ID   PDE4A_DROME             Reviewed;        1209 AA.
AC   Q9W4T4;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 2.
DT   24-JAN-2024, entry version 157.
DE   RecName: Full=3',5'-cyclic-AMP phosphodiesterase, isoform I {ECO:0000305};
DE            EC=3.1.4.53;
DE   AltName: Full=Learning/memory process protein;
DE   AltName: Full=Protein dunce;
DE   AltName: Full=cAMP-specific phosphodiesterase, isoform I {ECO:0000305};
GN   Name=dnc {ECO:0000312|EMBL:AAF45858.3}; ORFNames=CG32498;
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] {ECO:0000312|EMBL:AAF45858.3}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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:0000305, ECO:0000312|EMBL:AAF45858.3}
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-524.
RC   STRAIN=Oregon-R;
RX   PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA   Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA   Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA   Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA   Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA   Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA   Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA   McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA   Glover D.M.;
RT   "From sequence to chromosome: the tip of the X chromosome of D.
RT   melanogaster.";
RL   Science 287:2220-2222(2000).
RN   [4] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 495-1209, FUNCTION, CATALYTIC
RP   ACTIVITY, AND SUBUNIT.
RC   STRAIN=Canton-S {ECO:0000269|PubMed:1660926};
RX   PubMed=1660926; DOI=10.1016/0022-2836(91)90496-s;
RA   Qiu Y.H., Chen C.-N., Malone T., Richter L., Beckendorf S.K., Davis R.L.;
RT   "Characterization of the memory gene dunce of Drosophila melanogaster.";
RL   J. Mol. Biol. 222:553-565(1991).
CC   -!- FUNCTION: Hydrolyzes the second messenger cAMP, which is a key
CC       regulator of many important physiological processes (By similarity).
CC       Vital for female fertility. Required for learning/memory. {ECO:0000250,
CC       ECO:0000269|PubMed:1660926}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165,
CC         ChEBI:CHEBI:456215; EC=3.1.4.53;
CC         Evidence={ECO:0000269|PubMed:1660926};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC       Note=Binds 2 divalent metal cations per subunit. Site 1 may
CC       preferentially bind zinc ions, while site 2 has a preference for
CC       magnesium and/or manganese ions. {ECO:0000250};
CC   -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC       3',5'-cyclic AMP: step 1/1.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1660926}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing, Alternative initiation; Named isoforms=12;
CC       Name=I {ECO:0000269|PubMed:1660926}; Synonyms=B
CC       {ECO:0000303|PubMed:10731132}, S;
CC         IsoId=Q9W4T4-1; Sequence=Displayed;
CC       Name=II {ECO:0000269|PubMed:1660926}; Synonyms=I
CC       {ECO:0000303|PubMed:10731132}, J {ECO:0000303|PubMed:10731132};
CC         IsoId=P12252-1; Sequence=External;
CC       Name=III; Synonyms=E, P;
CC         IsoId=P12252-7; Sequence=External;
CC       Name=IV {ECO:0000269|PubMed:1660926}; Synonyms=A
CC       {ECO:0000303|PubMed:10731132};
CC         IsoId=P12252-3; Sequence=External;
CC       Name=V {ECO:0000269|PubMed:1660926}; Synonyms=C
CC       {ECO:0000303|PubMed:10731132};
CC         IsoId=P12252-4; Sequence=External;
CC       Name=VI {ECO:0000269|PubMed:1660926}; Synonyms=D
CC       {ECO:0000303|PubMed:10731132};
CC         IsoId=P12252-5; Sequence=External;
CC       Name=VII {ECO:0000269|PubMed:1660926}; Synonyms=L
CC       {ECO:0000303|PubMed:10731132};
CC         IsoId=P12252-6; Sequence=External;
CC       Name=F {ECO:0000303|PubMed:10731132};
CC         IsoId=Q8IRU4-1; Sequence=External;
CC       Name=G {ECO:0000303|PubMed:10731132};
CC         IsoId=Q9W4S9-2; Sequence=External;
CC       Name=N {ECO:0000303|PubMed:10731132};
CC         IsoId=Q9W4S9-1; Sequence=External;
CC       Name=R; Synonyms=Q;
CC         IsoId=P12252-8, Q9W4T0-1; Sequence=External;
CC       Name=U; Synonyms=T;
CC         IsoId=P12252-9; Sequence=External;
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC       PDE4 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA19668.1; Type=Erroneous gene model prediction; 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; AE014298; AAF45858.3; -; Genomic_DNA.
