CHLH_ARATH
ID CHLH_ARATH Reviewed; 1381 AA.
AC Q9FNB0; B9DI09; B9DI10; Q39049; Q8RY14;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Magnesium-chelatase subunit ChlH, chloroplastic;
DE Short=Mg-chelatase subunit H;
DE EC=6.6.1.1;
DE AltName: Full=ABA-binding protein;
DE AltName: Full=Mg-protoporphyrin IX chelatase subunit ChlH;
DE AltName: Full=Protein CONDITIONAL CHLORINA;
DE AltName: Full=Protein GENOMES UNCOUPLED 5;
DE AltName: Full=Protein RAPID TRANSPIRATION IN DETACHED LEAVES 1;
DE Flags: Precursor;
GN Name=CHLH; Synonyms=ABAR, CCH, GUN5, RTL1; OrderedLocusNames=At5g13630;
GN ORFNames=MSH12.9;
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].
RC STRAIN=cv. C24;
RX PubMed=8685276; DOI=10.1104/pp.111.1.61;
RA Gibson L., Marrison J., Leech R., Jensen P., Bassham D., Gibson M.,
RA Hunter C.;
RT "A putative Mg chelatase subunit from Arabidopsis thaliana cv. C24:
RT sequence and transcript analysis of the gene, import of the protein into
RT chloroplasts and in situ localisation of the transcript.";
RL Plant Physiol. 111:61-71(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 311-1381.
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PRO-642 AND ALA-990.
RX PubMed=11172074; DOI=10.1073/pnas.98.4.2053;
RA Mochizuki N., Brusslan J.A., Larkin R., Nagatani A., Chory J.;
RT "Arabidopsis genomes uncoupled 5 (GUN5) mutant reveals the involvement of
RT Mg-chelatase H subunit in plastid-to-nucleus signal transduction.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:2053-2058(2001).
RN [7]
RP INTERACTION WITH GUN4.
RX PubMed=12574634; DOI=10.1126/science.1079978;
RA Larkin R.M., Alonso J.M., Ecker J.R., Chory J.;
RT "GUN4, a regulator of chlorophyll synthesis and intracellular signaling.";
RL Science 299:902-906(2003).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17051210; DOI=10.1038/nature05176;
RA Shen Y.Y., Wang X.F., Wu F.Q., Du S.Y., Cao Z., Shang Y., Wang X.L.,
RA Peng C.C., Yu X.C., Zhu S.Y., Fan R.C., Xu Y.H., Zhang D.P.;
RT "The Mg-chelatase H subunit is an abscisic acid receptor.";
RL Nature 443:823-826(2006).
RN [9]
RP INDUCTION BY LIGHT.
RX PubMed=18846290; DOI=10.1039/b802596g;
RA Stephenson P.G., Terry M.J.;
RT "Light signalling pathways regulating the Mg-chelatase branchpoint of
RT chlorophyll synthesis during de-etiolation in Arabidopsis thaliana.";
RL Photochem. Photobiol. Sci. 7:1243-1252(2008).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19363094; DOI=10.1104/pp.109.135368;
RA Huang Y.S., Li H.M.;
RT "Arabidopsis CHLI2 can substitute for CHLI1.";
RL Plant Physiol. 150:636-645(2009).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19535472; DOI=10.1104/pp.109.140731;
RA Wu F.Q., Xin Q., Cao Z., Liu Z.Q., Du S.Y., Mei C., Zhao C.X., Wang X.F.,
RA Shang Y., Jiang T., Zhang X.F., Yan L., Zhao R., Cui Z.N., Liu R.,
RA Sun H.L., Yang X.L., Su Z., Zhang D.P.;
RT "The magnesium-chelatase H subunit binds abscisic acid and functions in
RT abscisic acid signaling: new evidence in Arabidopsis.";
RL Plant Physiol. 150:1940-1954(2009).
RN [12]
RP FUNCTION, INTERACTION WITH WRKY40, AND SUBCELLULAR LOCATION.
