PHR1_ARATH
ID PHR1_ARATH Reviewed; 409 AA.
AC Q94CL7; Q9M0H0;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Protein PHOSPHATE STARVATION RESPONSE 1 {ECO:0000303|PubMed:11511543};
DE Short=AtPHR1 {ECO:0000303|PubMed:11511543};
GN Name=PHR1 {ECO:0000303|PubMed:11511543};
GN OrderedLocusNames=At4g28610 {ECO:0000312|Araport:AT4G28610};
GN ORFNames=T5F17.60 {ECO:0000312|EMBL:CAB81449.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, INDUCTION BY PHOSPHATE, GENE
RP FAMILY, AND SUBCELLULAR LOCATION.
RX PubMed=11511543; DOI=10.1101/gad.204401;
RA Rubio V., Linhares F., Solano R., Martin A.C., Iglesias J., Leyva A.,
RA Paz-Ares J.;
RT "A conserved MYB transcription factor involved in phosphate starvation
RT signaling both in vascular plants and in unicellular algae.";
RL Genes Dev. 15:2122-2133(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP SUMOYLATION.
RX PubMed=15894620; DOI=10.1073/pnas.0500778102;
RA Miura K., Rus A., Sharkhuu A., Yokoi S., Karthikeyan A.S., Raghothama K.G.,
RA Baek D., Koo Y.D., Jin J.B., Bressan R.A., Yun D.-J., Hasegawa P.M.;
RT "The Arabidopsis SUMO E3 ligase SIZ1 controls phosphate deficiency
RT responses.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:7760-7765(2005).
RN [6]
RP FUNCTION.
RX PubMed=17643101; DOI=10.1038/ng2079;
RA Franco-Zorrilla J.M., Valli A., Todesco M., Mateos I., Puga M.I.,
RA Rubio-Somoza I., Leyva A., Weigel D., Garcia J.A., Paz-Ares J.;
RT "Target mimicry provides a new mechanism for regulation of microRNA
RT activity.";
RL Nat. Genet. 39:1033-1037(2007).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17927693; DOI=10.1111/j.1365-3040.2007.01734.x;
RA Nilsson L., Mueller R., Nielsen T.H.;
RT "Increased expression of the MYB-related transcription factor, PHR1, leads
RT to enhanced phosphate uptake in Arabidopsis thaliana.";
RL Plant Cell Environ. 30:1499-1512(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [10]
RP FUNCTION, AND SUBUNIT.
RX PubMed=20838596; DOI=10.1371/journal.pgen.1001102;
RA Bustos R., Castrillo G., Linhares F., Puga M.I., Rubio V., Perez-Perez J.,
RA Solano R., Leyva A., Paz-Ares J.;
RT "A central regulatory system largely controls transcriptional activation
RT and repression responses to phosphate starvation in Arabidopsis.";
RL PLoS Genet. 6:E1001102-E1001102(2010).
RN [11]
RP FUNCTION.
RX PubMed=21261953; DOI=10.1186/1471-2229-11-19;
RA Rouached H., Secco D., Arpat B., Poirier Y.;
RT "The transcription factor PHR1 plays a key role in the regulation of
RT sulfate shoot-to-root flux upon phosphate starvation in Arabidopsis.";
RL BMC Plant Biol. 11:19-19(2011).
RN [12]
RP FUNCTION.
RX PubMed=21910737; DOI=10.1111/j.1399-3054.2011.01520.x;
RA Nilsson L., Lundmark M., Jensen P.E., Nielsen T.H.;
RT "The Arabidopsis transcription factor PHR1 is essential for adaptation to
RT high light and retaining functional photosynthesis during phosphate
RT starvation.";
RL Physiol. Plantarum 144:35-47(2012).
RN [13]
RP FUNCTION.
RX PubMed=23788639; DOI=10.1074/jbc.m113.482281;
RA Bournier M., Tissot N., Mari S., Boucherez J., Lacombe E., Briat J.F.,
RA Gaymard F.;
RT "Arabidopsis ferritin 1 (AtFer1) gene regulation by the phosphate
RT starvation response 1 (AtPHR1) transcription factor reveals a direct
RT molecular link between iron and phosphate homeostasis.";
RL J. Biol. Chem. 288:22670-22680(2013).
RN [14]
RP FUNCTION.
RX PubMed=24420568; DOI=10.1093/jxb/ert444;
RA Khan G.A., Bouraine S., Wege S., Li Y., de Carbonnel M., Berthomieu P.,
RA Poirier Y., Rouached H.;
RT "Coordination between zinc and phosphate homeostasis involves the
RT transcription factor PHR1, the phosphate exporter PHO1, and its homologue
RT PHO1;H3 in Arabidopsis.";
RL J. Exp. Bot. 65:871-884(2014).
RN [15]
RP FUNCTION.
