PELP1_MOUSE
ID PELP1_MOUSE Reviewed; 1123 AA.
AC Q9DBD5; Q5F2E2; Q6PEM0; Q91YM9;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 153.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N;
RC TISSUE=Embryonic brain, Liver, and Mammary gland;
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 [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11481323; DOI=10.1074/jbc.m103783200;
RA Vadlamudi R.K., Wang R.-A., Mazumdar A., Kim Y.-S., Shin J., Sahin A.,
RA Kumar R.;
RT "Molecular cloning and characterization of PELP1, a novel human coregulator
RT of estrogen receptor alpha.";
RL J. Biol. Chem. 276:38272-38279(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-13, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-755, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, IDENTIFICATION IN THE 5FMC COMPLEX, INTERACTION OF THE 5FMC
RP COMPLEX WITH CHTOP AND ZNF148, INTERACTION WITH NOL9, AND SUBCELLULAR
RP LOCATION.
RX PubMed=22872859; DOI=10.1074/mcp.m112.017194;
RA Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J.,
RA Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.;
RT "Five friends of methylated chromatin target of protein-arginine-
RT methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation
RT to desumoylation.";
RL Mol. Cell. Proteomics 11:1263-1273(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
CC (PubMed:22872859). Component of the PELP1 complex involved in the
CC nucleolar steps of 28S rRNA maturation and the subsequent nucleoplasmic
CC transit of the pre-60S ribosomal subunit. Regulates pre-60S association
CC of the critical remodeling factor MDN1 (By similarity).
CC {ECO:0000250|UniProtKB:Q8IZL8, ECO:0000269|PubMed:22872859}.
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 (By similarity). Core component of the 5FMC
CC complex, at least composed of PELP1, LAS1L, TEX10, WDR18 and SENP3; the
CC complex interacts with methylated CHTOP and ZNF148. Interacts with NOL9
CC (PubMed:22872859). Interacts with BCAS3 (By similarity). Component of
CC the PELP1 complex, composed of at least PELP1, TEX10 and WDR18. The
CC complex interacts (via PELP1) with MDN1 (via its hexameric AAA ATPase
CC ring) and the pre-60S ribosome particles (By similarity).
CC {ECO:0000250|UniProtKB:Q8IZL8, ECO:0000269|PubMed:22872859}.
CC -!- INTERACTION:
CC Q9DBD5; P12813: Nr4a1; NbExp=3; IntAct=EBI-6909114, EBI-10896863;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q8IZL8}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:22872859}. Nucleus {ECO:0000269|PubMed:11481323,
CC ECO:0000269|PubMed:22872859}. Cytoplasm {ECO:0000269|PubMed:11481323,
CC ECO:0000269|PubMed:22872859}. Note=Mainly found in the nucleoplasm,
CC with low levels detected in the cytoplasm. Also found associated with
CC the plasma membrane. {ECO:0000269|PubMed:22872859}.
CC -!- TISSUE SPECIFICITY: Widely expressed with high levels in testis, ovary,
CC uterus and pituitary gland. {ECO:0000269|PubMed:11481323}.
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; AK005027; BAB23754.1; -; mRNA.
DR EMBL; AL596096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016444; AAH16444.1; -; mRNA.
DR EMBL; BC057987; AAH57987.1; -; mRNA.
DR EMBL; BC090620; AAH90620.1; -; mRNA.
DR CCDS; CCDS24945.1; -.
DR RefSeq; NP_083507.3; NM_029231.4.
DR AlphaFoldDB; Q9DBD5; -.
DR BioGRID; 217350; 7.
DR IntAct; Q9DBD5; 3.
DR STRING; 10090.ENSMUSP00000019065; -.
DR iPTMnet; Q9DBD5; -.
DR PhosphoSitePlus; Q9DBD5; -.
DR EPD; Q9DBD5; -.
DR jPOST; Q9DBD5; -.
DR MaxQB; Q9DBD5; -.
DR PaxDb; Q9DBD5; -.
DR PeptideAtlas; Q9DBD5; -.
DR PRIDE; Q9DBD5; -.
DR ProteomicsDB; 289347; -.
DR Antibodypedia; 23315; 286 antibodies from 33 providers.
DR DNASU; 75273; -.
DR Ensembl; ENSMUST00000019065; ENSMUSP00000019065; ENSMUSG00000018921.
DR GeneID; 75273; -.
DR KEGG; mmu:75273; -.
DR UCSC; uc007jup.2; mouse.
