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Proline-, glutamic acid- and leucine-rich protein 1 (Modulator of non-genomic activity of estrogen receptor)

 PELP1_RAT               Reviewed;        1130 AA.
Q56B11; Q3MIE2;
03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
24-MAY-2005, sequence version 2.
23-MAY-2018, entry version 92.
RecName: Full=Proline-, glutamic acid- and leucine-rich protein 1;
AltName: Full=Modulator of non-genomic activity of estrogen receptor;
Name=Pelp1; Synonyms=Mnar;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Hypothalamus;
PubMed=16141397; DOI=10.1210/en.2005-0276;
Khan M.M., Hadman M., Wakade C., De Sevilla L.M., Dhandapani K.M.,
Mahesh V.B., Vadlamudi R.K., Brann D.W.;
"Cloning, expression, and localization of MNAR/PELP1 in rodent brain:
colocalization in estrogen receptor-alpha- but not in gonadotropin-
releasing hormone-positive neurons.";
Endocrinology 146:5215-5227(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Coactivator of estrogen receptor-mediated transcription
and a corepressor of other nuclear hormone receptors and sequence-
specific transcription factors. Plays a role in estrogen receptor
(ER) genomic activity when present in the nuclear compartment by
activating the ER target genes in a hormonal stimulation dependent
manner. Can facilitate ER non-genomic signaling via SRC and PI3K
interaction in the cytosol. Plays a role in E2-mediated cell cycle
progression by interacting with RB1. May have important functional
implications in ER/growth factor cross-talk. Interacts with
several growth factor signaling components including EGFR and HRS.
Involved in nuclear receptor signaling via its interaction with AR
and NR3C1. May promote tumorigenesis via its interaction with and
modulation of several oncogenes including SRC, PI3K, STAT3 and
EGFR. Plays a role in cancer cell metastasis via its ability to
modulate E2-mediated cytoskeleton changes and cell migration via
its interaction with SRC and PI3K. Functions as the key
stabilizing component of the Five Friends of Methylated CHTOP
(5FMC) complex; the 5FMC complex is recruited to ZNF148 by
methylated CHTOP, leading to desumoylation of ZNF148 and
subsequent transactivation of ZNF148 target genes. Component of
the PELP1 complex involved in the nucleolar steps of 28S rRNA
maturation and the subsequent nucleoplasmic transit of the pre-60S
ribosomal subunit. Regulates pre-60S association of the critical
remodeling factor MDN1. {ECO:0000250|UniProtKB:Q8IZL8}.
-!- SUBUNIT: Interacts with HRS, RXRA, SUMO2, HDAC2, RB1 and STAT3.
Interacts with PI3K, SRC and EGFR in cytoplasm. Interacts with
ESR1 and ESR2 and this interaction is enhanced by 17-beta-
estradiol. Interacts with CREBBP, EP300, AR and NR3C1 in a ligand-
dependent manner. Forms two complexes in the presence of 17-beta-
estradiol; one with SRC and ESR1 and another with LCK and ESR1.
Interacts with histone H1 and H3 with a greater affinity for H1.
Component of some MLL1/MLL complex, at least composed of the core
components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well
as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C,
KANSL1, LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31,
RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7,
TAF9 and TEX10. Core component of the 5FMC complex, at least
composed of PELP1, LAS1L, TEX10, WDR18 and SENP3; the complex
interacts with methylated CHTOP and ZNF148. Interacts with NOL9.
Interacts with BCAS3. Component of the PELP1 complex, composed of
at least PELP1, TEX10 and WDR18. The complex interacts (via PELP1)
with MDN1 (via its hexameric AAA ATPase ring) and the pre-60S
ribosome particles. {ECO:0000250|UniProtKB:Q8IZL8}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000250|UniProtKB:Q8IZL8}. Nucleus, nucleoplasm
{ECO:0000250|UniProtKB:Q8IZL8}. Nucleus
{ECO:0000269|PubMed:16141397}. Cytoplasm
{ECO:0000269|PubMed:16141397}. Note=Mainly found in the
nucleoplasm, with low levels detected in the cytoplasm. Also found
associated with the plasma membrane.
{ECO:0000250|UniProtKB:Q8IZL8}.
