PRGC2_MOUSE
ID PRGC2_MOUSE Reviewed; 1014 AA.
AC Q8VHJ7; Q8C1C0;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Peroxisome proliferator-activated receptor gamma coactivator 1-beta;
DE Short=PGC-1-beta;
DE Short=PPAR-gamma coactivator 1-beta;
DE Short=PPARGC-1-beta;
DE AltName: Full=ERR ligand 1;
GN Name=Ppargc1b; Synonyms=Errl1, Pgc1, Pgc1b, Ppargc1;
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), TISSUE SPECIFICITY, MOTIFS,
RP FUNCTION, INDUCTION, AND SUBUNIT.
RC STRAIN=C57BL/6J;
RX PubMed=11733490; DOI=10.1074/jbc.c100631200;
RA Lin J., Puigserver P., Donovan J., Tarr P., Spiegelman B.M.;
RT "Peroxisome proliferator-activated receptor gamma coactivator 1beta (PGC-
RT 1beta), a novel PGC-1-related transcription coactivator associated with
RT host cell factor.";
RL J. Biol. Chem. 277:1645-1648(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
RP ESRRA AND ESRRG.
RX PubMed=14530391; DOI=10.1073/pnas.2135217100;
RA Kamei Y., Ohizumi H., Fujitani Y., Nemoto T., Tanaka T., Takahashi N.,
RA Kawada T., Miyoshi M., Ezaki O., Kakizuka A.;
RT "PPARgamma coactivator 1beta/ERR ligand 1 is an ERR protein ligand, whose
RT expression induces a high-energy expenditure and antagonizes obesity.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12378-12383(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 [4]
RP INTERACTION WITH ESRRG.
RX PubMed=12470660; DOI=10.1016/s0006-291x(02)02753-5;
RA Hentschke M., Suesens U., Borgmeyer U.;
RT "PGC-1 and PERC, coactivators of the estrogen receptor-related receptor
RT gamma.";
RL Biochem. Biophys. Res. Commun. 299:872-879(2002).
RN [5]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=12678921; DOI=10.1042/bj20030200;
RA Meirhaeghe A., Crowley V., Lenaghan C., Lelliott C., Green K., Stewart A.,
RA Hart K., Schinner S., Sethi J.K., Yeo G., Brand M.D., Cortright R.N.,
RA O'Rahilly S., Montague C., Vidal-Puig A.J.;
RT "Characterization of the human, mouse and rat PGC1 beta (peroxisome-
RT proliferator-activated receptor-gamma co-activator 1 beta) gene in vitro
RT and in vivo.";
RL Biochem. J. 373:155-165(2003).
RN [6]
RP FUNCTION, INTERACTION WITH SREBF1, AND INDUCTION.
RX PubMed=15680331; DOI=10.1016/j.cell.2004.11.043;
RA Lin J., Yang R., Tarr P.T., Wu P.-H., Handschin C., Li S., Yang W., Pei L.,
RA Uldry M., Tontonoz P., Newgard C.B., Spiegelman B.M.;
RT "Hyperlipidemic effects of dietary saturated fats mediated through PGC-
RT 1beta coactivation of SREBP.";
RL Cell 120:261-273(2005).
RN [7]
RP INTERACTION WITH PRDM16.
RX PubMed=17618855; DOI=10.1016/j.cmet.2007.06.001;
RA Seale P., Kajimura S., Yang W., Chin S., Rohas L.M., Uldry M.,
RA Tavernier G., Langin D., Spiegelman B.M.;
RT "Transcriptional control of brown fat determination by PRDM16.";
RL Cell Metab. 6:38-54(2007).
RN [8]
RP INTERACTION WITH PRDM16.
RX PubMed=18483224; DOI=10.1101/gad.1666108;
RA Kajimura S., Seale P., Tomaru T., Erdjument-Bromage H., Cooper M.P.,
RA Ruas J.L., Chin S., Tempst P., Lazar M.A., Spiegelman B.M.;
RT "Regulation of the brown and white fat gene programs through a PRDM16/CtBP
RT transcriptional complex.";
RL Genes Dev. 22:1397-1409(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145 AND SER-148, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
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).
CC -!- FUNCTION: Plays a role of stimulator of transcription factors and
CC nuclear receptors activities. Activates transcriptional activity of
CC estrogen receptor alpha, nuclear respiratory factor 1 (NRF1) and
CC glucocorticoid receptor in the presence of glucocorticoids. May play a
CC role in constitutive non-adrenergic-mediated mitochondrial biogenesis
CC as suggested by increased basal oxygen consumption and mitochondrial
CC number when overexpressed. May be part of the pathways regulating the
CC elevation of gluconeogenesis, beta-oxidation of fatty acids and
CC ketogenesis during fasting. Stimulates SREBP-mediated lipogenic gene
CC expression in the liver. Induces energy expenditure and antagonizes
CC obesity when overexpressed. Induces also the expression of
CC mitochondrial genes involved in oxidative metabolism. Induces the
CC expression of PERM1 in the skeletal muscle in an ESRRA-dependent
CC manner. {ECO:0000269|PubMed:11733490, ECO:0000269|PubMed:12678921,
CC ECO:0000269|PubMed:14530391, ECO:0000269|PubMed:15680331}.
