ZBT20_MOUSE
ID ZBT20_MOUSE Reviewed; 741 AA.
AC Q8K0L9; A6X916; Q9DBD4; Q9QZ87;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Zinc finger and BTB domain-containing protein 20;
DE AltName: Full=BTB/POZ domain zinc finger factor HOF;
DE AltName: Full=Zinc finger protein 288;
GN Name=Zbtb20; Synonyms=Zfp288;
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] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING,
RP SUBCELLULAR LOCATION, HOMODIMERIZATION, AND TISSUE SPECIFICITY.
RC TISSUE=Oligodendroglioma;
RX PubMed=11744704; DOI=10.1074/jbc.m110023200;
RA Mitchelmore C., Kjaerulff K.M., Pedersen H.C., Nielsen J.V.,
RA Rasmussen T.E., Fisker M.F., Finsen B., Pedersen K.M., Jensen N.A.;
RT "Characterization of two novel nuclear BTB/POZ domain zinc finger isoforms.
RT Association with differentiation of hippocampal neurons, cerebellar granule
RT cells, and macroglia.";
RL J. Biol. Chem. 277:7598-7609(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Kidney;
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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353; THR-357; THR-690 AND
RP THR-695, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, and Kidney;
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 SUMOYLATION WITH SUMO1.
RX PubMed=23213215; DOI=10.1073/pnas.1215366110;
RA Tirard M., Hsiao H.H., Nikolov M., Urlaub H., Melchior F., Brose N.;
RT "In vivo localization and identification of SUMOylated proteins in the
RT brain of His6-HA-SUMO1 knock-in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:21122-21127(2012).
RN [8]
RP FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=27446912; DOI=10.3389/fcell.2016.00058;
RA Alonso-Martin S., Rochat A., Mademtzoglou D., Morais J., de Reynies A.,
RA Aurade F., Chang T.H., Zammit P.S., Relaix F.;
RT "Gene expression profiling of muscle stem cells identifies novel regulators
RT of postnatal myogenesis.";
RL Front. Cell Dev. Biol. 4:58-58(2016).
CC -!- FUNCTION: May be a transcription factor that may be involved in
CC hematopoiesis, oncogenesis, and immune responses (By similarity). Plays
CC a role in postnatal myogenesis, may be involved in the regulation of
CC satellite cells self-renewal (PubMed:27446912).
CC {ECO:0000250|UniProtKB:Q9HC78, ECO:0000269|PubMed:27446912}.
CC -!- SUBUNIT: Can homodimerize. Binds to DNA.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:11744704}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=HOF-L;
CC IsoId=Q8K0L9-1; Sequence=Displayed;
CC Name=2; Synonyms=HOF-S;
CC IsoId=Q8K0L9-2; Sequence=VSP_032504;
CC -!- TISSUE SPECIFICITY: Specifically expressed in early hippocampal
CC neurons, cerebellar granule cells and gliogenic progenitors as well as
CC in differentiated glia (PubMed:11744704). Expressed in adult and aged
CC myogenic satellite cells (PubMed:27446912).
CC {ECO:0000269|PubMed:11744704, ECO:0000269|PubMed:27446912}.
CC -!- DEVELOPMENTAL STAGE: Not expressed during development, is induced
CC during establishment of satellite cells and acquisition of quiescence.
CC {ECO:0000269|PubMed:27446912}.
CC -!- PTM: Sumoylated with SUMO1. {ECO:0000269|PubMed:23213215}.
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DR EMBL; AF194030; AAF06015.1; -; mRNA.
DR EMBL; AK005028; BAB23755.1; -; mRNA.
DR EMBL; CT010512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031114; AAH31114.1; -; mRNA.
DR EMBL; BC056446; AAH56446.1; -; mRNA.
DR CCDS; CCDS28178.1; -. [Q8K0L9-1]
DR CCDS; CCDS49851.1; -. [Q8K0L9-2]
DR RefSeq; NP_001272734.1; NM_001285805.1. [Q8K0L9-1]
DR RefSeq; NP_062752.2; NM_019778.2. [Q8K0L9-1]
DR RefSeq; NP_851401.1; NM_181058.1. [Q8K0L9-2]
DR RefSeq; XP_006522475.1; XM_006522412.3. [Q8K0L9-1]
DR RefSeq; XP_006522476.1; XM_006522413.3. [Q8K0L9-1]
DR RefSeq; XP_006522477.1; XM_006522414.2. [Q8K0L9-1]
DR RefSeq; XP_006522478.1; XM_006522415.3.
DR RefSeq; XP_006522479.1; XM_006522416.3. [Q8K0L9-1]
DR RefSeq; XP_006522481.1; XM_006522418.3. [Q8K0L9-1]
DR RefSeq; XP_006522485.1; XM_006522422.3.
DR RefSeq; XP_006522487.1; XM_006522424.3. [Q8K0L9-2]
DR RefSeq; XP_011244291.1; XM_011245989.2. [Q8K0L9-1]
DR RefSeq; XP_011244292.1; XM_011245990.2. [Q8K0L9-1]
DR RefSeq; XP_017172580.1; XM_017317091.1.
DR RefSeq; XP_017172581.1; XM_017317092.1. [Q8K0L9-1]
DR RefSeq; XP_017172582.1; XM_017317093.1. [Q8K0L9-1]
DR RefSeq; XP_017172583.1; XM_017317094.1.
DR RefSeq; XP_017172584.1; XM_017317095.1.
DR RefSeq; XP_017172585.1; XM_017317096.1.
DR RefSeq; XP_017172586.1; XM_017317097.1.
DR RefSeq; XP_017172587.1; XM_017317098.1.
