PLDG1_ARATH
ID PLDG1_ARATH Reviewed; 858 AA.
AC Q9T053; O48544;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Phospholipase D gamma 1 {ECO:0000303|PubMed:9353280};
DE Short=AtPLDgamma1 {ECO:0000303|PubMed:9353280};
DE Short=PLD gamma 1 {ECO:0000303|PubMed:9353280};
DE EC=3.1.4.4 {ECO:0000269|PubMed:10441386, ECO:0000269|PubMed:17098468, ECO:0000269|PubMed:9353280};
DE AltName: Full=Choline phosphatase;
DE AltName: Full=Lecithinase D;
DE AltName: Full=Lipophosphodiesterase II;
GN Name=PLDGAMMA1 {ECO:0000303|PubMed:9353280};
GN OrderedLocusNames=At4g11850 {ECO:0000312|Araport:AT4G11850};
GN ORFNames=T26M18.60 {ECO:0000312|EMBL:CAB44323.1};
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 [MRNA], CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=9353280; DOI=10.1074/jbc.272.45.28267;
RA Qin W., Pappan K., Wang X.;
RT "Molecular heterogeneity of phospholipase D (PLD). Cloning of PLDgamma and
RT regulation of plant PLDgamma, -beta, and -alpha by polyphosphoinositides
RT and calcium.";
RL J. Biol. Chem. 272:28267-28273(1997).
RN [2]
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 [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 SUBSTRATE SPECIFICITY.
RX PubMed=9578608; DOI=10.1006/abbi.1998.0640;
RA Pappan K., Austin-Brown S., Chapman K.D., Wang X.;
RT "Substrate selectivities and lipid modulation of plant phospholipase D
RT alpha, -beta, and -gamma.";
RL Arch. Biochem. Biophys. 353:131-140(1998).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10441386; DOI=10.1006/abbi.1999.1325;
RA Pappan K., Wang X.;
RT "Plant phospholipase Dalpha is an acidic phospholipase active at near-
RT physiological Ca(2+) concentrations.";
RL Arch. Biochem. Biophys. 368:347-353(1999).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=10198096; DOI=10.1104/pp.119.4.1371;
RA Fan L., Zheng S., Cui D., Wang X.;
RT "Subcellular distribution and tissue expression of phospholipase Dalpha,
RT Dbeta, and Dgamma in Arabidopsis.";
RL Plant Physiol. 119:1371-1378(1999).
RN [8]
RP INDUCTION BY WOUNDING.
RX PubMed=11090221; DOI=10.2307/3871117;
RA Wang C., Zien C.A., Afitlhile M., Welti R., Hildebrand D.F., Wang X.;
RT "Involvement of phospholipase D in wound-induced accumulation of jasmonic
RT acid in arabidopsis.";
RL Plant Cell 12:2237-2246(2000).
RN [9]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11891260; DOI=10.1104/pp.010928;
RA Qin C., Wang X.;
RT "The Arabidopsis phospholipase D family. Characterization of a calcium-
RT independent and phosphatidylcholine-selective PLD zeta 1 with distinct
RT regulatory domains.";
RL Plant Physiol. 128:1057-1068(2002).
RN [10]
RP INDUCTION BY WOUNDING, TISSUE SPECIFICITY, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17098468; DOI=10.1016/j.bbalip.2006.09.017;
RA Qin C., Li M., Qin W., Bahn S.C., Wang C., Wang X.;
RT "Expression and characterization of Arabidopsis phospholipase Dgamma2.";
RL Biochim. Biophys. Acta 1761:1450-1458(2006).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680, 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 [13]
RP FUNCTION, INDUCTION BY ALUMINUM, AND DISRUPTION PHENOTYPE.
RX PubMed=22163277; DOI=10.1371/journal.pone.0028086;
RA Zhao J., Wang C., Bedair M., Welti R., Sumner L.W., Baxter I., Wang X.;
RT "Suppression of phospholipase Dgammas confers increased aluminum resistance
RT in Arabidopsis thaliana.";
RL PLoS ONE 6:E28086-E28086(2011).
