PELP1_MACMU
ID PELP1_MACMU Reviewed; 1130 AA.
AC Q1W1Y5;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 71.
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 Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Khan M., Hadman M., Brann D.;
RT "Cloning and localization of MNAR in monkey brain.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q8IZL8}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q8IZL8}. 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 -!- 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; DQ447200; ABE01044.1; -; mRNA.
DR RefSeq; NP_001035239.1; NM_001040149.1.
DR AlphaFoldDB; Q1W1Y5; -.
DR GeneID; 677854; -.
DR KEGG; mcc:677854; -.
DR CTD; 27043; -.
DR InParanoid; Q1W1Y5; -.
DR Proteomes; UP000006718; 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; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
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 2: Evidence at transcript 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_0000252136"
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 473..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..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 364..368
FT /note="LXXLL motif 8"
FT MOTIF 459..463
FT /note="LXXLL motif 9"
FT MOTIF 579..583
FT /note="LXXLL motif 10"
FT MOTIF 584..588
FT /note="LXXLL motif 11"
FT COMPBIAS 639..697
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..865
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..968
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..1000
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1098
FT /note="Acidic 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 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZL8"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZL8"
FT MOD_RES 488
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZL8"
FT MOD_RES 745
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZL8"
FT MOD_RES 1033
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZL8"
FT MOD_RES 1043
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZL8"
SQ SEQUENCE 1130 AA; 119676 MW; 82593EA7ED5B4E50 CRC64;
MAAAVLSGSS AGSAAGVPGG TGGLSAVNSG PRLRLLLLES VSGLLQPRTG SAVAPVHPPN
RSAPHLPGLM CLLRLHGSVG GAQNLSALGA LVSLSNARLS SIKTRFEGLC LLSLLVGESP
TELFQQHCVS WLRSIQQVLQ TQDPPATMEL AVAVLRDLLR YAAQLPALFR DISMNHLPGL
LTSLLGLRPE CEQSALEGMK ACMTYFPRAC GSLKGKLASF FLSRVDALSP QLQQLACECY
SRLPSLGAGF SQGLKHTESW EQELHSLLAS LHTLLGALYE GAETAPVQNE GPGVEMLLSS
EDGDAHVLLR LRQRFSGLAR CLGLMLSSEF GAPVSVPVQE ILDFICRTLS VSSKNISLHG
DGPLRLLLLP SIHLEALDLL SALILACGSR LLRFGILISR LLPQVLNSWS IGRDSLSPGQ
ERPYSTVRTK VYAGLELWVQ VCGASAGMLQ GGASGEALLT HLLSDISPPA DALKLRSPRG
SPDGSLQTGK PSAPKKLKLD VAEAMAPPSH RKGDSNANSD VCAAALKGLS RTILMCGPLI
KEETHRRLHD LVLPLVMGVQ QGEVLGSSPY TSSRCRRELY CLLLALLLAP SPRCPPPLAC
ALQAFSLGQR EDSLEVSSFC SEALVTCAAL THPRVPPLQP MGPTCPTPAP VPPPEAPSPF
RAPPFHPPGP MPSVGSMPSA GPMPSAGPMP SAGPVPSTRL GPPTTANHLG LSVSGLVSVP
PRLLPGPENH RSGSNEDPIL APSGTPPPTI PPDETFGGRV PRPAFVHYDK EEASDVEISL
ESDSDDSVVI VPEGLPPLPP PPPSGATPPP IAPTGPPTAS PPVPAKEEPE ELPAAPGPLP
PPPPPPPPVP GPVTLPPPQL VPEGTPGGVG PPALEEDLTV ININSSDEEE EEEEEGEEEE
EEEEEEEEDF EEEEEDEEEY FEEEEEEEEE FEEEFEEEEG ELEEEEEEED EEEEEELEEV
EELEFGTAGG EVEEGGPPPP TLPPALPPPE SPPKVQPEPE PEPGLLLEVE EPGAEEEHGA
DTAPTLAPEA LPSQGEVERE EGSPAAGPPP QELVEEEPSA PPTLLEEETE DGGDRVQPPP
ETPAEEEMET ETEAEALQEK EQDDTAAMLA DFIDCPPDDE KPPPPTEPDS
