PCKA1_ARATH
ID PCKA1_ARATH Reviewed; 671 AA.
AC Q9T074;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Phosphoenolpyruvate carboxykinase (ATP) 1 {ECO:0000303|PubMed:17283014};
DE Short=AtPCK1 {ECO:0000303|PubMed:19807880};
DE Short=PEP carboxykinase 1 {ECO:0000303|PubMed:17283014};
DE Short=PEPCK 1 {ECO:0000303|PubMed:17283014};
DE EC=4.1.1.49 {ECO:0000269|PubMed:19807880};
GN Name=PCK1 {ECO:0000303|PubMed:17283014};
GN OrderedLocusNames=At4g37870 {ECO:0000312|Araport:AT4G37870};
GN ORFNames=T28I19.150 {ECO:0000312|EMBL:CAB38935.1};
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].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [5]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=17283014; DOI=10.1093/pcp/pcm014;
RA Malone S., Chen Z.-H., Bahrami A.R., Walker R.P., Gray J.E., Leegood R.C.;
RT "Phosphoenolpyruvate carboxykinase in Arabidopsis: changes in gene
RT expression, protein and activity during vegetative and reproductive
RT development.";
RL Plant Cell Physiol. 48:441-450(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND THR-66, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, 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 IDENTIFICATION BY 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 [9]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=19807880; DOI=10.1111/j.1365-313x.2009.04040.x;
RA Brown N.J., Palmer B.G., Stanley S., Hajaji H., Janacek S.H., Astley H.M.,
RA Parsley K., Kajala K., Quick W.P., Trenkamp S., Fernie A.R., Maurino V.G.,
RA Hibberd J.M.;
RT "C acid decarboxylases required for C photosynthesis are active in the mid-
RT vein of the C species Arabidopsis thaliana, and are important in sugar and
RT amino acid metabolism.";
RL Plant J. 61:122-133(2010).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
CC -!- FUNCTION: Involved in the gluconeogenesis (PubMed:19807880). Catalyzes
CC the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP)
CC through direct phosphoryl transfer between the nucleoside triphosphate
CC and OAA (PubMed:19807880). {ECO:0000269|PubMed:19807880}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:18617, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC EC=4.1.1.49; Evidence={ECO:0000269|PubMed:19807880};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P22259};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P22259};
CC -!- ACTIVITY REGULATION: Allosterically activated by calcium. It may
CC represent the only case of a monomeric, allosteric enzyme.
CC {ECO:0000250|UniProtKB:P22259}.
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000250|UniProtKB:P22259}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P22259}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19807880}.
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons, flowers, siliques, seeds,
CC leaves, stems and roots (PubMed:17283014). Localized in mid-veins
CC (PubMed:19807880). {ECO:0000269|PubMed:17283014,
CC ECO:0000269|PubMed:19807880}.
CC -!- DEVELOPMENTAL STAGE: Accumulates transiently in germinating seeds (at
CC protein level) with a constant transcript level (PubMed:17283014).
CC Abundant in cotyledons (mostly in senescing cotyledons) during post-
CC germinative growth and in sink tissues, such as young leaves,
CC developing flowers, siliques and seeds (at protein level)
CC (PubMed:17283014, PubMed:19807880). In flowers, present in the
CC nectaries, stigma, endocarp of the fruit wall and in tissues involved
CC in the transfer of assimilates to the developing ovules and seeds, such
CC as the vasculature and seed coat (at protein level) (PubMed:17283014).
CC {ECO:0000269|PubMed:17283014, ECO:0000269|PubMed:19807880}.
CC -!- DISRUPTION PHENOTYPE: Strongly reduced phosphoenolpyruvate
CC carboxykinase activities in veins, leading to reduced alanine levels,
CC which is derived from phosphoenolpyruvate (PEP) via pyruvate, but
CC increased aspartate accumulation, derived from oxaloacetate.
CC {ECO:0000269|PubMed:19807880}.
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP)
CC family. {ECO:0000305}.
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DR EMBL; AL035709; CAB38935.1; -; Genomic_DNA.
DR EMBL; AL161592; CAB80452.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86847.1; -; Genomic_DNA.
DR EMBL; AF372922; AAK50062.1; -; mRNA.
DR EMBL; AY078035; AAL77736.1; -; mRNA.
DR PIR; T06034; T06034.
DR RefSeq; NP_195500.1; NM_119948.4.
DR AlphaFoldDB; Q9T074; -.
DR SMR; Q9T074; -.
DR BioGRID; 15224; 8.
DR IntAct; Q9T074; 6.
DR STRING; 3702.AT4G37870.1; -.
DR iPTMnet; Q9T074; -.
DR SwissPalm; Q9T074; -.
DR PaxDb; Q9T074; -.
DR PRIDE; Q9T074; -.
