ID   PDE7A_HUMAN             Reviewed;         482 AA.
AC   Q13946; A0AVH6; A8K436; A8K9G5; O15380; Q96T72;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   27-MAR-2024, entry version 198.
DE   RecName: Full=High affinity 3',5'-cyclic-AMP phosphodiesterase 7A {ECO:0000305};
DE            EC=3.1.4.53 {ECO:0000269|PubMed:8389765};
DE   AltName: Full=HCP1 {ECO:0000303|PubMed:8389765};
DE   AltName: Full=TM22;
DE   AltName: Full=cAMP-specific phosphodiesterase 7A {ECO:0000305};
GN   Name=PDE7A {ECO:0000303|PubMed:9195912, ECO:0000312|HGNC:HGNC:8791};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE7A1), FUNCTION, CATALYTIC ACTIVITY,
RP   AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=8389765; DOI=10.1016/s0021-9258(18)31474-1;
RA   Michaeli T., Bloom T.J., Martins T., Loughney K., Ferguson K., Riggs M.,
RA   Rodgers L., Beavo J.A., Wigler M.;
RT   "Isolation and characterization of a previously undetected human cAMP
RT   phosphodiesterase by complementation of cAMP phosphodiesterase-deficient
RT   Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 268:12925-12932(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE7A2), FUNCTION, CATALYTIC ACTIVITY,
RP   AND SUBCELLULAR LOCATION.
RC   TISSUE=Skeletal muscle;
RX   PubMed=9195912; DOI=10.1074/jbc.272.26.16152;
RA   Han P., Zhu X., Michaeli T.;
RT   "Alternative splicing of the high affinity cAMP-specific phosphodiesterase
RT   (PDE7A) mRNA in human skeletal muscle and heart.";
RL   J. Biol. Chem. 272:16152-16157(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE7A3).
RX   PubMed=11371644; DOI=10.1073/pnas.101131098;
RA   Glavas N.A., Ostenson C., Schaefer J.B., Vasta V., Beavo J.A.;
RT   "T cell activation up-regulates cyclic nucleotide phosphodiesterases 8A1
RT   and 7A3.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:6319-6324(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE7A1).
RC   TISSUE=Kidney, and Thymus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE7A2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   INTERACTION WITH CBFA2T3.
RX   PubMed=15470020; DOI=10.4049/jimmunol.173.8.4806;
RA   Asirvatham A.L., Galligan S.G., Schillace R.V., Davey M.P., Vasta V.,
RA   Beavo J.A., Carr D.W.;
RT   "A-kinase anchoring proteins interact with phosphodiesterases in T
RT   lymphocyte cell lines.";
RL   J. Immunol. 173:4806-4814(2004).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 130-482 IN COMPLEX WITH METAL
RP   IONS AND THE INHIBITOR IBMX, AND ACTIVITY REGULATION.
RX   PubMed=15994308; DOI=10.1074/jbc.m504398200;
RA   Wang H., Liu Y., Chen Y., Robinson H., Ke H.;
RT   "Multiple elements jointly determine inhibitor selectivity of cyclic
RT   nucleotide phosphodiesterases 4 and 7.";
RL   J. Biol. Chem. 280:30949-30955(2005).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 139-456 IN COMPLEX WITH METAL
RP   IONS, FUNCTION, AND COFACTOR.
RX   PubMed=19350606; DOI=10.1002/cmdc.200900043;
RA   Castano T., Wang H., Campillo N.E., Ballester S., Gonzalez-Garcia C.,
RA   Hernandez J., Perez C., Cuenca J., Perez-Castillo A., Martinez A.,
RA   Huertas O., Gelpi J.L., Luque F.J., Ke H., Gil C.;
RT   "Synthesis, structural analysis, and biological evaluation of
RT   thioxoquinazoline derivatives as phosphodiesterase 7 inhibitors.";
RL   ChemMedChem 4:866-876(2009).
CC   -!- FUNCTION: Hydrolyzes the second messenger cAMP, which is a key
CC       regulator of many important physiological processes (PubMed:8389765,
CC       PubMed:9195912, PubMed:19350606). May have a role in muscle signal
CC       transduction (PubMed:9195912). {ECO:0000269|PubMed:19350606,
CC       ECO:0000269|PubMed:8389765, ECO:0000269|PubMed:9195912}.
