSMUSG00000057604.
DR GeneID; 30937; -.
DR KEGG; mmu:30937; -.
DR UCSC; uc009ddv.2; mouse.
DR CTD; 29995; -.
DR MGI; MGI:1353635; Lmcd1.
DR VEuPathDB; HostDB:ENSMUSG00000057604; -.
DR eggNOG; KOG1704; Eukaryota.
DR GeneTree; ENSGT00940000158813; -.
DR HOGENOM; CLU_008937_1_0_1; -.
DR InParanoid; Q8VEE1; -.
DR OMA; MCSGFEP; -.
DR OrthoDB; 997264at2759; -.
DR PhylomeDB; Q8VEE1; -.
DR TreeFam; TF313265; -.
DR Reactome; R-MMU-5683826; Surfactant metabolism.
DR BioGRID-ORCS; 30937; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Lmcd1; mouse.
DR PRO; PR:Q8VEE1; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8VEE1; protein.
DR Bgee; ENSMUSG00000057604; Expressed in tarsal region and 182 other tissues.
DR ExpressionAtlas; Q8VEE1; baseline and differential.
DR Genevisible; Q8VEE1; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IMP:UniProtKB.
DR GO; GO:0010611; P:regulation of cardiac muscle hypertrophy; IMP:UniProtKB.
DR CDD; cd09829; PET_testin; 1.
DR InterPro; IPR010442; PET_domain.
DR InterPro; IPR033724; PET_testin.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 2.
DR Pfam; PF06297; PET; 1.
DR SMART; SM00132; LIM; 2.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
DR PROSITE; PS51303; PET; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; LIM domain; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..365
FT /note="LIM and cysteine-rich domains protein 1"
FT /id="PRO_0000075816"
FT DOMAIN 99..206
FT /note="PET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00636"
FT DOMAIN 241..306
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 307..365
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 200..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZU5"
SQ SEQUENCE 365 AA; 40996 MW; DB8AA836364E47D3 CRC64;
MAKVAKDLNP GVQKMSLGQQ QSARGVACLR CKGMCSGFEP HSWRKICKSC KCSQEEHCLS
SDLDDDRKIG RLLMDSKYAT LTARVKGGDG IRIYKRNRMI MTNPIATGKD PTFDTITYEW
APPGVTQKLG LQYMELIPKE RQPVTGTEGA LYRRRQLMHQ LPIYDQDPSR CRGLVENELK
AMEEFVKHYK SEALGVGEVA LPGQGGLPKE ENKTQEKPEG TETTAPTTNG SLGDPSKEVE
YVCELCKGAA PVDSPVVYAD RAGYSKQWHP TCFQCIKCSE PLVDLIYFWK DGAPWCGRHY
CESVRPRCSG CDEIIFSEDY QRVEDLAWHR KHFICEGCEQ LLSGRAYIVT KGQLLCPTCS
KSKRS
