ID PDE10_HUMAN Reviewed; 1055 AA.
AC Q9Y233; A0A3F2YP58; Q6FHX1; Q9HCP9; Q9NTV4; Q9ULW9; Q9Y5T1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2024, sequence version 2.
DT 27-MAR-2024, entry version 211.
DE RecName: Full=cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A;
DE EC=3.1.4.17 {ECO:0000269|PubMed:10373451, ECO:0000269|PubMed:10393245, ECO:0000269|PubMed:17389385, ECO:0000269|PubMed:27058447};
GN Name=PDE10A;
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 PDE10A2), SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION AT THR-282 BY PKA.
RC TISSUE=Fetal lung;
RX PubMed=10441464; DOI=10.1006/bbrc.1999.1013;
RA Kotera J., Fujishige K., Yuasa K., Omori K.;
RT "Characterization and phosphorylation of PDE10A2, a novel alternative
RT splice variant of human phosphodiesterase that hydrolyzes cAMP and cGMP.";
RL Biochem. Biophys. Res. Commun. 261:551-557(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE10A1), FUNCTION, CATALYTIC ACTIVITY,
RP PATHWAY, AND SUBCELLULAR LOCATION.
RC TISSUE=Fetal lung;
RX PubMed=10373451; DOI=10.1074/jbc.274.26.18438;
RA Fujishige K., Kotera J., Michibata H., Yuasa K., Takebayashi S.,
RA Okumura K., Omori K.;
RT "Cloning and characterization of a novel human phosphodiesterase that
RT hydrolyzes both cAMP and cGMP (PDE10A).";
RL J. Biol. Chem. 274:18438-18445(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PDE10A1 AND PDE10A2), FUNCTION,
RP CATALYTIC ACTIVITY, AND PATHWAY.
RC TISSUE=Fetal brain;
RX PubMed=10393245; DOI=10.1016/s0378-1119(99)00171-7;
RA Loughney K., Snyder P.B., Uher L., Rosman G.J., Ferguson K., Florio V.A.;
RT "Isolation and characterization of PDE10A, a novel human 3',5'-cyclic
RT nucleotide phosphodiesterase.";
RL Gene 234:109-117(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE10A1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE10A1).
RC TISSUE=Colon;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 342-1055, AND ALTERNATIVE SPLICING.
RX PubMed=10998054; DOI=10.1046/j.1432-1327.2000.01661.x;
RA Fujishige K., Kotera J., Yuasa K., Omori K.;
RT "The human phosphodiesterase PDE10A gene genomic organization and
RT evolutionary relatedness with other PDEs containing GAF domains.";
RL Eur. J. Biochem. 267:5943-5951(2000).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DOMAIN, AND ACTIVITY REGULATION.
RX PubMed=16330539; DOI=10.1074/jbc.m511468200;
RA Gross-Langenhoff M., Hofbauer K., Weber J., Schultz A., Schultz J.E.;
RT "cAMP is a ligand for the tandem GAF domain of human phosphodiesterase 10
RT and cGMP for the tandem GAF domain of phosphodiesterase 11.";
RL J. Biol. Chem. 281:2841-2846(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [11]
RP INVOLVEMENT IN IOLOD, VARIANTS IOLOD CYS-373 AND PRO-382, AND
RP CHARACTERIZATION OF VARIANTS IOLOD CYS-373 AND PRO-382.
RX PubMed=27058446; DOI=10.1016/j.ajhg.2016.03.015;
RA Diggle C.P., Sukoff Rizzo S.J., Popiolek M., Hinttala R., Schuelke J.P.,
RA Kurian M.A., Carr I.M., Markham A.F., Bonthron D.T., Watson C.,
RA Sharif S.M., Reinhart V., James L.C., Vanase-Frawley M.A., Charych E.,
RA Allen M., Harms J., Schmidt C.J., Ng J., Pysden K., Strick C., Vieira P.,
RA Mankinen K., Kokkonen H., Kallioinen M., Sormunen R., Rinne J.O.,
RA Johansson J., Alakurtti K., Huilaja L., Hurskainen T., Tasanen K.,
RA Anttila E., Marques T.R., Howes O., Politis M., Fahiminiya S., Nguyen K.Q.,
RA Majewski J., Uusimaa J., Sheridan E., Brandon N.J.;
RT "Biallelic mutations in PDE10A Lead to loss of striatal PDE10A and a
RT hyperkinetic movement disorder with onset in infancy.";
RL Am. J. Hum. Genet. 98:735-743(2016).
RN [12]
RP TISSUE SPECIFICITY, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INVOLVEMENT IN
RP ADSD2, VARIANTS ADSD2 LEU-566 AND LEU-600, AND CHARACTERIZATION OF VARIANTS
RP ADSD2 LEU-566 AND LEU-600.
RX PubMed=27058447; DOI=10.1016/j.ajhg.2016.02.015;
RA Mencacci N.E., Kamsteeg E.J., Nakashima K., R'Bibo L., Lynch D.S.,
RA Balint B., Willemsen M.A., Adams M.E., Wiethoff S., Suzuki K., Davies C.H.,
RA Ng J., Meyer E., Veneziano L., Giunti P., Hughes D., Raymond F.L.,
RA Carecchio M., Zorzi G., Nardocci N., Barzaghi C., Garavaglia B.,
RA Salpietro V., Hardy J., Pittman A.M., Houlden H., Kurian M.A., Kimura H.,
RA Vissers L.E., Wood N.W., Bhatia K.P.;
RT "De novo mutations in PDE10A cause childhood-onset chorea with bilateral
RT striatal lesions.";
RL Am. J. Hum. Genet. 98:763-771(2016).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 712-1042 IN COMPLEXES WITH AMP;
RP CAMP; GMP; CGMP AND MAGNESIUM, MUTAGENESIS OF ASP-830, FUNCTION, CATALYTIC
RP ACTIVITY, PATHWAY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17389385; DOI=10.1073/pnas.0700279104;
RA Wang H., Liu Y., Hou J., Zheng M., Robinson H., Ke H.;
RT "Structural insight into substrate specificity of phosphodiesterase 10.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5782-5787(2007).
RN [14] {ECO:0007744|PDB:2ZMF}
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 518-703 IN COMPLEX WITH CAMP,
RP DOMAIN, AND SUBUNIT.
RX PubMed=18477562; DOI=10.1074/jbc.m800595200;
RA Handa N., Mizohata E., Kishishita S., Toyama M., Morita S.,
RA Uchikubo-Kamo T., Akasaka R., Omori K., Kotera J., Terada T., Shirouzu M.,
RA Yokoyama S.;
RT "Crystal structure of the GAF-B domain from human phosphodiesterase 10A
RT complexed with its ligand, cAMP.";
RL J. Biol. Chem. 283:19657-19664(2008).
CC -!- FUNCTION: Plays a role in signal transduction by regulating the
CC intracellular concentration of cyclic nucleotides (PubMed:10373451,
CC PubMed:10393245, PubMed:16330539, PubMed:27058447, PubMed:17389385).
CC Can hydrolyze both cAMP and cGMP, but has higher affinity for cAMP and
CC is more efficient with cAMP as substrate (PubMed:10373451,
CC PubMed:10393245, PubMed:27058447, PubMed:17389385). May play a critical
CC role in regulating cAMP and cGMP levels in the striatum, a region of
CC the brain that contributes to the control of movement and cognition
CC (PubMed:27058447). {ECO:0000269|PubMed:10373451,
CC ECO:0000269|PubMed:10393245, ECO:0000269|PubMed:16330539,
CC ECO:0000269|PubMed:17389385, ECO:0000269|PubMed:27058447}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-
CC phosphate + H(+); Xref=Rhea:RHEA:14653, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57867, ChEBI:CHEBI:58464; EC=3.1.4.17;
CC Evidence={ECO:0000269|PubMed:10373451, ECO:0000269|PubMed:10393245,
CC ECO:0000269|PubMed:17389385, ECO:0000269|PubMed:27058447};
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; Evidence={ECO:0000269|PubMed:10373451,
CC ECO:0000269|PubMed:10393245, ECO:0000269|PubMed:16330539,
CC ECO:0000269|PubMed:17389385, ECO:0000269|PubMed:27058447};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746,
CC ChEBI:CHEBI:58115; Evidence={ECO:0000269|PubMed:10373451,
CC ECO:0000269|PubMed:10393245, ECO:0000269|PubMed:17389385,
CC ECO:0000269|PubMed:27058447};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:17389385};
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:0000269|PubMed:17389385};
CC -!- ACTIVITY REGULATION: Inhibited by dipyridamole and moderately by IBMX.
CC cGMP acts as an allosteric activator. {ECO:0000269|PubMed:16330539}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.26 uM for cAMP {ECO:0000269|PubMed:10373451};
CC KM=7.2 uM for cGMP {ECO:0000269|PubMed:10373451};
CC KM=56 nM for cAMP {ECO:0000269|PubMed:17389385};
CC KM=4.4 uM for cGMP {ECO:0000269|PubMed:17389385};
CC Vmax=507 nmol/min/mg enzyme for cAMP {ECO:0000269|PubMed:17389385};
CC Vmax=1860 nmol/min/mg enzyme for cGMP {ECO:0000269|PubMed:17389385};
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC 3',5'-cyclic AMP: step 1/1. {ECO:0000269|PubMed:10373451,
CC ECO:0000269|PubMed:10393245, ECO:0000269|PubMed:16330539,
CC ECO:0000269|PubMed:17389385, ECO:0000269|PubMed:27058447}.
