AC78C_DROME
ID AC78C_DROME Reviewed; 1718 AA.
AC Q9VP76; M9NG95; Q9VP75;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Adenylyl cyclase 78C {ECO:0000303|PubMed:10603085, ECO:0000312|FlyBase:FBgn0024150};
DE EC=4.6.1.1 {ECO:0000269|PubMed:10603085};
GN Name=Ac78C {ECO:0000303|PubMed:10603085, ECO:0000312|FlyBase:FBgn0024150};
GN ORFNames=CG10564 {ECO:0000312|FlyBase:FBgn0024150};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, AND DOMAIN.
RX PubMed=10603085; DOI=10.1007/pl00008186;
RA Cann M.J., Levin L.R.;
RT "Restricted expression of a truncated adenylyl cyclase in the cephalic
RT furrow of Drosophila melanogaster.";
RL Dev. Genes Evol. 210:34-40(2000).
RN [4] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19046378; DOI=10.1111/j.1460-9568.2008.06507.x;
RA Ueno K., Kidokoro Y.;
RT "Adenylyl cyclase encoded by AC78C participates in sugar perception in
RT Drosophila melanogaster.";
RL Eur. J. Neurosci. 28:1956-1966(2008).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23929551; DOI=10.1177/0748730413497179;
RA Duvall L.B., Taghert P.H.;
RT "E and M circadian pacemaker neurons use different PDF receptor signalosome
RT components in drosophila.";
RL J. Biol. Rhythms 28:239-248(2013).
CC -!- FUNCTION: [Isoform B]: Catalyzes the formation of the signaling
CC molecule cAMP in response to G-protein coupled receptor signaling
CC (PubMed:10603085, PubMed:23929551). Probably downstream of gustatory
CC receptors, involved in taste perception of sucrose, trehalose and
CC caffeine (PubMed:19046378). Has no role in bitter perception
CC (PubMed:19046378). In the circadian brain neuron evening cells (E-
CC cells), involved in circadian pacemaker synchronization by playing a
CC role in signaling downstream of the G protein-coupled receptor Pdfr,
CC probably in conjunction with other, as yet unidentified, adenylate
CC cyclases (PubMed:23929551). {ECO:0000269|PubMed:10603085,
CC ECO:0000269|PubMed:19046378, ECO:0000269|PubMed:23929551}.
CC -!- FUNCTION: [Isoform C]: Does not have adenylyl cyclase activity and it
CC is not involved in taste perception. {ECO:0000269|PubMed:10603085}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1;
CC Evidence={ECO:0000269|PubMed:10603085};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P30803};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P30803};
CC Note=Binds 2 magnesium ions per subunit. Is also active with manganese
CC (in vitro). {ECO:0000250|UniProtKB:P30803};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B {ECO:0000312|FlyBase:FBgn0024150}; Synonyms=L
CC {ECO:0000303|PubMed:10603085};
CC IsoId=Q9VP76-1; Sequence=Displayed;
CC Name=C {ECO:0000312|FlyBase:FBgn0024150}; Synonyms=S
CC {ECO:0000303|PubMed:10603085};
CC IsoId=Q9VP76-2; Sequence=VSP_059968;
CC -!- TISSUE SPECIFICITY: Expressed in labella, particularly in sugar-
CC sensitive gustatory receptor neurons (GRNs).
CC {ECO:0000269|PubMed:19046378}.
CC -!- DEVELOPMENTAL STAGE: Isoform B: Ubiquitously expressed in embryos,
CC larvae and adult (PubMed:10603085). Isoform C: Temporally restricted to
CC the earliest hours of embryogenesis before cellularization
CC (PubMed:10603085). As germ band extension commences, expression
CC decreases along the entire ventral surface of the embryo and is
CC restricted to the cephalic furrow (CF) and anterior and posterior
CC dorsal transverse folds (DTFs) (PubMed:10603085). By state 7,
CC restricted expression in the CF and DTFs on the dorsal and lateral
CC surfaces of the embryo (PubMed:10603085).
CC {ECO:0000269|PubMed:10603085}.
CC -!- DOMAIN: The protein contains two modules with six transmembrane helices
CC each; both are required for catalytic activity. Isolated N-terminal or
CC C-terminal guanylate cyclase domains have no catalytic activity, but
CC when they are brought together, enzyme activity is restored. The active
CC site is at the interface of the two domains. Both contribute substrate-
CC binding residues, but the catalytic metal ions are bound exclusively
CC via the N-terminal guanylate cyclase domain.
