CYA1_DROME
ID CYA1_DROME Reviewed; 2248 AA.
AC P32870; Q9TWA7; Q9VY17;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Ca(2+)/calmodulin-responsive adenylate cyclase;
DE EC=4.6.1.1;
DE AltName: Full=ATP pyrophosphate-lyase;
DE AltName: Full=Protein rutabaga;
GN Name=rut; ORFNames=CG9533;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Canton-S; TISSUE=Head;
RX PubMed=1739965; DOI=10.1016/0092-8674(92)90185-f;
RA Levin L.R., Han P.-L., Hwang P.M., Feinstein P.G., Davis R.L., Reed R.R.;
RT "The Drosophila learning and memory gene rutabaga encodes a
RT Ca2+/Calmodulin-responsive adenylyl cyclase.";
RL Cell 68:479-489(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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 [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
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).
CC -!- FUNCTION: This is a membrane-bound, calmodulin-sensitive adenylyl
CC cyclase. Inactivation of this cyclase leads to a learning and memory
CC defect.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by calcium/calmodulin and G protein.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Mushroom bodies of the fly brain.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; M81887; AAA28844.1; -; mRNA.
DR EMBL; AE014298; AAF48388.1; -; Genomic_DNA.
DR PIR; C42088; C42088.
DR PIR; D42088; D42088.
DR RefSeq; NP_511156.2; NM_078601.4.
DR AlphaFoldDB; P32870; -.
DR SMR; P32870; -.
DR BioGRID; 58765; 16.
DR IntAct; P32870; 6.
DR STRING; 7227.FBpp0073809; -.
DR GlyGen; P32870; 2 sites.
DR PaxDb; P32870; -.
DR EnsemblMetazoa; FBtr0073992; FBpp0073809; FBgn0003301.
DR GeneID; 32406; -.
DR KEGG; dme:Dmel_CG9533; -.
DR UCSC; CG9533-RA; d. melanogaster.
DR CTD; 32406; -.
DR FlyBase; FBgn0003301; rut.
DR VEuPathDB; VectorBase:FBgn0003301; -.
DR eggNOG; KOG3619; Eukaryota.
DR InParanoid; P32870; -.
DR OrthoDB; 594476at2759; -.
DR PhylomeDB; P32870; -.
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 SignaLink; P32870; -.
DR BioGRID-ORCS; 32406; 0 hits in 3 CRISPR screens.
DR ChiTaRS; rut; fly.
DR GenomeRNAi; 32406; -.
DR PRO; PR:P32870; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003301; Expressed in crop (Drosophila) and 20 other tissues.
DR ExpressionAtlas; P32870; baseline and differential.
DR Genevisible; P32870; DM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:FlyBase.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0004016; F:adenylate cyclase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008294; F:calcium- and calmodulin-responsive adenylate cyclase activity; IDA:FlyBase.
DR GO; GO:0005516; F:calmodulin 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:0007615; P:anesthesia-resistant memory; IMP:FlyBase.
DR GO; GO:0008306; P:associative learning; IDA:FlyBase.
DR GO; GO:0048675; P:axon extension; IMP:FlyBase.
DR GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
DR GO; GO:0006171; P:cAMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:FlyBase.
DR GO; GO:0007623; P:circadian rhythm; IMP:UniProtKB.
DR GO; GO:0001661; P:conditioned taste aversion; IMP:FlyBase.
DR GO; GO:0007619; P:courtship behavior; TAS:FlyBase.
DR GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IDA:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0007612; P:learning; IMP:FlyBase.
DR GO; GO:0007611; P:learning or memory; IMP:FlyBase.
DR GO; GO:0007617; P:mating behavior; TAS:FlyBase.
DR GO; GO:0072375; P:medium-term memory; IMP:FlyBase.
DR GO; GO:0007613; P:memory; IMP:FlyBase.
DR GO; GO:0007591; P:molting cycle, chitin-based cuticle; IGI:FlyBase.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:FlyBase.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:FlyBase.
DR GO; GO:0008355; P:olfactory learning; TAS:FlyBase.
DR GO; GO:0090328; P:regulation of olfactory learning; IMP:FlyBase.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; IMP:FlyBase.
DR GO; GO:0009408; P:response to heat; IMP:FlyBase.
DR GO; GO:0006979; P:response to oxidative stress; IMP:FlyBase.
