ID   CAPP1_ARATH             Reviewed;         967 AA.
AC   Q9MAH0; Q546E4;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=Phosphoenolpyruvate carboxylase 1;
DE            Short=AtPPC1 {ECO:0000303|PubMed:19228119};
DE            Short=PEPC 1;
DE            Short=PEPCase 1;
DE            EC=4.1.1.31 {ECO:0000269|PubMed:19228119};
DE   AltName: Full=107-kDa PEPC polypeptide;
GN   Name=PPC1; Synonyms=p107; OrderedLocusNames=At1g53310;
GN   ORFNames=F12M16.21;
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], TISSUE SPECIFICITY, AND NOMENCLATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=12805623; DOI=10.1104/pp.102.019653;
RA   Sanchez R., Cejudo F.J.;
RT   "Identification and expression analysis of a gene encoding a bacterial-type
RT   phosphoenolpyruvate carboxylase from Arabidopsis and rice.";
RL   Plant Physiol. 132:949-957(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-704, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Root;
RX   PubMed=18433157; DOI=10.1021/pr8000173;
RA   de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA   Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA   Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT   "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT   spectrometry and peptide chip analysis.";
RL   J. Proteome Res. 7:2458-2470(2008).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION AT SER-11, INDUCTION BY
RP   PHOSPHATE DEPRIVATION, ACTIVITY REGULATION, SUBUNIT, TISSUE SPECIFICITY,
RP   IDENTIFICATION BY MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   COFACTOR.
RC   STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX   PubMed=19228119; DOI=10.1042/bj20082397;
RA   Gregory A.L., Hurley B.A., Tran H.T., Valentine A.J., She Y.-M.,
RA   Knowles V.L., Plaxton W.C.;
RT   "In vivo regulatory phosphorylation of the phosphoenolpyruvate carboxylase
RT   AtPPC1 in phosphate-starved Arabidopsis thaliana.";
RL   Biochem. J. 420:57-65(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY
RP   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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, 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).
CC   -!- FUNCTION: Through the carboxylation of phosphoenolpyruvate (PEP) it
CC       forms oxaloacetate, a four-carbon dicarboxylic acid source for the
CC       tricarboxylic acid cycle. Contributes probably to the adaptation to
CC       inorganic phosphate (Pi) deprivation. {ECO:0000269|PubMed:19228119}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC         phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC         Evidence={ECO:0000269|PubMed:19228119};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28372;
CC         Evidence={ECO:0000305|PubMed:19228119};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:19228119};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:19228119};
CC       Note=Magnesium. Can also use manganese. {ECO:0000269|PubMed:19228119};
CC   -!- ACTIVITY REGULATION: By light-reversible phosphorylation (By
CC       similarity). Activated by inorganic phosphate (Pi) deprivation and
CC       glucose 6-phosphate. Inhibited by L-malate and L-aspartate.
CC       {ECO:0000250, ECO:0000269|PubMed:19228119}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.18 mM for PEP (Phospho-PPC1 at pH 7.3 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:19228119};
CC         KM=0.34 mM for PEP (Dephospho-PPC1 at pH 7.3 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:19228119};
CC       pH dependence:
CC         Optimum pH is 8-9. {ECO:0000269|PubMed:19228119};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:19228119}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in all plant organs, with higher levels
CC       in roots. {ECO:0000269|PubMed:12805623, ECO:0000269|PubMed:19228119}.
CC   -!- INDUCTION: Upon inorganic phosphate (Pi) deprivation.
CC       {ECO:0000269|PubMed:19228119}.
CC   -!- PTM: The phosphorylation of Ser-11 is reversibly promoted by inorganic
CC       phosphate (Pi) deprivation. Enhanced activity by phosphorylation at pH
CC       7.3 by lowering Km and sensitivity to inhibition by L-malate and L-
CC       aspartate, while enhancing activation by glucose 6-phosphate.
CC       {ECO:0000269|PubMed:19228119}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR   EMBL; AJ532901; CAD58725.1; -; mRNA.
DR   EMBL; AC008007; AAF69546.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE32921.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE32922.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE32923.1; -; Genomic_DNA.
