RBL_ARATH
ID RBL_ARATH Reviewed; 479 AA.
AC O03042;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Ribulose bisphosphate carboxylase large chain {ECO:0000255|HAMAP-Rule:MF_01338};
DE Short=RuBisCO large subunit {ECO:0000255|HAMAP-Rule:MF_01338};
DE EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01338};
DE Flags: Precursor;
GN Name=rbcL {ECO:0000255|HAMAP-Rule:MF_01338}; OrderedLocusNames=AtCg00490;
OS Arabidopsis thaliana (Mouse-ear cress).
OG Plastid; Chloroplast.
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 [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RA Zhu G., Jensen R.G., Bohnert H.J.;
RT "DNA sequence of ribulose-1,5-bisphosphate carboxylase/oxygenase large
RT subunit from Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR97-074(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10574454; DOI=10.1093/dnares/6.5.283;
RA Sato S., Nakamura Y., Kaneko T., Asamizu E., Tabata S.;
RT "Complete structure of the chloroplast genome of Arabidopsis thaliana.";
RL DNA Res. 6:283-290(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49.
RC STRAIN=cv. Columbia;
RX PubMed=9193094; DOI=10.1104/pp.114.2.623;
RA Isono K., Niwa Y., Satoh K., Kobayashi H.;
RT "Evidence for transcriptional regulation of plastid photosynthesis genes in
RT Arabidopsis thaliana roots.";
RL Plant Physiol. 114:623-630(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-446.
RA Tsukaya H., Ikeda H., Yokoyama J., Matsuura K., Kuroiwa H., Kuroiwa T.,
RA Iwatsuki K.;
RT "Morphological, physiological and molecular genetic characterization of
RT Arabidopsis himalaica, with reference to the analogous features of A.
RT thaliana.";
RL J. Plant Res. 110:15-23(1997).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Wassilewskija;
RX PubMed=12766230; DOI=10.1074/mcp.m300030-mcp200;
RA Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M.,
RA Garin J., Joyard J., Rolland N.;
RT "Proteomics of the chloroplast envelope membranes from Arabidopsis
RT thaliana.";
RL Mol. Cell. Proteomics 2:325-345(2003).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-330, 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 [8]
RP INTERACTION WITH RBCX1 AND RBCX2.
RX PubMed=21922322; DOI=10.1007/s11103-011-9823-8;
RA Kolesinski P., Piechota J., Szczepaniak A.;
RT "Initial characteristics of RbcX proteins from Arabidopsis thaliana.";
RL Plant Mol. Biol. 77:447-459(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT PRO-3, CLEAVAGE OF PROPEPTIDE [LARGE
RP SCALE ANALYSIS] AFTER SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [11]
RP INTERACTION WITH ABSCISIC ACID.
RX PubMed=26197050; DOI=10.1371/journal.pone.0133033;
RA Galka M.M., Rajagopalan N., Buhrow L.M., Nelson K.M., Switala J.,
RA Cutler A.J., Palmer D.R., Loewen P.C., Abrams S.R., Loewen M.C.;
RT "Identification of Interactions between Abscisic Acid and Ribulose-1,5-
RT Bisphosphate Carboxylase/Oxygenase.";
RL PLoS ONE 10:e0133033-e0133033(2015).
RN [12]
RP INTERACTION WITH BSD2.
RX PubMed=29217567; DOI=10.1126/science.aap9221;
RA Aigner H., Wilson R.H., Bracher A., Calisse L., Bhat J.Y., Hartl F.U.,
RA Hayer-Hartl M.;
RT "Plant RuBisCo assembly in E. coli with five chloroplast chaperones
RT including BSD2.";
RL Science 358:1272-1278(2017).
RN [13] {ECO:0007744|PDB:5IU0}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH TRANSITION-STATE
RP ANALOG 2-CABP AND MAGNESIUM ION, SUBUNIT, AND CARBOXYLATION AT LYS-201.
RX PubMed=29372894; DOI=10.1107/s2059798317017132;
RA Valegaard K., Hasse D., Andersson I., Gunn L.H.;
RT "Structure of Rubisco from Arabidopsis thaliana in complex with 2-
RT carboxyarabinitol-1,5-bisphosphate.";
RL Acta Crystallogr. D 74:1-9(2018).
CC -!- FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-
CC ribulose 1,5-bisphosphate, the primary event in carbon dioxide
CC fixation, as well as the oxidative fragmentation of the pentose
CC substrate in the photorespiration process. Both reactions occur
CC simultaneously and in competition at the same active site (Probable).
CC Binds to abscisic acid (ABA) (PubMed:26197050).
