CYAA_YEAST
ID CYAA_YEAST Reviewed; 2026 AA.
AC P08678; D6VWH0;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Adenylate cyclase {ECO:0000305};
DE EC=4.6.1.1 {ECO:0000269|PubMed:2934138};
DE AltName: Full=ATP pyrophosphate-lyase;
DE AltName: Full=Adenylyl cyclase;
GN Name=CYR1; Synonyms=CDC35, HSR1, SRA4; OrderedLocusNames=YJL005W;
GN ORFNames=J1401;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=2934138; DOI=10.1016/0092-8674(85)90179-5;
RA Kataoka T., Broek D., Wigler M.;
RT "DNA sequence and characterization of the S. cerevisiae gene encoding
RT adenylate cyclase.";
RL Cell 43:493-505(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RA de Haan M., Smits P.H.M., Grivell L.A.;
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1042-2026.
RX PubMed=3327602; DOI=10.1007/bf00418405;
RA Masson P., Lenzen G., Jacquemin J.M., Danchin A.;
RT "Yeast adenylate cyclase catalytic domain is carboxy terminal.";
RL Curr. Genet. 10:343-352(1986).
RN [6]
RP MUTAGENESIS OF THR-1651.
RX PubMed=1991451; DOI=10.1002/j.1460-2075.1991.tb07956.x;
RA Feger G., de Vendittis E., Vitelli A., Masturzo P., Zahn R., Verrotti A.C.,
RA Kavounis C., Pal G.P., Fasano O.;
RT "Identification of regulatory residues of the yeast adenylyl cyclase.";
RL EMBO J. 10:349-359(1991).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-376; THR-389 AND SER-487, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433; SER-487; SER-497 AND
RP SER-562, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [12]
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=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Plays essential roles in regulation of cellular metabolism by
CC catalyzing the synthesis of a second messenger, cAMP.
CC {ECO:0000269|PubMed:2934138}.
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:2934138};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15390;
CC Evidence={ECO:0000269|PubMed:2934138};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: The presence of GTP-bound RAS2 protein is required
CC in order to elicit a magnesium-dependent adenylyl cyclase activity.
CC {ECO:0000305|PubMed:2934138}.
CC -!- INTERACTION:
CC P08678; P10823: GPA2; NbExp=3; IntAct=EBI-5364, EBI-7382;
CC P08678; P17555: SRV2; NbExp=5; IntAct=EBI-5364, EBI-4024;
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000305}.
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DR EMBL; M12057; AAA34549.1; -; Genomic_DNA.
DR EMBL; Z49280; CAA89295.1; -; Genomic_DNA.
DR EMBL; X87611; CAA60917.1; -; Genomic_DNA.
DR EMBL; X03449; CAA27175.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08786.1; -; Genomic_DNA.
DR PIR; S56776; OYBY.
DR RefSeq; NP_012529.3; NM_001181439.3.
DR AlphaFoldDB; P08678; -.
DR SMR; P08678; -.
DR BioGRID; 33752; 208.
DR ComplexPortal; CPX-695; Adenylyl cyclase complex.
DR DIP; DIP-2317N; -.
DR IntAct; P08678; 25.
DR MINT; P08678; -.
DR STRING; 4932.YJL005W; -.
DR iPTMnet; P08678; -.
DR MaxQB; P08678; -.
DR PaxDb; P08678; -.
DR PRIDE; P08678; -.
DR EnsemblFungi; YJL005W_mRNA; YJL005W; YJL005W.
DR GeneID; 853452; -.
DR KEGG; sce:YJL005W; -.
DR SGD; S000003542; CYR1.
DR VEuPathDB; FungiDB:YJL005W; -.
DR eggNOG; KOG0618; Eukaryota.
DR GeneTree; ENSGT00940000161019; -.
DR HOGENOM; CLU_000430_3_0_1; -.
DR InParanoid; P08678; -.
DR OMA; HYAIRIF; -.
DR BioCyc; YEAST:YJL005W-MON; -.
DR Reactome; R-SCE-6803207; TP53 Regulates Transcription of Caspase Activators and Caspases.
DR PRO; PR:P08678; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P08678; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0004016; F:adenylate cyclase activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IGI:SGD.