RX PubMed=20543028; DOI=10.1105/tpc.110.073874;
RA Shang Y., Yan L., Liu Z.Q., Cao Z., Mei C., Xin Q., Wu F.Q., Wang X.F.,
RA Du S.Y., Jiang T., Zhang X.F., Zhao R., Sun H.L., Liu R., Yu Y.T.,
RA Zhang D.P.;
RT "The Mg-chelatase H subunit of Arabidopsis antagonizes a group of WRKY
RT transcription repressors to relieve ABA-responsive genes of inhibition.";
RL Plant Cell 22:1909-1935(2010).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF LEU-690.
RX PubMed=21562844; DOI=10.1007/s10265-011-0426-x;
RA Tsuzuki T., Takahashi K., Inoue S., Okigaki Y., Tomiyama M., Hossain M.A.,
RA Shimazaki K., Murata Y., Kinoshita T.;
RT "Mg-chelatase H subunit affects ABA signaling in stomatal guard cells, but
RT is not an ABA receptor in Arabidopsis thaliana.";
RL J. Plant Res. 124:527-538(2011).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=21467578; DOI=10.1105/tpc.110.082503;
RA Adhikari N.D., Froehlich J.E., Strand D.D., Buck S.M., Kramer D.M.,
RA Larkin R.M.;
RT "GUN4-porphyrin complexes bind the ChlH/GUN5 subunit of Mg-Chelatase and
RT promote chlorophyll biosynthesis in Arabidopsis.";
RL Plant Cell 23:1449-1467(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-50, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER SER-49, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE 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 [16]
RP INTERACTION WITH CHLI1 AND CHLD, FUNCTION, AND MUTAGENESIS OF PRO-642 AND
RP LEU-690.
RX PubMed=23011401; DOI=10.1007/s11103-012-9965-3;
RA Du S.Y., Zhang X.F., Lu Z., Xin Q., Wu Z., Jiang T., Lu Y., Wang X.F.,
RA Zhang D.P.;
RT "Roles of the different components of magnesium chelatase in abscisic acid
RT signal transduction.";
RL Plant Mol. Biol. 80:519-537(2012).
CC -!- FUNCTION: Multifunctional protein involved in chlorophyll synthesis,
CC plastid-to-nucleus retrograde signaling and abscisic acid (ABA)
CC perception. In chlorophyll synthesis, catalyzes the insertion of
CC magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX. The
CC reaction takes place in two steps, with an ATP-dependent activation
CC followed by an ATP-dependent chelation step. In addition to its
CC function in the Mg-chelatase enzyme, is required for the plastid-to-
CC nucleus retrograde signaling. The plastid-to-nucleus signal plays an
CC important role in the coordinated expression of both nuclear- and
CC chloroplast-localized genes that encode photosynthesis-related
CC proteins. Has a role in mediating ABA signaling in stomatal guard cells
CC and during seed germination. Binds ABA and is a positive regulator of
CC ABA signaling. {ECO:0000269|PubMed:11172074,
CC ECO:0000269|PubMed:17051210, ECO:0000269|PubMed:19363094,
CC ECO:0000269|PubMed:19535472, ECO:0000269|PubMed:20543028,
CC ECO:0000269|PubMed:21562844, ECO:0000269|PubMed:23011401}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Mg(2+) + protoporphyrin IX = ADP + 3 H(+) + Mg-
CC protoporphyrin IX + phosphate; Xref=Rhea:RHEA:13961,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18420,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57306,
CC ChEBI:CHEBI:60492, ChEBI:CHEBI:456216; EC=6.6.1.1;
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis.
CC -!- SUBUNIT: The magnesium chelatase complex is a heterotrimer consisting
CC of subunits CHLI, CHLD, AND CHLH. Interacts with GUN4, WRKY18, WRKY40,
CC WRKY60, CHLI1 and CHLD. {ECO:0000269|PubMed:12574634,
CC ECO:0000269|PubMed:20543028, ECO:0000269|PubMed:23011401}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Plastid, chloroplast
CC membrane; Peripheral membrane protein; Stromal side. Plastid,
CC chloroplast membrane; Peripheral membrane protein; Cytoplasmic side.
