LCOR_MOUSE
ID LCOR_MOUSE Reviewed; 433 AA.
AC Q6ZPI3; Q3U302; Q5CZW7; Q80VA8; Q8BGT2; Q8C9Q0;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Ligand-dependent corepressor;
DE Short=LCoR;
DE AltName: Full=Mblk1-related protein 2;
GN Name=Lcor; Synonyms=Kiaa1795, Mlr2;
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 [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12560079; DOI=10.1016/s0014-5793(02)03858-9;
RA Kunieda T., Park J.-M., Takeuchi H., Kubo T.;
RT "Identification and characterization of Mlr1,2: two mouse homologues of
RT Mblk-1, a transcription factor from the honeybee brain.";
RL FEBS Lett. 535:61-65(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Aorta, Dendritic cell, Thymus, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and Mammary gland;
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).
CC -!- FUNCTION: Repressor of ligand-dependent transcription activation by
CC various nuclear repressors. Repressor of ligand-dependent transcription
CC activation by ESR1, ESR2, NR3C1, PGR, RARA, RARB, RARG, RXRA and VDR
CC (By similarity). May act as transcription activator that binds DNA
CC elements with the sequence 5'-CCCTATCGATCGATCTCTACCT-3'. {ECO:0000250,
CC ECO:0000269|PubMed:12560079}.
CC -!- SUBUNIT: Interacts with ESR1 and ESR2 in the presence of estradiol.
CC Interacts with CTBP1, HDAC3 and HDAC6. Component of a large corepressor
CC complex that contains about 20 proteins, including CTBP1, CTBP2, HDAC1
CC and HDAC2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00320}.
CC -!- TISSUE SPECIFICITY: Detected in heart and kidney.
CC {ECO:0000269|PubMed:12560079}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98252.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE32988.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB076079; BAC20955.1; -; mRNA.
DR EMBL; AK129442; BAC98252.1; ALT_INIT; mRNA.
DR EMBL; AK041090; BAC30816.1; -; mRNA.
DR EMBL; AK041621; BAC31007.2; -; mRNA.
DR EMBL; AK155007; BAE32988.1; ALT_FRAME; mRNA.
DR EMBL; BC050068; AAH50068.1; -; mRNA.
DR EMBL; BC090652; AAH90652.1; -; mRNA.
DR CCDS; CCDS29810.1; -.
DR RefSeq; NP_742166.1; NM_172154.4.
DR RefSeq; XP_006526912.1; XM_006526849.3.
DR RefSeq; XP_006526913.1; XM_006526850.3.
DR AlphaFoldDB; Q6ZPI3; -.
DR SMR; Q6ZPI3; -.
DR BioGRID; 229316; 2.
DR DIP; DIP-60279N; -.
DR IntAct; Q6ZPI3; 1.
DR STRING; 10090.ENSMUSP00000067603; -.
DR iPTMnet; Q6ZPI3; -.
DR PhosphoSitePlus; Q6ZPI3; -.
DR EPD; Q6ZPI3; -.
DR jPOST; Q6ZPI3; -.
DR MaxQB; Q6ZPI3; -.
DR PaxDb; Q6ZPI3; -.
DR PRIDE; Q6ZPI3; -.
DR ProteomicsDB; 286181; -.
DR Antibodypedia; 30781; 231 antibodies from 25 providers.
DR DNASU; 212391; -.
DR Ensembl; ENSMUST00000067795; ENSMUSP00000067603; ENSMUSG00000025019.
DR Ensembl; ENSMUST00000163929; ENSMUSP00000126441; ENSMUSG00000025019.
DR GeneID; 212391; -.
DR KEGG; mmu:212391; -.
DR UCSC; uc008hly.1; mouse.
DR CTD; 84458; -.
DR MGI; MGI:2443930; Lcor.
DR VEuPathDB; HostDB:ENSMUSG00000025019; -.
DR eggNOG; KOG4565; Eukaryota.
DR GeneTree; ENSGT00940000154965; -.
DR HOGENOM; CLU_040042_0_0_1; -.
DR InParanoid; Q6ZPI3; -.
DR OrthoDB; 134164at2759; -.
DR PhylomeDB; Q6ZPI3; -.
DR TreeFam; TF319589; -.
DR BioGRID-ORCS; 212391; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Lcor; mouse.
DR PRO; PR:Q6ZPI3; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q6ZPI3; protein.
DR Bgee; ENSMUSG00000025019; Expressed in epithelium of stomach and 240 other tissues.
DR ExpressionAtlas; Q6ZPI3; baseline and differential.
DR Genevisible; Q6ZPI3; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:1990226; F:histone methyltransferase binding; ISO:MGI.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:MGI.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:MGI.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:1902466; P:positive regulation of histone H3-K27 trimethylation; IDA:ARUK-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR007889; HTH_Psq.
DR Pfam; PF05225; HTH_psq; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS50960; HTH_PSQ; 1.
PE 2: Evidence at transcript level;
KW Activator; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..433
FT /note="Ligand-dependent corepressor"
FT /id="PRO_0000236808"
FT DOMAIN 340..392
FT /note="HTH psq-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00320"
FT DNA_BIND 368..388
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00320"
FT REGION 1..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 53..57
FT /note="Interaction with nuclear receptors"
FT /evidence="ECO:0000250"
FT MOTIF 339..345
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JN0"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JN0"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JN0"
FT CROSSLNK 254
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JN0"
FT CROSSLNK 414
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96JN0"
FT CONFLICT 311
FT /note="S -> F (in Ref. 3; BAE32988)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="L -> P (in Ref. 4; AAH90652)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 433 AA; 47125 MW; 736656D1F7E9A041 CRC64;
MQRMIQQFAA EYTSKTSSTQ DPSQPNSTKN QSLPKASPVT TSPTAATTQN PVLSKLLMAD
QDSPLDLTVR KSQSEPSEQD GVLDLSTKKS PCASSTSLSH SPGCSSTQGN GRPGRPSQYR
PDGLRSGDGV PPRSLQDGTR EGFGHSTSLK VPLARSLQIS EELLSRNQLS TAASLGPSGL
QNHGQHLILS REASWAKPHY EFSLSRMKFR GNGALSNISD LPFLAENSAF PKMAHQTKQD
GKRDMSHSSP VDLKIPQVRG MDLSWESRTG DQYSYSSLVM GSQTESALSK KLRAILPKQN
RKSMLDAGPD SWGSDAEQST SGQPYPTSDQ EGDPGSKQPR KKRGRYRQYN SEILEEAISV
VMSGKMSVSK AQSIYGIPHS TLEYKVKERL GTLKNPPKKK MKLMRSEGPD VSVKIELDPQ
GEAAQSANES KTE