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic GMP degradation; GMP from
CC 3',5'-cyclic GMP: step 1/1. {ECO:0000269|PubMed:10373451,
CC ECO:0000269|PubMed:10393245, ECO:0000269|PubMed:17389385,
CC ECO:0000269|PubMed:27058447}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18477562}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10373451,
CC ECO:0000269|PubMed:10441464}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Name=3;
CC IsoId=Q9Y233-3; Sequence=Displayed;
CC Name=PDE10A1;
CC IsoId=Q9Y233-1; Sequence=VSP_062215;
CC Name=PDE10A2;
CC IsoId=Q9Y233-2; Sequence=VSP_062216;
CC -!- TISSUE SPECIFICITY: Abundant in the putamen and caudate nucleus regions
CC of brain and testis, moderately expressed in the thyroid gland,
CC pituitary gland, thalamus and cerebellum. {ECO:0000269|PubMed:10373451,
CC ECO:0000269|PubMed:27058447}.
CC -!- DOMAIN: The tandem GAF domains bind cAMP, and regulate enzyme activity.
CC The binding of cAMP stimulates enzyme activity.
CC {ECO:0000269|PubMed:16330539}.
CC -!- DOMAIN: Composed of a C-terminal catalytic domain containing two
CC divalent metal sites and an N-terminal regulatory domain which contains
CC one cyclic nucleotide-binding region. {ECO:0000269|PubMed:17389385,
CC ECO:0000269|PubMed:18477562}.
CC -!- PTM: [Isoform PDE10A2]: Phosphorylated on Thr-16.
CC {ECO:0000269|PubMed:10441464}.
CC -!- DISEASE: Dyskinesia, limb and orofacial, infantile-onset (IOLOD)
CC [MIM:616921]: An autosomal recessive, early-onset hyperkinetic movement
CC disorder characterized by axial hypotonia, dyskinesia of the limbs and
CC trunk, orofacial dyskinesia, drooling, and dysarthria. The severity of
CC the hyperkinesis is variable. {ECO:0000269|PubMed:27058446}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Striatal degeneration, autosomal dominant 2 (ADSD2)
CC [MIM:616922]: An autosomal dominant disorder characterized by striatal
CC degeneration and dysfunction of basal ganglia, resulting in
CC hyperkinesis. {ECO:0000269|PubMed:27058447}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative initiation. Based
CC on proteomic data. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000305}.
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DR EMBL; AB026816; BAA84467.1; -; mRNA.
DR EMBL; AB020593; BAA78034.1; -; mRNA.
DR EMBL; AF127479; AAD32595.1; -; mRNA.
DR EMBL; AF127480; AAD32596.1; -; mRNA.
DR EMBL; CR536567; CAG38804.1; -; mRNA.
DR EMBL; AL117345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL160160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF458352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF458359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC104858; AAI04859.1; -; mRNA.
DR EMBL; BC104860; AAI04861.1; -; mRNA.
DR EMBL; AB041798; BAB16383.1; -; Genomic_DNA.
DR RefSeq; NP_001124162.1; NM_001130690.2. [Q9Y233-2]
DR RefSeq; NP_006652.1; NM_006661.3. [Q9Y233-1]
DR RefSeq; XP_011533690.1; XM_011535388.2. [Q9Y233-1]
DR PDB; 2OUN; X-ray; 1.56 A; A/B=439-766.
DR PDB; 2OUP; X-ray; 1.56 A; A/B=439-766.
DR PDB; 2OUQ; X-ray; 1.90 A; A/B=439-766.
DR PDB; 2OUR; X-ray; 1.45 A; A/B=439-766.
DR PDB; 2OUS; X-ray; 1.45 A; A/B=439-766.
DR PDB; 2OUU; X-ray; 1.52 A; A/B=439-766.
DR PDB; 2OUV; X-ray; 1.56 A; A/B=439-766.
DR PDB; 2OUY; X-ray; 1.90 A; A/B=439-766.
DR PDB; 2WEY; X-ray; 2.80 A; A/B=439-779.
DR PDB; 2Y0J; X-ray; 2.43 A; A/B=432-764.
DR PDB; 2ZMF; X-ray; 2.10 A; A/B=246-427.
DR PDB; 3SN7; X-ray; 1.82 A; A/B=439-779.
DR PDB; 3SNI; X-ray; 1.90 A; A/B=439-779.
DR PDB; 3SNL; X-ray; 2.40 A; A/B=439-779.
DR PDB; 3UI7; X-ray; 2.28 A; A/B=432-760.
DR PDB; 3UUO; X-ray; 2.11 A; A/B=432-760.
DR PDB; 3WI2; X-ray; 2.26 A; A/B=439-779.
DR PDB; 3WS8; X-ray; 2.60 A; A/B=439-779.
DR PDB; 3WS9; X-ray; 2.99 A; A/B=439-779.
DR PDB; 3WYK; X-ray; 2.50 A; A/B=442-779.
DR PDB; 3WYL; X-ray; 2.68 A; A/B=442-779.
DR PDB; 3WYM; X-ray; 2.00 A; A/B=442-779.
DR PDB; 4AEL; X-ray; 2.20 A; A/B=439-779.
DR PDB; 4AJD; X-ray; 2.30 A; A/D=439-764.
DR PDB; 4AJF; X-ray; 1.90 A; A/D=439-764.
DR PDB; 4AJG; X-ray; 2.30 A; A/D=439-764.
DR PDB; 4AJM; X-ray; 2.40 A; A/D=439-764.
DR PDB; 4BBX; X-ray; 2.50 A; A/B=443-769.
DR PDB; 4DDL; X-ray; 2.07 A; A/B=442-779.
DR PDB; 4DFF; X-ray; 2.11 A; A/B=432-779.
DR PDB; 4FCB; X-ray; 2.10 A; A/B=439-779.
DR PDB; 4FCD; X-ray; 2.02 A; A/B=439-779.
DR PDB; 4HEU; X-ray; 2.00 A; A/B=442-759.
DR PDB; 4HF4; X-ray; 2.00 A; A/B=442-759.
DR PDB; 4LKQ; X-ray; 1.62 A; A/B=439-779.
DR PDB; 4LLJ; X-ray; 1.56 A; A/B=439-779.
DR PDB; 4LLK; X-ray; 1.55 A; A/B=439-779.
DR PDB; 4LLP; X-ray; 1.75 A; A/B=439-779.
DR PDB; 4LLX; X-ray; 1.75 A; A/B=439-779.
DR PDB; 4LM0; X-ray; 1.66 A; A/B=439-779.
DR PDB; 4LM1; X-ray; 1.60 A; A/B=439-779.
DR PDB; 4LM2; X-ray; 1.55 A; A/B=439-779.
DR PDB; 4LM3; X-ray; 1.49 A; A/B=439-779.
DR PDB; 4LM4; X-ray; 1.48 A; A/B=439-779.
DR PDB; 4MRW; X-ray; 1.96 A; A/B=439-779.
DR PDB; 4MRZ; X-ray; 1.58 A; A/B=439-779.
DR PDB; 4MS0; X-ray; 1.79 A; A/B=439-779.
DR PDB; 4MSA; X-ray; 1.62 A; A/B=439-779.
DR PDB; 4MSC; X-ray; 2.47 A; A/B=439-779.
DR PDB; 4MSE; X-ray; 2.81 A; A/B=439-779.
DR PDB; 4MSH; X-ray; 2.30 A; A/B=439-779.
DR PDB; 4MSN; X-ray; 2.30 A; A/B=439-779.
DR PDB; 4MUW; X-ray; 2.64 A; A/B=442-779.
DR PDB; 4MVH; X-ray; 2.50 A; A/B=442-779.
DR PDB; 4P0N; X-ray; 2.08 A; A/B=442-779.
DR PDB; 4P1R; X-ray; 2.24 A; A/B=442-779.
DR PDB; 4PHW; X-ray; 2.50 A; A/B=442-779.
DR PDB; 4TPM; X-ray; 2.77 A; A/B=442-779.
DR PDB; 4TPP; X-ray; 2.65 A; A/B=442-779.
DR PDB; 4WN1; X-ray; 3.13 A; A/B=439-779.
DR PDB; 4XY2; X-ray; 2.03 A; A/B=439-779.
DR PDB; 4YQH; X-ray; 2.31 A; A/B=439-759.
DR PDB; 4YS7; X-ray; 2.50 A; A/B=439-759.
DR PDB; 4ZO5; X-ray; 2.50 A; A/B=439-759.
DR PDB; 5AXP; X-ray; 1.95 A; A/B=442-779.
DR PDB; 5AXQ; X-ray; 1.77 A; A/B=442-779.
DR PDB; 5B4K; X-ray; 2.90 A; A/B=442-779.
DR PDB; 5B4L; X-ray; 2.40 A; A/B=442-779.
DR PDB; 5C1W; X-ray; 1.70 A; A/B=439-779.
DR PDB; 5C28; X-ray; 1.56 A; A/B=439-779.
DR PDB; 5C29; X-ray; 2.05 A; A/B=439-779.
DR PDB; 5C2A; X-ray; 2.00 A; A/B=439-779.
DR PDB; 5C2E; X-ray; 2.10 A; A/B=439-779.
DR PDB; 5C2H; X-ray; 2.09 A; A/B=439-779.