DR   EMBL; AY057507; AAL09748.1; -; mRNA.
DR   EMBL; BT000647; AAN18213.1; -; mRNA.
DR   PIR; D96573; D96573.
DR   RefSeq; NP_001031178.1; NM_001036101.2.
DR   RefSeq; NP_001031179.1; NM_001036102.3.
DR   RefSeq; NP_175738.1; NM_104209.3.
DR   PDB; 8OJ9; X-ray; 3.25 A; A/B/C=1-967.
DR   PDB; 8OJE; X-ray; 3.14 A; A/B/C/D/E/F/G/H=1-967.
DR   PDB; 8OJF; X-ray; 3.04 A; A/B=1-967.
DR   PDBsum; 8OJ9; -.
DR   PDBsum; 8OJE; -.
DR   PDBsum; 8OJF; -.
DR   AlphaFoldDB; Q9MAH0; -.
DR   SMR; Q9MAH0; -.
DR   BioGRID; 26990; 12.
DR   IntAct; Q9MAH0; 3.
DR   STRING; 3702.Q9MAH0; -.
DR   iPTMnet; Q9MAH0; -.
DR   MetOSite; Q9MAH0; -.
DR   PaxDb; 3702-AT1G53310-3; -.
DR   ProteomicsDB; 239179; -.
DR   EnsemblPlants; AT1G53310.1; AT1G53310.1; AT1G53310.
DR   EnsemblPlants; AT1G53310.2; AT1G53310.2; AT1G53310.
DR   EnsemblPlants; AT1G53310.3; AT1G53310.3; AT1G53310.
DR   GeneID; 841765; -.
DR   Gramene; AT1G53310.1; AT1G53310.1; AT1G53310.
DR   Gramene; AT1G53310.2; AT1G53310.2; AT1G53310.
DR   Gramene; AT1G53310.3; AT1G53310.3; AT1G53310.
DR   KEGG; ath:AT1G53310; -.
DR   Araport; AT1G53310; -.
DR   TAIR; AT1G53310; PPC1.
DR   eggNOG; ENOG502QPVS; Eukaryota.
DR   HOGENOM; CLU_006557_1_0_1; -.
DR   InParanoid; Q9MAH0; -.
DR   OMA; WKSIPTT; -.
DR   OrthoDB; 355614at2759; -.
DR   PhylomeDB; Q9MAH0; -.
DR   BRENDA; 4.1.1.31; 399.
DR   SABIO-RK; Q9MAH0; -.
DR   PRO; PR:Q9MAH0; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9MAH0; baseline and differential.
DR   GO; GO:0048046; C:apoplast; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IDA:TAIR.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   GO; GO:0016036; P:cellular response to phosphate starvation; IDA:UniProtKB.
DR   GO; GO:0048366; P:leaf development; IMP:TAIR.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
DR   HAMAP; MF_00595; PEPcase_type1; 1.
DR   InterPro; IPR021135; PEP_COase.
DR   InterPro; IPR022805; PEP_COase_bac/pln-type.
DR   InterPro; IPR018129; PEP_COase_Lys_AS.
DR   InterPro; IPR033129; PEPCASE_His_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF38; PHOSPHOENOLPYRUVATE CARBOXYLASE 1; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
DR   Genevisible; Q9MAH0; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Allosteric enzyme; Carbon dioxide fixation; Cytoplasm; Lyase;
KW   Magnesium; Manganese; Phosphoprotein; Photosynthesis; Reference proteome.
