P2C57_ARATH
ID P2C57_ARATH Reviewed; 388 AA.
AC P49599; Q3E9V3; Q3E9V4; Q9M0J6; Q9STP6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Protein phosphatase 2C 57 {ECO:0000303|PubMed:19021904};
DE Short=AtPP2C57 {ECO:0000303|PubMed:19021904};
DE EC=3.1.3.16 {ECO:0000269|PubMed:20126264};
DE AltName: Full=Protein phosphatase 2C PPH1 {ECO:0000303|PubMed:15130549};
DE Short=PP2C PPH1 {ECO:0000303|PubMed:15130549};
DE AltName: Full=Thylakoid-associated phosphatase of 38 kDa {ECO:0000303|PubMed:20126264};
GN Name=PPH1 {ECO:0000303|PubMed:15130549};
GN Synonyms=PP2C57 {ECO:0000303|PubMed:19021904},
GN TAP38 {ECO:0000303|PubMed:20126264};
GN OrderedLocusNames=At4g27800 {ECO:0000312|Araport:AT4G27800};
GN ORFNames=T27E11.40 {ECO:0000312|EMBL:CAB43968.1};
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-365 (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=7569999; DOI=10.1126/science.270.5235.467;
RA Schena M., Shalon D., Davis R.W., Brown P.O.;
RT "Quantitative monitoring of gene expression patterns with a complementary
RT DNA microarray.";
RL Science 270:467-470(1995).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15130549; DOI=10.1016/j.tplants.2004.03.007;
RA Schweighofer A., Hirt H., Meskiene I.;
RT "Plant PP2C phosphatases: emerging functions in stress signaling.";
RL Trends Plant Sci. 9:236-243(2004).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19021904; DOI=10.1186/1471-2164-9-550;
RA Xue T., Wang D., Zhang S., Ehlting J., Ni F., Jacab S., Zheng C., Zhong Y.;
RT "Genome-wide and expression analysis of protein phosphatase 2C in rice and
RT Arabidopsis.";
RL BMC Genomics 9:550-550(2008).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20126264; DOI=10.1371/journal.pbio.1000288;
RA Pribil M., Pesaresi P., Hertle A., Barbato R., Leister D.;
RT "Role of plastid protein phosphatase TAP38 in LHCII dephosphorylation and
RT thylakoid electron flow.";
RL PLoS Biol. 8:e1000288-e1000288(2010).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20176943; DOI=10.1073/pnas.0913810107;
RA Shapiguzov A., Ingelsson B., Samol I., Andres C., Kessler F., Rochaix J.D.,
RA Vener A.V., Goldschmidt-Clermont M.;
RT "The PPH1 phosphatase is specifically involved in LHCII dephosphorylation
RT and state transitions in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:4782-4787(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 59-351 IN COMPLEX WITH MANGANESE
RP IONS.
RX PubMed=25888588; DOI=10.1105/tpc.15.00102;
RA Wei X., Guo J., Li M., Liu Z.;
RT "Structural mechanism underlying the specific recognition between the
RT Arabidopsis state-transition phosphatase TAP38/PPH1 and phosphorylated
RT light-harvesting complex protein Lhcb1.";
RL Plant Cell 27:1113-1127(2015).
CC -!- FUNCTION: [Isoform 2]: Protein phosphatase specifically required for
CC efficient dephosphorylation of the light-harvesting complex II outer
CC antennae (LCHII) and transition from state 2 to state 1
CC (PubMed:20176943, PubMed:20126264). State transition plays a central
CC role in response to environmental changes and allows to adjust to
CC changing light conditions via the redistribution of light excitation
CC energy between photosystem II (PSII) and photosystem I (PSI) in a short
CC time by relocating LHCII proteins (Probable). Mainly responsible for
CC the dephosphorylation of Lhcb1 and Lhcb2 but not of the photosystem II
CC core proteins (PubMed:20176943). {ECO:0000269|PubMed:20126264,
CC ECO:0000269|PubMed:20176943, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:20126264};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630;
CC Evidence={ECO:0000269|PubMed:20126264};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:20126264};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47005;
CC Evidence={ECO:0000269|PubMed:20126264};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:25888588};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:25888588};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000269|PubMed:25888588};
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane {ECO:0000255}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:20176943}. Note=Associates with the stroma lamellae
CC of the thylakoid membranes. {ECO:0000269|PubMed:20176943}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P49599-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49599-2; Sequence=VSP_034837, VSP_034838;
CC Name=3;
CC IsoId=P49599-3; Sequence=VSP_034835, VSP_034836;
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA92889.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB43968.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL078579; CAB43968.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161571; CAB81429.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85393.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85394.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85395.1; -; Genomic_DNA.
DR EMBL; AY080875; AAL87346.1; -; mRNA.
DR EMBL; AY114060; AAM45108.1; -; mRNA.
DR EMBL; U34803; AAA92889.1; ALT_FRAME; mRNA.
DR PIR; C85323; C85323.
DR PIR; T09019; T09019.
DR RefSeq; NP_194509.1; NM_118918.5. [P49599-1]
DR RefSeq; NP_849459.1; NM_179128.2. [P49599-2]
DR RefSeq; NP_849460.1; NM_179129.1. [P49599-3]
DR PDB; 4YZG; X-ray; 1.60 A; A/B=59-351.
DR PDB; 4YZH; X-ray; 2.00 A; A=59-351.