DR CTD; 27043; -.
DR MGI; MGI:1922523; Pelp1.
DR VEuPathDB; HostDB:ENSMUSG00000018921; -.
DR eggNOG; ENOG502QQE7; Eukaryota.
DR GeneTree; ENSGT00730000111225; -.
DR HOGENOM; CLU_007599_0_0_1; -.
DR InParanoid; Q9DBD5; -.
DR OMA; GMKACMI; -.
DR OrthoDB; 427039at2759; -.
DR PhylomeDB; Q9DBD5; -.
DR TreeFam; TF331332; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 75273; 28 hits in 74 CRISPR screens.
DR ChiTaRS; Pelp1; mouse.
DR PRO; PR:Q9DBD5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9DBD5; protein.
DR Bgee; ENSMUSG00000018921; Expressed in ear vesicle and 254 other tissues.
DR ExpressionAtlas; Q9DBD5; baseline and differential.
DR Genevisible; Q9DBD5; MM.
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; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0032183; F:SUMO binding; ISO:MGI.
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:0007744|PubMed:19131326"
FT CHAIN 2..1123
FT /note="Proline-, glutamic acid- and leucine-rich protein 1"
FT /id="PRO_0000252137"
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..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..1123
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..678
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..828
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..869
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..966
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..992
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
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 751
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZL8"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1029
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZL8"
FT MOD_RES 1039
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZL8"
FT CONFLICT 566
FT /note="L -> P (in Ref. 3; AAH16444/AAH57987)"
FT /evidence="ECO:0000305"
FT CONFLICT 864
FT /note="Q -> L (in Ref. 1; BAB23754)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1123 AA; 118069 MW; 571BF1BD6A705067 CRC64;
MAAAVLSGAS AGSPAGAPGG PGGLSAVGSG PRLRLLLLES ISGLLQPRTA SPVAPVHPPI
QWAPHLPGLM CLLRLHGTAG GAQNLSALGA LVNLSNAHLG SIKTRFEGLC LLSLLIGESP
TELFQQHCVS WLRSIQQVLQ SQDSPSTMEL AVAVLRDLLR HASQLPTLFR DISTNHLPGL
LTSLLGLRPE CEQSALEGMK ACVTYFPRAC GSLKGKLASF FLSRLDSLNP QLQQLACECY
SRLPSLGAGF SQGLKHTENW EQELHSLLTS LHSLLGSLFE ETEPAPVQSE GPGIEMLLSH
SEDGNTHVLL QLRQRFSGLA RCLGLMLSSE FGAPVSVPVQ EILDLICRIL GISSKNINLL
GDGPLRLLLL PSLHLEALDL LSALILACGS RLLRFGALIS RLLPQVLNAW STGRDTLAPG
QERPYSTIRT KVYAILELWV QVCGASAGML QGGASGEALL THLLSDISPP ADALKLCSTR
GSSDGGLQSG KPSAPKKLKL DMGEALAPPS QRKGDRNANS DVCAAALRGL SRTILMCGPL
IKEETHRRLH DLVLPLVMSV QQGEVLGSSP YNSSCCRLGL YRLLLALLLA PSPRCPPPLA
CALKAFSLGQ WEDSLEVSSF CSEALVTCAA LTHPRVPPLQ SSGPACPTPA PVPPPEAPSS
FRAPAFHPPG PMPSIGAVPS TGPLPSAGPI PTVGSMASTG QVPSRPGPPA TANHLGLSVP
GLVSVPPRLL PGPENHRAGS GEDPVLAPSG TPPPSIPPDE TFGGRVPRPA FVHYDKEEAS
DVEISLESDS DDSVVIVPEG LPSLPPAPPS GTPPPAAPAG PPTASPPVPA KEDSEELPAT
PGPPPPPPPP PPPASGPVTL PPPQLVPEGT PGGGGPTAME EDLTVININS SDEEEEEEEE
EEEEDEDEEE EDFEEEEEDE EEYFEEEEEE EEFEEEFEEE EGELEEEEEE EEEELDEVED
VEFGSAGEVE EGGPPPPTLP PALPPSDSPK VQPEAEPEPG LLLEVEEPGP EEVPGPETAP
TLAPEVLPSQ EEGEQEVGSP AAGPPQELVE ESSAPPALLE EGTEGGGDKV PPPPETPAEE
METEAEVPAP QEKEQDDTAA MLADFIDCPP DDEKPPPATE PDS
