CYAA_DICDI
ID CYAA_DICDI Reviewed; 1407 AA.
AC Q03100; Q54TF5;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Adenylate cyclase, aggregation specific;
DE EC=4.6.1.1;
DE AltName: Full=ATP pyrophosphate-lyase;
DE AltName: Full=Adenylyl cyclase;
GN Name=acaA; Synonyms=aca; ORFNames=DDB_G0281545;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=1348970; DOI=10.1016/0092-8674(92)90411-5;
RA Pitt G.S., Milona N., Borleis J., Lin K.C., Reed R.R., Devreotes P.N.;
RT "Structurally distinct and stage-specific adenylyl cyclase genes play
RT different roles in Dictyostelium development.";
RL Cell 69:305-315(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8224844; DOI=10.1101/gad.7.11.2172;
RA Pitt G.S., Brandt R., Lin K.C., Devreotes P.N., Schaap P.;
RT "Extracellular cAMP is sufficient to restore developmental gene expression
RT and morphogenesis in Dictyostelium cells lacking the aggregation adenylyl
RT cyclase (ACA).";
RL Genes Dev. 7:2172-2180(1993).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF LEU-394.
RX PubMed=8702473; DOI=10.1074/jbc.271.31.18333;
RA Parent C.A., Devreotes P.N.;
RT "Constitutively active adenylyl cyclase mutant requires neither G proteins
RT nor cytosolic regulators.";
RL J. Biol. Chem. 271:18333-18336(1996).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=9812977; DOI=10.1074/jbc.273.47.30859;
RA Kim H.-J., Chang W.-T., Meima M., Gross J.D., Schaap P.;
RT "A novel adenylyl cyclase detected in rapidly developing mutants of
RT Dictyostelium.";
RL J. Biol. Chem. 273:30859-30862(1998).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF PHE-306; SER-498; LYS-504; GLU-593 AND
RP ILE-649.
RX PubMed=10811616; DOI=10.1093/emboj/19.10.2247;
RA Patel H., Guo K., Parent C., Gross J., Devreotes P.N., Weijer C.J.;
RT "A temperature-sensitive adenylyl cyclase mutant of Dictyostelium.";
RL EMBO J. 19:2247-2256(2000).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11356026; DOI=10.1006/dbio.2001.0232;
RA Verkerke-van Wijk I., Fukuzawa M., Devreotes P.N., Schaap P.;
RT "Adenylyl cyclase A expression is tip-specific in Dictyostelium slugs and
RT directs StatA nuclear translocation and CudA gene expression.";
RL Dev. Biol. 234:151-160(2001).
RN [8]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11422293; DOI=10.1046/j.1440-169x.2001.00572.x;
RA Tsujioka M., Yokoyama M., Nishio K., Kuwayama H., Morio T., Katoh M.,
RA Urushihara H., Saito T., Ochiai H., Tanaka Y., Takeuchi I., Maeda M.;
RT "Spatial expression patterns of genes involved in cyclic AMP responses in
RT Dictyostelium discoideum development.";
RL Dev. Growth Differ. 43:275-283(2001).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, CONSTITUTIVELY ACTIVE MUTANT, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=12600317; DOI=10.1016/s0092-8674(03)00081-3;
RA Kriebel P.W., Barr V.A., Parent C.A.;
RT "Adenylyl cyclase localization regulates streaming during chemotaxis.";
RL Cell 112:549-560(2003).
RN [10]
RP ACTIVITY REGULATION.
RX PubMed=15668169; DOI=10.1016/j.cub.2005.01.007;
RA Comer F.I., Lippincott C.K., Masbad J.J., Parent C.A.;
RT "The PI3K-mediated activation of CRAC independently regulates adenylyl
RT cyclase activation and chemotaxis.";
RL Curr. Biol. 15:134-139(2005).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15821137; DOI=10.1128/ec.4.4.775-786.2005;
RA Stepanovic V., Wessels D., Daniels K., Loomis W.F., Soll D.R.;
RT "Intracellular role of adenylyl cyclase in regulation of lateral pseudopod
RT formation during Dictyostelium chemotaxis.";
RL Eukaryot. Cell 4:775-786(2005).
RN [12]
RP DEVELOPMENTAL STAGE.