DR PDBsum; 4YZG; -.
DR PDBsum; 4YZH; -.
DR AlphaFoldDB; P49599; -.
DR SMR; P49599; -.
DR STRING; 3702.AT4G27800.1; -.
DR PaxDb; P49599; -.
DR PRIDE; P49599; -.
DR ProteomicsDB; 248723; -. [P49599-1]
DR EnsemblPlants; AT4G27800.1; AT4G27800.1; AT4G27800. [P49599-1]
DR EnsemblPlants; AT4G27800.2; AT4G27800.2; AT4G27800. [P49599-2]
DR EnsemblPlants; AT4G27800.3; AT4G27800.3; AT4G27800. [P49599-3]
DR GeneID; 828893; -.
DR Gramene; AT4G27800.1; AT4G27800.1; AT4G27800. [P49599-1]
DR Gramene; AT4G27800.2; AT4G27800.2; AT4G27800. [P49599-2]
DR Gramene; AT4G27800.3; AT4G27800.3; AT4G27800. [P49599-3]
DR KEGG; ath:AT4G27800; -.
DR Araport; AT4G27800; -.
DR TAIR; locus:2137400; AT4G27800.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_1_0_1; -.
DR InParanoid; P49599; -.
DR OMA; AWCHASA; -.
DR OrthoDB; 1044139at2759; -.
DR PhylomeDB; P49599; -.
DR PRO; PR:P49599; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P49599; baseline and differential.
DR Genevisible; P49599; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; IDA:TAIR.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; IDA:TAIR.
DR GO; GO:0016311; P:dephosphorylation; IMP:TAIR.
DR GO; GO:0009767; P:photosynthetic electron transport chain; IMP:TAIR.
DR GO; GO:0080005; P:photosystem stoichiometry adjustment; IMP:TAIR.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chloroplast; Hydrolase; Magnesium;
KW Manganese; Membrane; Metal-binding; Plastid; Protein phosphatase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..388
FT /note="Protein phosphatase 2C 57"
FT /id="PRO_0000057768"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 59..348
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 93
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25888588,
FT ECO:0007744|PDB:4YZG"
FT BINDING 93
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25888588,
FT ECO:0007744|PDB:4YZG"
FT BINDING 94
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25888588,
FT ECO:0007744|PDB:4YZG"
FT BINDING 296
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25888588,
FT ECO:0007744|PDB:4YZG"
FT BINDING 339
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25888588,
FT ECO:0007744|PDB:4YZG"
FT VAR_SEQ 323..326
FT /note="LACE -> ATCL (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_034835"
FT VAR_SEQ 327..388
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_034836"
FT VAR_SEQ 334..335
FT /note="DR -> VK (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034837"
FT VAR_SEQ 336..388
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034838"
FT CONFLICT 1..4
FT /note="MALL -> SNSS (in Ref. 4; AAA92889)"
FT /evidence="ECO:0000305"
FT CONFLICT 69..70
FT /note="RD -> QY (in Ref. 4; AAA92889)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="D -> N (in Ref. 4; AAA92889)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="W -> C (in Ref. 4; AAA92889)"
FT /evidence="ECO:0000305"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:4YZG"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:4YZG"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:4YZG"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:4YZG"
FT STRAND 86..98
FT /evidence="ECO:0007829|PDB:4YZG"
FT HELIX 99..115
FT /evidence="ECO:0007829|PDB:4YZG"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:4YZG"
FT HELIX 127..151
FT /evidence="ECO:0007829|PDB:4YZG"
FT STRAND 160..169
FT /evidence="ECO:0007829|PDB:4YZG"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:4YZG"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:4YZG"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:4YZG"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:4YZG"
FT HELIX 205..216
FT /evidence="ECO:0007829|PDB:4YZG"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:4YZG"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:4YZG"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:4YZG"
FT HELIX 245..254
FT /evidence="ECO:0007829|PDB:4YZG"
FT HELIX 260..264
FT /evidence="ECO:0007829|PDB:4YZG"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:4YZG"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:4YZG"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:4YZG"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:4YZG"
FT HELIX 304..318
FT /evidence="ECO:0007829|PDB:4YZG"
FT HELIX 321..334
FT /evidence="ECO:0007829|PDB:4YZG"
FT STRAND 341..347
FT /evidence="ECO:0007829|PDB:4YZG"
SQ SEQUENCE 388 AA; 42719 MW; 496ECCC786AEB802 CRC64;
MALLRPHLHR FHSNTLRHSA YPSADAGGGL VVYPTYGRHR CSAIAIDAPS SLTGVTPIRW
GYTSVQGFRD EMEDDIVIRS DAVDSFSYAA VFDGHAGSSS VKFLREELYK ECVGALQAGS
LLNGGDFAAI KEALIKAFES VDRNLLKWLE ANGDEEDESG STATVMIIRN DVSFIAHIGD
SCAVLSRSGQ IEELTDYHRP YGSSRAAIQE VKRVKEAGGW IVNGRICGDI AVSRAFGDIR
FKTKKNDMLK KGVDEGRWSE KFVSRIEFKG DMVVATPDIF QVPLTSDVEF IILASDGLWD
YMKSSDVVSY VRDQLRKHGN VQLACESLAQ VALDRRSQDN ISIIIADLGR TEWKNLPAQR
QNVVVELVQA ATTIGLVTVG IWMSSHLS
