LMCD1_HUMAN
ID LMCD1_HUMAN Reviewed; 365 AA.
AC Q9NZU5; B4DG80;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=LIM and cysteine-rich domains protein 1;
DE AltName: Full=Dyxin;
GN Name=LMCD1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10662546; DOI=10.1006/geno.1999.6049;
RA Bespalova I.N., Burmeister M.;
RT "Identification of a novel LIM domain gene, LMCD1, and chromosomal
RT localization in human and mouse.";
RL Genomics 63:69-74(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Holt H.H., Crosbie R.H., Saito F., Campbell K.P.;
RT "Identification of Dyxin: a novel intracellular binding partner of beta-
RT dystroglycan.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Amygdala, and Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [6]
RP INTERACTION WITH GATA6.
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 [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
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).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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 promoter
CC (By similarity). 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:0000250, ECO:0000269|PubMed:20026769}.
CC -!- SUBUNIT: Interacts with GATA1 and GATA4 (By similarity). Interacts with
CC beta-dystroglycan. Interacts with GATA6. {ECO:0000250,
CC ECO:0000269|PubMed:16199866}.
CC -!- INTERACTION:
CC Q9NZU5; P47224: RABIF; NbExp=3; IntAct=EBI-5774016, EBI-713992;
CC Q9NZU5; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-5774016, EBI-750487;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=May shuttle between the cytoplasm and the nucleus. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NZU5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NZU5-2; Sequence=VSP_053895;
CC -!- TISSUE SPECIFICITY: Expressed in the heart (at protein level).
CC Expressed in many tissues with highest abundance in skeletal muscle.
CC {ECO:0000269|PubMed:20026769}.
CC -!- DOMAIN: The LIM zinc-binding domains and the Cys-rich region mediate
CC interaction with GATA6. {ECO:0000250}.
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DR EMBL; AF169284; AAF34411.1; -; mRNA.
DR EMBL; AF216709; AAG36778.1; -; mRNA.
DR EMBL; AK022176; BAB13976.1; -; mRNA.
DR EMBL; AK294455; BAG57691.1; -; mRNA.
DR EMBL; AC087859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000646; AAH00646.1; -; mRNA.
DR CCDS; CCDS33688.1; -. [Q9NZU5-1]
DR CCDS; CCDS63534.1; -. [Q9NZU5-2]
DR RefSeq; NP_001265162.1; NM_001278233.1. [Q9NZU5-2]
DR RefSeq; NP_001265163.1; NM_001278234.1.
DR RefSeq; NP_001265164.1; NM_001278235.1.
DR RefSeq; NP_055398.1; NM_014583.3. [Q9NZU5-1]
DR AlphaFoldDB; Q9NZU5; -.
DR SMR; Q9NZU5; -.
DR BioGRID; 119020; 14.
DR IntAct; Q9NZU5; 10.
DR MINT; Q9NZU5; -.
DR STRING; 9606.ENSP00000157600; -.
DR iPTMnet; Q9NZU5; -.
DR MetOSite; Q9NZU5; -.
DR PhosphoSitePlus; Q9NZU5; -.
DR BioMuta; LMCD1; -.
DR DMDM; 20978521; -.
DR EPD; Q9NZU5; -.
DR jPOST; Q9NZU5; -.
DR MassIVE; Q9NZU5; -.
DR MaxQB; Q9NZU5; -.
DR PaxDb; Q9NZU5; -.
DR PeptideAtlas; Q9NZU5; -.
DR PRIDE; Q9NZU5; -.
DR ProteomicsDB; 4113; -.
DR ProteomicsDB; 83511; -. [Q9NZU5-1]
DR Antibodypedia; 10100; 153 antibodies from 18 providers.
DR DNASU; 29995; -.
DR Ensembl; ENST00000157600.8; ENSP00000157600.3; ENSG00000071282.12. [Q9NZU5-1]
DR Ensembl; ENST00000454244.4; ENSP00000396515.1; ENSG00000071282.12. [Q9NZU5-2]
DR GeneID; 29995; -.
DR KEGG; hsa:29995; -.
DR MANE-Select; ENST00000157600.8; ENSP00000157600.3; NM_014583.4; NP_055398.1.
DR UCSC; uc010hci.4; human. [Q9NZU5-1]
DR CTD; 29995; -.
DR DisGeNET; 29995; -.
DR GeneCards; LMCD1; -.
DR HGNC; HGNC:6633; LMCD1.
DR HPA; ENSG00000071282; Tissue enhanced (skeletal).
DR MIM; 604859; gene.
DR neXtProt; NX_Q9NZU5; -.
DR OpenTargets; ENSG00000071282; -.
DR PharmGKB; PA30401; -.
DR VEuPathDB; HostDB:ENSG00000071282; -.
DR eggNOG; KOG1704; Eukaryota.
DR GeneTree; ENSGT00940000158813; -.
DR HOGENOM; CLU_008937_1_0_1; -.
DR InParanoid; Q9NZU5; -.
DR OMA; MCSGFEP; -.
DR OrthoDB; 997264at2759; -.
DR PhylomeDB; Q9NZU5; -.
DR TreeFam; TF313265; -.
DR PathwayCommons; Q9NZU5; -.
DR Reactome; R-HSA-5683826; Surfactant metabolism.
DR SignaLink; Q9NZU5; -.
DR BioGRID-ORCS; 29995; 7 hits in 1074 CRISPR screens.
DR ChiTaRS; LMCD1; human.
DR GenomeRNAi; 29995; -.
DR Pharos; Q9NZU5; Tbio.
DR PRO; PR:Q9NZU5; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9NZU5; protein.
DR Bgee; ENSG00000071282; Expressed in hindlimb stylopod muscle and 173 other tissues.
DR ExpressionAtlas; Q9NZU5; baseline and differential.
DR Genevisible; Q9NZU5; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
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 Alternative splicing; Cytoplasm; LIM domain; Metal-binding; Nucleus;
KW Phosphoprotein; 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_0000075815"
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..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..73
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053895"
SQ SEQUENCE 365 AA; 40833 MW; D84BFD53C43D2DD7 CRC64;
MAKVAKDLNP GVKKMSLGQL QSARGVACLG CKGTCSGFEP HSWRKICKSC KCSQEDHCLT
SDLEDDRKIG RLLMDSKYST LTARVKGGDG IRIYKRNRMI MTNPIATGKD PTFDTITYEW
APPGVTQKLG LQYMELIPKE KQPVTGTEGA FYRRRQLMHQ LPIYDQDPSR CRGLLENELK
LMEEFVKQYK SEALGVGEVA LPGQGGLPKE EGKQQEKPEG AETTAATTNG SLSDPSKEVE
YVCELCKGAA PPDSPVVYSD RAGYNKQWHP TCFVCAKCSE PLVDLIYFWK DGAPWCGRHY
CESLRPRCSG CDEIIFAEDY QRVEDLAWHR KHFVCEGCEQ LLSGRAYIVT KGQLLCPTCS
KSKRS