DR ProteomicsDB; 236712; -.
DR EnsemblPlants; AT4G37870.1; AT4G37870.1; AT4G37870.
DR GeneID; 829943; -.
DR Gramene; AT4G37870.1; AT4G37870.1; AT4G37870.
DR KEGG; ath:AT4G37870; -.
DR Araport; AT4G37870; -.
DR TAIR; locus:2137594; AT4G37870.
DR eggNOG; ENOG502QQI5; Eukaryota.
DR HOGENOM; CLU_018247_0_1_1; -.
DR InParanoid; Q9T074; -.
DR OMA; MRYAGEM; -.
DR OrthoDB; 380257at2759; -.
DR PhylomeDB; Q9T074; -.
DR BioCyc; ARA:AT4G37870-MON; -.
DR BioCyc; MetaCyc:AT4G37870-MON; -.
DR UniPathway; UPA00138; -.
DR PRO; PR:Q9T074; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9T074; baseline and differential.
DR Genevisible; Q9T074; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004612; F:phosphoenolpyruvate carboxykinase (ATP) activity; IMP:TAIR.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IDA:TAIR.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR CDD; cd00484; PEPCK_ATP; 1.
DR Gene3D; 3.40.449.10; -; 1.
DR Gene3D; 3.90.228.20; -; 1.
DR HAMAP; MF_00453; PEPCK_ATP; 1.
DR InterPro; IPR001272; PEP_carboxykinase_ATP.
DR InterPro; IPR013035; PEP_carboxykinase_C.
DR InterPro; IPR008210; PEP_carboxykinase_N.
DR InterPro; IPR015994; PEPCK_ATP_CS.
DR PANTHER; PTHR30031; PTHR30031; 1.
DR Pfam; PF01293; PEPCK_ATP; 1.
DR SUPFAM; SSF68923; SSF68923; 1.
DR TIGRFAMs; TIGR00224; pckA; 1.
DR PROSITE; PS00532; PEPCK_ATP; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Calcium; Cytoplasm; Decarboxylase;
KW Gluconeogenesis; Lyase; Manganese; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..671
FT /note="Phosphoenolpyruvate carboxykinase (ATP) 1"
FT /id="PRO_0000203862"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22259"
FT BINDING 270
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q5SLL5"
FT BINDING 271
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q5SLL5"
FT BINDING 328
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22259"
FT BINDING 334
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q5SLL5"
FT BINDING 334
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P22259"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22259"
FT BINDING 353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q5SLL5"
FT BINDING 353
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P22259"
FT BINDING 369..377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22259,
FT ECO:0000255|PROSITE-ProRule:PRU00499"
FT BINDING 390
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P22259"
FT BINDING 404
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q5SLL5"
FT BINDING 418
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22259"
FT BINDING 455
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q5SLL5"
FT BINDING 455
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P22259"
FT BINDING 574..575
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22259"
FT BINDING 575
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q5SLL5"
FT BINDING 580
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q5SLL5"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19245862"
FT MOD_RES 66
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18433157"
SQ SEQUENCE 671 AA; 73405 MW; E2D71E8843778BD2 CRC64;
MSAGNGNATN GDGGFSFPKG PVMPKITTGA AKRGSGVCHD DSGPTVNATT IDELHSLQKK
RSAPTTPINQ NAAAAFAAVS EEERQKIQLQ SISASLASLT RESGPKVVRG DPAEKKTDGS
TTPAYAHGQH HSIFSPATGA VSDSSLKFTH VLYNLSPAEL YEQAIKYEKG SFITSNGALA
TLSGAKTGRA PRDKRVVRDA TTEDELWWGK GSPNIEMDEH TFMVNRERAV DYLNSLEKVF
VNDQYLNWDP ENRIKVRIVS ARAYHSLFMH NMCIRPTQEE LESFGTPDFT IYNAGQFPCN
RYTHYMTSST SVDLNLARRE MVILGTQYAG EMKKGLFSVM HYLMPKRRIL SLHSGCNMGK
DGDVALFFGL SGTGKTTLST DHNRYLIGDD EHCWTETGVS NIEGGCYAKC VDLSREKEPD
IWNAIKFGTV LENVVFDEHT REVDYSDKSV TENTRAAYPI EFIPNAKIPC VGPHPTNVIL
LACDAFGVLP PVSKLNLAQT MYHFISGYTA LVAGTEDGIK EPTATFSACF GAAFIMLHPT
KYAAMLAEKM KSQGATGWLV NTGWSGGSYG VGNRIKLAYT RKIIDAIHSG SLLKANYKKT
EIFGFEIPTE IEGIPSEILD PVNSWSDKKA HKDTLVKLGG LFKKNFEVFA NHKIGVDGKL
TEEILAAGPI F