CC -!- SUBUNIT: Interacts with estrogen receptor alpha/ESR1 (By similarity).
CC Interacts with hepatocyte nuclear factor 4-alpha/HNF4A, Sterol
CC regulatory binding transcription factor 1/SREBF1, PPAR-alpha/PPARA,
CC thyroid hormone receptor beta/THRB and host cell factor/HCFC1.
CC Interacts with estrogen-related receptor gamma/ESRRG and alpha/ESRRA.
CC Interacts with PRDM16. {ECO:0000250, ECO:0000269|PubMed:11733490,
CC ECO:0000269|PubMed:12470660, ECO:0000269|PubMed:14530391,
CC ECO:0000269|PubMed:15680331, ECO:0000269|PubMed:17618855,
CC ECO:0000269|PubMed:18483224}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VHJ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VHJ7-2; Sequence=VSP_019302;
CC -!- TISSUE SPECIFICITY: Ubiquitous with higher expression in heart, brown
CC adipose tissue, brain and skeletal muscle.
CC {ECO:0000269|PubMed:11733490, ECO:0000269|PubMed:12678921}.
CC -!- INDUCTION: Induced by fasting in the liver, but not by cold exposure in
CC brown adipose tissue. Induced also by saturated fatty acids in primary
CC hepatocytes. {ECO:0000269|PubMed:11733490,
CC ECO:0000269|PubMed:15680331}.
CC -!- DOMAIN: Contains 3 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif, which are usually
CC required for the association with nuclear receptors. {ECO:0000250}.
CC -!- MISCELLANEOUS: Transgenic mice overexpressing PPARGC1B exhibits
CC increased expression of medium-chain acyl CoA dehydrogenase. They are
CC hyperphagic but lean, with increased energy expenditure and resistance
CC to obesity.
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DR EMBL; AF453324; AAL47054.1; -; mRNA.
DR EMBL; AK028464; BAC25964.1; -; mRNA.
DR CCDS; CCDS29284.1; -. [Q8VHJ7-1]
DR CCDS; CCDS89250.1; -. [Q8VHJ7-2]
DR RefSeq; NP_573512.1; NM_133249.2. [Q8VHJ7-1]
DR AlphaFoldDB; Q8VHJ7; -.
DR SMR; Q8VHJ7; -.
DR BioGRID; 228460; 6.
DR IntAct; Q8VHJ7; 1.
DR STRING; 10090.ENSMUSP00000074771; -.
DR iPTMnet; Q8VHJ7; -.
DR PhosphoSitePlus; Q8VHJ7; -.
DR PaxDb; Q8VHJ7; -.
DR PRIDE; Q8VHJ7; -.
DR ProteomicsDB; 291589; -. [Q8VHJ7-1]
DR ProteomicsDB; 291590; -. [Q8VHJ7-2]
DR Antibodypedia; 27863; 124 antibodies from 29 providers.
DR DNASU; 170826; -.
DR Ensembl; ENSMUST00000063307; ENSMUSP00000069431; ENSMUSG00000033871. [Q8VHJ7-2]
DR Ensembl; ENSMUST00000075299; ENSMUSP00000074771; ENSMUSG00000033871. [Q8VHJ7-1]
DR GeneID; 170826; -.
DR KEGG; mmu:170826; -.
DR UCSC; uc008fbx.1; mouse. [Q8VHJ7-1]
DR UCSC; uc012bdq.1; mouse. [Q8VHJ7-2]
DR CTD; 133522; -.
DR MGI; MGI:2444934; Ppargc1b.
DR VEuPathDB; HostDB:ENSMUSG00000033871; -.
DR eggNOG; ENOG502QTA7; Eukaryota.
DR GeneTree; ENSGT00950000183137; -.
DR HOGENOM; CLU_014202_0_0_1; -.
DR InParanoid; Q8VHJ7; -.
DR OMA; PTKPCCH; -.
DR PhylomeDB; Q8VHJ7; -.
DR TreeFam; TF343068; -.
DR BioGRID-ORCS; 170826; 5 hits in 77 CRISPR screens.
DR ChiTaRS; Ppargc1b; mouse.
DR PRO; PR:Q8VHJ7; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8VHJ7; protein.
DR Bgee; ENSMUSG00000033871; Expressed in heart right ventricle and 222 other tissues.
