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 27-MAR-2024, entry version 168. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.Q94CL7; -. DR iPTMnet; Q94CL7; -. DR PaxDb; 3702-AT4G28610-1; -. 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; AT4G28610; PHR1. DR eggNOG; ENOG502QXMH; Eukaryota. DR HOGENOM; CLU_044541_2_1_1; -. DR InParanoid; Q94CL7; -. DR OMA; SDWPEWA; -. DR OrthoDB; 5491517at2759; -. 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:0006355; P:regulation of DNA-templated transcription; TAS:TAIR. DR GO; GO:0034765; P:regulation of monoatomic ion transmembrane transport; IMP:TAIR. DR GO; GO:1903842; P:response to arsenite ion; IMP:TAIR. DR GO; GO:0055063; P:sulfate ion homeostasis; IMP:TAIR. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. 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; IPR046955; PHR1-like. DR InterPro; IPR001005; SANT/Myb. DR NCBIfam; TIGR01557; myb_SHAQKYF; 1. DR PANTHER; PTHR31314; MYB FAMILY TRANSCRIPTION FACTOR PHL7-LIKE; 1. DR PANTHER; PTHR31314:SF21; PROTEIN PHOSPHATE STARVATION RESPONSE 1; 1. DR Pfam; PF14379; Myb_CC_LHEQLE; 1. DR Pfam; PF00249; Myb_DNA-binding; 1. DR SUPFAM; SSF46689; Homeodomain-like; 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 //