SLTM_MOUSE
ID SLTM_MOUSE Reviewed; 1031 AA.
AC Q8CH25; Q3UYE5; Q8BP76; Q8BR40; Q8VCF4; Q9CS57;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=SAFB-like transcription modulator;
DE AltName: Full=Modulator of estrogen-induced transcription;
DE AltName: Full=SAF-like transcription modulator;
GN Name=Sltm; Synonyms=Met;
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 [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17630952; DOI=10.1042/bj20070170;
RA Chan C.W., Lee Y.-B., Uney J., Flynn A., Tobias J.H., Norman M.;
RT "A novel member of the SAF (scaffold attachment factor)-box protein family
RT inhibits gene expression and induces apoptosis.";
RL Biochem. J. 407:355-362(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-582 (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 425-1031 (ISOFORM 1/2).
RC STRAIN=C57BL/6J;
RC TISSUE=Corpora quadrigemina, Embryo, and Medulla oblongata;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 528-1031 (ISOFORM 1/2).
RC STRAIN=FVB/N; TISSUE=Colon;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289 AND SER-552, AND
RP IDENTIFICATION BY 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289 AND SER-552, AND
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-999, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289; SER-549; SER-550;
RP SER-552 AND SER-999, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1014, AND IDENTIFICATION BY MASS
RP 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: When overexpressed, acts as a general inhibitor of
CC transcription that eventually leads to apoptosis.
CC {ECO:0000269|PubMed:17630952}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17630952}.
CC Note=Detected in punctate structures.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CH25-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CH25-2; Sequence=VSP_028834;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH19992.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC32471.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE22267.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF462146; AAO15605.1; -; mRNA.
DR EMBL; AK017839; BAB30967.1; -; mRNA.
DR EMBL; AK045723; BAC32471.1; ALT_INIT; mRNA.
DR EMBL; AK077578; BAC36873.1; -; mRNA.
DR EMBL; AK134756; BAE22267.1; ALT_INIT; mRNA.
DR EMBL; BC019992; AAH19992.1; ALT_INIT; mRNA.
DR CCDS; CCDS23322.1; -. [Q8CH25-1]
DR CCDS; CCDS90615.1; -. [Q8CH25-2]
DR RefSeq; NP_079966.2; NM_025690.3. [Q8CH25-1]
DR RefSeq; NP_080613.1; NM_026337.1. [Q8CH25-2]
DR AlphaFoldDB; Q8CH25; -.
DR SMR; Q8CH25; -.
DR BioGRID; 211628; 4.
DR IntAct; Q8CH25; 3.
DR MINT; Q8CH25; -.
DR STRING; 10090.ENSMUSP00000049112; -.
DR iPTMnet; Q8CH25; -.
DR PhosphoSitePlus; Q8CH25; -.
DR EPD; Q8CH25; -.
DR jPOST; Q8CH25; -.
DR MaxQB; Q8CH25; -.
DR PaxDb; Q8CH25; -.
DR PeptideAtlas; Q8CH25; -.
DR PRIDE; Q8CH25; -.
DR ProteomicsDB; 258697; -. [Q8CH25-1]
DR ProteomicsDB; 258698; -. [Q8CH25-2]
DR Antibodypedia; 25331; 149 antibodies from 19 providers.
DR DNASU; 66660; -.
DR Ensembl; ENSMUST00000049263; ENSMUSP00000049112; ENSMUSG00000032212. [Q8CH25-1]
DR Ensembl; ENSMUST00000216816; ENSMUSP00000149059; ENSMUSG00000032212. [Q8CH25-2]
DR GeneID; 66660; -.
DR KEGG; mmu:66660; -.
DR UCSC; uc009qok.1; mouse. [Q8CH25-2]
DR UCSC; uc009qol.1; mouse. [Q8CH25-1]
DR CTD; 79811; -.
DR MGI; MGI:1913910; Sltm.
DR VEuPathDB; HostDB:ENSMUSG00000032212; -.
DR eggNOG; KOG4661; Eukaryota.
DR GeneTree; ENSGT00940000156573; -.
DR HOGENOM; CLU_011145_1_0_1; -.
DR InParanoid; Q8CH25; -.
DR OMA; HEEMEGN; -.
DR OrthoDB; 803886at2759; -.
DR PhylomeDB; Q8CH25; -.
DR TreeFam; TF325240; -.
DR BioGRID-ORCS; 66660; 10 hits in 75 CRISPR screens.