DR Genevisible; Q8VHJ7; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016592; C:mediator complex; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0050682; F:AF-2 domain binding; ISS:UniProtKB.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; IMP:DFLAT.
DR GO; GO:0060346; P:bone trabecula formation; IMP:DFLAT.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IDA:DFLAT.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006390; P:mitochondrial transcription; IMP:DFLAT.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:DFLAT.
DR GO; GO:0001503; P:ossification; IMP:DFLAT.
DR GO; GO:0010694; P:positive regulation of alkaline phosphatase activity; IMP:DFLAT.
DR GO; GO:0045780; P:positive regulation of bone resorption; IMP:DFLAT.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IMP:DFLAT.
DR GO; GO:0042327; P:positive regulation of phosphorylation; IMP:DFLAT.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:DFLAT.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR CDD; cd12356; RRM_PPARGC1B; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034605; PGC-1.
DR InterPro; IPR034621; PGC-1beta.
DR InterPro; IPR034177; PPARGC1B_RRM.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR15528; PTHR15528; 1.
DR PANTHER; PTHR15528:SF12; PTHR15528:SF12; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Transcription;
KW Transcription regulation.
FT CHAIN 1..1014
FT /note="Peroxisome proliferator-activated receptor gamma
FT coactivator 1-beta"
FT /id="PRO_0000240159"
FT DOMAIN 893..967
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..91
FT /note="Abolishes DNA transcriptional activity when missing"
FT /evidence="ECO:0000250"
FT REGION 113..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 140..144
FT /note="LXXLL motif 1"
FT MOTIF 156..160
FT /note="LXXLL motif 2"
FT MOTIF 343..347
FT /note="LXXLL motif 3"
FT MOTIF 683..686
FT /note="HCFC1-binding-motif (HBM)"
FT COMPBIAS 165..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..448
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..817
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YN6"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YN6"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YN6"
FT VAR_SEQ 1..26
FT /note="MAGNDCGALLDEELSSFFLNYLSDTQ -> MKSSRPSSSTISLTRRSAEGLE
FT EVDHEALDRDGCGRRRLADM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019302"
FT CONFLICT 55
FT /note="A -> P (in Ref. 3; BAC25964)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="K -> R (in Ref. 3; BAC25964)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1014 AA; 112075 MW; 004BCB7797EAFD1F CRC64;
MAGNDCGALL DEELSSFFLN YLSDTQGGDS GEEQLCADLP ELDLSQLDAS DFDSATCFGE
LQWCPETSET EPSQYSPDDS ELFQIDSENE ALLAALTKTL DDIPEDDVGL AAFPELDEGD
TPSCTPASPA PLSAPPSPTL ERLLSPASDV DELSLLQKLL LATSSPTASS DALKDGATWS
QTSLSSRSQR PCVKVDGTQD KKTPTLRAQS RPCTELHKHL TSVLPCPRVK ACSPTPHPSP
RLLSKEEEEE VGEDCPSPWP TPASPQDSLA QDTASPDSAQ PPEEDVRAMV QLIRYMHTYC
LPQRKLPQRA PEPIPQACSS LSRQVQPRSR HPPKAFWTEF SILRELLAQD ILCDVSKPYR
LAIPVYASLT PQSRPRPPKD SQASPAHSAM AEEVRITASP KSTGPRPSLR PLRLEVKRDV
NKPTRQKREE DEEEEEEEEE EEEEKEEEEE EWGRKRPGRG LPWTKLGRKM DSSVCPVRRS
RRLNPELGPW LTFTDEPLGA LPSMCLDTET HNLEEDLGSL TDSSQGRQLP QGSQIPALES
PCESGCGDTD EDPSCPQPTS RDSSRCLMLA LSQSDSLGKK SFEESLTVEL CGTAGLTPPT
TPPYKPMEED PFKPDTKLSP GQDTAPSLPS PEALPLTATP GASHKLPKRH PERSELLSHL
QHATTQPVSQ AGQKRPFSCS FGDHDYCQVL RPEAALQRKV LRSWEPIGVH LEDLAQQGAP
LPTETKAPRR EANQNCDPTH KDSMQLRDHE IRASLTKHFG LLETALEGED LASCKSPEYD
TVFEDSSSSS GESSFLLEEE EEEEEGGEED DEGEDSGVSP PCSDHCPYQS PPSKASRQLC
SRSRSSSGSS SCSSWSPATR KNFRRESRGP CSDGTPSVRH ARKRREKAIG EGRVVYIRNL
SSDMSSRELK KRFEVFGEIV ECQVLTRSKR GQKHGFITFR CSEHAALSVR NGATLRKRNE
PSFHLSYGGL RHFRWPRYTD YDPTSEESLP SSGKSKYEAM DFDSLLKEAQ QSLH