RX PubMed=16607013; DOI=10.1128/ec.5.4.658-664.2006;
RA Siol O., Dingermann T., Winckler T.;
RT "The C-module DNA-binding factor mediates expression of the dictyostelium
RT aggregation-specific adenylyl cyclase ACA.";
RL Eukaryot. Cell 5:658-664(2006).
RN [13]
RP ACTIVITY REGULATION.
RX PubMed=16267269; DOI=10.1091/mbc.e05-08-0781;
RA Comer F.I., Parent C.A.;
RT "Phosphoinositide 3-kinase activity controls the chemoattractant-mediated
RT activation and adaptation of adenylyl cyclase.";
RL Mol. Biol. Cell 17:357-366(2006).
CC -!- FUNCTION: Coordinates cell aggregation by synthesizing the cAMP that
CC influences differentiation and morphogenesis of cells within a
CC developing multicellular structure. {ECO:0000269|PubMed:10811616,
CC ECO:0000269|PubMed:12600317, ECO:0000269|PubMed:1348970,
CC ECO:0000269|PubMed:15821137, ECO:0000269|PubMed:8224844,
CC ECO:0000269|PubMed:8702473}.
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:1348970, ECO:0000269|PubMed:8702473};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:8702473};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000269|PubMed:8702473};
CC -!- ACTIVITY REGULATION: Regulated by cyclic AMP receptor 1 through a
CC guanine nucleotide binding protein and protein CRAC. Both positively
CC and negatively regulated by extracellular cAMP; this regulation is part
CC of the mechanism that establishes the oscillatory cAMP waves during
CC aggregation. {ECO:0000269|PubMed:1348970, ECO:0000269|PubMed:15668169,
CC ECO:0000269|PubMed:16267269, ECO:0000269|PubMed:8702473}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 mM for cAMP {ECO:0000269|PubMed:8702473};
CC Vmax=20 pmol/min/mg enzyme {ECO:0000269|PubMed:8702473};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12600317}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:12600317}. Cell projection,
CC uropodium {ECO:0000269|PubMed:12600317}. Note=In non-polarized cells
CC ACA is uniformly distributed at the membrane but upon polarization it
CC becomes highly enriched at the uropodium.
CC -!- TISSUE SPECIFICITY: Expressed throughout the structure in the tipped
CC mound and finger. Expressed primarily in the prestalk region of the
CC slug. In the early culminant expression is increased in the posterior
CC prespore and anterior-most regions and expands into the developing
CC stalk. In the mid and late culminant it is expressed throughout the
CC stalk. {ECO:0000269|PubMed:11356026, ECO:0000269|PubMed:11422293}.
CC -!- DEVELOPMENTAL STAGE: Expressed during development. First detected at 3
CC hours of development. Levels increase during aggregation and peak at 6
CC hours. Levels decrease after tight aggregate formation.
CC {ECO:0000269|PubMed:11356026, ECO:0000269|PubMed:11422293,
CC ECO:0000269|PubMed:1348970, ECO:0000269|PubMed:16607013}.
CC -!- DISRUPTION PHENOTYPE: No cAMP synthesis. Cells are unable to aggregate,
CC stimulation with cAMP pulses restores aggregation but slug and fruiting
CC body formation remains very inefficient. When placed in a cAMP gradient
CC mutants lacking ACA acquire polarity and migrate along the gradient but
CC fail to align in a head to tail fashion and form streams. They are also
CC unable to suppress lateral pseudopod formation, resulting in abnormal
CC turns and inefficient chemotaxis. Transfer of the temperature-sensitive
CC mutant tsaca2 to a temperature of 28 degrees Celsius leads to
CC developmental arrest that is reversible when the temperature is shifted
CC down to 22 degrees Celsius. In mutants with a constitutively active
CC ACA, localization to the uropodium in polarized cells is reduced and
CC these mutants fail to stream in a cAMP gradient.
CC {ECO:0000269|PubMed:12600317, ECO:0000269|PubMed:1348970,
CC ECO:0000269|PubMed:15821137, ECO:0000269|PubMed:8224844,
CC ECO:0000269|PubMed:9812977}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; L05499; AAA33163.1; -; Genomic_DNA.
DR EMBL; L05496; AAA33163.1; JOINED; Genomic_DNA.
DR EMBL; L05497; AAA33163.1; JOINED; Genomic_DNA.
