HNRL1_MOUSE
ID HNRL1_MOUSE Reviewed; 859 AA.
AC Q8VDM6; Q3U201; Q3UPB0; Q6AZA7; Q8BY45; Q8K365;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein U-like protein 1;
GN Name=Hnrnpul1; Synonyms=Hnrpul1;
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] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Spleen, and Thymus;
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 MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Embryo, and Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195 AND THR-210, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-639; ARG-645; ARG-659 AND
RP ARG-664, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Acts as a basic transcriptional regulator. Represses basic
CC transcription driven by several virus and cellular promoters. When
CC associated with BRD7, activates transcription of glucocorticoid-
CC responsive promoter in the absence of ligand-stimulation. Also plays a
CC role in mRNA processing and transport. Binds avidly to poly(G) and
CC poly(C) RNA homopolymers in vitro (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with BRD7, PRMT2, TP53 and NXF1. Associates with
CC histones and BRD7 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8VDM6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VDM6-2; Sequence=VSP_017553;
CC Name=3;
CC IsoId=Q8VDM6-3; Sequence=VSP_017554, VSP_017555;
CC -!- DOMAIN: The RGG-box domain is methylated. {ECO:0000250}.
CC -!- PTM: Methylated. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27844.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK042090; BAC31161.1; -; mRNA.
DR EMBL; AK143666; BAE25486.1; -; mRNA.
DR EMBL; AK155604; BAE33342.1; -; mRNA.
DR EMBL; BC021506; AAH21506.1; -; mRNA.
DR EMBL; BC027844; AAH27844.1; ALT_INIT; mRNA.
DR EMBL; BC078642; AAH78642.1; -; mRNA.
DR CCDS; CCDS20995.1; -. [Q8VDM6-1]
DR CCDS; CCDS39841.1; -. [Q8VDM6-3]
DR CCDS; CCDS90188.1; -. [Q8VDM6-2]
DR RefSeq; NP_659171.1; NM_144922.2. [Q8VDM6-1]
DR RefSeq; NP_835190.1; NM_178089.2. [Q8VDM6-3]
DR RefSeq; XP_006539918.1; XM_006539855.3.
DR RefSeq; XP_006539919.1; XM_006539856.2. [Q8VDM6-2]
DR AlphaFoldDB; Q8VDM6; -.
DR SMR; Q8VDM6; -.
DR BioGRID; 231344; 17.
DR IntAct; Q8VDM6; 2.
DR STRING; 10090.ENSMUSP00000037268; -.
DR iPTMnet; Q8VDM6; -.
DR PhosphoSitePlus; Q8VDM6; -.
DR EPD; Q8VDM6; -.
DR jPOST; Q8VDM6; -.
DR MaxQB; Q8VDM6; -.
DR PaxDb; Q8VDM6; -.
DR PeptideAtlas; Q8VDM6; -.
DR PRIDE; Q8VDM6; -.
DR ProteomicsDB; 273304; -. [Q8VDM6-1]
DR ProteomicsDB; 273305; -. [Q8VDM6-2]
DR ProteomicsDB; 273306; -. [Q8VDM6-3]
DR Antibodypedia; 17170; 184 antibodies from 27 providers.
DR DNASU; 232989; -.
DR Ensembl; ENSMUST00000043765; ENSMUSP00000037268; ENSMUSG00000040725. [Q8VDM6-2]
DR Ensembl; ENSMUST00000108401; ENSMUSP00000104038; ENSMUSG00000040725. [Q8VDM6-3]
DR Ensembl; ENSMUST00000206832; ENSMUSP00000146263; ENSMUSG00000040725. [Q8VDM6-1]
DR GeneID; 232989; -.
DR KEGG; mmu:232989; -.
DR UCSC; uc009ftu.1; mouse. [Q8VDM6-1]
DR UCSC; uc009ftw.1; mouse. [Q8VDM6-3]
DR CTD; 11100; -.
DR MGI; MGI:2443517; Hnrnpul1.
DR VEuPathDB; HostDB:ENSMUSG00000040725; -.
DR eggNOG; KOG2242; Eukaryota.
DR GeneTree; ENSGT00940000157823; -.
DR HOGENOM; CLU_012140_0_1_1; -.
DR InParanoid; Q8VDM6; -.
DR OMA; VMEPQIP; -.
DR OrthoDB; 778148at2759; -.
DR PhylomeDB; Q8VDM6; -.
DR TreeFam; TF317301; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 232989; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Hnrnpul1; mouse.
DR PRO; PR:Q8VDM6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8VDM6; protein.
DR Bgee; ENSMUSG00000040725; Expressed in humerus cartilage element and 246 other tissues.
DR Genevisible; Q8VDM6; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0009615; P:response to virus; IEA:InterPro.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd12884; SPRY_hnRNP; 1.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR027025; hnRNP_U-like_1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035778; SPRY_hnRNP_U.