CC {ECO:0000269|PubMed:26197050, ECO:0000305|PubMed:29372894}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-
CC bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870,
CC ChEBI:CHEBI:58272; EC=4.1.1.39; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01338, ECO:0000305|PubMed:29372894};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate +
CC 2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033,
CC ChEBI:CHEBI:58272; Evidence={ECO:0000255|HAMAP-Rule:MF_01338,
CC ECO:0000305|PubMed:29372894};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01338,
CC ECO:0000269|PubMed:29372894};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01338,
CC ECO:0000269|PubMed:29372894};
CC -!- SUBUNIT: Heterohexadecamer of 8 large chains and 8 small chains;
CC disulfide-linked. The disulfide link is formed within the large subunit
CC homodimers (PubMed:29372894). Interacts with RBCX1 and RBCX1
CC (PubMed:21922322). An intermediate complex made of eight RbcL subunits
CC interacts with the chaperone BSD2 (PubMed:29217567).
CC {ECO:0000269|PubMed:21922322, ECO:0000269|PubMed:29217567,
CC ECO:0000269|PubMed:29372894}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_01338, ECO:0000269|PubMed:12766230}.
CC -!- PTM: The disulfide bond which can form in the large chain dimeric
CC partners within the hexadecamer appears to be associated with oxidative
CC stress and protein turnover. {ECO:0000255|HAMAP-Rule:MF_01338}.
CC -!- MISCELLANEOUS: The basic functional RuBisCO is composed of a large
CC chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO
CC this homodimer is arranged in a barrel-like tetramer with the small
CC subunits forming a tetrameric 'cap' on each end of the 'barrel'.
CC {ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000269|PubMed:29372894}.
CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type I
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01338}.
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DR EMBL; U91966; AAB68400.1; -; Genomic_DNA.
DR EMBL; AP000423; BAA84393.1; -; Genomic_DNA.
DR EMBL; AB003522; BAA20946.1; -; Genomic_DNA.
DR EMBL; D88901; BAA19595.1; -; Genomic_DNA.
DR RefSeq; NP_051067.1; NC_000932.1.
DR PDB; 5IU0; X-ray; 1.50 A; A/B=1-479.
DR PDBsum; 5IU0; -.
DR AlphaFoldDB; O03042; -.
DR SMR; O03042; -.
DR BioGRID; 29958; 11.
DR IntAct; O03042; 2.
DR MINT; O03042; -.
DR STRING; 3702.ATCG00490.1; -.
DR iPTMnet; O03042; -.
DR SWISS-2DPAGE; O03042; -.
DR PaxDb; O03042; -.
DR PRIDE; O03042; -.
DR ProteomicsDB; 236513; -.
DR EnsemblPlants; ATCG00490.1; ATCG00490.1; ATCG00490.
DR GeneID; 844754; -.
DR Gramene; ATCG00490.1; ATCG00490.1; ATCG00490.
DR KEGG; ath:ArthCp030; -.
DR Araport; ATCG00490; -.
DR TAIR; locus:504954672; ATCG00490.
DR eggNOG; ENOG502QTI9; Eukaryota.
DR HOGENOM; CLU_031450_2_0_1; -.
DR InParanoid; O03042; -.
DR OMA; EYRETYW; -.
DR OrthoDB; 474428at2759; -.
DR BioCyc; ARA:ATCG00490-MON; -.
DR BioCyc; MetaCyc:ATCG00490-MON; -.
DR BRENDA; 4.1.1.39; 399.
DR PRO; PR:O03042; -.
DR Proteomes; UP000006548; Chloroplast.
DR ExpressionAtlas; O03042; baseline and differential.
DR Genevisible; O03042; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009853; P:photorespiration; IEA:UniProtKB-KW.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
DR CDD; cd08212; RuBisCO_large_I; 1.
DR Gene3D; 3.20.20.110; -; 1.
DR Gene3D; 3.30.70.150; -; 1.
DR HAMAP; MF_01338; RuBisCO_L_type1; 1.
DR InterPro; IPR033966; RuBisCO.
DR InterPro; IPR020878; RuBisCo_large_chain_AS.
DR InterPro; IPR000685; RuBisCO_lsu_C.
DR InterPro; IPR036376; RuBisCO_lsu_C_sf.
DR InterPro; IPR017443; RuBisCO_lsu_fd_N.
DR InterPro; IPR036422; RuBisCO_lsu_N_sf.
DR InterPro; IPR020888; RuBisCO_lsuI.
DR PANTHER; PTHR42704; PTHR42704; 1.
DR Pfam; PF00016; RuBisCO_large; 1.
DR Pfam; PF02788; RuBisCO_large_N; 1.
DR SFLD; SFLDS00014; RuBisCO; 1.
DR SUPFAM; SSF51649; SSF51649; 1.
DR SUPFAM; SSF54966; SSF54966; 1.