DR PDB; 5DH4; X-ray; 2.20 A; A/B=439-779.
DR PDB; 5DH5; X-ray; 2.00 A; A/B=439-779.
DR PDB; 5EDE; X-ray; 2.20 A; A/C/D=447-760, B=448-760.
DR PDB; 5EDG; X-ray; 2.30 A; A/B/C/D=447-760.
DR PDB; 5EDH; X-ray; 2.03 A; A/B/C/D=448-760.
DR PDB; 5EDI; X-ray; 2.20 A; A/B/C/D=442-760.
DR PDB; 5I2R; X-ray; 2.50 A; A/B/C/D=447-763.
DR PDB; 5K9R; X-ray; 2.70 A; A/B=448-759.
DR PDB; 5SDU; X-ray; 2.15 A; A/B/C/D=439-779.
DR PDB; 5SDV; X-ray; 2.15 A; A/B/C/D=439-779.
DR PDB; 5SDW; X-ray; 2.35 A; A/B/C/D=439-779.
DR PDB; 5SDX; X-ray; 2.19 A; A/B/C/D=439-779.
DR PDB; 5SDY; X-ray; 2.20 A; A=439-779.
DR PDB; 5SDZ; X-ray; 2.35 A; A/B/C/D=439-779.
DR PDB; 5SE0; X-ray; 2.01 A; A/B/C/D=439-779.
DR PDB; 5SE1; X-ray; 2.30 A; A=439-779.
DR PDB; 5SE2; X-ray; 2.20 A; A/B/C/D=439-779.
DR PDB; 5SE3; X-ray; 2.14 A; A/B/C/D=439-779.
DR PDB; 5SE4; X-ray; 2.50 A; A/B/C/D=439-779.
DR PDB; 5SE5; X-ray; 2.08 A; A/B/C/D=439-779.
DR PDB; 5SE6; X-ray; 1.95 A; A/B/C/D=439-779.
DR PDB; 5SE7; X-ray; 2.17 A; A/B/C/D=439-779.
DR PDB; 5SE8; X-ray; 1.99 A; A/B/C/D=439-779.
DR PDB; 5SE9; X-ray; 1.94 A; A/B/C/D=439-779.
DR PDB; 5SEA; X-ray; 2.00 A; A/B/C/D=439-779.
DR PDB; 5SEB; X-ray; 2.28 A; A/B/C/D=439-779.
DR PDB; 5SEC; X-ray; 2.03 A; A/B/C/D=439-779.
DR PDB; 5SED; X-ray; 2.32 A; A/B/C/D=439-779.
DR PDB; 5SEE; X-ray; 2.35 A; A=439-779.
DR PDB; 5SEF; X-ray; 2.29 A; A/B/C/D=439-779.
DR PDB; 5SEG; X-ray; 2.29 A; A/B/C/D=439-779.
DR PDB; 5SEH; X-ray; 2.10 A; A/B/C/D=439-779.
DR PDB; 5SEI; X-ray; 2.37 A; A/B/C/D=439-779.
DR PDB; 5SEJ; X-ray; 2.44 A; A/B/C/D=439-779.
DR PDB; 5SEK; X-ray; 2.15 A; A/B/C/D=439-779.
DR PDB; 5SEL; X-ray; 2.20 A; A/B/C/D=439-779.
DR PDB; 5SEM; X-ray; 2.10 A; A/B/C/D=439-779.
DR PDB; 5SEN; X-ray; 2.04 A; A/B/C/D=439-779.
DR PDB; 5SEO; X-ray; 2.10 A; A/B/C/D=439-779.
DR PDB; 5SEP; X-ray; 2.10 A; A/B/C/D=439-779.
DR PDB; 5SEQ; X-ray; 2.18 A; A/B/C/D=439-779.
DR PDB; 5SER; X-ray; 2.25 A; A/B/C/D=439-779.
DR PDB; 5SES; X-ray; 2.11 A; A/B/C/D=439-779.
DR PDB; 5SET; X-ray; 2.40 A; A=439-779.
DR PDB; 5SEU; X-ray; 2.09 A; A/B/C/D=439-779.
DR PDB; 5SEV; X-ray; 2.31 A; A/B/C/D=439-779.
DR PDB; 5SEW; X-ray; 2.30 A; A=439-779.
DR PDB; 5SEX; X-ray; 1.99 A; A/B/C/D=439-779.
DR PDB; 5SEY; X-ray; 2.29 A; A/B/C/D=439-779.
DR PDB; 5SEZ; X-ray; 1.99 A; A/B/C/D=439-779.
DR PDB; 5SF0; X-ray; 2.10 A; A/B/C/D=439-779.
DR PDB; 5SF1; X-ray; 2.11 A; A/B/C/D=439-779.
DR PDB; 5SF2; X-ray; 2.02 A; A=439-779.
DR PDB; 5SF3; X-ray; 2.15 A; A/B/C/D=439-779.
DR PDB; 5SF4; X-ray; 2.25 A; A/B/C/D=439-779.
DR PDB; 5SF5; X-ray; 1.98 A; A/B/C/D=439-779.
DR PDB; 5SF6; X-ray; 2.03 A; A/B/C/D=439-779.
DR PDB; 5SF7; X-ray; 2.08 A; A/B/C/D=439-779.
DR PDB; 5SF8; X-ray; 2.15 A; A/B/C/D=439-779.
DR PDB; 5SF9; X-ray; 2.37 A; A/B/C/D=439-779.
DR PDB; 5SFA; X-ray; 2.32 A; A/B/C/D=439-779.
DR PDB; 5SFB; X-ray; 1.98 A; A/B/C/D=439-779.
DR PDB; 5SFC; X-ray; 2.18 A; A/B/C/D=439-779.
DR PDB; 5SFD; X-ray; 2.05 A; A/B/C/D=439-779.
DR PDB; 5SFE; X-ray; 1.86 A; A/B/C/D=439-779.
DR PDB; 5SFF; X-ray; 2.16 A; A/B/C/D=439-779.
DR PDB; 5SFG; X-ray; 2.31 A; A/B/C/D=439-779.
DR PDB; 5SFH; X-ray; 2.29 A; A/B/C/D=439-779.
DR PDB; 5SFI; X-ray; 2.01 A; A/B/C/D=439-779.
DR PDB; 5SFJ; X-ray; 2.41 A; A/B/C/D=439-779.
DR PDB; 5SFK; X-ray; 2.33 A; A/B/C/D=439-779.
DR PDB; 5SFL; X-ray; 2.13 A; A/B/C/D=439-779.
DR PDB; 5SFM; X-ray; 2.16 A; A/B/C/D=439-779.
DR PDB; 5SFN; X-ray; 2.02 A; A/B/C/D=439-779.
DR PDB; 5SFO; X-ray; 1.96 A; A/B/C/D=439-779.
DR PDB; 5SFP; X-ray; 2.00 A; A/B/C/D=439-779.
DR PDB; 5SFQ; X-ray; 2.21 A; A/B/C/D=439-779.
DR PDB; 5SFR; X-ray; 2.04 A; A/B/C/D=439-779.
DR PDB; 5SFS; X-ray; 2.24 A; A/B/C/D=439-779.
DR PDB; 5SFT; X-ray; 2.32 A; A/B/C/D=439-779.
DR PDB; 5SFU; X-ray; 2.40 A; A/B/C/D=439-779.
DR PDB; 5SFV; X-ray; 2.41 A; A/B/C/D=439-779.
DR PDB; 5SFW; X-ray; 2.15 A; A/B/C/D=439-779.
DR PDB; 5SFX; X-ray; 2.04 A; A/B/C/D=439-779.
DR PDB; 5SFY; X-ray; 2.08 A; A/B/C/D=439-779.
DR PDB; 5SFZ; X-ray; 2.16 A; A/B/C/D=439-779.
DR PDB; 5SG0; X-ray; 2.06 A; A/B/C/D=439-779.
DR PDB; 5SG1; X-ray; 2.41 A; A/B/C/D=439-779.
DR PDB; 5SG2; X-ray; 2.15 A; A/B/C/D=439-779.
DR PDB; 5SG3; X-ray; 1.98 A; A/B/C/D=439-779.
DR PDB; 5SG4; X-ray; 2.30 A; A=439-779.
DR PDB; 5SG5; X-ray; 2.17 A; A/B/C/D=439-779.
DR PDB; 5SG6; X-ray; 1.96 A; A/B/C/D=439-779.
DR PDB; 5SG7; X-ray; 2.30 A; A/B/C/D=439-779.
DR PDB; 5SG8; X-ray; 2.16 A; A/B/C/D=439-779.
DR PDB; 5SG9; X-ray; 2.13 A; A/B/C/D=439-779.
DR PDB; 5SGB; X-ray; 2.39 A; A/B/C/D=439-779.
DR PDB; 5SGC; X-ray; 2.09 A; A/B/C/D=439-779.
DR PDB; 5SGD; X-ray; 2.54 A; A/B/C/D=439-779.
DR PDB; 5SGE; X-ray; 2.20 A; A/B/C/D=439-779.
DR PDB; 5SGF; X-ray; 2.30 A; A/B/C/D=439-779.
DR PDB; 5SGG; X-ray; 2.09 A; A/B/C/D=439-779.
DR PDB; 5SGH; X-ray; 1.97 A; A/B/C/D=439-779.
DR PDB; 5SGI; X-ray; 1.97 A; A/B/C/D=439-779.
