GSE1_HUMAN
ID GSE1_HUMAN Reviewed; 1217 AA.
AC Q14687; D3DUM4; Q8IY61; Q96GA4; Q9BW09;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Genetic suppressor element 1;
GN Name=GSE1; Synonyms=KIAA0182;
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 [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Bone marrow;
RX PubMed=8724849; DOI=10.1093/dnares/3.1.17;
RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. V. The
RT coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 3:17-24(1996).
RN [2]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ALA-936.
RC TISSUE=Lung, and Placenta;
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 IDENTIFICATION IN THE BHC COMPLEX WITH GTF2I; HDAC1; HDAC2; HMG20B; KDM1A;
RP PHF21A; RCOR1; ZMYM2; ZMYM3 AND ZNF217.
RX PubMed=12493763; DOI=10.1074/jbc.m208992200;
RA Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.;
RT "A candidate X-linked mental retardation gene is a component of a new
RT family of histone deacetylase-containing complexes.";
RL J. Biol. Chem. 278:7234-7239(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826; SER-909 AND SER-1101,
RP AND IDENTIFICATION 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-766; SER-857; THR-907
RP AND SER-909, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-496 AND LYS-739, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-857 AND SER-909, AND
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 [9]
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 [10]
RP IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-84; THR-433; SER-826;
RP SER-828; SER-857; SER-909 AND SER-1101, AND IDENTIFICATION BY MASS
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-909, AND IDENTIFICATION BY
RP 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).
RN [13]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-305, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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).
RN [14]
RP DOWN-REGULATION BY MIR-489-5P.
RX PubMed=26828271; DOI=10.1016/j.bbrc.2016.01.168;
RA Chai P., Tian J., Zhao D., Zhang H., Cui J., Ding K., Liu B.;
RT "GSE1 negative regulation by miR-489-5p promotes breast cancer cell
RT proliferation and invasion.";
RL Biochem. Biophys. Res. Commun. 471:123-128(2016).
RN [15]
RP VARIANT [LARGE SCALE ANALYSIS] TRP-627.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- SUBUNIT: May be a component of a BHC histone deacetylase complex that
CC contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST,
CC PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I.
CC {ECO:0000269|PubMed:12493763}.
CC -!- INTERACTION:
CC Q14687; Q6P1W5: C1orf94; NbExp=8; IntAct=EBI-372619, EBI-946029;
CC Q14687; A2RRN7: CADPS; NbExp=3; IntAct=EBI-372619, EBI-10179719;
CC Q14687; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-372619, EBI-3866279;
CC Q14687; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-372619, EBI-749051;
CC Q14687; Q08379: GOLGA2; NbExp=9; IntAct=EBI-372619, EBI-618309;
CC Q14687; Q96PV6: LENG8; NbExp=3; IntAct=EBI-372619, EBI-739546;
CC Q14687; Q15311: RALBP1; NbExp=4; IntAct=EBI-372619, EBI-749285;
CC Q14687; Q93062: RBPMS; NbExp=3; IntAct=EBI-372619, EBI-740322;
CC Q14687; Q9P2K3: RCOR3; NbExp=9; IntAct=EBI-372619, EBI-743428;
CC Q14687; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-372619, EBI-1504830;
CC Q14687; Q06455-4: RUNX1T1; NbExp=3; IntAct=EBI-372619, EBI-10224192;
CC Q14687; Q8WW24: TEKT4; NbExp=5; IntAct=EBI-372619, EBI-750487;
CC Q14687; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-372619, EBI-1105213;
CC Q14687; Q12933: TRAF2; NbExp=3; IntAct=EBI-372619, EBI-355744;
CC Q14687; P14373: TRIM27; NbExp=5; IntAct=EBI-372619, EBI-719493;
CC Q14687; Q15654: TRIP6; NbExp=5; IntAct=EBI-372619, EBI-742327;
CC Q14687; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-372619, EBI-746595;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q14687-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14687-2; Sequence=VSP_021820;
CC Name=3;
CC IsoId=Q14687-3; Sequence=VSP_021821;
CC -!- INDUCTION: Negatively regulated by miR-489-5p.