DR PANTHER; PTHR12381:SF41; PTHR12381:SF41; 1.
DR Pfam; PF02037; SAP; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00513; SAP; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Ribonucleoprotein;
KW RNA-binding; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..859
FT /note="Heterogeneous nuclear ribonucleoprotein U-like
FT protein 1"
FT /id="PRO_0000227556"
FT DOMAIN 3..37
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 192..389
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT REPEAT 613..615
FT /note="1-1"
FT REPEAT 620..622
FT /note="1-2"
FT REPEAT 639..641
FT /note="1-3"
FT REPEAT 645..647
FT /note="1-4"
FT REPEAT 659..661
FT /note="1-5"
FT REGION 1..103
FT /note="Necessary for interaction with HRMT1L1"
FT /evidence="ECO:0000250"
FT REGION 36..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..859
FT /note="Necessary for interaction with TP53"
FT /evidence="ECO:0000250"
FT REGION 457..595
FT /note="Necessary for interaction with BRD7 and
FT transcriptional activation"
FT /evidence="ECO:0000250"
FT REGION 595..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..661
FT /note="5 X 3 AA repeats of R-G-G"
FT REGION 613..661
FT /note="Necessary for transcription repression"
FT /evidence="ECO:0000250"
FT COMPBIAS 52..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..724
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..811
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 210
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUJ2"
FT MOD_RES 639
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 645
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 645
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 659
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 659
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 664
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 674
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUJ2"
FT MOD_RES 721
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUJ2"
FT CROSSLNK 117
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9BUJ2"
FT CROSSLNK 117
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9BUJ2"
FT CROSSLNK 143
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9BUJ2"
FT CROSSLNK 143
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9BUJ2"
FT CROSSLNK 147
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BUJ2"
FT CROSSLNK 163
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BUJ2"
FT CROSSLNK 271
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BUJ2"
FT CROSSLNK 450
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BUJ2"
FT CROSSLNK 540
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BUJ2"
FT VAR_SEQ 1..100
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017553"
FT VAR_SEQ 335..340
FT /note="DFECGN -> VLELQV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017554"
FT VAR_SEQ 341..859
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017555"
FT CONFLICT 657
FT /note="N -> Y (in Ref. 1; BAE33342)"
FT /evidence="ECO:0000305"
FT CONFLICT 665
FT /note="S -> T (in Ref. 1; BAE33342)"
FT /evidence="ECO:0000305"
FT CONFLICT 672
FT /note="Q -> L (in Ref. 1; BAE33342)"
FT /evidence="ECO:0000305"
FT CONFLICT 686
FT /note="N -> Y (in Ref. 1; BAE33342)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 859 AA; 96002 MW; 197328B681DF260E CRC64;
MDVRRLKVNE LREELQRRGL DTRGLKAELA ERLLAALEAE EPEDERELEA DDDPGLPGHN
NEEVETEGGS ELEGTAQPPP PGLQPHPEPG GYSGPDGHYV MDNITRQNQF YETPVIKQEN
ESSYDRRPLD MEPQQQVYHP ELKTEMKQEA PPSFLPPEAS QLKTDRPQFQ NRKRPFEENR
GRGYFEHRED RRGRSPQPPA EEDEDDFDDT LVAIDTYNCD LHFKVARDRS SGYPLTIEGF
AYLWSGARAS YGVRRGRVCF EMKINEEISV KHLPSTEPDP HVVRIGWSLD SCSTQLGEEP
FSYGYGGTGK KSTNSRFENY GDKFAENDVI GCFADFECGN DVELSFTKNG KWMGIAFRIQ
KEALGGQALY PHVLVKNCAV EFNFGQRAEP YCSVLPGFTF IQHLPLSERI RGTIGPKSKA
ECEILMMVGL PAAGKTTWAI KHAASNPSKK YNILGTNAIM DKMRVMGLRR QRNYAGRWDV
LIQQATQCLN RLIQIAARKK RNYILDQTNV YGSAQRRKMR PFEGFQRKAI VICPTDEDLK
DRTVKRTDEE GKDVPDHAVL EMKANFTLPD VGDFLDEVLF IELQREEADK LVRQYNEEGR
KAGPPPEKRF DSRGGGFRGR GGGGGFQRYD NRGPPGGNRG GFQNRGGGGG SGGGGGNYRG
GFNRSGGGGY NQNRWGNNNR DNNNSNNRGN YNRAPQQQPP PQQPPPPQPP PQQPPPPPSY
SPARNPPGAS SYNKNSNIPG SSANTSTPTV SSYTPPQPSY SQPPYNQGGY TQGYTAPPPP
PPPPPAYNYG SYGPYNPAPY TPPPPPTAQT YPQPSYNQYQ QYAQQWSQYY QNQSQWPPYY
GNYDYGGYSG STQGGTSTQ