DR PDB; 5SGJ; X-ray; 2.66 A; A/B/C/D=439-779.
DR PDB; 5SGK; X-ray; 2.13 A; A/B/C/D=439-779.
DR PDB; 5SGL; X-ray; 2.28 A; A/B/C/D=439-779.
DR PDB; 5SGM; X-ray; 2.20 A; A=439-779.
DR PDB; 5SGN; X-ray; 2.07 A; A/B/C/D=439-779.
DR PDB; 5SGO; X-ray; 2.30 A; A/B/C/D=439-779.
DR PDB; 5SGP; X-ray; 1.95 A; A/B/C/D=439-779.
DR PDB; 5SGQ; X-ray; 2.04 A; A/B/C/D=439-779.
DR PDB; 5SGR; X-ray; 2.04 A; A/B/C/D=439-779.
DR PDB; 5SGS; X-ray; 2.03 A; A/B/C/D=439-779.
DR PDB; 5SGT; X-ray; 2.26 A; A/B/C/D=439-779.
DR PDB; 5SGU; X-ray; 2.14 A; A/B/C/D=439-779.
DR PDB; 5SGV; X-ray; 2.00 A; A/B/C/D=439-779.
DR PDB; 5SGW; X-ray; 1.90 A; A/B/C/D=439-779.
DR PDB; 5SGX; X-ray; 1.93 A; A/B/C/D=439-779.
DR PDB; 5SGY; X-ray; 2.36 A; A/B/C/D=439-779.
DR PDB; 5SGZ; X-ray; 2.20 A; A/B/C/D=439-779.
DR PDB; 5SH0; X-ray; 2.29 A; A/B/C/D=439-779.
DR PDB; 5SH1; X-ray; 2.20 A; A/B/C/D=439-779.
DR PDB; 5SH2; X-ray; 2.19 A; A/B/C/D=439-779.
DR PDB; 5SH3; X-ray; 1.98 A; A/B/C/D=439-779.
DR PDB; 5SH4; X-ray; 2.22 A; A/B/C/D=439-779.
DR PDB; 5SH5; X-ray; 2.30 A; A/B/C/D=439-779.
DR PDB; 5SH6; X-ray; 1.98 A; A/B/C/D=439-779.
DR PDB; 5SH7; X-ray; 2.66 A; A/B/C/D=439-779.
DR PDB; 5SH8; X-ray; 2.00 A; A/B/C/D=439-779.
DR PDB; 5SH9; X-ray; 2.06 A; A/B/C/D=439-779.
DR PDB; 5SHA; X-ray; 2.24 A; A/B/C/D=439-779.
DR PDB; 5SHB; X-ray; 1.95 A; A/B/C/D=439-779.
DR PDB; 5SHC; X-ray; 2.33 A; A/B/C/D=439-779.
DR PDB; 5SHD; X-ray; 2.60 A; A/B/C/D=439-779.
DR PDB; 5SHE; X-ray; 2.19 A; A/B/C/D=439-779.
DR PDB; 5SHF; X-ray; 2.28 A; A/B/C/D=439-779.
DR PDB; 5SHG; X-ray; 2.12 A; A/B/C/D=439-779.
DR PDB; 5SHH; X-ray; 2.15 A; A/B/C/D=439-779.
DR PDB; 5SHI; X-ray; 2.10 A; A/B/C/D=439-779.
DR PDB; 5SHJ; X-ray; 2.30 A; A/B/C/D=439-779.
DR PDB; 5SHK; X-ray; 2.00 A; A/B/C/D=439-779.
DR PDB; 5SHL; X-ray; 2.35 A; A/B/C/D=439-779.
DR PDB; 5SHM; X-ray; 2.26 A; A/B/C/D=439-779.
DR PDB; 5SHN; X-ray; 2.03 A; A/B/C/D=439-779.
DR PDB; 5SHO; X-ray; 1.90 A; A=439-779.
DR PDB; 5SHP; X-ray; 2.18 A; A/B/C/D=439-779.
DR PDB; 5SHQ; X-ray; 2.08 A; A/B/C/D=439-779.
DR PDB; 5SHR; X-ray; 1.98 A; A/B/C/D=439-779.
DR PDB; 5SHS; X-ray; 2.30 A; A/B/C/D=439-779.
DR PDB; 5SHT; X-ray; 2.27 A; A/B/C/D=439-779.
DR PDB; 5SHU; X-ray; 1.98 A; A/B/C/D=439-779.
DR PDB; 5SHV; X-ray; 1.95 A; A/B/C/D=439-779.
DR PDB; 5SHW; X-ray; 2.19 A; A/B/C/D=439-779.
DR PDB; 5SHX; X-ray; 2.16 A; A/B/C/D=439-779.
DR PDB; 5SHY; X-ray; 2.30 A; A=439-779.
DR PDB; 5SHZ; X-ray; 2.55 A; A/B/C/D=439-779.
DR PDB; 5SI0; X-ray; 2.27 A; A/B/C/D=439-779.
DR PDB; 5SI1; X-ray; 1.75 A; A=439-779.
DR PDB; 5SI2; X-ray; 2.40 A; A/B/C/D=439-779.
DR PDB; 5SI3; X-ray; 2.40 A; A/B/C/D=439-779.
DR PDB; 5SI4; X-ray; 2.39 A; A/B/C/D=439-779.
DR PDB; 5SI5; X-ray; 2.27 A; A/B/C/D=439-779.
DR PDB; 5SI6; X-ray; 2.00 A; A/B/C/D=439-779.
DR PDB; 5SI7; X-ray; 2.10 A; A/B/C/D=439-779.
DR PDB; 5SI8; X-ray; 2.10 A; A/B/C/D=439-779.
DR PDB; 5SI9; X-ray; 2.01 A; A/B/C/D=439-779.
DR PDB; 5SIA; X-ray; 2.27 A; A/B/C/D=439-779.
DR PDB; 5SIB; X-ray; 2.54 A; A/B/C/D=439-779.
DR PDB; 5SID; X-ray; 1.98 A; A/B/C/D=439-779.
DR PDB; 5SIE; X-ray; 2.12 A; A/B/C/D=439-779.
DR PDB; 5SIF; X-ray; 2.20 A; A/B/C/D=439-779.
DR PDB; 5SIG; X-ray; 2.03 A; A/B/C/D=439-779.
DR PDB; 5SIH; X-ray; 1.90 A; A/B/C/D=439-779.
DR PDB; 5SII; X-ray; 2.18 A; A/B/C/D=439-779.
DR PDB; 5SIJ; X-ray; 2.55 A; A/B/C/D=439-779.
DR PDB; 5SIK; X-ray; 2.10 A; A/B/C/D=439-779.
DR PDB; 5SIL; X-ray; 2.50 A; A=439-779.
DR PDB; 5SIM; X-ray; 1.75 A; A=439-779.
DR PDB; 5SIN; X-ray; 2.40 A; A/B/C/D=439-779.
DR PDB; 5SIO; X-ray; 2.20 A; A/B/C/D=439-779.
DR PDB; 5SIP; X-ray; 2.03 A; A/B/C/D=439-779.
DR PDB; 5SIQ; X-ray; 1.97 A; A/B/C/D=439-779.
DR PDB; 5SIR; X-ray; 2.50 A; A/B/C/D=439-779.
DR PDB; 5SIS; X-ray; 1.85 A; A=439-779.
DR PDB; 5SIT; X-ray; 1.99 A; A/B/C/D=439-779.
DR PDB; 5SIU; X-ray; 2.01 A; A/B/C/D=439-779.
DR PDB; 5SIV; X-ray; 2.20 A; A/B/C/D=439-779.
DR PDB; 5SIW; X-ray; 2.13 A; A/B/C/D=439-779.
DR PDB; 5SIX; X-ray; 2.29 A; A=439-779.
DR PDB; 5SIY; X-ray; 2.03 A; A/B/C/D=439-779.
DR PDB; 5SIZ; X-ray; 2.10 A; A/B/C/D=439-779.
DR PDB; 5SJ0; X-ray; 2.35 A; A/B/C/D=439-779.
DR PDB; 5SJ1; X-ray; 2.16 A; A/B/C/D=439-779.
DR PDB; 5SJ2; X-ray; 1.99 A; A/B/C/D=439-779.
DR PDB; 5SJ3; X-ray; 2.10 A; A/B/C/D=439-779.
DR PDB; 5SJ4; X-ray; 2.77 A; A/B/C/D=439-779.
DR PDB; 5SJ5; X-ray; 2.49 A; A/B/C/D=439-779.
DR PDB; 5SJ6; X-ray; 2.15 A; A/B/C/D=439-779.
DR PDB; 5SJ7; X-ray; 2.14 A; A/B/C/D=439-779.
DR PDB; 5SJ8; X-ray; 2.49 A; A/B/C/D=439-779.
DR PDB; 5SJ9; X-ray; 2.39 A; A/B/C/D=439-779.
DR PDB; 5SJA; X-ray; 2.13 A; A/B/C/D=439-779.
DR PDB; 5SJB; X-ray; 2.20 A; A/B/C/D=439-779.
DR PDB; 5SJC; X-ray; 2.08 A; A=439-779.
DR PDB; 5SJD; X-ray; 2.16 A; A/B/C/D=439-779.
DR PDB; 5SJE; X-ray; 2.10 A; A/B/C/D=439-779.
DR PDB; 5SJF; X-ray; 2.05 A; A/B/C/D=439-779.