DR RefSeq; XP_017172588.1; XM_017317099.1. [Q8K0L9-2]
DR RefSeq; XP_017172589.1; XM_017317100.1.
DR RefSeq; XP_017172590.1; XM_017317101.1.
DR RefSeq; XP_017172591.1; XM_017317102.1.
DR RefSeq; XP_017172592.1; XM_017317103.1.
DR RefSeq; XP_017172593.1; XM_017317104.1.
DR RefSeq; XP_017172594.1; XM_017317105.1.
DR AlphaFoldDB; Q8K0L9; -.
DR SMR; Q8K0L9; -.
DR BioGRID; 208015; 19.
DR IntAct; Q8K0L9; 2.
DR MINT; Q8K0L9; -.
DR STRING; 10090.ENSMUSP00000110339; -.
DR iPTMnet; Q8K0L9; -.
DR PhosphoSitePlus; Q8K0L9; -.
DR jPOST; Q8K0L9; -.
DR MaxQB; Q8K0L9; -.
DR PaxDb; Q8K0L9; -.
DR PeptideAtlas; Q8K0L9; -.
DR PRIDE; Q8K0L9; -.
DR ProteomicsDB; 275122; -. [Q8K0L9-1]
DR ProteomicsDB; 275123; -. [Q8K0L9-2]
DR Antibodypedia; 16495; 161 antibodies from 25 providers.
DR DNASU; 56490; -.
DR Ensembl; ENSMUST00000079441; ENSMUSP00000078410; ENSMUSG00000022708. [Q8K0L9-1]
DR Ensembl; ENSMUST00000114690; ENSMUSP00000110338; ENSMUSG00000022708. [Q8K0L9-2]
DR Ensembl; ENSMUST00000114691; ENSMUSP00000110339; ENSMUSG00000022708. [Q8K0L9-2]
DR Ensembl; ENSMUST00000114694; ENSMUSP00000110342; ENSMUSG00000022708. [Q8K0L9-1]
DR Ensembl; ENSMUST00000114695; ENSMUSP00000110343; ENSMUSG00000022708. [Q8K0L9-1]
DR GeneID; 56490; -.
DR KEGG; mmu:56490; -.
DR UCSC; uc007zga.3; mouse. [Q8K0L9-1]
DR CTD; 26137; -.
DR MGI; MGI:1929213; Zbtb20.
DR VEuPathDB; HostDB:ENSMUSG00000022708; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158617; -.
DR HOGENOM; CLU_019055_0_0_1; -.
DR InParanoid; Q8K0L9; -.
DR OMA; EQQFMAG; -.
DR PhylomeDB; Q8K0L9; -.
DR TreeFam; TF335684; -.
DR BioGRID-ORCS; 56490; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Zbtb20; mouse.
DR PRO; PR:Q8K0L9; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8K0L9; protein.
DR Bgee; ENSMUSG00000022708; Expressed in rostral migratory stream and 257 other tissues.
DR ExpressionAtlas; Q8K0L9; baseline and differential.
DR Genevisible; Q8K0L9; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IMP:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:CACAO.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:CACAO.
DR GO; GO:0045821; P:positive regulation of glycolytic process; IMP:UniProtKB.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IDA:CACAO.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:CACAO.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:CACAO.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 5.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..741
FT /note="Zinc finger and BTB domain-containing protein 20"
FT /id="PRO_0000325961"
FT DOMAIN 104..167
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 578..600
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 606..628
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 634..656
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 662..684
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 715..737
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 211
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC78"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 357
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 690
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 695
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 330
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9HC78"
FT CROSSLNK 330
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9HC78"
FT CROSSLNK 371
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9HC78"
FT CROSSLNK 723
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9HC78"
FT VAR_SEQ 1..73
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11744704,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_032504"
FT CONFLICT 88
FT /note="N -> D (in Ref. 2; BAB23755)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="A -> D (in Ref. 1; AAF06015)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 741 AA; 81034 MW; 04C0744D66BFE418 CRC64;
MLERKKPKTA ENQKASEENE ITQPGGSSAK PALPCLNFEA VLSPAPALIH STHSLTNSHA
HTGSSDCDIS CKGMTERIHS INLHNFSNSV LETLNEQRNR GHFCDVTVRI HGSMLRAHRC
VLAAGSPFFQ DKLLLGYSDI EIPSVVSVQS VQKLIDFMYS GVLRVSQSEA LQILTAASIL
QIKTVIDECT RIVSQNVGDV FPGIQDSGQD TPRGTPESGT SGQSSDTESG YLQSHPQHSV
DRIYSALYAC SMQNGSGERS FYSGAVVSHH ETALGLPRDH HMEDPSWITR IHERSQQMER
YLSTTPETTH CRKQPRPVRI QTLVGNIHIK QEMEDDYDYY GQQRVQILER NESEECTEDT
DQAEGTESEP KGESFDSGVS SSIGTEPDSV EQQFGAAAPR DGQAEPAQPE QAAEAPAESS
AQPNQLEPGA SSPERSNESE MDNTVITVSN SSDKGVLQQP SVNTSIGQPL PSTQLYLRQT
ETLTSNLRMP LTLTSNTQVI GTAGNTYLPA LFTTQPAGSG PKPFLFSLPQ PLTGQQTQFV
TVSQPGLSTF TAQLPAPQPL ASSAGHSTAS GQGDKKPYEC TLCNKTFTAK QNYVKHMFVH
TGEKPHQCSI CWRSFSLKDY LIKHMVTHTG VRAYQCSICN KRFTQKSSLN VHMRLHRGEK
SYECYICKKK FSHKTLLERH VALHSASNGT PPAGTPPGAR AGPPGVVACT EGTTYVCSVC
PAKFDQIEQF NDHMRMHVSD G