DR   EMBL; AL024484; CAA19668.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; NP_726846.1; NM_166959.2. [Q9W4T4-1]
DR   RefSeq; NP_726847.2; NM_166960.3. [Q9W4T4-1]
DR   AlphaFoldDB; Q9W4T4; -.
DR   SMR; Q9W4T4; -.
DR   BioGRID; 57834; 17.
DR   IntAct; Q9W4T4; 1.
DR   STRING; 7227.FBpp0305507; -.
DR   GlyGen; Q9W4T4; 1 site, 1 O-linked glycan (1 site).
DR   PaxDb; 7227-FBpp0305507; -.
DR   DNASU; 31309; -.
DR   EnsemblMetazoa; FBtr0070509; FBpp0070485; FBgn0000479. [Q9W4T4-1]
DR   EnsemblMetazoa; FBtr0333315; FBpp0305507; FBgn0000479. [Q9W4T4-1]
DR   GeneID; 31309; -.
DR   UCSC; CG32498-RA; d. melanogaster. [Q9W4T4-1]
DR   AGR; FB:FBgn0000479; -.
DR   CTD; 31309; -.
DR   FlyBase; FBgn0000479; dnc.
DR   VEuPathDB; VectorBase:FBgn0000479; -.
DR   eggNOG; KOG3689; Eukaryota.
DR   GeneTree; ENSGT00940000155190; -.
DR   HOGENOM; CLU_007660_0_0_1; -.
DR   InParanoid; Q9W4T4; -.
DR   OrthoDB; 240889at2759; -.
DR   PhylomeDB; Q9W4T4; -.
DR   Reactome; R-DME-180024; DARPP-32 events.
DR   Reactome; R-DME-418555; G alpha (s) signalling events.
DR   UniPathway; UPA00762; UER00747.
DR   BioGRID-ORCS; 31309; 1 hit in 3 CRISPR screens.
DR   ChiTaRS; dnc; fly.
DR   GenomeRNAi; 31309; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0000479; Expressed in brain and 29 other cell types or tissues.
DR   ExpressionAtlas; Q9W4T4; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; ISS:FlyBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007615; P:anesthesia-resistant memory; IMP:FlyBase.
DR   GO; GO:0008306; P:associative learning; IMP:FlyBase.
DR   GO; GO:0048675; P:axon extension; IMP:FlyBase.
DR   GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase.
DR   GO; GO:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0007268; P:chemical synaptic transmission; IMP:FlyBase.
DR   GO; GO:0007623; P:circadian rhythm; TAS:FlyBase.
DR   GO; GO:0001661; P:conditioned taste aversion; IMP:FlyBase.
DR   GO; GO:0007619; P:courtship behavior; TAS:FlyBase.
DR   GO; GO:0007612; P:learning; 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:0106072; P:negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:FlyBase.
DR   GO; GO:0046958; P:nonassociative learning; TAS:FlyBase.
DR   GO; GO:0008355; P:olfactory learning; TAS:FlyBase.
DR   GO; GO:0010738; P:regulation of protein kinase A signaling; IMP:FlyBase.
DR   GO; GO:0007614; P:short-term memory; IMP:FlyBase.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0040040; P:thermosensory behavior; IMP:FlyBase.
DR   CDD; cd00077; HDc; 1.
DR   Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR040844; PDE4_UCR.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR   InterPro; IPR023174; PDEase_CS.
DR   PANTHER; PTHR11347:SF219; CAMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE, ISOFORM I; 1.
DR   PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR   Pfam; PF18100; PDE4_UCR; 1.
DR   Pfam; PF00233; PDEase_I; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS00126; PDEASE_I_1; 1.
DR   PROSITE; PS51845; PDEASE_I_2; 1.
DR   Genevisible; Q9W4T4; DM.