DR PDB; 5SJG; X-ray; 1.97 A; A/B/C/D=439-779.
DR PDB; 5SJH; X-ray; 2.10 A; A/B/C/D=439-779.
DR PDB; 5SJI; X-ray; 1.98 A; A/B/C/D=439-779.
DR PDB; 5SJJ; X-ray; 2.10 A; A/B/C/D=439-779.
DR PDB; 5SJK; X-ray; 2.24 A; A/B/C/D=439-779.
DR PDB; 5SJL; X-ray; 2.64 A; A/B/C/D=439-779.
DR PDB; 5SJM; X-ray; 2.30 A; A/B/C/D=439-779.
DR PDB; 5SJN; X-ray; 2.05 A; A/B/C/D=439-779.
DR PDB; 5SJO; X-ray; 2.10 A; A/B/C/D=439-779.
DR PDB; 5SJP; X-ray; 2.25 A; A/B/C/D=439-779.
DR PDB; 5SJQ; X-ray; 2.12 A; A/B/C/D=439-779.
DR PDB; 5SJR; X-ray; 2.10 A; A/B/C/D=439-779.
DR PDB; 5SJS; X-ray; 2.70 A; A/B/C/D=439-779.
DR PDB; 5SJT; X-ray; 2.10 A; A/B/C/D=439-779.
DR PDB; 5SJU; X-ray; 1.97 A; A/B/C/D=439-779.
DR PDB; 5SJV; X-ray; 1.94 A; A/B/C/D=439-779.
DR PDB; 5SJW; X-ray; 1.95 A; A/B/C/D=439-779.
DR PDB; 5SJX; X-ray; 2.06 A; A/B/C/D=439-779.
DR PDB; 5SJY; X-ray; 2.20 A; A/B/C/D=439-779.
DR PDB; 5SJZ; X-ray; 2.19 A; A/B/C/D=439-779.
DR PDB; 5SK0; X-ray; 2.02 A; A/B/C/D=439-779.
DR PDB; 5SK1; X-ray; 2.30 A; A/B/C/D=439-779.
DR PDB; 5SK2; X-ray; 2.14 A; A/B/C/D=439-779.
DR PDB; 5SK3; X-ray; 2.32 A; A/B/C/D=439-779.
DR PDB; 5SK4; X-ray; 2.00 A; A/B/C/D=439-779.
DR PDB; 5SK5; X-ray; 1.95 A; A/B/C/D=439-779.
DR PDB; 5SK6; X-ray; 2.20 A; A/B/C/D=439-779.
DR PDB; 5SK7; X-ray; 2.29 A; A/B/C/D=439-779.
DR PDB; 5SK8; X-ray; 2.30 A; A=439-779.
DR PDB; 5SK9; X-ray; 2.82 A; A/B/C/D=439-779.
DR PDB; 5SKA; X-ray; 2.21 A; A/B/C/D=439-779.
DR PDB; 5SKB; X-ray; 2.35 A; A/B/C/D=439-779.
DR PDB; 5SKC; X-ray; 2.60 A; A/B/C/D=439-779.
DR PDB; 5SKD; X-ray; 2.30 A; A/B/C/D=439-779.
DR PDB; 5SKE; X-ray; 2.20 A; A/B/C/D=439-779.
DR PDB; 5SKF; X-ray; 2.10 A; A/B/C/D=439-779.
DR PDB; 5SKG; X-ray; 2.03 A; A/B/C/D=439-779.
DR PDB; 5SKH; X-ray; 2.10 A; A/B/C/D=439-779.
DR PDB; 5SKI; X-ray; 2.16 A; A/B/C/D=439-779.
DR PDB; 5SKJ; X-ray; 2.74 A; A/B/C/D=439-779.
DR PDB; 5SKK; X-ray; 2.15 A; A/B/C/D=439-779.
DR PDB; 5SKL; X-ray; 2.20 A; A/B/C/D=439-779.
DR PDB; 5SKM; X-ray; 1.91 A; A/B/C/D=439-779.
DR PDB; 5SKN; X-ray; 1.90 A; A/B/C/D=439-779.
DR PDB; 5SKO; X-ray; 2.10 A; A=439-779.
DR PDB; 5SKP; X-ray; 2.00 A; A/B/C/D=439-779.
DR PDB; 5SKQ; X-ray; 2.00 A; A/B/C/D=439-779.
DR PDB; 5SKR; X-ray; 1.99 A; A/B/C/D=439-779.
DR PDB; 5SKS; X-ray; 2.31 A; A/B/C/D=439-779.
DR PDB; 5SKT; X-ray; 2.02 A; A/B/C/D=439-779.
DR PDB; 5SKU; X-ray; 2.20 A; A/B/C/D=439-779.
DR PDB; 5SKV; X-ray; 2.60 A; A/B/C/D=439-779.
DR PDB; 5UWF; X-ray; 1.87 A; C/D=439-779.
DR PDB; 5XUI; X-ray; 2.77 A; A/B=439-779.
DR PDB; 5XUJ; X-ray; 2.44 A; A/B=439-779.
DR PDB; 5ZNL; X-ray; 2.80 A; A/B=439-760.
DR PDB; 6IJH; X-ray; 2.60 A; A/B=439-779.
DR PDB; 6IJI; X-ray; 2.70 A; A/B=439-760.
DR PDB; 6KDX; X-ray; 2.44 A; A/B=439-779.
DR PDB; 6KDZ; X-ray; 3.10 A; A/B=439-779.
DR PDB; 6KE0; X-ray; 2.95 A; A/B=439-779.
DR PDB; 6KO0; X-ray; 2.60 A; A/B=439-759.
DR PDB; 6KO1; X-ray; 2.70 A; A/B=439-759.
DR PDB; 6KZE; X-ray; 2.50 A; A/B=439-760.
DR PDB; 6MSA; X-ray; 2.06 A; A/B=439-766.
DR PDB; 6MSC; X-ray; 2.36 A; A/B=439-766.
DR PDB; 7BPI; X-ray; 2.40 A; A/B=439-760.
DR PDB; 7QPF; X-ray; 1.70 A; A/B=432-764.
DR PDB; 7QPM; X-ray; 2.40 A; A/B=432-764.
DR PDB; 7QPQ; X-ray; 2.20 A; A/B=432-764.
DR PDB; 7QPV; X-ray; 2.30 A; A/B=432-764.
DR PDB; 7QQ4; X-ray; 2.45 A; A/B=432-764.
DR PDB; 8DI4; X-ray; 2.02 A; A/B=439-779.
DR PDBsum; 2OUN; -.
DR PDBsum; 2OUP; -.
DR PDBsum; 2OUQ; -.
DR PDBsum; 2OUR; -.
DR PDBsum; 2OUS; -.
DR PDBsum; 2OUU; -.
DR PDBsum; 2OUV; -.
DR PDBsum; 2OUY; -.
DR PDBsum; 2WEY; -.
DR PDBsum; 2Y0J; -.
DR PDBsum; 2ZMF; -.
DR PDBsum; 3SN7; -.
DR PDBsum; 3SNI; -.
DR PDBsum; 3SNL; -.
DR PDBsum; 3UI7; -.
DR PDBsum; 3UUO; -.
DR PDBsum; 3WI2; -.
DR PDBsum; 3WS8; -.
DR PDBsum; 3WS9; -.
DR PDBsum; 3WYK; -.
DR PDBsum; 3WYL; -.
DR PDBsum; 3WYM; -.
DR PDBsum; 4AEL; -.
DR PDBsum; 4AJD; -.
DR PDBsum; 4AJF; -.
DR PDBsum; 4AJG; -.
DR PDBsum; 4AJM; -.
DR PDBsum; 4BBX; -.
DR PDBsum; 4DDL; -.
DR PDBsum; 4DFF; -.
DR PDBsum; 4FCB; -.
DR PDBsum; 4FCD; -.
DR PDBsum; 4HEU; -.
DR PDBsum; 4HF4; -.
DR PDBsum; 4LKQ; -.
DR PDBsum; 4LLJ; -.
DR PDBsum; 4LLK; -.
DR PDBsum; 4LLP; -.
DR PDBsum; 4LLX; -.
DR PDBsum; 4LM0; -.
DR PDBsum; 4LM1; -.
DR PDBsum; 4LM2; -.
DR PDBsum; 4LM3; -.
DR PDBsum; 4LM4; -.
DR PDBsum; 4MRW; -.
DR PDBsum; 4MRZ; -.
DR PDBsum; 4MS0; -.
DR PDBsum; 4MSA; -.
DR PDBsum; 4MSC; -.
DR PDBsum; 4MSE; -.
DR PDBsum; 4MSH; -.
DR PDBsum; 4MSN; -.
DR PDBsum; 4MUW; -.
DR PDBsum; 4MVH; -.
DR PDBsum; 4P0N; -.
DR PDBsum; 4P1R; -.
DR PDBsum; 4PHW; -.
DR PDBsum; 4TPM; -.
DR PDBsum; 4TPP; -.
DR PDBsum; 4WN1; -.
DR PDBsum; 4XY2; -.
DR PDBsum; 4YQH; -.
DR PDBsum; 4YS7; -.
DR PDBsum; 4ZO5; -.
DR PDBsum; 5AXP; -.
DR PDBsum; 5AXQ; -.
DR PDBsum; 5B4K; -.
DR PDBsum; 5B4L; -.
DR PDBsum; 5C1W; -.
DR PDBsum; 5C28; -.