-!- TISSUE SPECIFICITY: Expressed in ovary, uterus, muscle and many
regions of brain including hypothalamus, cortex, hippocampus and
pituitary. Expressed in neurin and glia cells.
{ECO:0000269|PubMed:16141397}.
-!- DOMAIN: The Glu-rich region mediates histones interaction.
{ECO:0000250}.
-!- DOMAIN: The Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are required for
the association with nuclear receptor ESR1. {ECO:0000250}.
-!- PTM: Transiently sumoylated, preferentially conjugated to SUMO2 or
SUMO3. Sumoylation causes nucleolar exclusion of PELP1 and
promotes the recruitment of MDN1 to pre-60S particles.
Desumoylation by SUMO isopeptidase SENP3 is needed to release both
PELP1 and MDN1 from pre-ribosomes. {ECO:0000250|UniProtKB:Q8IZL8}.
-!- SIMILARITY: Belongs to the RIX1/PELP1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY970831; AAX81519.2; -; mRNA.
EMBL; BC101890; AAI01891.1; -; mRNA.
RefSeq; NP_001019441.2; NM_001024270.2.
UniGene; Rn.11628; -.
IntAct; Q56B11; 3.
MINT; Q56B11; -.
STRING; 10116.ENSRNOP00000026102; -.
iPTMnet; Q56B11; -.
PhosphoSitePlus; Q56B11; -.
PaxDb; Q56B11; -.
PRIDE; Q56B11; -.
GeneID; 360552; -.
KEGG; rno:360552; -.
UCSC; RGD:1306320; rat.
CTD; 27043; -.
RGD; 1306320; Pelp1.
eggNOG; ENOG410IJ4S; Eukaryota.
eggNOG; ENOG4110K7C; LUCA.
HOGENOM; HOG000115494; -.
HOVERGEN; HBG080634; -.
InParanoid; Q56B11; -.
KO; K16913; -.
PhylomeDB; Q56B11; -.
TreeFam; TF331332; -.
PRO; PR:Q56B11; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0035327; C:transcriptionally active chromatin; ISS:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0071391; P:cellular response to estrogen stimulus; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR031193; PELP1.
InterPro; IPR012583; RIX1_N.
InterPro; IPR012980; Uncharacterised_NUC202.
PANTHER; PTHR45115; PTHR45115; 1.
Pfam; PF08166; NUC202; 2.
Pfam; PF08167; RIX1; 1.
SUPFAM; SSF48371; SSF48371; 3.
1: Evidence at protein level;
Acetylation; Activator; Complete proteome; Cytoplasm; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q8IZL8}.
CHAIN 2 1130 Proline-, glutamic acid- and leucine-rich
protein 1.
/FTId=PRO_0000252138.
MOTIF 33 37 LXXLL motif 1.
MOTIF 69 73 LXXLL motif 2.
MOTIF 111 115 LXXLL motif 3.
MOTIF 155 159 LXXLL motif 4.
MOTIF 177 181 LXXLL motif 5.
MOTIF 264 268 LXXLL motif 6.
MOTIF 271 275 LXXLL motif 7.
MOTIF 365 369 LXXLL motif 8.
MOTIF 460 464 LXXLL motif 9.
MOTIF 580 584 LXXLL motif 10.
MOTIF 585 589 LXXLL motif 11.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q8IZL8}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000250|UniProtKB:Q9DBD5}.
MOD_RES 478 478 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IZL8}.
MOD_RES 482 482 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IZL8}.
MOD_RES 757 757 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8IZL8}.
MOD_RES 761 761 Phosphoserine.
{ECO:0000250|UniProtKB:Q9DBD5}.
MOD_RES 1034 1034 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IZL8}.
MOD_RES 1044 1044 Phosphoserine.
{ECO:0000250|UniProtKB:Q8IZL8}.
CONFLICT 190 190 Q -> E (in Ref. 2; AAI01891).
{ECO:0000305}.
CONFLICT 519 519 D -> N (in Ref. 2; AAI01891).
{ECO:0000305}.
CONFLICT 824 824 I -> T (in Ref. 2; AAI01891).
{ECO:0000305}.
CONFLICT 913 913 V -> E (in Ref. 2; AAI01891).
{ECO:0000305}.
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


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