PE   1: Evidence at protein level;
KW   Alternative initiation; Alternative splicing; cAMP; Hydrolase;
KW   Metal-binding; Reference proteome.
FT   CHAIN           1..1209
FT                   /note="3',5'-cyclic-AMP phosphodiesterase, isoform I"
FT                   /id="PRO_0000198817"
FT   DOMAIN          795..1124
FT                   /note="PDEase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT   REGION          16..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          59..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          442..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          626..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          754..792
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1146..1209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..342
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..649
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        754..768
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        775..790
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1163..1179
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        871
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         871..875
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /evidence="ECO:0000250"
FT   BINDING         875
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         911
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         912
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /evidence="ECO:0000250"
FT   BINDING         912
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         912
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         1029
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /evidence="ECO:0000250"
FT   BINDING         1029
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         1080
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /evidence="ECO:0000250"
FT   SITE            1032
FT                   /note="Binds AMP, but not cAMP"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        1097
FT                   /note="D -> S (in Ref. 4; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1166
FT                   /note="S -> T (in Ref. 4; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1181..1182
FT                   /note="SG -> R (in Ref. 4; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1209 AA;  129413 MW;  A7E00D5BA862C1BE CRC64;
     MMRLARFTQG FSFNKNVAKH RGSGSSNGTG NGSGTGNGQG LGGSCSANGL AATGGVGGGG
     GSGSGGGGCG SGSGSGSGKR KSKARTKCFG GTVFRCCLPC RGGGSAAPAT SPPQTPAQTP
     DELKVIPEDC NLEKSAEQKR DLLERNNKED DLLNRTVSGS ELDLYGGAGG GTKKHSLADT
     IDTSVTTPIS LKTLINDVDE ELDQQLSAAD IAAASLASGL VARRAEPETL SDASVSPTAV
     VQQQQQQQQQ LQQPLLQSQP HFVPSSGNIL SQVTLYSGSN PSTNPCQSAV QNQGQNSNPN
     PNQNPNTNPN QNQQRCSCQP QTSPLPHIKE EEESDQANFK HQTSLKEHQP LPPPITIATG
     YCGSCESVHH SSATSSSAGT VPPGGQQTQE YIAGTSSTPS PRIKLKFRKP HKSCWSRIVL
     APIGSAGGSS SATTVIGSNS NETLASSSTT GGTATTTQNS SSVSVAAHHR LTSSSASALA
     TSHPSNSQLL PTSKMQAEQG SIGDLQKYHS RYLKNRRHTL ANVRFDVENG QGARSPLEGG
     SPSAGLVLQN LPQRRESFLY RSDSDFEMSP KSMSRNSSIA SERFKEQEAS ILVDRSHGED
     LIVTPFAQIL ASLRSVRNNL LSLTNVPASN KSRRPNQSSS ASRSGNPPGA PLSQGEEAYT
     RLATDTIEEL DWCLDQLETI QTHRSVSDMA SLKFKRMLNK ELSHFSESSR SGNQISEYIC
     STFLDKQQEF DLPSLRVEDN PELVAANAAA GQQSAGQYAR SRSPRGPPMS QISGVKRPLS
     HTNSFTGERL PTFGVETPRE NELGTLLGEL DTWGIQIFSI GEFSVNRPLT CVAYTIFQSR
     ELLTSLMIPP KTFLNFMSTL EDHYVKDNPF HNSLHAADVT QSTNVLLNTP ALEGVFTPLE
     VGGALFAACI HDVDHPGLTN QFLVNSSSEL ALMYNDESVL ENHHLAVAFK LLQNQGCDIF
     CNMQKKQRQT LRKMVIDIVL STDMSKHMSL LADLKTMVET KKVAGSGVLL LDNYTDRIQV
     LENLVHCADL SNPTKPLPLY KRWVALLMEE FFLQGDKERE SGMDISPMCD RHNATIEKSQ
     VGFIDYIVHP LWETWADLVH PDAQDILDTL EENRDYYQSM IPPSPPPSGV DENPQEDRIR
     FQVTLEESDQ ENLAELEEGD ESGGESTTTG TTGTTAASAL SGAGGGGGGG GGMAPRTGGC
     QNQPQHGGM
//