DR PDBsum; 5C29; -.
DR PDBsum; 5C2A; -.
DR PDBsum; 5C2E; -.
DR PDBsum; 5C2H; -.
DR PDBsum; 5DH4; -.
DR PDBsum; 5DH5; -.
DR PDBsum; 5EDE; -.
DR PDBsum; 5EDG; -.
DR PDBsum; 5EDH; -.
DR PDBsum; 5EDI; -.
DR PDBsum; 5I2R; -.
DR PDBsum; 5K9R; -.
DR PDBsum; 5SDU; -.
DR PDBsum; 5SDV; -.
DR PDBsum; 5SDW; -.
DR PDBsum; 5SDX; -.
DR PDBsum; 5SDY; -.
DR PDBsum; 5SDZ; -.
DR PDBsum; 5SE0; -.
DR PDBsum; 5SE1; -.
DR PDBsum; 5SE2; -.
DR PDBsum; 5SE3; -.
DR PDBsum; 5SE4; -.
DR PDBsum; 5SE5; -.
DR PDBsum; 5SE6; -.
DR PDBsum; 5SE7; -.
DR PDBsum; 5SE8; -.
DR PDBsum; 5SE9; -.
DR PDBsum; 5SEA; -.
DR PDBsum; 5SEB; -.
DR PDBsum; 5SEC; -.
DR PDBsum; 5SED; -.
DR PDBsum; 5SEE; -.
DR PDBsum; 5SEF; -.
DR PDBsum; 5SEG; -.
DR PDBsum; 5SEH; -.
DR PDBsum; 5SEI; -.
DR PDBsum; 5SEJ; -.
DR PDBsum; 5SEK; -.
DR PDBsum; 5SEL; -.
DR PDBsum; 5SEM; -.
DR PDBsum; 5SEN; -.
DR PDBsum; 5SEO; -.
DR PDBsum; 5SEP; -.
DR PDBsum; 5SEQ; -.
DR PDBsum; 5SER; -.
DR PDBsum; 5SES; -.
DR PDBsum; 5SET; -.
DR PDBsum; 5SEU; -.
DR PDBsum; 5SEV; -.
DR PDBsum; 5SEW; -.
DR PDBsum; 5SEX; -.
DR PDBsum; 5SEY; -.
DR PDBsum; 5SEZ; -.
DR PDBsum; 5SF0; -.
DR PDBsum; 5SF1; -.
DR PDBsum; 5SF2; -.
DR PDBsum; 5SF3; -.
DR PDBsum; 5SF4; -.
DR PDBsum; 5SF5; -.
DR PDBsum; 5SF6; -.
DR PDBsum; 5SF7; -.
DR PDBsum; 5SF8; -.
DR PDBsum; 5SF9; -.
DR PDBsum; 5SFA; -.
DR PDBsum; 5SFB; -.
DR PDBsum; 5SFC; -.
DR PDBsum; 5SFD; -.
DR PDBsum; 5SFE; -.
DR PDBsum; 5SFF; -.
DR PDBsum; 5SFG; -.
DR PDBsum; 5SFH; -.
DR PDBsum; 5SFI; -.
DR PDBsum; 5SFJ; -.
DR PDBsum; 5SFK; -.
DR PDBsum; 5SFL; -.
DR PDBsum; 5SFM; -.
DR PDBsum; 5SFN; -.
DR PDBsum; 5SFO; -.
DR PDBsum; 5SFP; -.
DR PDBsum; 5SFQ; -.
DR PDBsum; 5SFR; -.
DR PDBsum; 5SFS; -.
DR PDBsum; 5SFT; -.
DR PDBsum; 5SFU; -.
DR PDBsum; 5SFV; -.
DR PDBsum; 5SFW; -.
DR PDBsum; 5SFX; -.
DR PDBsum; 5SFY; -.
DR PDBsum; 5SFZ; -.
DR PDBsum; 5SG0; -.
DR PDBsum; 5SG1; -.
DR PDBsum; 5SG2; -.
DR PDBsum; 5SG3; -.
DR PDBsum; 5SG4; -.
DR PDBsum; 5SG5; -.
DR PDBsum; 5SG6; -.
DR PDBsum; 5SG7; -.
DR PDBsum; 5SG8; -.
DR PDBsum; 5SG9; -.
DR PDBsum; 5SGB; -.
DR PDBsum; 5SGC; -.
DR PDBsum; 5SGD; -.
DR PDBsum; 5SGE; -.
DR PDBsum; 5SGF; -.
DR PDBsum; 5SGG; -.
DR PDBsum; 5SGH; -.
DR PDBsum; 5SGI; -.
DR PDBsum; 5SGJ; -.
DR PDBsum; 5SGK; -.
DR PDBsum; 5SGL; -.
DR PDBsum; 5SGM; -.
DR PDBsum; 5SGN; -.
DR PDBsum; 5SGO; -.
DR PDBsum; 5SGP; -.
DR PDBsum; 5SGQ; -.
DR PDBsum; 5SGR; -.
DR PDBsum; 5SGS; -.
DR PDBsum; 5SGT; -.
DR PDBsum; 5SGU; -.
DR PDBsum; 5SGV; -.
DR PDBsum; 5SGW; -.
DR PDBsum; 5SGX; -.
DR PDBsum; 5SGY; -.
DR PDBsum; 5SGZ; -.
DR PDBsum; 5SH0; -.
DR PDBsum; 5SH1; -.
DR PDBsum; 5SH2; -.
DR PDBsum; 5SH3; -.
DR PDBsum; 5SH4; -.
DR PDBsum; 5SH5; -.
DR PDBsum; 5SH6; -.
DR PDBsum; 5SH7; -.
DR PDBsum; 5SH8; -.
DR PDBsum; 5SH9; -.
DR PDBsum; 5SHA; -.
DR PDBsum; 5SHB; -.
DR PDBsum; 5SHC; -.
DR PDBsum; 5SHD; -.
DR PDBsum; 5SHE; -.
DR PDBsum; 5SHF; -.
DR PDBsum; 5SHG; -.
DR PDBsum; 5SHH; -.
DR PDBsum; 5SHI; -.
DR PDBsum; 5SHJ; -.
DR PDBsum; 5SHK; -.
DR PDBsum; 5SHL; -.
DR PDBsum; 5SHM; -.
DR PDBsum; 5SHN; -.
DR PDBsum; 5SHO; -.
DR PDBsum; 5SHP; -.
DR PDBsum; 5SHQ; -.
DR PDBsum; 5SHR; -.
DR PDBsum; 5SHS; -.
DR PDBsum; 5SHT; -.
DR PDBsum; 5SHU; -.
DR PDBsum; 5SHV; -.
DR PDBsum; 5SHW; -.
DR PDBsum; 5SHX; -.
DR PDBsum; 5SHY; -.
DR PDBsum; 5SHZ; -.
DR PDBsum; 5SI0; -.
DR PDBsum; 5SI1; -.
DR PDBsum; 5SI2; -.
DR PDBsum; 5SI3; -.
DR PDBsum; 5SI4; -.
DR PDBsum; 5SI5; -.
DR PDBsum; 5SI6; -.
DR PDBsum; 5SI7; -.
DR PDBsum; 5SI8; -.
DR PDBsum; 5SI9; -.
DR PDBsum; 5SIA; -.
DR PDBsum; 5SIB; -.
DR PDBsum; 5SID; -.
DR PDBsum; 5SIE; -.
DR PDBsum; 5SIF; -.
DR PDBsum; 5SIG; -.
DR PDBsum; 5SIH; -.
DR PDBsum; 5SII; -.
DR PDBsum; 5SIJ; -.
DR PDBsum; 5SIK; -.
DR PDBsum; 5SIL; -.
DR PDBsum; 5SIM; -.
DR PDBsum; 5SIN; -.
DR PDBsum; 5SIO; -.
DR PDBsum; 5SIP; -.
DR PDBsum; 5SIQ; -.
DR PDBsum; 5SIR; -.
DR PDBsum; 5SIS; -.
DR PDBsum; 5SIT; -.
DR PDBsum; 5SIU; -.
DR PDBsum; 5SIV; -.
DR PDBsum; 5SIW; -.
DR PDBsum; 5SIX; -.
DR PDBsum; 5SIY; -.
DR PDBsum; 5SIZ; -.
DR PDBsum; 5SJ0; -.
DR PDBsum; 5SJ1; -.
DR PDBsum; 5SJ2; -.
DR PDBsum; 5SJ3; -.
DR PDBsum; 5SJ4; -.
DR PDBsum; 5SJ5; -.
DR PDBsum; 5SJ6; -.
DR PDBsum; 5SJ7; -.
DR PDBsum; 5SJ8; -.
DR PDBsum; 5SJ9; -.
DR PDBsum; 5SJA; -.
DR PDBsum; 5SJB; -.
DR PDBsum; 5SJC; -.
DR PDBsum; 5SJD; -.
DR PDBsum; 5SJE; -.
DR PDBsum; 5SJF; -.
DR PDBsum; 5SJG; -.
DR PDBsum; 5SJH; -.
DR PDBsum; 5SJI; -.
DR PDBsum; 5SJJ; -.
DR PDBsum; 5SJK; -.
DR PDBsum; 5SJL; -.
DR PDBsum; 5SJM; -.
DR PDBsum; 5SJN; -.
DR PDBsum; 5SJO; -.
DR PDBsum; 5SJP; -.