CC Note=Predominantly associated with the chloroplast envelope. Spans the
CC chloroplast envelope and is its N- and C-termini are exposed to the
CC cytosol (PubMed:20543028). {ECO:0000269|PubMed:20543028}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FNB0-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17051210}.
CC -!- INDUCTION: By red, far-red and blue light. Down-regulated by white
CC light. {ECO:0000269|PubMed:18846290}.
CC -!- DISRUPTION PHENOTYPE: Pale-green phenotype with low survival rates
CC during de-etiolation and severe embryonic lethality when homozygous.
CC Chli1 and chli2 double mutants are albino.
CC {ECO:0000269|PubMed:11172074, ECO:0000269|PubMed:19363094}.
CC -!- MISCELLANEOUS: Plants silencing CHLH show significant ABA-insensitive
CC phenotypes in seed germination, post-germination growth arrest by ABA
CC and ABA-induced promotion of stomatal closure and inhibition of
CC stomatal opening. In contrast, plants over-expressing ABAR display ABA-
CC hypersensitive phenotypes (PubMed:17051210).
CC {ECO:0000305|PubMed:17051210}.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunit H family.
CC {ECO:0000305}.
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DR EMBL; Z68495; CAA92802.1; -; mRNA.
DR EMBL; AB006704; BAB08689.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91919.1; -; Genomic_DNA.
DR EMBL; AY070133; AAL47483.1; -; mRNA.
DR EMBL; AY078971; AAL79577.1; -; mRNA.
DR EMBL; BT002311; AAN73308.1; -; mRNA.
DR EMBL; AK317719; BAH20377.1; -; mRNA.
DR EMBL; AK317718; BAH20376.1; -; mRNA.
DR PIR; S71288; S71288.
DR RefSeq; NP_196867.1; NM_121366.4. [Q9FNB0-1]
DR PDB; 5EWU; X-ray; 1.25 A; A/B=994-1381.
DR PDBsum; 5EWU; -.
DR AlphaFoldDB; Q9FNB0; -.
DR SMR; Q9FNB0; -.
DR BioGRID; 16485; 6.
DR STRING; 3702.AT5G13630.1; -.
DR iPTMnet; Q9FNB0; -.
DR PaxDb; Q9FNB0; -.
DR PRIDE; Q9FNB0; -.
DR ProteomicsDB; 246997; -. [Q9FNB0-1]
DR EnsemblPlants; AT5G13630.1; AT5G13630.1; AT5G13630. [Q9FNB0-1]
DR GeneID; 831207; -.
DR Gramene; AT5G13630.1; AT5G13630.1; AT5G13630. [Q9FNB0-1]
DR KEGG; ath:AT5G13630; -.
DR Araport; AT5G13630; -.
DR TAIR; locus:2173234; AT5G13630.
DR eggNOG; ENOG502QT3B; Eukaryota.
DR HOGENOM; CLU_002017_1_2_1; -.
DR InParanoid; Q9FNB0; -.
DR OMA; WETGQAM; -.
DR PhylomeDB; Q9FNB0; -.
DR BioCyc; MetaCyc:AT5G13630-MON; -.
DR UniPathway; UPA00668; -.
DR PRO; PR:Q9FNB0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNB0; baseline and differential.
DR Genevisible; Q9FNB0; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; NAS:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0010007; C:magnesium chelatase complex; TAS:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016851; F:magnesium chelatase activity; ISS:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR CDD; cd10150; CobN_like; 1.
DR InterPro; IPR011771; BchH.
DR InterPro; IPR003672; CobN/Mg_chltase.
DR InterPro; IPR022571; Mg_chelatase_H_N.
DR PANTHER; PTHR44119; PTHR44119; 1.
DR Pfam; PF02514; CobN-Mg_chel; 1.
DR Pfam; PF11965; DUF3479; 1.
DR TIGRFAMs; TIGR02025; BchH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Chlorophyll biosynthesis; Chloroplast; Ligase; Membrane;
KW Nucleotide-binding; Photosynthesis; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 50..1381
FT /note="Magnesium-chelatase subunit ChlH, chloroplastic"
FT /id="PRO_0000418765"
FT MOD_RES 50
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 642
FT /note="P->L: In cch; semi-dwarf plants with pale green
FT leaves and ABA-insensitive stomatal movment."