DR ChiTaRS; Sltm; mouse.
DR PRO; PR:Q8CH25; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8CH25; protein.
DR Bgee; ENSMUSG00000032212; Expressed in undifferentiated genital tubercle and 269 other tissues.
DR ExpressionAtlas; Q8CH25; baseline and differential.
DR Genevisible; Q8CH25; MM.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0050684; P:regulation of mRNA processing; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR034780; SLTM.
DR PANTHER; PTHR15683:SF5; PTHR15683:SF5; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Coiled coil; Isopeptide bond;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW RNA-binding; Transcription; Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH9"
FT CHAIN 2..1031
FT /note="SAFB-like transcription modulator"
FT /id="PRO_0000307799"
FT DOMAIN 22..56
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 384..462
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 107..182
FT /evidence="ECO:0000255"
FT COILED 608..727
FT /evidence="ECO:0000255"
FT COMPBIAS 78..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..197
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..870
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..906
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH9"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH9"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH9"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH9"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 401
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH9"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH9"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH9"
FT MOD_RES 786
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH9"
FT MOD_RES 797
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH9"
FT MOD_RES 812
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH9"
FT MOD_RES 906
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH9"
FT MOD_RES 920
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH9"
FT MOD_RES 995
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH9"
FT MOD_RES 999
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1011
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH9"
FT MOD_RES 1014
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1016
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH9"
FT MOD_RES 1018
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH9"
FT MOD_RES 1021
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH9"
FT CROSSLNK 500
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH9"
FT CROSSLNK 881
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH9"
FT CROSSLNK 1021
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH9"
FT CROSSLNK 1024
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NWH9"
FT VAR_SEQ 197..214
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028834"
FT CONFLICT 4
FT /note="A -> R (in Ref. 2; BAB30967)"
FT /evidence="ECO:0000305"
FT CONFLICT 985
FT /note="R -> Q (in Ref. 2; BAE22267)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1031 AA; 116919 MW; DBD3F617F816C79C CRC64;
MAAAAGAVVA SAASGPAEGK KITELRVIDL RSELKRRNLD INGVKTVLVS RLKQAIEEEG
GDPDNIELTV STDTPNKKPT KGKGKKQEAD ELSGDASVED DSFVKDCELE NQETHDQDGN
EELKDLEEFG ENEEEIVHSQ ELLSTEENKT TQEFVEAEAI EDREKEDIES QETEAQEGED
DTFLTAQDGE EEENEKDIAG SGDGTQEVSK PLPSEGSLAE ADHTAHEEME ANATGKEAED
DNISVTIQAE DAITLDFDGD DLLETGKNVK ITDSEASKPK DVQDAIAQSP EKEAKDYEMN
PNHKDGKKED SVKGEPVEKE ARESAKKAES GDKEKDTLKK GPSSTGASGQ AKSSSKESKD
SKTSSKDDKG STGSAGGSSG SSTKNIWVSG LSSNTKAADL KNLFGKYGKV LSAKVVTNAR
SPGAKCYGIV TMSSSTEVSR CVAHLHRTEL HGQLISVEKV KGDPSKKEMK KENDEKSSSR
SAGDKKNASD RSAKTQASIK KEEKRSSEKS EKKESKDTKK IEKDEKNDDG PSGQTSESLK
KSEEKKRISS KSPGHMVILN QTKGDHCRPS RRGRYEKGHG RSKEKERASL DKKRDKDYRR
KEILPFEKMK EQRLREHLVR FERLKQAVEF RRRKEIAERE RRERERIRII REREERERLQ
RERERLEIER QKLERERMER ERLERERIRI EQERRREAER IAREREELRR QQQQLRYEQE
KRNSLKRPRD VDHRRDDPYW SENKKLSLDT EARFGHGSDY RQQSRFLDFS HRERARFPDT
ASVQSSFERR ERFVGQSEGK KPRPAARREE PSFERYPKNF SDSRRNEPPP PRNELRETDR
REVRGERDER RTVILHDRPE VAHPRHPRET VPNPSRPTSW KSEANMSTEK RESRVERPER
SGREVSGHTV RGAPPGNRSS ASGYGTREGE RGVIADRGSG TQHYPEERHV VERHGRDTSG
PRKEWHGPPS QGPSYHDTRR MGDGRAGAGM ITQHSSTASP VNRIVQMSGN SLPRGSSSGF
KPFKSGPPRR F