CC {ECO:0000269|PubMed:26828271}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA11499.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D80004; BAA11499.2; ALT_INIT; mRNA.
DR EMBL; CH471114; EAW95445.1; -; Genomic_DNA.
DR EMBL; CH471114; EAW95447.1; -; Genomic_DNA.
DR EMBL; BC000753; AAH00753.2; -; mRNA.
DR EMBL; BC009854; AAH09854.2; -; mRNA.
DR EMBL; BC037556; AAH37556.1; -; mRNA.
DR EMBL; BQ214916; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS10952.1; -. [Q14687-1]
DR CCDS; CCDS45539.1; -. [Q14687-2]
DR CCDS; CCDS62007.1; -. [Q14687-3]
DR RefSeq; NP_001127945.1; NM_001134473.2. [Q14687-2]
DR RefSeq; NP_001265113.1; NM_001278184.1. [Q14687-3]
DR RefSeq; NP_055430.1; NM_014615.3. [Q14687-1]
DR AlphaFoldDB; Q14687; -.
DR SMR; Q14687; -.
DR BioGRID; 116808; 131.
DR CORUM; Q14687; -.
DR IntAct; Q14687; 83.
DR MINT; Q14687; -.
DR STRING; 9606.ENSP00000253458; -.
DR iPTMnet; Q14687; -.
DR MetOSite; Q14687; -.
DR PhosphoSitePlus; Q14687; -.
DR BioMuta; GSE1; -.
DR DMDM; 126302550; -.
DR EPD; Q14687; -.
DR jPOST; Q14687; -.
DR MassIVE; Q14687; -.
DR MaxQB; Q14687; -.
DR PaxDb; Q14687; -.
DR PeptideAtlas; Q14687; -.
DR PRIDE; Q14687; -.
DR ProteomicsDB; 60121; -. [Q14687-1]
DR ProteomicsDB; 60122; -. [Q14687-2]
DR ProteomicsDB; 60123; -. [Q14687-3]
DR Antibodypedia; 30633; 48 antibodies from 19 providers.
DR DNASU; 23199; -.
DR Ensembl; ENST00000253458.12; ENSP00000253458.6; ENSG00000131149.19. [Q14687-1]
DR Ensembl; ENST00000393243.5; ENSP00000376934.1; ENSG00000131149.19. [Q14687-3]
DR Ensembl; ENST00000405402.6; ENSP00000384839.2; ENSG00000131149.19. [Q14687-2]
DR GeneID; 23199; -.
DR KEGG; hsa:23199; -.
DR MANE-Select; ENST00000253458.12; ENSP00000253458.6; NM_014615.5; NP_055430.1.
DR UCSC; uc002fiw.4; human. [Q14687-1]
DR CTD; 23199; -.
DR DisGeNET; 23199; -.
DR GeneCards; GSE1; -.
DR HGNC; HGNC:28979; GSE1.
DR HPA; ENSG00000131149; Low tissue specificity.
DR MIM; 616886; gene.
DR neXtProt; NX_Q14687; -.
DR OpenTargets; ENSG00000131149; -.
DR PharmGKB; PA143485512; -.
DR VEuPathDB; HostDB:ENSG00000131149; -.
DR eggNOG; ENOG502QR0Q; Eukaryota.
DR GeneTree; ENSGT00700000104539; -.
DR HOGENOM; CLU_009387_0_0_1; -.
DR InParanoid; Q14687; -.
DR OMA; CWSPRGC; -.
DR OrthoDB; 207938at2759; -.
DR PhylomeDB; Q14687; -.
DR TreeFam; TF332496; -.
DR PathwayCommons; Q14687; -.
DR SignaLink; Q14687; -.
DR BioGRID-ORCS; 23199; 36 hits in 1081 CRISPR screens.
DR ChiTaRS; GSE1; human.
DR GeneWiki; KIAA0182; -.
DR GenomeRNAi; 23199; -.
DR Pharos; Q14687; Tdark.
DR PRO; PR:Q14687; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q14687; protein.
DR Bgee; ENSG00000131149; Expressed in corpus epididymis and 210 other tissues.
DR ExpressionAtlas; Q14687; baseline and differential.
DR Genevisible; Q14687; HS.
