PELP1_RAT
ID PELP1_RAT Reviewed; 1130 AA.
AC Q56B11; Q3MIE2;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Proline-, glutamic acid- and leucine-rich protein 1;
DE AltName: Full=Modulator of non-genomic activity of estrogen receptor;
GN Name=Pelp1; Synonyms=Mnar;
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 [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Hypothalamus;
RX PubMed=16141397; DOI=10.1210/en.2005-0276;
RA Khan M.M., Hadman M., Wakade C., De Sevilla L.M., Dhandapani K.M.,
RA Mahesh V.B., Vadlamudi R.K., Brann D.W.;
RT "Cloning, expression, and localization of MNAR/PELP1 in rodent brain:
RT colocalization in estrogen receptor-alpha- but not in gonadotropin-
RT releasing hormone-positive neurons.";
RL Endocrinology 146:5215-5227(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Coactivator of estrogen receptor-mediated transcription and a
CC corepressor of other nuclear hormone receptors and sequence-specific
CC transcription factors. Plays a role in estrogen receptor (ER) genomic
CC activity when present in the nuclear compartment by activating the ER
CC target genes in a hormonal stimulation dependent manner. Can facilitate
CC ER non-genomic signaling via SRC and PI3K interaction in the cytosol.
CC Plays a role in E2-mediated cell cycle progression by interacting with
CC RB1. May have important functional implications in ER/growth factor
CC cross-talk. Interacts with several growth factor signaling components
CC including EGFR and HRS. Functions as the key stabilizing component of
CC the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex
CC is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of
CC ZNF148 and subsequent transactivation of ZNF148 target genes. Component
CC of the PELP1 complex involved in the nucleolar steps of 28S rRNA
CC maturation and the subsequent nucleoplasmic transit of the pre-60S
CC ribosomal subunit. Regulates pre-60S association of the critical
CC remodeling factor MDN1. {ECO:0000250|UniProtKB:Q8IZL8}.
CC -!- SUBUNIT: Interacts with HRS, RXRA, SUMO2, HDAC2, RB1 and STAT3.
CC Interacts with PI3K, SRC and EGFR in cytoplasm. Interacts with ESR1,
CC the interaction is enhanced by 17-beta-estradiol; the interaction
CC increases ESR1 transcriptional activity (By similarity). Interacts with
CC CREBBP and EP300 in a ligand-dependent manner (By similarity). Forms
CC two complexes in the presence of 17-beta-estradiol; one with SRC and
CC ESR1 and another with LCK and ESR1. Interacts with histone H1 and H3
CC with a greater affinity for H1. Component of some MLL1/MLL complex, at
CC least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1,
CC WDR5 and RBBP5, as well as the facultative components BAP18, CHD8,
CC E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1,
CC PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4,
CC TAF6, TAF7, TAF9 and TEX10. Core component of the 5FMC complex, at
CC least composed of PELP1, LAS1L, TEX10, WDR18 and SENP3; the complex
CC interacts with methylated CHTOP and ZNF148. Interacts with NOL9.
CC Interacts with BCAS3. Component of the PELP1 complex, composed of at
CC least PELP1, TEX10 and WDR18. The complex interacts (via PELP1) with
CC MDN1 (via its hexameric AAA ATPase ring) and the pre-60S ribosome
CC particles. {ECO:0000250|UniProtKB:Q8IZL8}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q8IZL8}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q8IZL8}. Nucleus {ECO:0000269|PubMed:16141397}.
CC Cytoplasm {ECO:0000269|PubMed:16141397}. Note=Mainly found in the
CC nucleoplasm, with low levels detected in the cytoplasm. Also found
CC associated with the plasma membrane. {ECO:0000250|UniProtKB:Q8IZL8}.
CC -!- TISSUE SPECIFICITY: Expressed in ovary, uterus, muscle and many regions
CC of brain including hypothalamus, cortex, hippocampus and pituitary.
CC Expressed in neurin and glia cells. {ECO:0000269|PubMed:16141397}.
CC -!- DOMAIN: The Glu-rich region mediates histones interaction.
CC {ECO:0000250|UniProtKB:Q8IZL8}.
CC -!- DOMAIN: The Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are required for the
CC association with nuclear receptor ESR1. {ECO:0000250|UniProtKB:Q8IZL8}.
CC -!- PTM: Transiently sumoylated, preferentially conjugated to SUMO2 or
CC SUMO3. Sumoylation causes nucleolar exclusion of PELP1 and promotes the
CC recruitment of MDN1 to pre-60S particles. Desumoylation by SUMO
CC isopeptidase SENP3 is needed to release both PELP1 and MDN1 from pre-
CC ribosomes. {ECO:0000250|UniProtKB:Q8IZL8}.
CC -!- SIMILARITY: Belongs to the RIX1/PELP1 family. {ECO:0000305}.
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DR EMBL; AY970831; AAX81519.2; -; mRNA.
DR EMBL; BC101890; AAI01891.1; -; mRNA.
DR RefSeq; NP_001019441.2; NM_001024270.2.
DR AlphaFoldDB; Q56B11; -.
DR BioGRID; 262017; 1.
DR IntAct; Q56B11; 3.
DR MINT; Q56B11; -.
DR STRING; 10116.ENSRNOP00000026102; -.
DR iPTMnet; Q56B11; -.
DR PhosphoSitePlus; Q56B11; -.
DR jPOST; Q56B11; -.
DR PaxDb; Q56B11; -.
DR PRIDE; Q56B11; -.
DR GeneID; 360552; -.
DR KEGG; rno:360552; -.