DR PDBsum; 5SJQ; -.
DR PDBsum; 5SJR; -.
DR PDBsum; 5SJS; -.
DR PDBsum; 5SJT; -.
DR PDBsum; 5SJU; -.
DR PDBsum; 5SJV; -.
DR PDBsum; 5SJW; -.
DR PDBsum; 5SJX; -.
DR PDBsum; 5SJY; -.
DR PDBsum; 5SJZ; -.
DR PDBsum; 5SK0; -.
DR PDBsum; 5SK1; -.
DR PDBsum; 5SK2; -.
DR PDBsum; 5SK3; -.
DR PDBsum; 5SK4; -.
DR PDBsum; 5SK5; -.
DR PDBsum; 5SK6; -.
DR PDBsum; 5SK7; -.
DR PDBsum; 5SK8; -.
DR PDBsum; 5SK9; -.
DR PDBsum; 5SKA; -.
DR PDBsum; 5SKB; -.
DR PDBsum; 5SKC; -.
DR PDBsum; 5SKD; -.
DR PDBsum; 5SKE; -.
DR PDBsum; 5SKF; -.
DR PDBsum; 5SKG; -.
DR PDBsum; 5SKH; -.
DR PDBsum; 5SKI; -.
DR PDBsum; 5SKJ; -.
DR PDBsum; 5SKK; -.
DR PDBsum; 5SKL; -.
DR PDBsum; 5SKM; -.
DR PDBsum; 5SKN; -.
DR PDBsum; 5SKO; -.
DR PDBsum; 5SKP; -.
DR PDBsum; 5SKQ; -.
DR PDBsum; 5SKR; -.
DR PDBsum; 5SKS; -.
DR PDBsum; 5SKT; -.
DR PDBsum; 5SKU; -.
DR PDBsum; 5SKV; -.
DR PDBsum; 5UWF; -.
DR PDBsum; 5XUI; -.
DR PDBsum; 5XUJ; -.
DR PDBsum; 5ZNL; -.
DR PDBsum; 6IJH; -.
DR PDBsum; 6IJI; -.
DR PDBsum; 6KDX; -.
DR PDBsum; 6KDZ; -.
DR PDBsum; 6KE0; -.
DR PDBsum; 6KO0; -.
DR PDBsum; 6KO1; -.
DR PDBsum; 6KZE; -.
DR PDBsum; 6MSA; -.
DR PDBsum; 6MSC; -.
DR PDBsum; 7BPI; -.
DR PDBsum; 7QPF; -.
DR PDBsum; 7QPM; -.
DR PDBsum; 7QPQ; -.
DR PDBsum; 7QPV; -.
DR PDBsum; 7QQ4; -.
DR PDBsum; 8DI4; -.
DR AlphaFoldDB; Q9Y233; -.
DR SMR; Q9Y233; -.
DR BioGRID; 116057; 7.
DR IntAct; Q9Y233; 2.
DR STRING; 9606.ENSP00000355847; -.
DR BindingDB; Q9Y233; -.
DR ChEMBL; CHEMBL4409; -.
DR DrugBank; DB08384; 2-({4-[4-(pyridin-4-ylmethyl)-1H-pyrazol-3-yl]phenoxy}methyl)quinoline.
DR DrugBank; DB08386; 2-{[4-(4-pyridin-4-yl-1H-pyrazol-3-yl)phenoxy]methyl}quinoline.
DR DrugBank; DB08383; 4,5-bis(4-methoxyphenyl)-2-thiophen-2-yl-1H-imidazole.
DR DrugBank; DB08389; 6,7-DIMETHOXY-4-[(3R)-3-(2-NAPHTHYLOXY)PYRROLIDIN-1-YL]QUINAZOLINE.
DR DrugBank; DB00201; Caffeine.
DR DrugBank; DB00975; Dipyridamole.
DR DrugBank; DB08387; Mardepodect.
DR DrugBank; DB01113; Papaverine.
DR DrugBank; DB08391; PQ-10.
DR DrugBank; DB08811; Tofisopam.
DR DrugBank; DB09283; Trapidil.
DR DrugBank; DB08814; Triflusal.
DR DrugCentral; Q9Y233; -.
DR GuidetoPHARMACOLOGY; 1310; -.
DR GlyGen; Q9Y233; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y233; -.
DR PhosphoSitePlus; Q9Y233; -.
DR SwissPalm; Q9Y233; -.
DR BioMuta; PDE10A; -.
DR DMDM; 7993747; -.
DR EPD; Q9Y233; -.
DR jPOST; Q9Y233; -.
DR MassIVE; Q9Y233; -.
DR MaxQB; Q9Y233; -.
DR PaxDb; 9606-ENSP00000438284; -.
DR PeptideAtlas; Q9Y233; -.
DR ProteomicsDB; 85625; -. [Q9Y233-1]
DR ProteomicsDB; 85626; -. [Q9Y233-2]
DR Pumba; Q9Y233; -.
DR Antibodypedia; 33512; 285 antibodies from 27 providers.
DR DNASU; 10846; -.
DR Ensembl; ENST00000539869.4; ENSP00000438284.3; ENSG00000112541.19. [Q9Y233-3]
DR GeneID; 10846; -.
DR KEGG; hsa:10846; -.
DR MANE-Select; ENST00000539869.4; ENSP00000438284.3; NM_001385079.1; NP_001372008.1.
DR UCSC; uc003quo.4; human. [Q9Y233-3]
DR AGR; HGNC:8772; -.
DR CTD; 10846; -.
DR DisGeNET; 10846; -.
DR GeneCards; PDE10A; -.
DR HGNC; HGNC:8772; PDE10A.
DR HPA; ENSG00000112541; Tissue enriched (brain).
DR MalaCards; PDE10A; -.
DR MIM; 610652; gene.
DR MIM; 616921; phenotype.
DR MIM; 616922; phenotype.
DR neXtProt; NX_Q9Y233; -.
DR OpenTargets; ENSG00000112541; -.
DR Orphanet; 494541; Childhood-onset benign chorea with striatal involvement.
DR Orphanet; 494526; Infantile-onset generalized dyskinesia with orofacial involvement.
DR PharmGKB; PA33120; -.
DR VEuPathDB; HostDB:ENSG00000112541; -.
DR eggNOG; KOG3689; Eukaryota.
DR GeneTree; ENSGT00940000156543; -.
DR HOGENOM; CLU_006980_1_0_1; -.
DR InParanoid; Q9Y233; -.
DR OrthoDB; 5479253at2759; -.
DR PhylomeDB; Q9Y233; -.
DR TreeFam; TF316499; -.
DR BRENDA; 3.1.4.17; 2681.
DR PathwayCommons; Q9Y233; -.
DR Reactome; R-HSA-418457; cGMP effects.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR SABIO-RK; Q9Y233; -.
DR SignaLink; Q9Y233; -.
DR SIGNOR; Q9Y233; -.
DR UniPathway; UPA00762; UER00747.
DR UniPathway; UPA00763; UER00748.
DR BioGRID-ORCS; 10846; 7 hits in 1161 CRISPR screens.
DR ChiTaRS; PDE10A; human.
DR EvolutionaryTrace; Q9Y233; -.
DR GeneWiki; PDE10A; -.
DR GenomeRNAi; 10846; -.
DR Pharos; Q9Y233; Tclin.
DR PRO; PR:Q9Y233; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9Y233; Protein.
DR Bgee; ENSG00000112541; Expressed in adrenal tissue and 144 other cell types or tissues.
DR ExpressionAtlas; Q9Y233; baseline and differential.
DR Genevisible; Q9Y233; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:RHEA.
DR GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:RHEA.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; TAS:ProtInc.
DR GO; GO:0030552; F:cAMP binding; IDA:UniProtKB.
DR GO; GO:0030553; F:cGMP binding; NAS:UniProtKB.