FT /evidence="ECO:0000269|PubMed:11172074,
FT ECO:0000269|PubMed:23011401"
FT MUTAGEN 690
FT /note="L->F: In rtl1; semi-dwarf plants with pale green
FT leaves and ABA-insensitive stomatal movment."
FT /evidence="ECO:0000269|PubMed:21562844,
FT ECO:0000269|PubMed:23011401"
FT MUTAGEN 990
FT /note="A->V: In gun5; semi-dwarf plants with pale green
FT leaves."
FT /evidence="ECO:0000269|PubMed:11172074"
FT CONFLICT 224
FT /note="V -> G (in Ref. 4; AAL79577)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="N -> K (in Ref. 1; CAA92802)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="A -> P (in Ref. 1; CAA92802)"
FT /evidence="ECO:0000305"
FT CONFLICT 739
FT /note="L -> V (in Ref. 1; CAA92802)"
FT /evidence="ECO:0000305"
FT CONFLICT 987..989
FT /note="NIH -> TSI (in Ref. 1; CAA92802)"
FT /evidence="ECO:0000305"
FT CONFLICT 1110..1111
FT /note="EL -> DV (in Ref. 1; CAA92802)"
FT /evidence="ECO:0000305"
FT HELIX 999..1019
FT /evidence="ECO:0007829|PDB:5EWU"
FT TURN 1020..1022
FT /evidence="ECO:0007829|PDB:5EWU"
FT STRAND 1026..1032
FT /evidence="ECO:0007829|PDB:5EWU"
FT HELIX 1034..1040
FT /evidence="ECO:0007829|PDB:5EWU"
FT HELIX 1043..1052
FT /evidence="ECO:0007829|PDB:5EWU"
FT STRAND 1054..1058
FT /evidence="ECO:0007829|PDB:5EWU"
FT STRAND 1064..1069
FT /evidence="ECO:0007829|PDB:5EWU"
FT HELIX 1072..1075
FT /evidence="ECO:0007829|PDB:5EWU"
FT STRAND 1081..1086
FT /evidence="ECO:0007829|PDB:5EWU"
FT HELIX 1088..1093
FT /evidence="ECO:0007829|PDB:5EWU"
FT HELIX 1095..1109
FT /evidence="ECO:0007829|PDB:5EWU"
FT HELIX 1115..1117
FT /evidence="ECO:0007829|PDB:5EWU"
FT HELIX 1119..1131
FT /evidence="ECO:0007829|PDB:5EWU"
FT HELIX 1135..1138
FT /evidence="ECO:0007829|PDB:5EWU"
FT STRAND 1142..1144
FT /evidence="ECO:0007829|PDB:5EWU"
FT HELIX 1154..1160
FT /evidence="ECO:0007829|PDB:5EWU"
FT HELIX 1166..1177
FT /evidence="ECO:0007829|PDB:5EWU"
FT HELIX 1186..1188
FT /evidence="ECO:0007829|PDB:5EWU"
FT STRAND 1190..1192
FT /evidence="ECO:0007829|PDB:5EWU"
FT HELIX 1194..1202
FT /evidence="ECO:0007829|PDB:5EWU"
FT STRAND 1206..1211
FT /evidence="ECO:0007829|PDB:5EWU"
FT TURN 1213..1215
FT /evidence="ECO:0007829|PDB:5EWU"
FT TURN 1218..1220
FT /evidence="ECO:0007829|PDB:5EWU"
FT HELIX 1223..1227
FT /evidence="ECO:0007829|PDB:5EWU"