RX PubMed=24753539; DOI=10.1104/pp.114.237990;
RA Klecker M., Gasch P., Peisker H., Doermann P., Schlicke H., Grimm B.,
RA Mustroph A.;
RT "A Shoot-specific hypoxic response of Arabidopsis sheds light on the role
RT of the phosphate-responsive transcription factor PHOSPHATE STARVATION
RT RESPONSE1.";
RL Plant Physiol. 165:774-790(2014).
RN [16]
RP FUNCTION, AND INTERACTION WITH SPX1.
RX PubMed=25271326; DOI=10.1073/pnas.1404654111;
RA Puga M.I., Mateos I., Charukesi R., Wang Z., Franco-Zorrilla J.M.,
RA de Lorenzo L., Irigoyen M.L., Masiero S., Bustos R., Rodriguez J.,
RA Leyva A., Rubio V., Sommer H., Paz-Ares J.;
RT "SPX1 is a phosphate-dependent inhibitor of PHOSPHATE STARVATION RESPONSE 1
RT in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:14947-14952(2014).
RN [17]
RP FUNCTION.
RX PubMed=25680792; DOI=10.1093/jxb/eru535;
RA Pant B.D., Burgos A., Pant P., Cuadros-Inostroza A., Willmitzer L.,
RA Scheible W.R.;
RT "The transcription factor PHR1 regulates lipid remodeling and
RT triacylglycerol accumulation in Arabidopsis thaliana during phosphorus
RT starvation.";
RL J. Exp. Bot. 66:1907-1918(2015).
RN [18]
RP FUNCTION, AND LACK OF INTERACTION WITH PHL2 AND PHL3.
RX PubMed=26586833; DOI=10.1104/pp.15.01336;
RA Sun L., Song L., Zhang Y., Zheng Z., Liu D.;
RT "Arabidopsis PHL2 and PHR1 act redundantly as the key components of the
RT central regulatory system controlling transcriptional responses to
RT phosphate starvation.";
RL Plant Physiol. 170:499-514(2016).
CC -!- FUNCTION: Transcription factor involved in phosphate starvation
CC signaling (PubMed:11511543, PubMed:17927693, PubMed:26586833). Binds as
CC a dimer to P1BS, an imperfect palindromic sequence 5'-GNATATNC-3', to
CC promote the expression of inorganic phosphate (Pi) starvation-
CC responsive genes (PubMed:11511543, PubMed:20838596, PubMed:26586833).
CC SPX1 is a competitive inhibitor of this DNA-binding (PubMed:25271326).
CC PHR1 binding to its targets is low Pi-dependent (PubMed:25271326).
CC Regulates the expression of miR399 (PubMed:20838596). Regulates the
CC expression of IPS1 (At3g09922), a non-coding RNA that mimics the target
CC of miR399 to block the cleavage of PHO2 under Pi-deficient conditions
CC (PubMed:17643101). Regulates lipid remodeling and triacylglycerol
CC accumulation during phosphorus starvation (PubMed:25680792). Required
CC for the shoot-specific hypoxic response (PubMed:24753539). Regulates
CC FER1 expression upon phosphate starvation, linking iron and phosphate
CC homeostasis (PubMed:23788639). Contributes to the homeostasis of both
CC sulfate and phosphate in plants under phosphate deficiency
CC (PubMed:21261953). Required for adaptation to high light and retaining
CC functional photosynthesis during phosphate starvation
CC (PubMed:21910737). Involved in the coregulation of Zn and Pi
CC homeostasis (PubMed:24420568). {ECO:0000269|PubMed:11511543,
CC ECO:0000269|PubMed:17643101, ECO:0000269|PubMed:17927693,
CC ECO:0000269|PubMed:20838596, ECO:0000269|PubMed:21261953,
CC ECO:0000269|PubMed:21910737, ECO:0000269|PubMed:23788639,
CC ECO:0000269|PubMed:24420568, ECO:0000269|PubMed:24753539,
CC ECO:0000269|PubMed:25271326, ECO:0000269|PubMed:25680792,
CC ECO:0000269|PubMed:26586833}.
CC -!- SUBUNIT: Homodimers and heterodimers (PubMed:20838596,
CC PubMed:11511543). Interacts with SPX1 in a Pi-dependent manner
CC (PubMed:25271326). Does not interact with PHL2 or PHL3
CC (PubMed:26586833). {ECO:0000269|PubMed:11511543,
CC ECO:0000269|PubMed:25271326, ECO:0000269|PubMed:26586833}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11511543}. Note=The
CC localization to the nucleus is independent of the Pi status.
CC {ECO:0000269|PubMed:11511543}.
CC -!- INDUCTION: Only moderately up-regulated by Pi starvation.
CC {ECO:0000269|PubMed:11511543}.
CC -!- PTM: Sumoylated by SIZ1. Sumoylation controls phosphate deficiency
CC responses. {ECO:0000269|PubMed:15894620}.
CC -!- DISRUPTION PHENOTYPE: Strongly reduced shoot growth, and slightly
CC increased root growth. Reduced expression of phosphate starvation-
CC induced (PSI) genes, decreased cellular inorganic phosphate (Pi)
CC content and shoot-to-root ratio, and impaired anthocyanin accumulation
CC (PubMed:17927693). {ECO:0000269|PubMed:17927693}.