DR UCSC; RGD:1306320; rat.
DR CTD; 27043; -.
DR RGD; 1306320; Pelp1.
DR eggNOG; ENOG502QQE7; Eukaryota.
DR InParanoid; Q56B11; -.
DR OrthoDB; 427039at2759; -.
DR PhylomeDB; Q56B11; -.
DR TreeFam; TF331332; -.
DR Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q56B11; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR GO; GO:0032183; F:SUMO binding; ISO:RGD.
DR GO; GO:0071391; P:cellular response to estrogen stimulus; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR012583; RIX1_N.
DR InterPro; IPR012980; Uncharacterised_NUC202.
DR Pfam; PF08166; NUC202; 2.
DR Pfam; PF08167; RIX1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8IZL8"
FT CHAIN 2..1130
FT /note="Proline-, glutamic acid- and leucine-rich protein 1"
FT /id="PRO_0000252138"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..80
FT /note="Required for modulation of ESR1 transcriptional
FT activity"
FT /evidence="ECO:0000250|UniProtKB:Q8IZL8"
FT REGION 121..189
FT /note="Required for modulation of ESR1 transcriptional
FT activity"
FT /evidence="ECO:0000250|UniProtKB:Q8IZL8"
FT REGION 639..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 33..37
FT /note="LXXLL motif 1"
FT MOTIF 69..73
FT /note="LXXLL motif 2"
FT MOTIF 111..115
FT /note="LXXLL motif 3"
FT MOTIF 155..159
FT /note="LXXLL motif 4"
FT MOTIF 177..181
FT /note="LXXLL motif 5"
FT MOTIF 264..268
FT /note="LXXLL motif 6"
FT MOTIF 271..275
FT /note="LXXLL motif 7"
FT MOTIF 365..369
FT /note="LXXLL motif 8"
FT MOTIF 460..464
FT /note="LXXLL motif 9"
FT MOTIF 580..584
FT /note="LXXLL motif 10"
FT MOTIF 585..589
FT /note="LXXLL motif 11"
FT COMPBIAS 640..660
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..688
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..833
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..874
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..971
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..997
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZL8"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBD5"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZL8"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZL8"
FT MOD_RES 757
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZL8"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBD5"
FT MOD_RES 1034
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZL8"
FT MOD_RES 1044
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZL8"
FT CONFLICT 190
FT /note="Q -> E (in Ref. 2; AAI01891)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="D -> N (in Ref. 2; AAI01891)"
FT /evidence="ECO:0000305"
FT CONFLICT 824
FT /note="I -> T (in Ref. 2; AAI01891)"
FT /evidence="ECO:0000305"
FT CONFLICT 913
FT /note="V -> E (in Ref. 2; AAI01891)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1130 AA; 119139 MW; A5216F56C80D0BE8 CRC64;
MAAAVLSGPT TGSPAGAPGG PGGLSAAGSG PRLRLLLLES VSGLLQPRTG SHVAPVHPPI
QWAPYLPGLM CLLRLHGTAG GAQNLSALGA LVNLSNAHLS SIKTRFEGLC LLSLLVGESP
TELFQQHCVS WLRSIQQVLQ SQDSPPTMEL AVAILRDLLR YASQLPTLFR DISTNHLPGL
LTSLLGLRPQ CEQSALEGMK ACVTYFPRAC GFLKGKLASF FLSRLDSLNP QLQQLACECY
SRLPSLGAGF SQGLKHTENW EQELHSLLTS LHSLLGSLFE ETETAPVQSE GPGVEMLLSP
SEDDNTHVLL QLWQRFSGLA RCLGLMLSSE FGAPVSVPVQ EILDLICRIL GISSKNINLL
GDGPLRLLLL PSLHLEALDL LSALILACGG RLLRFGALIS RLLPQVLNTW STGRDALAPG
QERPYSTIRT KVYAILELWV QVCGASAGML QGGASGEALL THLLSDISPP ADALKLCSTR
GSSDGGLQSG KPSAPKKLKL DMGEALAPPS QRKGDRNADS DVCAAALRGL SRTILMCGPL
VKEETHRRLH DLVLPLVMSV QQGEVLGSSP YNSSCCRLEL YRLLLALLLA PSPRCPPPLS
CALKAFSLGQ WEDSLEVSSF CSEALVTCSA LTHPRVPPLQ SSGPACPTPA PVPPPEAPSS
FRAPAFHTPG PMPSIGALPS PGPVPSAGPI PTVGSMSSAG SVPSTGPVPS RPGPPATANH
LGLAVPGLVS VPPRLLPGSE NHRAGSGEDP VLAPSGTPPP SIPPDETFGG RVPRPAFVHY
DKEEASDVEI SLESDSDDSV VIVPEGLPSL PPPPSGTPPP VAPIGPPTAS PPVPAKEDSE
ELPATPGPLP PPPPPPPPVS GPVTLPPPQL VPEGTPGGGG PTAMEEDLTV ININSSDEEE
EEEEEEEEED EDVEEEDFEE EEEDEEEYFE EEEEEEEFEE EFEEEEGELE EEEEEEEEEL
EEVEDVEFGS AGEVEEGGPP PPTLPPALPP TDSPKVQPEA EPEPGLLLEV EEPGAEDGPG
PEIAPTLAPE VLPSQEEVER EGESPTAGPP QELVEEESSA PPTLLEEGTE GGGDKVPPPP
ETPAQEEMET ETEASAPQGK EQDDTAAMLA DFIDCPPDDE KPPPATEPDS