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:8389765, ECO:0000269|PubMed:9195912};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000269|PubMed:19350606};
CC       Note=Binds 2 divalent metal cations per subunit (PubMed:19350606). Site
CC       1 may preferentially bind zinc ions, while site 2 has a preference for
CC       magnesium and/or manganese ions (PubMed:19350606).
CC       {ECO:0000269|PubMed:19350606};
CC   -!- ACTIVITY REGULATION: Insensitive to all selective PDE inhibitors.
CC       {ECO:0000269|PubMed:15994308}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.2 uM for 3',5'-cyclic AMP {ECO:0000269|PubMed:8389765};
CC   -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC       3',5'-cyclic AMP: step 1/1. {ECO:0000269|PubMed:8389765,
CC       ECO:0000269|PubMed:9195912}.
CC   -!- SUBUNIT: Interacts with CBFA2T3. {ECO:0000269|PubMed:15470020,
CC       ECO:0000269|PubMed:15994308, ECO:0000269|PubMed:19350606}.
CC   -!- SUBCELLULAR LOCATION: [Isoform PDE7A1]: Cytoplasm, cytosol
CC       {ECO:0000269|PubMed:9195912}. Note=PDE7A1 (57 kDa) is located mostly to
CC       soluble cellular fractions. {ECO:0000269|PubMed:9195912}.
CC   -!- SUBCELLULAR LOCATION: [Isoform PDE7A2]: Cytoplasm
CC       {ECO:0000269|PubMed:9195912}. Note=PDE7A2 (50 kDa) is located to
CC       particulate cellular fractions. {ECO:0000269|PubMed:9195912}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=PDE7A1 {ECO:0000303|PubMed:9195912};
CC         IsoId=Q13946-1; Sequence=Displayed;
CC       Name=PDE7A2 {ECO:0000303|PubMed:9195912};
CC         IsoId=Q13946-2; Sequence=VSP_004593;
CC       Name=PDE7A3 {ECO:0000303|PubMed:11371644};
CC         IsoId=Q13946-3; Sequence=VSP_038645, VSP_038646;
CC   -!- TISSUE SPECIFICITY: [Isoform PDE7A1]: Found at high levels in skeletal
CC       muscle and at low levels in a variety of tissues including brain and
CC       heart (PubMed:9195912). It is expressed as well in two T-cell lines
CC       (PubMed:9195912). {ECO:0000269|PubMed:9195912}.
CC   -!- TISSUE SPECIFICITY: [Isoform PDE7A2]: Found abundantly in skeletal
CC       muscle and at low levels in heart. {ECO:0000269|PubMed:9195912}.
CC   -!- DEVELOPMENTAL STAGE: [Isoform PDE7A1]: Developmentally regulated
CC       (PubMed:9195912). PDE7A1 and PDE7A2 are found in several fetal tissues,
CC       expression is reduced throughout development (PubMed:9195912). It
CC       persists strongly only in adult skeletal muscle (PubMed:9195912).
CC       {ECO:0000269|PubMed:9195912}.
CC   -!- DEVELOPMENTAL STAGE: [Isoform PDE7A2]: Developmentally regulated
CC       (PubMed:9195912). PDE7A1 and PDE7A2 are found in several fetal tissues,
CC       expression is reduced throughout development (PubMed:9195912). It
CC       persists strongly only in adult skeletal muscle (PubMed:9195912).
CC       {ECO:0000269|PubMed:9195912}.
CC   -!- DOMAIN: Composed of a C-terminal catalytic domain containing two
CC       putative divalent metal sites and an N-terminal regulatory domain.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC       PDE7 subfamily. {ECO:0000305}.
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DR   EMBL; L12052; AAA35644.2; -; mRNA.
DR   EMBL; U67932; AAB65772.1; -; mRNA.
DR   EMBL; AF332652; AAK57640.1; -; mRNA.
DR   EMBL; AK290801; BAF83490.1; -; mRNA.
DR   EMBL; AK292680; BAF85369.1; -; mRNA.
DR   EMBL; AC055822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC100812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC126360; AAI26361.1; -; mRNA.
DR   CCDS; CCDS34901.1; -. [Q13946-2]
DR   CCDS; CCDS56538.1; -. [Q13946-1]
DR   RefSeq; NP_001229247.1; NM_001242318.2. [Q13946-1]
DR   RefSeq; NP_002594.1; NM_002603.3. [Q13946-2]
DR   RefSeq; XP_011515842.1; XM_011517540.2. [Q13946-2]
DR   PDB; 1ZKL; X-ray; 1.67 A; A=130-482.
DR   PDB; 3G3N; X-ray; 2.40 A; A=139-456.
