PDE4B_DROME
ID PDE4B_DROME Reviewed; 1070 AA.
AC P12252; M9PGD1; M9PGX1; O76918; Q8IRU3; Q8IRU6; Q8IRU8; Q8IRV0; Q8MRN3;
AC Q8T8M0; Q9NF62; Q9W4S8; Q9W4T0; Q9W4T1;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 4.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=cAMP-specific 3',5'-cyclic phosphodiesterase;
DE EC=3.1.4.53 {ECO:0000269|PubMed:1660926};
DE AltName: Full=Learning/memory process protein;
DE AltName: Full=Protein dunce;
GN Name=dnc; 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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS III; IV AND R),
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 293-1070 (ISOFORMS II; V AND
RP VI), NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 356-1070 (ISOFORM I),
RP SEQUENCE REVISION, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=Canton-S;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 699-1070.
RX PubMed=3025834; DOI=10.1073/pnas.83.24.9313;
RA Chen C.-N., Denome S., Davis R.L.;
RT "Molecular analysis of cDNA clones and the corresponding genomic coding
RT sequences of the Drosophila dunce+ gene, the structural gene for cAMP
RT phosphodiesterase.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:9313-9317(1986).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING
RP (ISOFORMS I; G AND VII).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM VII).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278;
CC Evidence={ECO:0000305|PubMed:1660926};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:Q07343};
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|UniProtKB:Q07343};
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC 3',5'-cyclic AMP: step 1/1. {ECO:0000250|UniProtKB:Q07343}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1660926}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=12;
CC Name=II; Synonyms=I, J;
CC IsoId=P12252-1; Sequence=Displayed;
CC Name=IV; Synonyms=A;
CC IsoId=P12252-3; Sequence=VSP_004585, VSP_004586;
CC Name=V; Synonyms=C;
CC IsoId=P12252-4; Sequence=VSP_004588;
CC Name=VI; Synonyms=D;
CC IsoId=P12252-5; Sequence=VSP_004589;
CC Name=VII; Synonyms=L;
CC IsoId=P12252-6; Sequence=VSP_004587;
CC Name=III; Synonyms=E, P;
CC IsoId=P12252-7; Sequence=VSP_018826;
CC Name=R; Synonyms=Q;
CC IsoId=P12252-8, Q9W4T0-1;
CC Sequence=VSP_054955, VSP_054958;
CC Name=U; Synonyms=T;
CC IsoId=P12252-9; Sequence=VSP_054956, VSP_054957;
CC Name=I; Synonyms=B, S;
CC IsoId=Q9W4T4-1; Sequence=External;
CC Name=F;
CC IsoId=Q8IRU4-1; Sequence=External;
CC Name=G;
CC IsoId=Q9W4S9-2; Sequence=External;
CC Name=N;
CC IsoId=Q9W4S9-1; Sequence=External;
CC -!- MISCELLANEOUS: [Isoform III]: Produced by alternative initiation at
CC Met-429 of isoform II. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC PDE4 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC34201.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA38960.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAD24781.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X55167; CAA38960.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X55168; CAA38960.1; JOINED; Genomic_DNA.
DR EMBL; X55169; CAA38960.1; JOINED; Genomic_DNA.
DR EMBL; X55170; CAA38960.1; JOINED; Genomic_DNA.
DR EMBL; X55171; CAA38960.1; JOINED; Genomic_DNA.
DR EMBL; X55172; CAA38960.1; JOINED; Genomic_DNA.
DR EMBL; X55173; CAA38960.1; JOINED; Genomic_DNA.
DR EMBL; X55174; CAA38960.1; JOINED; Genomic_DNA.
DR EMBL; X55175; CAA38960.1; JOINED; Genomic_DNA.
DR EMBL; M14982; AAC34201.1; ALT_INIT; Unassigned_DNA.
DR EMBL; M14978; AAC34201.1; JOINED; Unassigned_DNA.
DR EMBL; M14979; AAC34201.1; JOINED; Unassigned_DNA.
DR EMBL; M14980; AAC34201.1; JOINED; Unassigned_DNA.
DR EMBL; M14981; AAC34201.1; JOINED; Unassigned_DNA.
DR EMBL; AE014298; AAF45861.2; -; Genomic_DNA.
DR EMBL; AE014298; AAF45862.3; -; Genomic_DNA.
DR EMBL; AE014298; AAF45865.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09600.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09601.3; -; Genomic_DNA.
DR EMBL; AE014298; AAN09602.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09604.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09607.2; -; Genomic_DNA.