DR InterPro; IPR022207; GSE-like.
DR InterPro; IPR042337; GSE1.
DR PANTHER; PTHR17608; PTHR17608; 1.
DR Pfam; PF12540; DUF3736; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Methylation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1217
FT /note="Genetic suppressor element 1"
FT /id="PRO_0000050730"
FT REGION 1..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 321..403
FT /evidence="ECO:0000255"
FT COILED 1127..1201
FT /evidence="ECO:0000255"
FT COMPBIAS 11..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..575
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1089
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1115
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U3C9"
FT MOD_RES 305
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 433
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 496
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 739
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 766
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 826
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 828
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 857
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 907
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 909
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..104
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021820"
FT VAR_SEQ 3..75
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8724849"
FT /id="VSP_021821"
FT VARIANT 627
FT /note="R -> W (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs757859891)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035926"
FT VARIANT 936
FT /note="V -> A (in dbSNP:rs17853763)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_029546"
FT VARIANT 1153
FT /note="R -> Q (in dbSNP:rs2303203)"
FT /id="VAR_029547"
FT CONFLICT 444
FT /note="G -> S (in Ref. 1; BAA11499)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1217 AA; 136164 MW; 4291FBE301B70F36 CRC64;
MKGMSHEPKS PSLGMLSTAT RTTATVNPLT PSPLNGALVP SGSPATSSAL SAQAAPSSSF
AAALRKLAKQ AEEPRGSSLS SESSPVSSPA TNHSSPASTP KRVPMGPIIV PPGGHSVPST
PPVVTIAPTK TVNGVWRSES RQDAGSRSSS GGRERLIVEP PLPQEKAGGP AIPSHLLSTP
YPFGLSPSSV VQDSRFPPLN LQRPVHHVVP PSTVTEDYLR SFRPYHTTDD LRMSSLPPLG
LDPATAAAYY HPSYLAPHPF PHPAFRMDDS YCLSALRSPF YPIPTPGSLP PLHPSAMHLH
LSGVRYPPEL SHSSLAALHS ERMSGLSAER LQMDEELRRE RERERERERE READREREKE
REREREKERE QEKEREREKE RERELERQRE QRAREKELLA AKALEPSFLP VAELHGLRGH
ATEERGKPSE QLTPTRAEKL KDAGLQAPKP VQHPLHPVPT PHHTVPSLIS NHGIFSLPSS
SAATALLIQR TNEEEKWLAR QRRLRQEKED RQSQVSEFRQ QVLEQHLDMG RPPVPAEAEH
RPESTTRPGP NRHEPGGRDP PQHFGGPPPL ISPKPQLHAA PTALWNPVSL MDNTLETRRA
ESHSLHSHPA AFEPSRQAAV PLVKVERVFC PEKAEEGPRK REPAPLDKYQ PPPPPPREGG
SLEHQPFLPG PGPFLAELEK STQTILGQQR ASLPQAATFG ELSGPLKPGS PYRPPVPRAP
DPAYIYDEFL QQRRRLVSKL DLEERRRREA QEKGYYYDLD DSYDESDEEE VRAHLRCVAE
QPPLKLDTSS EKLEFLQLFG LTTQQQKEEL VAQKRRKRRR MLRERSPSPP TIQSKRQTPS
PRLALSTRYS PDEMNNSPNF EEKKKFLTIF NLTHISAEKR KDKERLVEML RAMKQKALSA
AVADSLTNSP RDSPAVSLSE PATQQASLDV EKPVGVAASL SDIPKAAEPG KLEQVRPQEL
SRVQELAPAS GEKARLSEAP GGKKSLSMLH YIRGAAPKDI PVPLSHSTNG KSKPWEPFVA
EEFAHQFHES VLQSTQKALQ KHKGSVAVLS AEQNHKVDTS VHYNIPELQS SSRAPPPQHN
GQQEPPTARK GPPTQELDRD SEEEEEEDDE DGEDEEEVPK RKWQGIEAVF EAYQEHIEEQ
NLERQVLQTQ CRRLEARHYS LSLTAEQLSH SVAELRSQKQ KMVSERERLQ AELDHLRKCL
ALPAMHWPRG YLKGYPR
