PELP1_XENLA
ID PELP1_XENLA Reviewed; 1012 AA.
AC Q58HI1;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 64.
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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=15831520; DOI=10.1210/me.2004-0531;
RA Haas D., White S.N., Lutz L.B., Rasar M., Hammes S.R.;
RT "The modulator of nongenomic actions of the estrogen receptor (MNAR)
RT regulates transcription-independent androgen receptor-mediated signaling:
RT evidence that MNAR participates in G protein-regulated meiosis in Xenopus
RT laevis oocytes.";
RL Mol. Endocrinol. 19:2035-2046(2005).
CC -!- FUNCTION: Coactivator of estrogen receptor-mediated transcription and a
CC corepressor of other nuclear hormone receptors and sequence-specific
CC transcription factors. Regulates oocyte maturation. Enhances androgen
CC receptor (AR)-mediated transcription in a SRC-dependent manner.
CC {ECO:0000269|PubMed:15831520}.
CC -!- SUBUNIT: Component of some MLL1/MLL complex (By similarity). Forms a
CC signaling complex with SRC and estrogen receptors. {ECO:0000250,
CC ECO:0000269|PubMed:15831520}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in oocyte. {ECO:0000269|PubMed:15831520}.
CC -!- DOMAIN: The Glu-rich region mediates histones interaction.
CC {ECO:0000250}.
CC -!- DOMAIN: The Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are required for the
CC association with nuclear receptor ESR1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RIX1/PELP1 family. {ECO:0000305}.
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DR EMBL; AY949838; AAX49552.1; -; mRNA.
DR RefSeq; NP_001089105.1; NM_001095636.1.
DR AlphaFoldDB; Q58HI1; -.
DR IntAct; Q58HI1; 1.
DR MINT; Q58HI1; -.
DR GeneID; 733329; -.
DR KEGG; xla:733329; -.
DR CTD; 733329; -.
DR Xenbase; XB-GENE-866388; pelp1.L.
DR OrthoDB; 427039at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 733329; Expressed in egg cell and 20 other tissues.
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: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 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 Activator; Cytoplasm; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription.
FT CHAIN 1..1012
FT /note="Proline-, glutamic acid- and leucine-rich protein 1"
FT /id="PRO_0000252139"
FT REGION 586..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 21..25
FT /note="LXXLL motif 1"
FT MOTIF 63..67
FT /note="LXXLL motif 2"
FT MOTIF 107..111
FT /note="LXXLL motif 3"
FT MOTIF 129..133
FT /note="LXXLL motif 4"
FT MOTIF 216..220
FT /note="LXXLL motif 5"
FT MOTIF 223..227
FT /note="LXXLL motif 6"
FT MOTIF 317..321
FT /note="LXXLL motif 7"
FT MOTIF 415..419
FT /note="LXXLL motif 8"
FT MOTIF 524..528
FT /note="LXXLL motif 9"
FT MOTIF 529..533
FT /note="LXXLL motif 10"
FT COMPBIAS 610..647
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..755
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..846
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..879
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..939
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..959
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..975
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1012 AA; 110459 MW; 76B54E60A2034BD3 CRC64;
MEVTIAGILE RDLSEGELAE AIRGLREHGA FRGEGLPAAM SGLLSSCNSR LTSASSRIEG
LSLLALAVEE SPTDVFVQHC VSWLRSLLQI IQSQDPPRVV SLAVFVLRSL LAHSSALPEL
SREISTNHIP GLLTSLLGLR RQCLVPALEG IRSCFLSYPR ACGSLRGKLT AFLLSLLDAE
NQQIQEVACQ CYSLLPSLGS GFSQGIKHTE NWERQIQSVI CSLHSVFLQL YQGSETDTAR
YEGSGTELEF PSVEDDGTHG VLQLARRFTA LGQCMRLLLR EQFPAPVRVP VSDILSLVCR
VVNVSPKNLS WHGEESLKLL LLPRVHSSIL EILEATIIAC GPRLLPFSAV ICRLFPQLLL
SWAAVKGITG IPSGQERPYS SLRCSVYRVL ETWVTTCGIS SGVLQGPMHH SDILLANLLS
DITPPTDAIK MSTFVQLGAK KQKVSEVGDD DFQSHRKRDN TANVELCAAA LKGLCCVILH
CGSVIKEDVH RRLQELSIPL LLRLQQGSDQ WLGPYISSDC RKELYRLLLC LTLTPNPKLP
APLHCAIRIF RGGTTEESLQ VSRFSTEALA ICRILIHPRV PSLQRPLPHL APRPSVQSDA
PTLRPPAALS TFPAMPPANH LPPRPTVPAM STEPPIPAAV PSPPPEESFG EKPRRAVFIH
FDKEEPSDVE ISLESDSDDS VVIVPEGLFA KSDSKPEPSP PAVKPPTEEV TEQVAPSAVP
SSSTAAPPPP PPPPAPPVCA GPSSAPVPIA EAPPPPQQEV DTVININSSD DEEDGEEDEE
EGLYDDEDEE DYYDEEEDED LEGLEEDDYD YEEDEEGITE EEEEDLEEEG EDDEEEVEDE
ECLMPDEMQI GSEAEEIPDG IETSSLHEGE LEEGPPRLSP VQEDEAVDTG LLMLVESEDR
EPSGEAPGEG LPESDLTRSP PQPPVLTPPS PPDEPPPMEE SDVPPLEEPD LEVAPVAEEP
VEETEEKKPE EVTVEKPEPE PEEEEQIADA DAMLADFVDC PPDDDKLPEP CT