DR EMBL; AE014298; AGB95048.1; -; Genomic_DNA.
DR EMBL; AE014298; AGB95049.1; -; Genomic_DNA.
DR EMBL; AL121800; CAD24781.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY119511; AAM50165.1; -; mRNA.
DR PIR; S65543; S65543.
DR RefSeq; NP_001259201.1; NM_001272272.1. [P12252-7]
DR RefSeq; NP_001259202.1; NM_001272273.1. [P12252-8]
DR RefSeq; NP_001259203.1; NM_001272274.1. [P12252-9]
DR RefSeq; NP_726849.1; NM_166961.2. [P12252-1]
DR RefSeq; NP_726850.1; NM_166962.2. [P12252-4]
DR RefSeq; NP_726851.3; NM_166963.2. [P12252-9]
DR RefSeq; NP_726852.2; NM_166964.2. [P12252-5]
DR RefSeq; NP_726853.2; NM_166965.2. [P12252-1]
DR RefSeq; NP_726854.2; NM_166966.3. [P12252-8]
DR RefSeq; NP_726855.1; NM_166967.2. [P12252-3]
DR RefSeq; NP_726857.1; NM_166969.2. [P12252-7]
DR RefSeq; NP_726859.2; NM_166971.2. [P12252-6]
DR AlphaFoldDB; P12252; -.
DR SMR; P12252; -.
DR BioGRID; 57834; 17.
DR IntAct; P12252; 3.
DR DNASU; 31309; -.
DR EnsemblMetazoa; FBtr0070511; FBpp0070487; FBgn0000479. [P12252-1]
DR EnsemblMetazoa; FBtr0070512; FBpp0070488; FBgn0000479. [P12252-4]
DR EnsemblMetazoa; FBtr0070513; FBpp0070489; FBgn0000479. [P12252-1]
DR EnsemblMetazoa; FBtr0070515; FBpp0070491; FBgn0000479. [P12252-5]
DR EnsemblMetazoa; FBtr0070517; FBpp0070493; FBgn0000479. [P12252-3]
DR EnsemblMetazoa; FBtr0070518; FBpp0070494; FBgn0000479. [P12252-7]
DR EnsemblMetazoa; FBtr0070522; FBpp0070498; FBgn0000479. [P12252-6]
DR EnsemblMetazoa; FBtr0333312; FBpp0305504; FBgn0000479. [P12252-7]
DR EnsemblMetazoa; FBtr0333313; FBpp0305505; FBgn0000479. [P12252-8]
DR EnsemblMetazoa; FBtr0333314; FBpp0305506; FBgn0000479. [P12252-8]
DR EnsemblMetazoa; FBtr0333316; FBpp0305508; FBgn0000479. [P12252-9]
DR EnsemblMetazoa; FBtr0333317; FBpp0305509; FBgn0000479. [P12252-9]
DR GeneID; 31309; -.
DR UCSC; CG32498-RA; d. melanogaster. [P12252-1]
DR CTD; 31309; -.
DR FlyBase; FBgn0000479; dnc.
DR VEuPathDB; VectorBase:FBgn0000479; -.
DR GeneTree; ENSGT00940000155190; -.
DR OMA; ANTCFEV; -.
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 tissues.
DR ExpressionAtlas; P12252; baseline and differential.
DR Genevisible; P12252; DM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IBA:GO_Central.
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: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:0007613; P:memory; 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; -; 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 Pfam; PF18100; PDE4_UCR; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Alternative splicing; cAMP; Hydrolase;
KW Metal-binding; Reference proteome.