DR GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IDA:ComplexPortal.
DR GO; GO:0007265; P:Ras protein signal transduction; IGI:SGD.
DR CDD; cd07302; CHD; 1.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.30.70.1230; -; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR013716; Adenylate_cyclase_G-a-bd.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR InterPro; IPR000159; RA_dom.
DR Pfam; PF08509; Ad_cyc_g-alpha; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF13855; LRR_8; 4.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00789; Ad_cyc_g-alpha; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00369; LRR_TYP; 11.
DR SMART; SM00332; PP2Cc; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS51450; LRR; 15.
DR PROSITE; PS51746; PPM_2; 1.
DR PROSITE; PS50200; RA; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; cAMP biosynthesis; Leucine-rich repeat; Lyase;
KW Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..2026
FT /note="Adenylate cyclase"
FT /id="PRO_0000195731"
FT DOMAIN 676..755
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REPEAT 795..814
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 815..838
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 842..862
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 863..885
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 886..908
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 910..931
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 932..955
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 957..976
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 977..999
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 1001..1016
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 1017..1040
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 1042..1062
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 1063..1086
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 1088..1109
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 1110..1132
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 1134..1156
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 1188..1209
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 1210..1232
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 1233..1256
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 1258..1280
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 1285..1308
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 1319..1344
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT DOMAIN 1357..1624
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT DOMAIN 1668..1805
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1673
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1716
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 376
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 389
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 1651
FT /note="T->D: Attenuation of the response to Ras proteins."
FT /evidence="ECO:0000269|PubMed:1991451"
FT MUTAGEN 1651
FT /note="T->I: Weak Ras-independent activity."
FT /evidence="ECO:0000269|PubMed:1991451"
FT CONFLICT 262
FT /note="S -> L (in Ref. 1; AAA34549)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="S -> L (in Ref. 1; AAA34549)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="D -> H (in Ref. 1; AAA34549)"