DR PROSITE; PS00157; RUBISCO_LARGE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calvin cycle; Carbon dioxide fixation;
KW Chloroplast; Disulfide bond; Lyase; Magnesium; Metal-binding;
KW Monooxygenase; Oxidoreductase; Phosphoprotein; Photorespiration;
KW Photosynthesis; Plastid; Reference proteome.
FT PROPEP 1..2
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338,
FT ECO:0007744|PubMed:22223895"
FT /id="PRO_0000031119"
FT CHAIN 3..479
FT /note="Ribulose bisphosphate carboxylase large chain"
FT /id="PRO_0000031120"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT ACT_SITE 294
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29372894,
FT ECO:0007744|PDB:5IU0"
FT BINDING 123
FT /ligand="substrate"
FT /note="in homodimeric partner"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338,
FT ECO:0000269|PubMed:29372894, ECO:0007744|PDB:5IU0"
FT BINDING 173..177
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29372894,
FT ECO:0007744|PDB:5IU0"
FT BINDING 201..204
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29372894,
FT ECO:0007744|PDB:5IU0"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338,
FT ECO:0000269|PubMed:29372894, ECO:0007744|PDB:5IU0"
FT BINDING 203
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338,
FT ECO:0000269|PubMed:29372894, ECO:0007744|PDB:5IU0"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338,
FT ECO:0000269|PubMed:29372894, ECO:0007744|PDB:5IU0"
FT BINDING 294..295
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29372894,
FT ECO:0007744|PDB:5IU0"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338,
FT ECO:0000269|PubMed:29372894, ECO:0007744|PDB:5IU0"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29372894,
FT ECO:0007744|PDB:5IU0"
FT BINDING 379..381
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29372894,
FT ECO:0007744|PDB:5IU0"
FT SITE 334
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT MOD_RES 3
FT /note="N-acetylproline"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 201
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338,
FT ECO:0000269|PubMed:29372894, ECO:0007744|PDB:5IU0"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT MOD_RES 330
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT DISULFID 247
FT /note="Interchain; in linked form"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01338"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:5IU0"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:5IU0"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:5IU0"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:5IU0"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:5IU0"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:5IU0"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:5IU0"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:5IU0"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:5IU0"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:5IU0"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:5IU0"
FT STRAND 130..139
FT /evidence="ECO:0007829|PDB:5IU0"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:5IU0"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:5IU0"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:5IU0"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:5IU0"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:5IU0"
FT HELIX 182..193
FT /evidence="ECO:0007829|PDB:5IU0"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:5IU0"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:5IU0"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:5IU0"
FT HELIX 214..232
FT /evidence="ECO:0007829|PDB:5IU0"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:5IU0"
FT HELIX 247..260
FT /evidence="ECO:0007829|PDB:5IU0"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:5IU0"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:5IU0"
FT HELIX 274..287
FT /evidence="ECO:0007829|PDB:5IU0"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:5IU0"
FT HELIX 298..302
FT /evidence="ECO:0007829|PDB:5IU0"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:5IU0"
FT HELIX 311..321
FT /evidence="ECO:0007829|PDB:5IU0"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:5IU0"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:5IU0"
FT HELIX 339..350
FT /evidence="ECO:0007829|PDB:5IU0"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:5IU0"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:5IU0"
FT STRAND 375..381
FT /evidence="ECO:0007829|PDB:5IU0"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:5IU0"
FT HELIX 387..394
FT /evidence="ECO:0007829|PDB:5IU0"
FT STRAND 396..401
FT /evidence="ECO:0007829|PDB:5IU0"
FT HELIX 404..407
FT /evidence="ECO:0007829|PDB:5IU0"
FT HELIX 413..432
FT /evidence="ECO:0007829|PDB:5IU0"
FT HELIX 437..448
FT /evidence="ECO:0007829|PDB:5IU0"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:5IU0"
FT HELIX 453..462
FT /evidence="ECO:0007829|PDB:5IU0"
SQ SEQUENCE 479 AA; 52955 MW; 3086705F3C8FEF75 CRC64;
MSPQTETKAS VGFKAGVKEY KLTYYTPEYE TKDTDILAAF RVTPQPGVPP EEAGAAVAAE
SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV PGEETQFIAY VAYPLDLFEE GSVTNMFTSI
VGNVFGFKAL AALRLEDLRI PPAYTKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL
SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEAIYKSQA ETGEIKGHYL
NATAGTCEEM IKRAVFAREL GVPIVMHDYL TGGFTANTSL SHYCRDNGLL LHIHRAMHAV
IDRQKNHGMH FRVLAKALRL SGGDHIHAGT VVGKLEGDRE STLGFVDLLR DDYVEKDRSR
GIFFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN
RVALEACVQA RNEGRDLAVE GNEIIREACK WSPELAAACE VWKEITFNFP TIDKLDGQE