FT CHAIN 1..1070
FT /note="cAMP-specific 3',5'-cyclic phosphodiesterase"
FT /id="PRO_0000023342"
FT DOMAIN 656..985
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1040
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 732
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 732..736
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250"
FT BINDING 736
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 772
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 773
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250"
FT BINDING 773
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 773
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 890
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250"
FT BINDING 890
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 941
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250"
FT SITE 893
FT /note="Binds AMP, but not cAMP"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..549
FT /note="Missing (in isoform VII)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_004587"
FT VAR_SEQ 1..428
FT /note="Missing (in isoform III)"
FT /evidence="ECO:0000303|PubMed:1660926"
FT /id="VSP_018826"
FT VAR_SEQ 1..369
FT /note="Missing (in isoform IV)"
FT /evidence="ECO:0000303|PubMed:1660926"
FT /id="VSP_004585"
FT VAR_SEQ 1..367
FT /note="Missing (in isoform R)"
FT /evidence="ECO:0000303|PubMed:1660926"
FT /id="VSP_054955"
FT VAR_SEQ 1..355
FT /note="Missing (in isoform U)"
FT /evidence="ECO:0000305"
FT /id="VSP_054956"
FT VAR_SEQ 356..385
FT /note="GLHDMLKRAQGRSPLSPRISFPGSDSDLFG -> MQAEQGSIGDLQKYHSRY
FT LKNRRHTLANVR (in isoform U)"
FT /evidence="ECO:0000305"
FT /id="VSP_054957"
FT VAR_SEQ 368..385
FT /note="SPLSPRISFPGSDSDLFG -> MVCSFCCCCYNFRNSPSS (in isoform
FT R)"
FT /evidence="ECO:0000303|PubMed:1660926"
FT /id="VSP_054958"
FT VAR_SEQ 370..385
FT /note="LSPRISFPGSDSDLFG -> MVCSFCCCCYNFRNSP (in isoform
FT IV)"
FT /evidence="ECO:0000303|PubMed:1660926"
FT /id="VSP_004586"
FT VAR_SEQ 444..456
FT /note="Missing (in isoform V)"
FT /evidence="ECO:0000303|PubMed:1660926"
FT /id="VSP_004588"
FT VAR_SEQ 493..494
FT /note="Missing (in isoform VI)"
FT /evidence="ECO:0000303|PubMed:1660926"
FT /id="VSP_004589"
FT CONFLICT 958
FT /note="D -> S (in Ref. 1; CAA38960 and 2; AAC34201)"
FT /evidence="ECO:0000305"
FT CONFLICT 1027
FT /note="S -> T (in Ref. 1; CAA38960 and 2; AAC34201)"
FT /evidence="ECO:0000305"
FT CONFLICT 1042..1043
FT /note="SG -> R (in Ref. 1; CAA38960 and 2; AAC34201)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1070 AA; 115079 MW; 50A63BF7BCC8EDD9 CRC64;
MSQESNGGPA AGGGAAAAPP PPPQYIITTP SEVDPDEVRS MADLELGSPE KQVQVQSQKF
SSTSSTTKVA THSFSMSSSA GTTGQQSKQD SAQQIQQLQQ LQQLQQLQQQ QQQQQSQRII
SSSTRSQSLQ SSTIVGEATT ITSGAAQILS ASAAASLAQQ LKAQSSTSII TSSEQRTSTS
TSSSSSTRYI ASGSSNLAGG NSNSASSASS KTRFQSFLQQ PEGAHGFLTA HQKHVRQFVR
STSAHSEAAA GVAGARAEKC IRSASTQIDD ASVAGVVESA GNLTDSSATG GSMQLSMSKL
GLQQSSSILI SKSAETIEMK SSSAGMRTQL TLSGGFLAPP GNRKITILSP IHAPPGLHDM
LKRAQGRSPL SPRISFPGSD SDLFGFDVEN GQGARSPLEG GSPSAGLVLQ NLPQRRESFL
YRSDSDFEMS PKSMSRNSSI ASERFKEQEA SILVDRSHGE DLIVTPFAQI LASLRSVRNN
LLSLTNVPAS NKSRRPNQSS SASRSGNPPG APLSQGEEAY TRLATDTIEE LDWCLDQLET
IQTHRSVSDM ASLKFKRMLN KELSHFSESS RSGNQISEYI CSTFLDKQQE FDLPSLRVED
NPELVAANAA AGQQSAGQYA RSRSPRGPPM SQISGVKRPL SHTNSFTGER LPTFGVETPR
ENELGTLLGE LDTWGIQIFS IGEFSVNRPL TCVAYTIFQS RELLTSLMIP PKTFLNFMST
LEDHYVKDNP FHNSLHAADV TQSTNVLLNT PALEGVFTPL EVGGALFAAC IHDVDHPGLT
NQFLVNSSSE LALMYNDESV LENHHLAVAF KLLQNQGCDI FCNMQKKQRQ TLRKMVIDIV
LSTDMSKHMS LLADLKTMVE TKKVAGSGVL LLDNYTDRIQ VLENLVHCAD LSNPTKPLPL
YKRWVALLME EFFLQGDKER ESGMDISPMC DRHNATIEKS QVGFIDYIVH PLWETWADLV
HPDAQDILDT LEENRDYYQS MIPPSPPPSG VDENPQEDRI RFQVTLEESD QENLAELEEG
DESGGESTTT GTTGTTAASA LSGAGGGGGG GGGMAPRTGG CQNQPQHGGM