CC -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
CC phosphodiesteric bond to generate phosphatidic acids (PA). Plays an
CC important role in various cellular processes, including phytohormone
CC action, vesicular trafficking, secretion, cytoskeletal arrangement,
CC meiosis, tumor promotion, pathogenesis, membrane deterioration and
CC senescence (PubMed:10441386). Can use phosphatidylserine (PS) and
CC phosphatidylethanolamine (PE) as substrates only in the presence of
CC PIP2. Can use phosphatidylcholine (PC), phosphatidylglycerol (PG) or N-
CC acylphosphatidylethanolamine (NAPE) as substrates in the presence of PE
CC and PIP2 (PubMed:9578608, PubMed:17098468). Involved in membrane lipid
CC modulation under aluminum (Al) stress and negatively modulate plant
CC tolerance to Al (PubMed:22163277). {ECO:0000269|PubMed:10441386,
CC ECO:0000269|PubMed:17098468, ECO:0000269|PubMed:22163277,
CC ECO:0000269|PubMed:9578608}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4;
CC Evidence={ECO:0000269|PubMed:10441386, ECO:0000269|PubMed:17098468,
CC ECO:0000269|PubMed:9353280};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:17098468, ECO:0000269|PubMed:9353280};
CC Note=Ca(2+). Requires micromolar level (PIP2-dependent).
CC {ECO:0000269|PubMed:17098468, ECO:0000269|PubMed:9353280};
CC -!- ACTIVITY REGULATION: Inhibited by neomycin. Up-regulated by PIP2
CC binding. {ECO:0000269|PubMed:9353280}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5 to 8.5. {ECO:0000269|PubMed:10441386,
CC ECO:0000269|PubMed:17098468};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10198096}. Membrane
CC {ECO:0000269|PubMed:10198096}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10198096}. Note=Found mainly associated with
CC intracellular membranes but also with mitochondrial membranes, nuclei
CC and clathrin-coated vesicles. Not found in chloroplast.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots and flowers, moderately
CC in stems, leaves and seedlings and low in siliques. Not detected in
CC seeds. {ECO:0000269|PubMed:10198096, ECO:0000269|PubMed:17098468}.
CC -!- INDUCTION: Activated by wounding, heavy metal, methyl salicylate,
CC osmotic and salt stresses (PubMed:11090221, PubMed:17098468). Up-
CC regulated by aluminum stress (PubMed:22163277).
CC {ECO:0000269|PubMed:11090221, ECO:0000269|PubMed:17098468,
CC ECO:0000269|PubMed:22163277}.
CC -!- DOMAIN: C2 domain is a calcium-binding fold, and the binding promotes
CC the protein association with membranes. In PLD gamma, all the calcium-
CC coordinating acidic amino acids are conserved. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Increased tolerance to aluminum.
CC {ECO:0000269|PubMed:22163277}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-11 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB87672.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF027408; AAB87672.1; ALT_FRAME; mRNA.
DR EMBL; AL078606; CAB44323.1; -; Genomic_DNA.
DR EMBL; AL161532; CAB78228.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83058.1; -; Genomic_DNA.
DR EMBL; AY099569; AAM20421.1; -; mRNA.
DR EMBL; BT002140; AAN72151.1; -; mRNA.
DR PIR; T09344; T09344.
DR RefSeq; NP_192922.1; NM_117255.3.
DR AlphaFoldDB; Q9T053; -.
DR SMR; Q9T053; -.
DR BioGRID; 12089; 5.
DR IntAct; Q9T053; 1.
DR STRING; 3702.AT4G11850.1; -.
DR iPTMnet; Q9T053; -.
DR PaxDb; Q9T053; -.
DR PRIDE; Q9T053; -.
DR ProteomicsDB; 235037; -.
DR EnsemblPlants; AT4G11850.1; AT4G11850.1; AT4G11850.
DR GeneID; 826791; -.
DR Gramene; AT4G11850.1; AT4G11850.1; AT4G11850.
DR KEGG; ath:AT4G11850; -.
DR Araport; AT4G11850; -.
DR TAIR; locus:2137045; AT4G11850.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_004684_0_0_1; -.
