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   24-JAN-2024, entry version 126.
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; 10090-ENSMUSP00000067603; -.
DR   ProteomicsDB; 286181; -.
DR   Antibodypedia; 30781; 265 antibodies from 26 providers.
DR   DNASU; 212391; -.
DR   Ensembl; ENSMUST00000067795.13; ENSMUSP00000067603.6; ENSMUSG00000025019.18.
DR   Ensembl; ENSMUST00000163929.2; ENSMUSP00000126441.2; ENSMUSG00000025019.18.
DR   GeneID; 212391; -.
DR   KEGG; mmu:212391; -.
DR   UCSC; uc008hly.1; mouse.
DR   AGR; MGI:2443930; -.
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   PhylomeDB; Q6ZPI3; -.
DR   TreeFam; TF319589; -.
DR   BioGRID-ORCS; 212391; 2 hits in 77 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 242 other cell types or tissues.
DR   ExpressionAtlas; Q6ZPI3; baseline and differential.
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:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IDA:ARUK-UCL.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR007889; HTH_Psq.
DR   PANTHER; PTHR21545:SF14; LIGAND-DEPENDENT COREPRESSOR; 1.
DR   PANTHER; PTHR21545; TRANSCRIPTION FACTOR MLR1/2; 1.
DR   Pfam; PF05225; HTH_psq; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   PROSITE; PS50960; HTH_PSQ; 1.
DR   Genevisible; Q6ZPI3; MM.
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
//