DR GO; GO:0007614; P:short-term memory; IMP:FlyBase.
DR GO; GO:0030431; P:sleep; IMP: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; 2.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Calmodulin-binding; cAMP biosynthesis; Glycoprotein; Lyase;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..2248
FT /note="Ca(2+)/calmodulin-responsive adenylate cyclase"
FT /id="PRO_0000195716"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..705
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 706..726
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 730..750
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 770..791
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 792..813
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 814..834
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 842..867
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 868..888
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 889..2248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 275..402
FT /note="Guanylate cyclase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT DOMAIN 963..1107
FT /note="Guanylate cyclase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1217..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1420..1448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1483..1530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1561..1617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1663..1685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1739..1826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1902..2057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2077..2112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2190..2248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1492..1530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1563..1577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1578..1595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1596..1614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1739..1820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1949..1964
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1979..1994
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1995..2024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2025..2040
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2190..2239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 281
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 324
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 324
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT CARBOHYD 800
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 807
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 1026
FT /note="G->R: Abolishes catalytic activity."
FT CONFLICT 64
FT /note="A -> V (in Ref. 1; AAA28844)"
FT /evidence="ECO:0000305"
FT CONFLICT 596
FT /note="G -> S (in Ref. 1; AAA28844)"
FT /evidence="ECO:0000305"
FT CONFLICT 1286..1287
FT /note="QH -> HQ (in Ref. 1; AAA28844)"
FT /evidence="ECO:0000305"
FT CONFLICT 1291
FT /note="Q -> QH (in Ref. 1; AAA28844)"
FT /evidence="ECO:0000305"
FT CONFLICT 1406
FT /note="S -> G (in Ref. 1; AAA28844)"
FT /evidence="ECO:0000305"
FT CONFLICT 1507
FT /note="Q -> H (in Ref. 1; AAA28844)"
FT /evidence="ECO:0000305"