FT HELIX 1230..1236
FT /evidence="ECO:0007829|PDB:5EWU"
FT STRAND 1244..1249
FT /evidence="ECO:0007829|PDB:5EWU"
FT STRAND 1251..1254
FT /evidence="ECO:0007829|PDB:5EWU"
FT STRAND 1256..1259
FT /evidence="ECO:0007829|PDB:5EWU"
FT HELIX 1260..1270
FT /evidence="ECO:0007829|PDB:5EWU"
FT TURN 1271..1273
FT /evidence="ECO:0007829|PDB:5EWU"
FT HELIX 1275..1283
FT /evidence="ECO:0007829|PDB:5EWU"
FT HELIX 1285..1306
FT /evidence="ECO:0007829|PDB:5EWU"
FT HELIX 1311..1321
FT /evidence="ECO:0007829|PDB:5EWU"
FT HELIX 1325..1334
FT /evidence="ECO:0007829|PDB:5EWU"
FT HELIX 1336..1351
FT /evidence="ECO:0007829|PDB:5EWU"
FT HELIX 1359..1375
FT /evidence="ECO:0007829|PDB:5EWU"
SQ SEQUENCE 1381 AA; 153574 MW; 8EBAD26670A7B336 CRC64;
MASLVYSPFT LSTSKAEHLS SLTNSTKHSF LRKKHRSTKP AKSFFKVKSA VSGNGLFTQT
NPEVRRIVPI KRDNVPTVKI VYVVLEAQYQ SSLSEAVQSL NKTSRFASYE VVGYLVEELR
DKNTYNNFCE DLKDANIFIG SLIFVEELAI KVKDAVEKER DRMDAVLVFP SMPEVMRLNK
LGSFSMSQLG QSKSPFFQLF KRKKQGSAGF ADSMLKLVRT LPKVLKYLPS DKAQDARLYI
LSLQFWLGGS PDNLQNFVKM ISGSYVPALK GVKIEYSDPV LFLDTGIWHP LAPTMYDDVK
EYWNWYDTRR DTNDSLKRKD ATVVGLVLQR SHIVTGDDSH YVAVIMELEA RGAKVVPIFA
GGLDFSGPVE KYFVDPVSKQ PIVNSAVSLT GFALVGGPAR QDHPRAIEAL KKLDVPYLVA
VPLVFQTTEE WLNSTLGLHP IQVALQVALP ELDGAMEPIV FAGRDPRTGK SHALHKRVEQ
LCIRAIRWGE LKRKTKAEKK LAITVFSFPP DKGNVGTAAY LNVFASIFSV LRDLKRDGYN
VEGLPENAET LIEEIIHDKE AQFSSPNLNV AYKMGVREYQ DLTPYANALE ENWGKPPGNL
NSDGENLLVY GKAYGNVFIG VQPTFGYEGD PMRLLFSKSA SPHHGFAAYY SYVEKIFKAD
AVLHFGTHGS LEFMPGKQVG MSDACFPDSL IGNIPNVYYY AANNPSEATI AKRRSYANTI
SYLTPPAENA GLYKGLKQLS ELISSYQSLK DTGRGPQIVS SIISTAKQCN LDKDVDLPDE
GLELSPKDRD SVVGKVYSKI MEIESRLLPC GLHVIGEPPS AMEAVATLVN IAALDRPEDE
ISALPSILAE CVGREIEDVY RGSDKGILSD VELLKEITDA SRGAVSAFVE KTTNSKGQVV
DVSDKLTSLL GFGINEPWVE YLSNTKFYRA NRDKLRTVFG FLGECLKLVV MDNELGSLMQ
ALEGKYVEPG PGGDPIRNPK VLPTGKNIHA LDPQAIPTTA AMASAKIVVE RLVERQKLEN
EGKYPETIAL VLWGTDNIKT YGESLGQVLW MIGVRPIADT FGRVNRVEPV SLEELGRPRI
DVVVNCSGVF RDLFINQMNL LDRAIKMVAE LDEPVEQNFV RKHALEQAEA LGIDIREAAT
RVFSNASGSY SANISLAVEN SSWNDEKQLQ DMYLSRKSFA FDSDAPGAGM AEKKQVFEMA
LSTAEVTFQN LDSSEISLTD VSHYFDSDPT NLVQSLRKDK KKPSSYIADT TTANAQVRTL
SETVRLDART KLLNPKWYEG MMSSGYEGVR EIEKRLSNTV GWSATSGQVD NWVYEEANST
FIQDEEMLNR LMNTNPNSFR KMLQTFLEAN GRGYWDTSAE NIEKLKELYS QVEDKIEGID
R