DR   PDB; 4PM0; X-ray; 2.10 A; A=130-482.
DR   PDB; 4Y2B; X-ray; 2.20 A; A=130-482.
DR   PDBsum; 1ZKL; -.
DR   PDBsum; 3G3N; -.
DR   PDBsum; 4PM0; -.
DR   PDBsum; 4Y2B; -.
DR   AlphaFoldDB; Q13946; -.
DR   SMR; Q13946; -.
DR   BioGRID; 111176; 17.
DR   IntAct; Q13946; 6.
DR   STRING; 9606.ENSP00000385632; -.
DR   BindingDB; Q13946; -.
DR   ChEMBL; CHEMBL3012; -.
DR   DrugBank; DB08602; 3-(2,6-difluorophenyl)-2-(methylthio)quinazolin-4(3H)-one.
DR   DrugBank; DB07954; 3-isobutyl-1-methyl-7H-xanthine.
DR   DrugBank; DB00201; Caffeine.
DR   DrugBank; DB09283; Trapidil.
DR   DrugCentral; Q13946; -.
DR   GuidetoPHARMACOLOGY; 1305; -.
DR   iPTMnet; Q13946; -.
DR   PhosphoSitePlus; Q13946; -.
DR   BioMuta; PDE7A; -.
DR   DMDM; 3182958; -.
DR   EPD; Q13946; -.
DR   jPOST; Q13946; -.
DR   MassIVE; Q13946; -.
DR   MaxQB; Q13946; -.
DR   PaxDb; 9606-ENSP00000385632; -.
DR   PeptideAtlas; Q13946; -.
DR   ProteomicsDB; 59762; -. [Q13946-1]
DR   ProteomicsDB; 59763; -. [Q13946-2]
DR   ProteomicsDB; 59764; -. [Q13946-3]
DR   Antibodypedia; 4363; 254 antibodies from 28 providers.
DR   DNASU; 5150; -.
DR   Ensembl; ENST00000379419.8; ENSP00000368730.4; ENSG00000205268.11. [Q13946-2]
DR   Ensembl; ENST00000396642.7; ENSP00000379881.3; ENSG00000205268.11. [Q13946-3]
DR   Ensembl; ENST00000401827.8; ENSP00000385632.4; ENSG00000205268.11. [Q13946-1]
DR   GeneID; 5150; -.
DR   KEGG; hsa:5150; -.
DR   MANE-Select; ENST00000401827.8; ENSP00000385632.4; NM_001242318.3; NP_001229247.1.
DR   UCSC; uc003xvp.4; human. [Q13946-1]
DR   AGR; HGNC:8791; -.
DR   CTD; 5150; -.
DR   DisGeNET; 5150; -.
DR   GeneCards; PDE7A; -.
DR   HGNC; HGNC:8791; PDE7A.
DR   HPA; ENSG00000205268; Tissue enhanced (lymphoid).
DR   MIM; 171885; gene.
DR   neXtProt; NX_Q13946; -.
DR   OpenTargets; ENSG00000205268; -.
DR   PharmGKB; PA33139; -.
DR   VEuPathDB; HostDB:ENSG00000205268; -.
DR   eggNOG; KOG3689; Eukaryota.
DR   GeneTree; ENSGT00940000157658; -.
DR   HOGENOM; CLU_005940_6_5_1; -.
DR   InParanoid; Q13946; -.
DR   OMA; RHTIHET; -.
DR   OrthoDB; 240889at2759; -.
DR   PhylomeDB; Q13946; -.
DR   TreeFam; TF314638; -.
DR   BRENDA; 3.1.4.53; 2681.
DR   PathwayCommons; Q13946; -.
DR   Reactome; R-HSA-418555; G alpha (s) signalling events.
DR   SignaLink; Q13946; -.
DR   UniPathway; UPA00762; UER00747.
DR   BioGRID-ORCS; 5150; 13 hits in 1162 CRISPR screens.
DR   ChiTaRS; PDE7A; human.
DR   EvolutionaryTrace; Q13946; -.
DR   GeneWiki; PDE7A; -.
DR   GenomeRNAi; 5150; -.
DR   Pharos; Q13946; Tclin.
DR   PRO; PR:Q13946; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q13946; Protein.
DR   Bgee; ENSG00000205268; Expressed in secondary oocyte and 188 other cell types or tissues.
DR   ExpressionAtlas; Q13946; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019933; P:cAMP-mediated signaling; IDA:UniProtKB.