FT CONFLICT 1511..1514
FT /note="HQQP -> QPQS (in Ref. 1; AAA28844)"
FT /evidence="ECO:0000305"
FT CONFLICT 1682
FT /note="H -> Q (in Ref. 1; AAA28844)"
FT /evidence="ECO:0000305"
FT CONFLICT 1696
FT /note="A -> T (in Ref. 1; AAA28844)"
FT /evidence="ECO:0000305"
FT CONFLICT 1771..1772
FT /note="Missing (in Ref. 1; AAA28844)"
FT /evidence="ECO:0000305"
FT CONFLICT 1801
FT /note="S -> G (in Ref. 1; AAA28844)"
FT /evidence="ECO:0000305"
FT CONFLICT 1912
FT /note="H -> HH (in Ref. 1; AAA28844)"
FT /evidence="ECO:0000305"
FT CONFLICT 1950
FT /note="H -> N (in Ref. 1; AAA28844)"
FT /evidence="ECO:0000305"
FT CONFLICT 2218
FT /note="H -> Q (in Ref. 1; AAA28844)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2248 AA; 248824 MW; F7E6B4656A2D073C CRC64;
MDHAVKATRG RPLNTLRFEN DELECLYQRY TLKLQRFSVL GVVALVFVLC GVMAALSLTF
NNAATFHNIF NAIVCGLFAV VLVLLQCSVI KDHHLPTLCY GILLFTASIC VVSMPTLGSV
FPVDTKEVMA EGVWQIVFVV FLAYAMMPLQ IWEAVAFGIA LPSVHISLTV YKIFTDALRY
LEYNQLIANI VIFIGVNVAG LVVNIMMERA QRRTFLDTRN CIASRLEIQD ENEKLERLLL
SVLPQHVAMQ MKNDILSPVA GQFHRIYIQK HENVSILFAD IVGFTVLSSQ CSAQELVRLL
NELFGRFDQL AHDNHCLRIK ILGDCYYCVS GLPEPRKDHA KCAVEMGLDM IDAIATVVEA
TDVILNMRVG IHTGRVLCGV LGLRKWQFDV WSNDVTLANH MESGGEPGRV HVTRATLDSL
SGEYEVEAGH GDERSSYLRD HGVDTFFIVP PPHRRKPLML NTLGVRSAIG SRRKLSFRNV
SNVVMQLLHT IKFSEPVPFS NIATGSFPSA ASALGGGVSV GGGGGGGGGG VARGSTCEAN
SGNVQVSEKG SRKVIRLQKI LHATPPPHGM GYGSVVGSGG GVDSGISGGG GCVSGGIAGG
GGVQVTVGTN PNSTASTISR IHRHNHKNNK SQSKVADKFK RPFRKRHSVA AHHQPTNRVN
RFLSQAINAR SVDCDKSEHV DRLTLRFRQS DMEREYHKDF DLGFTTAMGC SLLLLILGAA
LQVTALPRTL ILLLLFLFAF IWVSAILMLL LAVRLKWIIW DISESFSLRM AITIFTVILI
YSVGQVNVFT CVSDHPCSGN GTTSFQNDSH RKCSLPQYVS LSAAFAFLSV SVFLRLPIIF
KSLLVLGMGT IYGLFIELSH QNIFECYDNR VNASIPLHLI SLARIAIFMI AILVHGRLVE
GTARLDFLWQ LQASQEKKEM DVLQESNKRI LHNLLPAHVA AHFLDAQFRN NMELYHQSYA
KVGVIFASVP NFNEFYTEMD GSDQGLECLR LLNEIIADFD ELLKEDRFRG IDKIKTVGST
YMAVVGLIPE YKIQPNDPNS VRRHMTALIE YVKAMRHSLQ EINSHSYNNF MLRVGINIGP
VVAGVIGARK PQYDIWGNTV NVASRMDSTG VPGYSQVTQE VVDSLVGSHF EFRCRGTIKV
KGKGDMVTYF LCDSGNKSLN GEVRNAMSLP QSLHAPDYYM KVSQFPENRV NTDTYSKKEN
GHLYAGNGVE EQQLLLQHQH KQHDPLPLPA PPPPVHHHLH QQQQQRLNSK LQKQPIFMAN
GGLPNIRENG NGHNGEHQQQ QQQQQQHQQQ QQQQQQHGGF MVATTTPPAA VAVPLQPQHH
QLQFQHPHQH PLPSAVSVPV QHQILLHHQL QLQHQPVPSV MLREFNIIEN PTSGGRHQQM
EQLPPHHGSL DLSGMGMGVG AGVLGSDCFM MPRRDRERTY VPPLNQHGHH PPHHLHSNLN
LNQSQHPPSF TSLGYGQCRE SEPLLHASSV APVAKIMPMQ HAPKYEPPRY TSPHTMLSQQ
HQQQQQQQHQ HQQPQSQSAQ DQQTHPAQDP HPLQRQYAMY SQQPQLPPKP VLRTYMKPLP
KLPTDLEESR DMSSTDDLSS RPHSPSMSSS DESYSKTTEG EGEGDEDSPR MVNGGHLHHR
NGYHLPAGGL VNPLQWLYPC DIQVDPTSPV VDMAHLHDFE LSSTTESQGH HTNSNTTSNT
QHKGDSCNSF DFQKAAVGTA AGAAIATKSP FERELQRLLN ESSRARCLAT ATTTAGAIST
TDQTASNGSR ELSYSLSNGK LSSANGHGVG GSGSGSGSGS GSGSAVGNGS GGSGSSNGNL
SGGSGSNSNS GNNNSSHHKT EQQQNMDHEH LAGGKLLGSN SFMIAKHPVG LEAIKEITRN
KNPSESSQMQ TSDTESCEIL HENRNQMHVL AMLEMHTAKE LNGSHAHHGQ HHQQPQRTHR
QRPRSKELQY SHESLDGLDG AVQSQSQQRH QRYHHHHHHQ QRQQQQQRYN HVQEQEERDD
TEDNLADEEF EDDEVGRDVR QKRLQKSELN HKRSEVATEA GNHHDDEVEE EDDDDDEEED
HRNGGREAAP LTNGSMRGLE ANVINDELKY GATHLNHQSM DSNPLESQSE WSDDDCREEA
TGGAESTGYI TDEPGLENIS LLNEAGLTDA EGALSDVNSL YNAPDVDDTS VSSRASSRLL
SLDSLSGLYD CDLDSKHELA IVNASHKISS KFGQPLSPAQ QQHQQQQQQQ QQQQQQHHQQ
QLQQNPQHTQ AQSHLAPVQF QSAEELRE