CC -!- SIMILARITY: Belongs to the MYB-CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB81449.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ310799; CAC59689.1; -; mRNA.
DR EMBL; AL161573; CAB81449.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85512.1; -; Genomic_DNA.
DR EMBL; AY081290; AAL91179.1; -; mRNA.
DR EMBL; BT002187; AAN72198.1; -; mRNA.
DR PIR; T10655; T10655.
DR RefSeq; NP_194590.2; NM_119003.4.
DR PDB; 6J4K; X-ray; 1.58 A; A/B=224-283.
DR PDB; 6J4R; X-ray; 2.80 A; A/B/C/D=225-282.
DR PDB; 6J5B; X-ray; 2.70 A; A/C/D/F/H/J=224-283.
DR PDB; 6TO5; X-ray; 2.38 A; AAAA/AAAB=280-359.
DR PDB; 6TO9; X-ray; 2.45 A; AAAA/AAAB=280-359.
DR PDB; 6TOC; X-ray; 1.85 A; AAA/BBB=280-359.
DR PDBsum; 6J4K; -.
DR PDBsum; 6J4R; -.
DR PDBsum; 6J5B; -.
DR PDBsum; 6TO5; -.
DR PDBsum; 6TO9; -.
DR PDBsum; 6TOC; -.
DR AlphaFoldDB; Q94CL7; -.
DR SMR; Q94CL7; -.
DR STRING; 3702.AT4G28610.1; -.
DR iPTMnet; Q94CL7; -.
DR PaxDb; Q94CL7; -.
DR PRIDE; Q94CL7; -.
DR ProteomicsDB; 234721; -.
DR EnsemblPlants; AT4G28610.1; AT4G28610.1; AT4G28610.
DR GeneID; 828979; -.
DR Gramene; AT4G28610.1; AT4G28610.1; AT4G28610.
DR KEGG; ath:AT4G28610; -.
DR Araport; AT4G28610; -.
DR TAIR; locus:2139865; AT4G28610.
DR eggNOG; ENOG502QXMH; Eukaryota.
DR HOGENOM; CLU_044541_2_1_1; -.
DR InParanoid; Q94CL7; -.
DR OMA; SDWPEWA; -.
DR OrthoDB; 812231at2759; -.
DR PhylomeDB; Q94CL7; -.
DR PRO; PR:Q94CL7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94CL7; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0071486; P:cellular response to high light intensity; IMP:TAIR.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IMP:TAIR.
DR GO; GO:0007623; P:circadian rhythm; IEP:TAIR.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:1903842; P:response to arsenite ion; IMP:TAIR.
DR GO; GO:0055063; P:sulfate ion homeostasis; IMP:TAIR.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR025756; Myb_CC_LHEQLE.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR006447; Myb_dom_plants.
DR InterPro; IPR044848; PHR1-like.
DR PANTHER; PTHR31314; PTHR31314; 1.
DR Pfam; PF14379; Myb_CC_LHEQLE; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR TIGRFAMs; TIGR01557; myb_SHAQKYF; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..409
FT /note="Protein PHOSPHATE STARVATION RESPONSE 1"
FT /id="PRO_0000436713"
FT DOMAIN 222..282
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 253..278
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 314..334
FT /evidence="ECO:0000255"
FT MOTIF 327..332
FT /note="LHEQLE"
FT /evidence="ECO:0000305"
FT COMPBIAS 12..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT HELIX 232..244
FT /evidence="ECO:0007829|PDB:6J4K"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:6J4K"
FT HELIX 253..260
FT /evidence="ECO:0007829|PDB:6J4K"
FT HELIX 267..279
FT /evidence="ECO:0007829|PDB:6J4K"
SQ SEQUENCE 409 AA; 45546 MW; 2C59836D75FE33C3 CRC64;
MEARPVHRSG SRDLTRTSSI PSTQKPSPVE DSFMRSDNNS QLMSRPLGQT YHLLSSSNGG
AVGHICSSSS SGFATNLHYS TMVSHEKQQH YTGSSSNNAV QTPSNNDSAW CHDSLPGGFL
DFHETNPAIQ NNCQIEDGGI AAAFDDIQKR SDWHEWADHL ITDDDPLMST NWNDLLLETN
SNSDSKDQKT LQIPQPQIVQ QQPSPSVELR PVSTTSSNSN NGTGKARMRW TPELHEAFVE
AVNSLGGSER ATPKGVLKIM KVEGLTIYHV KSHLQKYRTA RYRPEPSETG SPERKLTPLE
HITSLDLKGG IGITEALRLQ MEVQKQLHEQ LEIQRNLQLR IEEQGKYLQM MFEKQNSGLT
KGTASTSDSA AKSEQEDKKT ADSKEVPEEE TRKCEELESP QPKRPKIDN