DR EMBL; L05498; AAA33163.1; JOINED; Genomic_DNA.
DR EMBL; AAFI02000042; EAL66534.2; -; Genomic_DNA.
DR PIR; B42239; B42239.
DR RefSeq; XP_640636.2; XM_635544.2.
DR AlphaFoldDB; Q03100; -.
DR SMR; Q03100; -.
DR STRING; 44689.DDB0214814; -.
DR PaxDb; Q03100; -.
DR EnsemblProtists; EAL66534; EAL66534; DDB_G0281545.
DR GeneID; 8623247; -.
DR KEGG; ddi:DDB_G0281545; -.
DR dictyBase; DDB_G0281545; acaA.
DR eggNOG; KOG3619; Eukaryota.
DR HOGENOM; CLU_253935_0_0_1; -.
DR InParanoid; Q03100; -.
DR OMA; KVGRTHI; -.
DR Reactome; R-DDI-163615; PKA activation.
DR Reactome; R-DDI-170660; Adenylate cyclase activating pathway.
DR Reactome; R-DDI-170670; Adenylate cyclase inhibitory pathway.
DR Reactome; R-DDI-418597; G alpha (z) signalling events.
DR Reactome; R-DDI-5610787; Hedgehog 'off' state.
DR PRO; PR:Q03100; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0071944; C:cell periphery; IDA:dictyBase.
DR GO; GO:0031254; C:cell trailing edge; IDA:dictyBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:dictyBase.
DR GO; GO:1903561; C:extracellular vesicle; IDA:dictyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0097708; C:intracellular vesicle; IDA:dictyBase.
DR GO; GO:0005771; C:multivesicular body; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0031259; C:uropod membrane; IDA:dictyBase.
DR GO; GO:0004016; F:adenylate cyclase activity; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007015; P:actin filament organization; IMP:dictyBase.
DR GO; GO:0140582; P:adenylate cyclase-activating G protein-coupled cAMP receptor signaling pathway; IMP:dictyBase.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0061939; P:c-di-GMP signaling; IMP:dictyBase.
DR GO; GO:0006171; P:cAMP biosynthetic process; IDA:dictyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0031271; P:lateral pseudopodium assembly; IMP:dictyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:dictyBase.
DR GO; GO:0008360; P:regulation of cell shape; IMP:dictyBase.
DR GO; GO:0050920; P:regulation of chemotaxis; IMP:dictyBase.
DR GO; GO:0031285; P:regulation of sorocarp stalk cell differentiation; IMP:dictyBase.
DR GO; GO:0010447; P:response to acidic pH; IDA:dictyBase.
DR GO; GO:0031000; P:response to caffeine; IDA:dictyBase.
DR GO; GO:1902168; P:response to catechin; IDA:dictyBase.
DR GO; GO:1904643; P:response to curcumin; IDA:dictyBase.
DR GO; GO:0010042; P:response to manganese ion; IDA:dictyBase.
DR GO; GO:0010225; P:response to UV-C; IDA:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IGI:dictyBase.
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; IPR029787; Nucleotide_cyclase.
DR Pfam; PF00211; Guanylate_cyc; 3.
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 ATP-binding; cAMP biosynthesis; Cell projection; Lyase; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1407
FT /note="Adenylate cyclase, aggregation specific"
FT /id="PRO_0000195714"
FT TOPO_DOM 1..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..962
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 963..979
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 992..1012
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1018..1038
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1071..1091
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1105..1125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1378..1398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1399..1407
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 438..661
FT /note="Guanylate cyclase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT DOMAIN 1189..1311
FT /note="Guanylate cyclase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 28..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 443
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 443
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 444
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 488
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 488
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT MUTAGEN 306
FT /note="F->L: In temperature-sensitive mutant tsaca2."
FT /evidence="ECO:0000269|PubMed:10811616"
FT MUTAGEN 394
FT /note="L->S: Constitutive activity."
FT /evidence="ECO:0000269|PubMed:8702473"
FT MUTAGEN 498
FT /note="S->G: In temperature-sensitive mutant tsaca2."
FT /evidence="ECO:0000269|PubMed:10811616"
FT MUTAGEN 504
FT /note="K->E: In temperature-sensitive mutant tsaca2."