CC {ECO:0000305|PubMed:10603085}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in sugar gustatory
CC neurons results in reduced sucrose response and no alteration in
CC response to water (PubMed:19046378). RNAi-mediated knockdown in the
CC pacemaker dorsal lateral neurons (LNDs) results in reduced Pigment-
CC dispersing factor (Pdf) response in the circadian brain neurons evening
CC cells (E-cells) (PubMed:23929551). Isoform B: Results in reduced
CC sucrose and trehalose substances response and no alteration of water
CC response or bitter perception (PubMed:19046378).
CC {ECO:0000269|PubMed:19046378, ECO:0000269|PubMed:23929551}.
CC -!- MISCELLANEOUS: [Isoform C]: Catalytically inactive.
CC {ECO:0000269|PubMed:10603085}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255, ECO:0000255|RuleBase:RU000405}.
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DR EMBL; AE014296; AAF51680.3; -; Genomic_DNA.
DR EMBL; AE014296; AFH04528.1; -; Genomic_DNA.
DR RefSeq; NP_001246857.1; NM_001259928.2. [Q9VP76-2]
DR RefSeq; NP_524194.3; NM_079470.5. [Q9VP76-1]
DR AlphaFoldDB; Q9VP76; -.
DR SMR; Q9VP76; -.
DR IntAct; Q9VP76; 3.
DR STRING; 7227.FBpp0290915; -.
DR EnsemblMetazoa; FBtr0301701; FBpp0290915; FBgn0024150. [Q9VP76-1]
DR EnsemblMetazoa; FBtr0305501; FBpp0293953; FBgn0024150. [Q9VP76-2]
DR GeneID; 40333; -.
DR KEGG; dme:Dmel_CG10564; -.
DR UCSC; CG10564-RA; d. melanogaster. [Q9VP76-1]
DR CTD; 40333; -.
DR FlyBase; FBgn0024150; Ac78C.
DR VEuPathDB; VectorBase:FBgn0024150; -.
DR HOGENOM; CLU_001072_3_1_1; -.
DR InParanoid; Q9VP76; -.
DR OMA; TLNCLND; -.
DR OrthoDB; 107368at2759; -.
DR PhylomeDB; Q9VP76; -.
DR Reactome; R-DME-163615; PKA activation.
DR Reactome; R-DME-170660; Adenylate cyclase activating pathway.
DR Reactome; R-DME-170670; Adenylate cyclase inhibitory pathway.
DR Reactome; R-DME-5610787; Hedgehog 'off' state.
DR BioGRID-ORCS; 40333; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 40333; -.
DR PRO; PR:Q9VP76; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0024150; Expressed in ectoderm and 18 other tissues.
DR ExpressionAtlas; Q9VP76; baseline and differential.
DR Genevisible; Q9VP76; DM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004016; F:adenylate cyclase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006171; P:cAMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0007623; P:circadian rhythm; IMP:UniProtKB.
DR GO; GO:0001582; P:detection of chemical stimulus involved in sensory perception of sweet taste; IMP:FlyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0031000; P:response to caffeine; IDA:FlyBase.
DR GO; GO:0009744; P:response to sucrose; IDA:FlyBase.
DR GO; GO:0010353; P:response to trehalose; IDA:FlyBase.
DR CDD; cd07302; CHD; 2.
DR Gene3D; 3.30.70.1230; -; 2.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR032628; AC_N.
DR InterPro; IPR009398; Adcy_conserved_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR Pfam; PF16214; AC_N; 1.
DR Pfam; PF06327; DUF1053; 1.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR SMART; SM00044; CYCc; 2.
