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   24-JAN-2024, entry version 156.
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; 10090-ENSMUSP00000074771; -.
DR   ProteomicsDB; 291589; -. [Q8VHJ7-1]
DR   ProteomicsDB; 291590; -. [Q8VHJ7-2]
DR   Antibodypedia; 27863; 154 antibodies from 30 providers.
DR   DNASU; 170826; -.
DR   Ensembl; ENSMUST00000063307.6; ENSMUSP00000069431.6; ENSMUSG00000033871.15. [Q8VHJ7-2]
DR   Ensembl; ENSMUST00000075299.13; ENSMUSP00000074771.7; ENSMUSG00000033871.15. [Q8VHJ7-1]
DR   GeneID; 170826; -.
DR   KEGG; mmu:170826; -.
DR   UCSC; uc008fbx.1; mouse. [Q8VHJ7-1]
DR   UCSC; uc012bdq.1; mouse. [Q8VHJ7-2]
DR   AGR; MGI:2444934; -.
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; EPTKPCC; -.
DR   OrthoDB; 3134278at2759; -.
DR   PhylomeDB; Q8VHJ7; -.
DR   TreeFam; TF343068; -.
DR   BioGRID-ORCS; 170826; 5 hits in 82 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 223 other cell types or tissues.
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 DNA-templated transcription; 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:0045893; P:positive regulation of DNA-templated transcription; IMP:DFLAT.
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:0006355; P:regulation of DNA-templated transcription; ISS:UniProtKB.
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; IPR034177; PPARGC1B_RRM.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR15528; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1 PGC-1 -RELATED; 1.
DR   PANTHER; PTHR15528:SF12; PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA COACTIVATOR 1-BETA; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   Genevisible; Q8VHJ7; MM.
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
//