FT /evidence="ECO:0000269|PubMed:10811616"
FT MUTAGEN 593
FT /note="E->V: In temperature-sensitive mutant tsaca2."
FT /evidence="ECO:0000269|PubMed:10811616"
FT MUTAGEN 649
FT /note="I->T: In temperature-sensitive mutant tsaca2."
FT /evidence="ECO:0000269|PubMed:10811616"
FT CONFLICT 567..568
FT /note="NN -> TT (in Ref. 1; AAA33163)"
FT /evidence="ECO:0000305"
FT CONFLICT 578..579
FT /note="NN -> TT (in Ref. 1; AAA33163)"
FT /evidence="ECO:0000305"
FT CONFLICT 940
FT /note="L -> Y (in Ref. 1; AAA33163)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1407 AA; 159702 MW; C7A115B4AE417007 CRC64;
MASSSPMFND HAIARSKYAL NSVLQQTNEL HDGNGGGGYT PSSPHLGGVS LNKSQNQPYT
QYNNGGGGGG GGGGHINPMH LNLNSITNNH NNHHNHHPNT LSTPHNNNHN NNNHSTSHHP
HSNSVANGGH LSQSITQQRG GLADLANAVI NRKNRSDSVQ TKMKPTDSAS NIESWAKVEK
FSSSIFDSEK SKKSNIFQKY TLRLKNSYEK GYLHQHYNSQ IMLLRITNLI GIVAVSYGFT
KEAIFMLIAI RILCFNLFAF SIFLSFLRNR ELYKKLFHPL FLFSFTTFFI TILLEYKTTT
TTLILFLYVV IFCCLYALGC LLFIWMVMCN LMNAICFIIF IFLESTLDRN NLISFVIYIL
TMFLVGASHL YVLEKFRKES FIAEKKLIKE SNILKNEKEK SSKLLNNILP DFIIENIVYD
FEKRDIVIPE PEEYKSCSIL CFDIVQFTNM SAKLDSPSRL VDLLTQVFRE FDTVVLRNGC
QKIKTDGDAY ICACGLKSKK KAKKQMPNSK STPLLQSTSS TSVNNIDLDK DNKDNNNNNN
NNKNSNNNFK NKNNIINNNN NSNSNNNNNN NSNNNNINNS GNDDDDEEIE DSELEHFEKL
IDVAIEIMNL DVLKETGNTE GIQVQFRCGI AAGSVYGGVI GSQKYQFDIW GDTIARSHTL
EQLGQPGKVH VGETIMTHKN WLKKWQYNYN IVSNSECKDQ EHDYEFHKAH GECITSYFVD
WKDDYREKKK KDLSCDFSIN KVLNAETIES KSNNNNYNNN NYNNNNYNNN YNNNNLNNNS
NNNNNEYGSS SSSSSVLGEA VTEQIDCNNT NPPLQHKKSQ SILTNNENDI VSPSLTSNSP
ILDTTVNNNN NNNNTNNNNK NQNNIYGNNN NNEEDFKIKS KSNSSFEIEM SNIKKPKSRF
IDRVMGILHH VKISNDKIDK EIIQIDEDFV KVTKLRKYFL FFENLTTEKF FHKYVIINNV
VETKFFLVIG LILHLMFYLD DHIMDSAPYF NSNVIYLVMG IAFLVYIGLS FTRIFRTPLV
YQIAFFILLC AFGVCTVLEL IRFQNPLARS SLTRVCATLF YLNVFHSLNF LSVLFLNLFI
FSFFIICSIL ISPTLTNHLY ETDYIGFVIV LLIQICSSYG MKLAMRKAWV VNCKINFKTI
SVNKEKDKFN FLLKSIFPQS ALTKLRDMID TPNIETKGIV YVQPHQDVSI MFIQIAGFQE
YDEPKDLIKK LNDIFSFFDG LLNQKYGGTV EKIKTIGNTY MAVSGLDGSP SFLEKMSDFA
LDVKAYTNSV AISRVVRIGI SHGPLVAGCI GISRAKFDVW GDTANTASRM QSNAQDNEIM
VTHSVYERLN KLFYFDDEKE ILVKGKGKMV THVLKGKKDL EQTNKWFTKP PEVWEVNATP
AGIASPLSGT LLGEIGSFTT PRFHLSS