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; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR   InterPro; IPR023174; PDEase_CS.
DR   PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR   PANTHER; PTHR11347:SF96; HIGH AFFINITY CAMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE 7A; 1.
DR   Pfam; PF00233; PDEase_I; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00471; HDc; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS00126; PDEASE_I_1; 1.
DR   PROSITE; PS51845; PDEASE_I_2; 1.
DR   Genevisible; Q13946; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; cAMP; Cytoplasm; Hydrolase;
KW   Metal-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..482
FT                   /note="High affinity 3',5'-cyclic-AMP phosphodiesterase 7A"
FT                   /id="PRO_0000198833"
FT   DOMAIN          136..458
FT                   /note="PDEase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT   ACT_SITE        212
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O76083"
FT   BINDING         216
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:15994308,
FT                   ECO:0000269|PubMed:19350606"
FT   BINDING         252
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:15994308,
FT                   ECO:0000269|PubMed:19350606"
FT   BINDING         253
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:15994308,
FT                   ECO:0000269|PubMed:19350606"
FT   BINDING         253
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:15994308,
FT                   ECO:0000269|PubMed:19350606"
FT   BINDING         362
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:15994308,
FT                   ECO:0000269|PubMed:19350606"
FT   MOD_RES         84
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..46
FT                   /note="MEVCYQLPVLPLDRPVPQHVLSRRGAISFSSSSALFGCPNPRQLSQ -> MG
FT                   ITLIWCLALVLIKWITSK (in isoform PDE7A2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:9195912"
FT                   /id="VSP_004593"
FT   VAR_SEQ         416..424
FT                   /note="FMTYLVEPL -> NYTYLDIAG (in isoform PDE7A3)"
FT                   /evidence="ECO:0000303|PubMed:11371644"
FT                   /id="VSP_038645"
FT   VAR_SEQ         425..482
FT                   /note="Missing (in isoform PDE7A3)"
FT                   /evidence="ECO:0000303|PubMed:11371644"
FT                   /id="VSP_038646"
FT   VARIANT         76
FT                   /note="G -> E (in dbSNP:rs11557049)"
FT                   /id="VAR_056661"
FT   CONFLICT        204
FT                   /note="D -> G (in Ref. 4; BAF83490)"
FT                   /evidence="ECO:0000305"
FT   HELIX           140..148
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   TURN            149..152
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   HELIX           158..164
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   HELIX           169..180
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   HELIX           183..186
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   HELIX           191..203
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   STRAND          209..213
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   HELIX           214..228
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   HELIX           231..234
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   HELIX           239..251
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   TURN            252..255
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   HELIX           261..266
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   HELIX           270..274
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   TURN            275..277
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   HELIX           280..296
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   TURN            297..301
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   HELIX           304..319
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   HELIX           323..325
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   HELIX           326..339
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   HELIX           347..362
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   HELIX           365..367
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   HELIX           370..393
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   TURN            404..406
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   HELIX           409..419
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   HELIX           421..431
FT                   /evidence="ECO:0007829|PDB:1ZKL"
FT   HELIX           435..453
FT                   /evidence="ECO:0007829|PDB:1ZKL"
SQ   SEQUENCE   482 AA;  55505 MW;  3B3C8F6E9154F88C CRC64;
     MEVCYQLPVL PLDRPVPQHV LSRRGAISFS SSSALFGCPN PRQLSQRRGA ISYDSSDQTA
     LYIRMLGDVR VRSRAGFESE RRGSHPYIDF RIFHSQSEIE VSVSARNIRR LLSFQRYLRS
     SRFFRGTAVS NSLNILDDDY NGQAKCMLEK VGNWNFDIFL FDRLTNGNSL VSLTFHLFSL
     HGLIEYFHLD MMKLRRFLVM IQEDYHSQNP YHNAVHAADV TQAMHCYLKE PKLANSVTPW
     DILLSLIAAA THDLDHPGVN QPFLIKTNHY LATLYKNTSV LENHHWRSAV GLLRESGLFS
     HLPLESRQQM ETQIGALILA TDISRQNEYL SLFRSHLDRG DLCLEDTRHR HLVLQMALKC
     ADICNPCRTW ELSKQWSEKV TEEFFHQGDI EKKYHLGVSP LCDRHTESIA NIQIGFMTYL
     VEPLFTEWAR FSNTRLSQTM LGHVGLNKAS WKGLQREQSS SEDTDAAFEL NSQLLPQENR
     LS
//