GNL1_HUMAN
ID GNL1_HUMAN Reviewed; 607 AA.
AC P36915; B0S838; Q96CT5;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Guanine nucleotide-binding protein-like 1;
DE AltName: Full=GTP-binding protein HSR1;
GN Name=GNL1; Synonyms=HSR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=T-cell;
RX PubMed=8180467; DOI=10.1007/bf00292335;
RA Vernet C., Ribouchon M.-T., Chimini G., Pontarotti P.;
RT "Structure and evolution of a member of a new subfamily of GTP-binding
RT proteins mapping to the human MHC class I region.";
RL Mamm. Genome 5:100-105(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle, and Skin;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-33; SER-34; THR-48;
RP THR-50; SER-51; SER-324; SER-561; SER-562 AND SER-563, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-48; THR-50 AND SER-51, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-48; THR-50; SER-51 AND
RP SER-68, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-48; THR-50 AND SER-51, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Possible regulatory or functional link with the
CC histocompatibility cluster.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P36915-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P36915-2; Sequence=VSP_026992, VSP_026993;
CC -!- DOMAIN: In contrast to other GTP-binding proteins, this family is
CC characterized by a circular permutation of the GTPase motifs described
CC by a G4-G1-G3 pattern.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR EMBL; L25665; AAA66492.1; -; mRNA.
DR EMBL; BT006648; AAP35294.1; -; mRNA.
DR EMBL; AL662800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX000357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX248518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX927220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR388372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR936927; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03294.1; -; Genomic_DNA.
DR EMBL; BC013959; AAH13959.1; -; mRNA.
DR EMBL; BC018366; AAH18366.1; -; mRNA.
DR CCDS; CCDS4680.1; -. [P36915-1]
DR PIR; I57013; I57013.
DR RefSeq; NP_005266.2; NM_005275.3. [P36915-1]
DR RefSeq; XP_005249072.1; XM_005249015.3. [P36915-1]
DR AlphaFoldDB; P36915; -.
DR BioGRID; 109056; 92.
DR IntAct; P36915; 16.
DR STRING; 9606.ENSP00000365806; -.
DR iPTMnet; P36915; -.
DR PhosphoSitePlus; P36915; -.
DR BioMuta; GNL1; -.
DR DMDM; 158939140; -.
DR EPD; P36915; -.
DR jPOST; P36915; -.
DR MassIVE; P36915; -.
DR MaxQB; P36915; -.
DR PaxDb; P36915; -.
DR PeptideAtlas; P36915; -.
DR PRIDE; P36915; -.
DR ProteomicsDB; 55237; -. [P36915-1]
DR ProteomicsDB; 55238; -. [P36915-2]
DR Antibodypedia; 26307; 253 antibodies from 30 providers.
DR DNASU; 2794; -.
DR Ensembl; ENST00000376621.8; ENSP00000365806.3; ENSG00000204590.13. [P36915-1]
DR Ensembl; ENST00000383596.6; ENSP00000373090.2; ENSG00000206492.11. [P36915-1]
DR Ensembl; ENST00000417834.5; ENSP00000403576.1; ENSG00000226882.9. [P36915-1]
DR Ensembl; ENST00000428189.5; ENSP00000409074.1; ENSG00000229470.9. [P36915-1]
DR Ensembl; ENST00000437917.5; ENSP00000411162.1; ENSG00000228581.9. [P36915-1]
DR Ensembl; ENST00000441604.5; ENSP00000394290.1; ENSG00000235986.9. [P36915-1]
DR Ensembl; ENST00000454829.5; ENSP00000409367.1; ENSG00000232143.9. [P36915-1]
DR GeneID; 2794; -.
DR KEGG; hsa:2794; -.
DR MANE-Select; ENST00000376621.8; ENSP00000365806.3; NM_005275.5; NP_005266.2.
DR UCSC; uc003nqh.4; human. [P36915-1]
DR CTD; 2794; -.
DR DisGeNET; 2794; -.
DR GeneCards; GNL1; -.
DR HGNC; HGNC:4413; GNL1.
DR HPA; ENSG00000204590; Low tissue specificity.
DR MIM; 143024; gene.
DR neXtProt; NX_P36915; -.
DR OpenTargets; ENSG00000204590; -.
DR PharmGKB; PA28792; -.
DR VEuPathDB; HostDB:ENSG00000204590; -.
DR eggNOG; KOG1424; Eukaryota.
DR GeneTree; ENSGT00940000158047; -.
DR HOGENOM; CLU_013649_1_1_1; -.
DR InParanoid; P36915; -.
DR OMA; CDFPVRP; -.
DR PhylomeDB; P36915; -.
DR TreeFam; TF324569; -.
DR PathwayCommons; P36915; -.
DR SignaLink; P36915; -.
DR BioGRID-ORCS; 2794; 36 hits in 1070 CRISPR screens.
DR ChiTaRS; GNL1; human.
DR GenomeRNAi; 2794; -.
DR Pharos; P36915; Tbio.
DR PRO; PR:P36915; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P36915; protein.
DR Bgee; ENSG00000204590; Expressed in right testis and 97 other tissues.
DR ExpressionAtlas; P36915; baseline and differential.
DR Genevisible; P36915; HS.
DR GO; GO:0005615; C:extracellular space; NAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; NAS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; NAS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR GO; GO:0002456; P:T cell mediated immunity; NAS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR043358; GNL1-like.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45709; PTHR45709; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; GTP-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..607
FT /note="Guanine nucleotide-binding protein-like 1"
FT /id="PRO_0000122441"
FT DOMAIN 178..418
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..583
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 225..228
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 367..374
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 411..415
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 48
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 50
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..177
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8180467"
FT /id="VSP_026992"
FT VAR_SEQ 178..183
FT /note="WRQLWR -> MEAAVA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8180467"
FT /id="VSP_026993"
FT CONFLICT 232..233
FT /note="PA -> RR (in Ref. 1; AAA66492)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="Missing (in Ref. 1; AAA66492)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="E -> EQ (in Ref. 1; AAA66492)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="L -> V (in Ref. 1; AAA66492)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 607 AA; 68661 MW; F8EBB4EDBB73D929 CRC64;
MPRKKPFSVK QKKKQLQDKR ERKRGLQDGL RSSSNSRSGS RERREEQTDT SDGESVTHHI
RRLNQQPSQG LGPRGYDPNR YRLHFERDSR EEVERRKRAA REQVLQPVSA ELLELDIREV
YQPGSVLDFP RRPPWSYEMS KEQLMSQEER SFQDYLGKIH GAYSSEKLSY FEHNLETWRQ
LWRVLEMSDI VLLITDIRHP VVNFPPALYE YVTGELGLAL VLVLNKVDLA PPALVVAWKH
YFHQHYPQLH VVLFTSFPRD PRTPQDPSSV LKKSRRRGRG WTRALGPEQL LRACEAITVG
KVDLSSWREK IARDVAGATW GNGSGEEEEE EDGPAVLVEQ QTDSAMEPTG PTQERYKDGV
VTIGCVGFPN VGKSSLINGL VGRKVVSVSR TPGHTRYFQT YFLTPSVKLC DCPGLIFPSL
LPRQLQVLAG IYPIAQIQEP YTAVGYLASR IPVQALLHLR HPEAEDPSAE HPWCAWDICE
AWAEKRGYKT AKAARNDVYR AANSLLRLAV DGRLSLCFHP PGYSEQKGTW ESHPETTELV
VLQGRVGPAG DEEEEEEEEL SSSCEEEGEE DRDADEEGEG DEETPTSAPG SSLAGRNPYA
LLGEDEC