FT /evidence="ECO:0000305"
FT CONFLICT 709
FT /note="R -> I (in Ref. 1; AAA34549)"
FT /evidence="ECO:0000305"
FT CONFLICT 962
FT /note="L -> P (in Ref. 1; AAA34549)"
FT /evidence="ECO:0000305"
FT CONFLICT 1388
FT /note="L -> S (in Ref. 1; AAA34549)"
FT /evidence="ECO:0000305"
FT CONFLICT 1427
FT /note="E -> D (in Ref. 4; CAA27175)"
FT /evidence="ECO:0000305"
FT CONFLICT 1461
FT /note="A -> T (in Ref. 4; CAA27175)"
FT /evidence="ECO:0000305"
FT CONFLICT 1566
FT /note="A -> S (in Ref. 1; AAA34549)"
FT /evidence="ECO:0000305"
FT CONFLICT 1735
FT /note="V -> G (in Ref. 1; AAA34549)"
FT /evidence="ECO:0000305"
FT CONFLICT 1956
FT /note="I -> V (in Ref. 4; CAA27175)"
FT /evidence="ECO:0000305"
FT CONFLICT 1996
FT /note="C -> F (in Ref. 1; AAA34549)"
FT /evidence="ECO:0000305"
FT CONFLICT 2009..2026
FT /note="NVVDELLQMVKNAKDLST -> MLLTNFYKWLRTQRIYQLEFCS (in
FT Ref. 4; CAA27175)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2026 AA; 227834 MW; BEAB7419AB6989D0 CRC64;
MSSKPDTGSE ISGPQRQEEQ EQQIEQSSPT EANDRSIHDE VPKVKKRHEQ NSGHKSRRNS
AYSYYSPRSL SMTKSRESIT PNGMDDVSIS NVEHPRPTEP KIKRGPYLLK KTLSSLSMTS
ANSTHDDNKD HGYALNSSKT HNYTSTHNHH DGHHDHHHVQ FFPNRKPSLA ETLFKRFSGS
NSHDGNKSGK ESKVANLSLS TVNPAPANRK PSKDSTLSNH LADNVPSTLR RKVSSLVRGS
SVHDINNGIA DKQIRPKAVA QSENTLHSSD VPNSKRSHRK SFLLGSTSSS SSRRGSNVSS
MTNSDSASMA TSGSHVLQHN VSNVSPTTKS KDSVNSESAD HTNNKSEKVT PEYNENIPEN
SNSDNKREAT TPTIETPISC KPSLFRLDTN LEDVTDITKT VPPTAVNSTL NSTHGTETAS
PKTVIMPEGP RKSVSMADLS VAAAAPNGEF TSTSNDRSQW VAPQSWDVET KRKKTKPKGR
SKSRRSSIDA DELDPMSPGP PSKKDSRHHH DRKDNESMVT AGDSNSSFVD ICKENVPNDS
KTALDTKSVN RLKSNLAMSP PSIRYAPSNL DGDYDTSSTS SSLPSSSISS EDTSSCSDSS
SYTNAYMEAN REQDNKTPIL NKTKSYTKKF TSSSVNMNSP DGAQSSGLLL QDEKDDEVEC
QLEHYYKDFS DLDPKRHYAI RIFNTDDTFT TLSCTPATTV EEIIPALKRK FNITAQGNFQ
ISLKVGKLSK ILRPTSKPIL IERKLLLLNG YRKSDPLHIM GIEDLSFVFK FLFHPVTPSH
FTPEQEQRIM RSEFVHVDLR NMDLTTPPII FYQHTSEIES LDVSNNANIF LPLEFIESSI
KLLSLRMVNI RASKFPSNIT KAYKLVSLEL QRNFIRKVPN SIMKLSNLTI LNLQCNELES
LPAGFVELKN LQLLDLSSNK FMHYPEVINY CTNLLQIDLS YNKIQSLPQS TKYLVKLAKM
NLSHNKLNFI GDLSEMTDLR TLNLRYNRIS SIKTNASNLQ NLFLTDNRIS NFEDTLPKLR
ALEIQENPIT SISFKDFYPK NMTSLTLNKA QLSSIPGELL TKLSFLEKLE LNQNNLTRLP
QEISKLTKLV FLSVARNKLE YIPPELSQLK SLRTLDLHSN NIRDFVDGME NLELTSLNIS
SNAFGNSSLE NSFYHNMSYG SKLSKSLMFF IAADNQFDDA MWPLFNCFVN LKVLNLSYNN
FSDVSHMKLE SITELYLSGN KLTTLSGDTV LKWSSLKTLM LNSNQMLSLP AELSNLSQLS
VFDVGANQLK YNISNYHYDW NWRNNKELKY LNFSGNRRFE IKSFISHDID ADLSDLTVLP
QLKVLGLMDV TLNTTKVPDE NVNFRLRTTA SIINGMRYGV ADTLGQRDYV SSRDVTFERF
RGNDDECLLC LHDSKNQNAD YGHNISRIVR DIYDKILIRQ LERYGDETDD NIKTALRFSF
LQLNKEINGM LNSVDNGADV ANLSYADLLS GACSTVIYIR GKKLFAANLG DCMAILSKNN
GDYQTLTKQH LPTKREEYER IRISGGYVNN GKLDGVVDVS RAVGFFDLLP HIHASPDISV
VTLTKADEML IVATHKLWEY MDVDTVCDIA RENSTDPLRA AAELKDHAMA YGCTENITIL
CLALYENIQQ QNRFTLNKNS LMTRRSTFED TTLRRLQPEI SPPTGNLAMV FTDIKSSTFL
WELFPNAMRT AIKTHNDIMR RQLRIYGGYE VKTEGDAFMV AFPTPTSGLT WCLSVQLKLL
DAQWPEEITS VQDGCQVTDR NGNIIYQGLS VRMGIHWGCP VPELDLVTQR MDYLGPMVNK
AARVQGVADG GQIAMSSDFY SEFNKIMKYH ERVVKGKESL KEVYGEEIIG EVLEREIAML
ESIGWAFFDF GEHKLKGLET KELVTIAYPK ILASRHEFAS EDEQSKLINE TMLFRLRVIS
NRLESIMSAL SGGFIELDSR TEGSYIKFNP KVENGIMQSI SEKDALLFFD HVITRIESSV
ALLHLRQQRC SGLEICRNDK TSARSNIFNV VDELLQMVKN AKDLST
