LRIF1_RAT
ID LRIF1_RAT Reviewed; 748 AA.
AC Q499M7;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Ligand-dependent nuclear receptor-interacting factor 1;
GN Name=Lrif1;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 476-748.
RC TISSUE=Prostate;
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: Together with SMCHD1, involved in chromosome X inactivation
CC in females by promoting the compaction of heterochromatin. Also able to
CC repress the ligand-induced transcriptional activity of retinoic acid
CC receptor alpha (RARA), possibly through direct recruitment of histone
CC deacetylases. {ECO:0000250|UniProtKB:Q5T3J3}.
CC -!- SUBUNIT: Interacts with RARA. Interacts with SMCHD1; leading to
CC recruitment to inactivated chromosome X in females. Interacts (via
CC PxVxL motif) with HP1 (CBX1/HP1-beta, CBX3/HP1-gamma and CBX5/HP1-
CC alpha). {ECO:0000250|UniProtKB:Q5T3J3}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q5T3J3}.
CC Nucleus matrix {ECO:0000250|UniProtKB:Q5T3J3}. Note=Localizes to Barr
CC body; recruited by SMCHD1. {ECO:0000250|UniProtKB:Q5T3J3}.
CC -!- DOMAIN: The Pro-Xaa-Val-Xaa-Leu (PxVxL) motif mediates interaction with
CC HP1 (CBX1/HP1-beta, CBX3/HP1-gamma and CBX5/HP1-alpha).
CC {ECO:0000250|UniProtKB:Q5T3J3}.
CC -!- SIMILARITY: Belongs to the LRIF1 family. {ECO:0000305}.
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DR EMBL; AABR03012529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC099834; AAH99834.1; -; mRNA.
DR AlphaFoldDB; Q499M7; -.
DR SMR; Q499M7; -.
DR STRING; 10116.ENSRNOP00000024036; -.
DR PaxDb; Q499M7; -.
DR UCSC; RGD:1306520; rat.
DR RGD; 1306520; Lrif1.
DR eggNOG; ENOG502QU1A; Eukaryota.
DR InParanoid; Q499M7; -.
DR PhylomeDB; Q499M7; -.
DR PRO; PR:Q499M7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0001740; C:Barr body; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; IEA:InterPro.
DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR026191; LRIF1.
DR PANTHER; PTHR16131; PTHR16131; 1.
DR Pfam; PF15741; LRIF1; 1.
PE 2: Evidence at transcript level;
KW Chromosome; Coiled coil; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..748
FT /note="Ligand-dependent nuclear receptor-interacting factor
FT 1"
FT /id="PRO_0000250688"
FT REGION 416..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 715..748
FT /evidence="ECO:0000255"
FT MOTIF 559..563
FT /note="PxVxL motif"
FT /evidence="ECO:0000250|UniProtKB:Q5T3J3"
FT MOTIF 604..607
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q5T3J3"
FT MOTIF 618..621
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q5T3J3"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T3J3"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T3J3"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T3J3"
FT MOD_RES 710
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5T3J3"
FT CROSSLNK 436
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5T3J3"
FT CROSSLNK 583
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5T3J3"
FT CROSSLNK 680
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5T3J3"
SQ SEQUENCE 748 AA; 82669 MW; A8B2E898770D896A CRC64;
MSNRLQTVFL KTAEEKSGSH CISGCMYQVV PTIGTDGKKL LQLLPIPKSS GNLIPVVQSP
VMSHGLKGNT EKPVQVTFQT QISSSSTSAS VQLPVLQPAN TTKYFLTGTI DTSGKDRVTS
MGTGNFTPPI SNTQNHGVKI HRLTRQTFTI PPSTQNDSSY FIVNTPSLPA NVNSSTLPSG
PPLTIPAHAE VKPVLASPLP PLVQQKILGT VTTSTSGTVE ASQIPAVFYV SPVNSVKIIV
DKKTQNIYHK PVTFSTSQIP PNVATKTQLN SGQHPQAAPV NLIFQEYLQP GIPCLVPVKS
SNNVPSKVFN TFVDRKTLGD NTVGTPLLST NSSSRTQSIS VPIKDDGLIM FNGKVLLNKK
GTYGLPSKID QQNSVSSDIP LKDSSQVVSS SLVTEISREV LSSVLVKSKS FQLKTKSLSN
SQPAPMAHIK PEKSEKVERP SFSVTSPHTT NQSTHCLKQS KIVFINPVFS DGFRTGQNTP
RKENLIQNIR SSVDAATVTS QQCVFRDQEP QTQYEMASIL KKDIQERSNK KYSQGNHTKA
SYLKNDAEFK KIFGLTKDLR VCLTRIPDHL SSTKSFDSFN NLKSSSYKDA NVVMKEEKKQ
SFSKKRNAKP MKKMDYTKRR KIENASDMVM NVMNGTDVAN SQLLSSILPI SDIAQHNIIT
SHSTTREDKR TETEHCCHEK QEKGTLSSST SFEQSNYFNK NYTEDIFPVT PPELEETIRD
EKIRRLKQIL REKEAALEEL RKKMHQKQ