DR GO; GO:0004118; F:cGMP-stimulated cyclic-nucleotide 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:0046069; P:cGMP catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0010754; P:negative regulation of cGMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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:SF111; CAMP AND CAMP-INHIBITED CGMP 3',5'-CYCLIC PHOSPHODIESTERASE 10A; 1.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Alternative initiation;
KW Alternative splicing; cAMP; cAMP-binding; cGMP; cGMP-binding; Cytoplasm;
KW Disease variant; Hydrolase; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1055
FT /note="cAMP and cAMP-inhibited cGMP 3',5'-cyclic
FT phosphodiesterase 10A"
FT /id="PRO_0000198843"
FT DOMAIN 367..510
FT /note="GAF 1"
FT DOMAIN 542..688
FT /note="GAF 2"
FT DOMAIN 718..1035
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 791
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O76083"
FT BINDING 562..563
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000269|PubMed:18477562,
FT ECO:0007744|PDB:2ZMF"
FT BINDING 606..607
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000269|PubMed:18477562,
FT ECO:0007744|PDB:2ZMF"
FT BINDING 640
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000269|PubMed:18477562,
FT ECO:0007744|PDB:2ZMF"
FT BINDING 659
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000269|PubMed:18477562,
FT ECO:0007744|PDB:2ZMF"
FT BINDING 791
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000269|PubMed:17389385"
FT BINDING 791
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000269|PubMed:17389385"
FT BINDING 795
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17389385"
FT BINDING 829
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17389385"
FT BINDING 830
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17389385"
FT BINDING 830
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17389385"
FT BINDING 940
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17389385"
FT BINDING 992
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000269|PubMed:17389385"
FT BINDING 992
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000269|PubMed:17389385"
FT MOD_RES 282
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:10441464"
FT VAR_SEQ 1..289
FT /note="MASLEEPLAPRPQGPLPAAGDEPGCGPGKLRPEPRLSAAGGGSAAGPGPAPE
FT WPGRGRAERAAPPRPPLSSAGRPSPAGGPGALSARGGGCGWVAARAPLALAFSSRVPSS
FT SPSFFYFWPPPPPPPPSFLPSSSAFHLPVRLPGREGAAAAAAAGGGGDAGGGGGGGQEA
FT APLSVPTSSSHRGGGGSGGGRRRLFLSPALQGLLLPARAGPRPPPPPRLPLGQAARRAG
FT SPGFPGAGPGGGGQTPRRPQGASFALAAAAALLFGSDMEDGPSNNASCFRRLTECFLSP
FT S -> MRIEERKSQHLTG (in isoform PDE10A1)"
FT /id="VSP_062215"
FT VAR_SEQ 1..266
FT /note="Missing (in isoform PDE10A2)"
FT /id="VSP_062216"
FT VARIANT 373
FT /note="Y -> C (in IOLOD; decreased protein abundance;
FT dbSNP:rs778899140)"
FT /evidence="ECO:0000269|PubMed:27058446"
FT /id="VAR_076798"
FT VARIANT 382
FT /note="A -> P (in IOLOD; decreased protein abundance;
FT dbSNP:rs875989839)"
FT /evidence="ECO:0000269|PubMed:27058446"
FT /id="VAR_076799"
FT VARIANT 566
FT /note="F -> L (in ADSD2; no effect on basal 3',5'-cyclic-
FT nucleotide phosphodiesterase activity; the mutation
FT severely disrupts the stimulatory effect on the enzyme
FT activity mediated by cAMP binding; dbSNP:rs875989841)"
FT /evidence="ECO:0000269|PubMed:27058447"
FT /id="VAR_076800"
FT VARIANT 579
FT /note="L -> P"
FT /id="VAR_008797"
FT VARIANT 600
FT /note="F -> L (in ADSD2; no effect on basal 3',5'-cyclic-
FT nucleotide phosphodiesterase activity; the mutation
FT severely disrupts the stimulatory effect on the enzyme
FT activity mediated by cAMP binding; dbSNP:rs875989840)"
FT /evidence="ECO:0000269|PubMed:27058447"
FT /id="VAR_076801"
FT VARIANT 982
FT /note="R -> K (in dbSNP:rs2224252)"
FT /id="VAR_047822"
FT VARIANT 983
FT /note="D -> N (in dbSNP:rs2860112)"
FT /id="VAR_047823"
FT MUTAGEN 830
FT /note="D->A: Loss of activity and of zinc binding."
FT /evidence="ECO:0000269|PubMed:17389385"
FT MUTAGEN 830
FT /note="D->N: Reduces activity 1000-fold."
FT /evidence="ECO:0000269|PubMed:17389385"
FT CONFLICT 933
FT /note="G -> S (in Ref. 4; CAG38804)"
FT /evidence="ECO:0000305"
FT HELIX 247..262
FT /evidence="ECO:0007829|PDB:2ZMF"
FT HELIX 267..282
FT /evidence="ECO:0007829|PDB:2ZMF"
FT STRAND 284..293
FT /evidence="ECO:0007829|PDB:2ZMF"
FT TURN 294..297
FT /evidence="ECO:0007829|PDB:2ZMF"
FT STRAND 298..304
FT /evidence="ECO:0007829|PDB:2ZMF"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:2ZMF"
FT HELIX 329..337
FT /evidence="ECO:0007829|PDB:2ZMF"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:2ZMF"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:2ZMF"
FT HELIX 355..360
FT /evidence="ECO:0007829|PDB:2ZMF"
FT STRAND 367..374
FT /evidence="ECO:0007829|PDB:2ZMF"
FT STRAND 377..387
FT /evidence="ECO:0007829|PDB:2ZMF"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:2ZMF"
FT HELIX 395..419
FT /evidence="ECO:0007829|PDB:2ZMF"
FT HELIX 443..449
FT /evidence="ECO:0007829|PDB:2OUR"
FT HELIX 456..461
FT /evidence="ECO:0007829|PDB:2OUR"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:3UI7"
FT HELIX 470..475
FT /evidence="ECO:0007829|PDB:2OUR"
FT HELIX 476..488
FT /evidence="ECO:0007829|PDB:2OUR"
FT TURN 490..492
FT /evidence="ECO:0007829|PDB:3SNI"
FT HELIX 495..507
FT /evidence="ECO:0007829|PDB:2OUR"
FT STRAND 513..516
FT /evidence="ECO:0007829|PDB:2OUR"
FT HELIX 517..532
FT /evidence="ECO:0007829|PDB:2OUR"
FT HELIX 533..537
FT /evidence="ECO:0007829|PDB:2OUR"
FT HELIX 540..552
FT /evidence="ECO:0007829|PDB:2OUR"
FT TURN 553..556
FT /evidence="ECO:0007829|PDB:2OUR"
FT HELIX 562..567
FT /evidence="ECO:0007829|PDB:2OUR"
FT HELIX 571..575
FT /evidence="ECO:0007829|PDB:2OUR"
FT STRAND 577..579
FT /evidence="ECO:0007829|PDB:2OUS"
FT HELIX 580..593
FT /evidence="ECO:0007829|PDB:2OUR"
FT TURN 596..598
FT /evidence="ECO:0007829|PDB:3SN7"
FT TURN 600..603
FT /evidence="ECO:0007829|PDB:2OUR"
FT HELIX 606..622
FT /evidence="ECO:0007829|PDB:2OUR"
FT HELIX 625..640
FT /evidence="ECO:0007829|PDB:2OUR"
FT STRAND 646..648
FT /evidence="ECO:0007829|PDB:3WI2"
FT HELIX 649..664
FT /evidence="ECO:0007829|PDB:2OUR"
FT HELIX 666..669
FT /evidence="ECO:0007829|PDB:2OUR"
FT HELIX 672..695
FT /evidence="ECO:0007829|PDB:2OUR"
FT HELIX 702..704
FT /evidence="ECO:0007829|PDB:2OUR"
FT HELIX 706..711
FT /evidence="ECO:0007829|PDB:2OUR"
FT HELIX 712..722
FT /evidence="ECO:0007829|PDB:2OUR"
FT HELIX 724..734
FT /evidence="ECO:0007829|PDB:2OUR"
FT HELIX 736..738
FT /evidence="ECO:0007829|PDB:2OUR"
FT HELIX 739..757
FT /evidence="ECO:0007829|PDB:2OUR"
FT HELIX 762..765
FT /evidence="ECO:0007829|PDB:5C28"
SQ SEQUENCE 1055 AA; 114946 MW; 9FD62FD5851B001A CRC64;
MASLEEPLAP RPQGPLPAAG DEPGCGPGKL RPEPRLSAAG GGSAAGPGPA PEWPGRGRAE
RAAPPRPPLS SAGRPSPAGG PGALSARGGG CGWVAARAPL ALAFSSRVPS SSPSFFYFWP
PPPPPPPSFL PSSSAFHLPV RLPGREGAAA AAAAGGGGDA GGGGGGGQEA APLSVPTSSS
HRGGGGSGGG RRRLFLSPAL QGLLLPARAG PRPPPPPRLP LGQAARRAGS PGFPGAGPGG
GGQTPRRPQG ASFALAAAAA LLFGSDMEDG PSNNASCFRR LTECFLSPSL TDEKVKAYLS
LHPQVLDEFV SESVSAETVE KWLKRKNNKS EDESAPKEVS RYQDTNMQGV VYELNSYIEQ
RLDTGGDNQL LLYELSSIIK IATKADGFAL YFLGECNNSL CIFTPPGIKE GKPRLIPAGP
ITQGTTVSAY VAKSRKTLLV EDILGDERFP RGTGLESGTR IQSVLCLPIV TAIGDLIGIL
ELYRHWGKEA FCLSHQEVAT ANLAWASVAI HQVQVCRGLA KQTELNDFLL DVSKTYFDNI
VAIDSLLEHI MIYAKNLVNA DRCALFQVDH KNKELYSDLF DIGEEKEGKP VFKKTKEIRF
SIEKGIAGQV ARTGEVLNIP DAYADPRFNR EVDLYTGYTT RNILCMPIVS RGSVIGVVQM
VNKISGSAFS KTDENNFKMF AVFCALALHC ANMYHRIRHS ECIYRVTMEK LSYHSICTSE
EWQGLMQFTL PVRLCKEIEL FHFDIGPFEN MWPGIFVYMV HRSCGTSCFE LEKLCRFIMS
VKKNYRRVPY HNWKHAVTVA HCMYAILQNN HTLFTDLERK GLLIACLCHD LDHRGFSNSY
LQKFDHPLAA LYSTSTMEQH HFSQTVSILQ LEGHNIFSTL SSSEYEQVLE IIRKAIIATD
LALYFGNRKQ LEEMYQTGSL NLNNQSHRDR VIGLMMTACD LCSVTKLWPV TKLTANDIYA
EFWAEGDEMK KLGIQPIPMM DRDKKDEVPQ GQLGFYNAVA IPCYTTLTQI LPPTEPLLKA
CRDNLSQWEK VIRGEETATW ISSPSVAQKA AASED
//