DR SUPFAM; SSF55073; SSF55073; 2.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; cAMP biosynthesis; Cell membrane; Lyase;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1718
FT /note="Adenylyl cyclase 78C"
FT /evidence="ECO:0000305"
FT /id="PRO_0000445797"
FT TOPO_DOM 1..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..366
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..397
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..422
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467..476
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 498..1023
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1024..1044
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1045..1048
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1049..1069
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1070..1094
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1095..1115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1116..1241
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1242..1262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1264..1284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1285..1301
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1302..1322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1323..1718
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 41..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1628..1693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1628..1670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1679..1693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 580..585
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 580
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 580
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 581
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 622..624
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 624
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 624
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 672
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 1440
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1517..1519
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1524..1528
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1564
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT VAR_SEQ 1..496
FT /note="Missing (in isoform C)"
FT /id="VSP_059968"
SQ SEQUENCE 1718 AA; 189013 MW; 4CED55D0AF4FF87D CRC64;
MDVELEEEEE RICLRTAEEG QLANMDDDKL VSDEVHLRQL SATPSSAFSL QHSRGSDTKE
EAPPEGGTMG GKSAAPREEG EPDERVVLRR AVDKGAIALA QIDDLKLEGD DDDEAVVNGE
EVDGLGLSNP AAQTTDDEQI TVNGTGAAAT SSVAADAASS EQDAASTAMA TPDMSKIPRL
PGDGAQMEDN GSGDLPPSLR ASTTSILSNL RKKQQGGPLR GGVAKQTPLR VQSVRIVEAK
RAYGPKRRTE SCSIFGNSNF EHDLESGNSL ASIPGQSQRP LNNEMYSAFK SGNVVKGILC
PSLTNSFKQS SLERSYLTYT HRQRQKSLII VNVVDFVLKI VLAFVWIMRR SELGPIESDD
GTSMATAITW SVCCGIANMA ICFLGYWRCF ANNYLHWAAV CTWVLFNIQG FVGQGVGFAD
REYLVWYILF VIFVPYAMLP LPLKWCVVGG TITASCHLAV ITIIKLQHGE ATINPECVLF
QIFANFILYT AINVAGMYTK YLTDRGQRLA FIETHKAMEH KKESEKELQR TQKLLDSILP
NIVNNQIRSE MYKGTDPTVE TQFNKLYVYP MDNVSILFAD IKGFTELASK TSAQQLVKIL
NDLFARFDRI AEDNHCLRVK LLGDCYYCVS QFESDNWKTR PDHAVCSVET GLHMIKAIKD
VRLHTHVDLN MRIGIHSGSV MCGVLGNKKW HFDVWSNDVI IANHMESGGI PGRVHISEAT
LKCLNDAYEV EPGNGGCRDN HLKMLNVKTY LIKRTEPLRP KRRFGTRSSA HLAGSVATAA
PPCATPTALP KSISASGSGS IGGVTATGND GASIDGRSLE YAATIAVPAQ QPTQLLQQQQ
KKNISLNSLP NVVEGVAMDS RRIRNGCGVM GGAGGTGGGG TGPCGMSTVS SPTAMMSAPL
EVQLRPRNGA CSIQNLAEAI DGKGLIIEDE STTDWIPEIP FKNLNSPEDG LNRADSILVD
TKEDHRVSVA VLDEEIDEFI EQNIQINSNK EIRREYLNPW TLKFKDKSQE QKFCQLREDM
FRSNMLCVFV IWIFMVLCQV IIIPRCTRLI ICLSVGTVIL TFCCVLVMAE EFPGLPRCLK
TNSAKLVHQR QRRTLFICGV IVSMCMLSAI GLVLCPSSTY IGTADEHSRF LRMVSPYSNI
SMTEKEFKLN VYLSATIHHN ITISTPASGG PTPLVDITSS GPSDEFVRST LNALTLNLTP
PLPQSHRPYT LTTNGHSVSL SNLSYSDASV MQSSSDVEGQ CAHPEYLVFT WVLCLVSLAT
ALKLYYLVKA LMALAMVAFY TTLIMMKFGS GDSFSLVELS RLGMPLGVQM LILLISFLVM
VCYHARLVEV TSRLDFIWKE QAERELTNMK SNRALNDTLI KNILPDHVAT YYLSDEHTDE
LYSKMHNLCG VMFASIPNFQ DFYSEDIDNG KACIRILNEI ICDFDELLEE PRFASVEKIK
TVGATYMAAA GLNHEHLRLR GETSEDSVCD LVEFAFAMKQ KLEEINGDAF NNFQLRVGIC
SGPLVSGVIG ARKPVYDIWG NTVNVASRMD STGENWRVQV PENTAELLCS RGYTCVKRGE
IAVKGKGMMT TFYVHPKGIS ESQLISPVRM PAGIPLAQTP NLQRQTSHHG SFSAVVFGML
QASKRSTAIA GTPTGTPSPQ IRRGHRGSTF SSVRLSQKST TVNPVRRNTT RVRGRSYRQK
KSSSNNSIVT QASSSYMPSF RRIDQIETTI SKSHNDAL