FT   CHAIN           1..967
FT                   /note="Phosphoenolpyruvate carboxylase 1"
FT                   /id="PRO_0000166657"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        602
FT                   /evidence="ECO:0000250"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:19228119,
FT                   ECO:0007744|PubMed:18433157, ECO:0007744|PubMed:19245862,
FT                   ECO:0007744|PubMed:19376835"
FT   MOD_RES         704
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18433157"
FT   HELIX           9..19
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   STRAND          24..27
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           30..49
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           51..70
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           73..84
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           88..115
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           127..131
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   TURN            133..135
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           139..149
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           154..163
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   STRAND          165..170
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           180..196
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           203..221
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           233..240
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           242..246
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           248..264
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   TURN            265..267
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   STRAND          278..283
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   TURN            285..287
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           297..325
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           333..342
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   TURN            355..357
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           366..390
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           398..400
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           405..421
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           425..428
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           431..442
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   TURN            443..445
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   STRAND          446..454
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           455..468
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   TURN            474..476
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           479..491
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   STRAND          492..494
FT                   /evidence="ECO:0007829|PDB:8OJ9"
FT   STRAND          499..501
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           505..518
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           522..524
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   STRAND          525..533
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           536..548
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   STRAND          556..561
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           564..579
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           581..587
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   STRAND          590..595
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           597..604
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           606..627
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   STRAND          630..635
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           640..642
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   STRAND          643..645
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           646..654
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   STRAND          659..668
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           670..677
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           680..699
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           707..728
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           734..740
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   STRAND          741..743
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           744..750
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   STRAND          757..760
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   TURN            765..767
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           770..779
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           784..787
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           790..800
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           804..814
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           816..830
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           834..844
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           847..849
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           850..871
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   TURN            876..879
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           881..909
FT                   /evidence="ECO:0007829|PDB:8OJE"
FT   HELIX           935..938
FT                   /evidence="ECO:0007829|PDB:8OJ9"
FT   STRAND          943..945
FT                   /evidence="ECO:0007829|PDB:8OJ9"
FT   HELIX           948..963
FT                   /evidence="ECO:0007829|PDB:8OJE"
SQ   SEQUENCE   967 AA;  110286 MW;  BD3E8F98E2046EEE CRC64;
     MANRKLEKMA SIDVHLRQLV PGKVSEDDKL VEYDALLLDR FLDILQDLHG EDLRETVQEL
     YEHSAEYEGK HEPKKLEELG SVLTSLDPGD SIVIAKAFSH MLNLANLAEE VQIAYRRRIK
     KLKKGDFVDE SSATTESDLE ETFKKLVGDL NKSPEEIFDA LKNQTVDLVL TAHPTQSVRR
     SLLQKHGRIR DCLAQLYAKD ITPDDKQELD EALQREIQAA FRTDEIKRTP PTPQDEMRAG
     MSYFHETIWK GVPKFLRRVD TALKNIGIEE RVPYNAPLIQ FSSWMGGDRD GNPRVTPEVT
     RDVCLLARMM AATMYFNQIE DLMFEMSMWR CNDELRARAD EVHANSRKDA AKHYIEFWKS
     IPTTEPYRVI LGDVRDKLYH TRERAHQLLS NGHSDVPVEA TFINLEQFLE PLELCYRSLC
     SCGDRPIADG SLLDFLRQVS TFGLSLVRLD IRQESDRHTD VLDAITTHLD IGSYREWSEE
     RRQEWLLSEL SGKRPLFGSD LPKTEEIADV LDTFHVIAEL PADSFGAYII SMATAPSDVL
     AVELLQRECR VKQPLRVVPL FEKLADLEAA PAAVARLFSV DWYKNRINGK QEVMIGYSDS
     GKDAGRLSAA WQLYKAQEEL VKVAKEYGVK LTMFHGRGGT VGRGGGPTHL AILSQPPDTI
     NGSLRVTVQG EVIEQSFGEE HLCFRTLQRF TAATLEHGMR PPISPKPEWR ALLDEMAVVA
     TEEYRSVVFQ EPRFVEYFRL ATPELEYGRM NIGSRPSKRK PSGGIESLRA IPWIFAWTQT
     RFHLPVWLGF GSAIRHVIEK DVRNLHMLQD MYQHWPFFRV TIDLIEMVFA KGDPGIAALY
     DKLLVSEELW PFGEKLRANF EETKKLILQT AGHKDLLEGD PYLKQRLRLR DSYITTLNVC
     QAYTLKRIRD PSYHVTLRPH ISKEIAESSK PAKELIELNP TSEYAPGLED TLILTMKGIA
     AGLQNTG
//