DR InParanoid; Q9T053; -.
DR OMA; HDEDTRQ; -.
DR OrthoDB; 133306at2759; -.
DR PhylomeDB; Q9T053; -.
DR BioCyc; ARA:AT4G11850-MON; -.
DR BioCyc; MetaCyc:AT4G11850-MON; -.
DR BRENDA; 3.1.4.4; 399.
DR PRO; PR:Q9T053; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9T053; baseline and differential.
DR Genevisible; Q9T053; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:TAIR.
DR GO; GO:0004630; F:phospholipase D activity; IDA:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0045087; P:innate immune response; IDA:TAIR.
DR GO; GO:0006643; P:membrane lipid metabolic process; IMP:TAIR.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
DR GO; GO:0010044; P:response to aluminum ion; IMP:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR024632; PLipase_D_C.
DR InterPro; IPR015679; PLipase_D_fam.
DR InterPro; IPR011402; PLipase_D_pln.
DR PANTHER; PTHR18896; PTHR18896; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12357; PLD_C; 1.
DR Pfam; PF00614; PLDc; 2.
DR PIRSF; PIRSF036470; PLD_plant; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50035; PLD; 2.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Hydrolase; Lipid degradation; Lipid metabolism;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..858
FT /note="Phospholipase D gamma 1"
FT /id="PRO_0000218812"
FT DOMAIN 27..163
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 364..399
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 704..731
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 369
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 371
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 376
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 709
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 711
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 716
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT BINDING 225
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 369
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 405
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 437
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 565
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 709
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 772
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 114..115
FT /note="MQ -> IE (in Ref. 1; AAB87672)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="Q -> E (in Ref. 1; AAB87672)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="A -> S (in Ref. 1; AAB87672)"
FT /evidence="ECO:0000305"
FT CONFLICT 634..635
FT /note="MQ -> IE (in Ref. 1; AAB87672)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 858 AA; 95588 MW; 334AF9DB9E3A7A73 CRC64;
MAYHPAYTET MSMGGGSSHG GGQQYVPFAT SSGSLRVELL HGNLDIWVKE AKHLPNMDGF
HNRLGGMLSG LGRKKVEGEK SSKITSDPYV TVSISGAVIG RTFVISNSEN PVWMQHFDVP
VAHSAAEVHF VVKDSDIIGS QIMGAVGIPT EQLCSGNRIE GLFPILNSSG KPCKQGAVLG
LSIQYTPMER MRLYQMGVGS GNECVGVPGT YFPLRKGGRV TLYQDAHVDD GTLPSVHLDG
GIQYRHGKCW EDMADAIRQA RRLIYITGWS VFHPVRLVRR TNDPTEGTLG ELLKVKSQEG
VRVLVLVWDD PTSRSLLGFK TQGVMNTSDE ETRRFFKHSS VQVLLCPRSG GKGHSFIKKS
EVGTIYTHHQ KTVIVDAEAA QNRRKIVAFV GGLDLCNGRF DTPKHPLFRT LKTLHKDDFH
NPNFVTTADD GPREPWHDLH SKIDGPAAYD VLANFEERWM KASKPRGIGK LKSSSDDSLL
RIDRIPDIVG LSEASSANDN DPESWHVQVF RSIDSSSVKG FPKDPKEATG RNLLCGKNIL
IDMSIHAAYV KAIRSAQHFI YIENQYFLGS SFNWDSNKDL GANNLIPMEI ALKIANKIRA
REKFAAYIVI PMWPEGAPTS NPIQRILYWQ HKTMQMMYQT IYKALVEVGL DSQFEPQDFL
NFFCLGTREV PVGTVSVYNS PRKPPQPNAN ANAAQVQALK SRRFMIYVHS KGMVVDDEFV
LIGSANINQR SLEGTRDTEI AMGGYQPHYS WAMKGSRPHG QIFGYRMSLW AEHLGFLEQG
FEEPENMECV RRVRQLSELN WRQYAAEEVT EMSGHLLKYP VQVDRTGKVS SLPGCETFPD
LGGKIIGSFL ALQENLTI
