ID PDE10_RAT Reviewed; 794 AA.
AC Q9QYJ6; Q6S9E6; Q6S9E7; Q6S9E8; Q6S9E9; Q9QYJ5;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 136.
DE RecName: Full=cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A;
DE EC=3.1.4.17 {ECO:0000269|PubMed:10583409, ECO:0000269|PubMed:14752115};
GN Name=Pde10a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING,
RP FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=10583409; DOI=10.1046/j.1432-1327.1999.00963.x;
RA Fujishige K., Kotera J., Omori K.;
RT "Striatum- and testis-specific phosphodiesterase PDE10A isolation and
RT characterization of a rat PDE10A.";
RL Eur. J. Biochem. 266:1118-1127(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5 AND 6), TISSUE SPECIFICITY,
RP CATALYTIC ACTIVITY, AND INDUCTION.
RC STRAIN=Wistar;
RX PubMed=14752115; DOI=10.1074/jbc.m312500200;
RA O'Connor V., Genin A., Davis S., Karishma K.K., Doyere V., De Zeeuw C.I.,
RA Sanger G., Hunt S.P., Richter-Levin G., Mallet J., Laroche S.,
RA Bliss T.V.P., French P.J.;
RT "Differential amplification of intron-containing transcripts reveals long
RT term potentiation-associated up-regulation of specific Pde10A
RT phosphodiesterase splice variants.";
RL J. Biol. Chem. 279:15841-15849(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 452-794 IN COMPLEXES WITH ZINC;
RP MAGNESIUM AND A SYNTHETIC INHIBITOR, AND COFACTOR.
RX PubMed=17228859; DOI=10.1021/jm060653b;
RA Chappie T.A., Humphrey J.M., Allen M.P., Estep K.G., Fox C.B., Lebel L.A.,
RA Liras S., Marr E.S., Menniti F.S., Pandit J., Schmidt C.J., Tu M.,
RA Williams R.D., Yang F.V.;
RT "Discovery of a series of 6,7-dimethoxy-4-pyrrolidylquinazoline PDE10A
RT inhibitors.";
RL J. Med. Chem. 50:182-185(2007).
CC -!- FUNCTION: Plays a role in signal transduction by regulating the
CC intracellular concentration of cyclic nucleotides. Can hydrolyze both
CC cAMP and cGMP, but has higher affinity for cAMP and is more efficient
CC with cAMP as substrate. {ECO:0000269|PubMed:10583409}.
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:10583409, ECO:0000269|PubMed:14752115};
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:10583409};
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:10583409,
CC ECO:0000269|PubMed:14752115};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:17228859};
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:17228859};
CC -!- ACTIVITY REGULATION: Inhibited by dipyridamole and moderately by IBMX,
CC zaprinast and rolipram. {ECO:0000269|PubMed:10583409}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.26 uM for cAMP {ECO:0000269|PubMed:10583409};
CC KM=9.3 uM for cGMP {ECO:0000269|PubMed:10583409};
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC 3',5'-cyclic AMP: step 1/1. {ECO:0000269|PubMed:10583409,
CC ECO:0000269|PubMed:14752115}.
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic GMP degradation; GMP from
CC 3',5'-cyclic GMP: step 1/1. {ECO:0000269|PubMed:10583409,
CC ECO:0000269|PubMed:14752115}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9Y233}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10583409}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=PDE10A2 {ECO:0000303|PubMed:14752115};
CC IsoId=Q9QYJ6-1; Sequence=Displayed;
CC Name=2; Synonyms=PDE10A3 {ECO:0000303|PubMed:14752115};
CC IsoId=Q9QYJ6-2; Sequence=VSP_035921;
CC Name=3; Synonyms=PDE10A11 {ECO:0000303|PubMed:14752115};
CC IsoId=Q9QYJ6-3; Sequence=VSP_035922;
CC Name=4; Synonyms=PDE10A12 {ECO:0000303|PubMed:14752115};
CC IsoId=Q9QYJ6-4; Sequence=VSP_035923;
CC Name=5; Synonyms=PDE10A13 {ECO:0000303|PubMed:14752115};
CC IsoId=Q9QYJ6-5; Sequence=VSP_035920;
CC Name=6; Synonyms=PDE10A14 {ECO:0000303|PubMed:14752115};
CC IsoId=Q9QYJ6-6; Sequence=VSP_035919;
CC -!- TISSUE SPECIFICITY: Detected in striatum and testis (at protein level).
CC Detected in whole brain, hippocampus, olfactory bulb, striatum neurons
CC and testis. {ECO:0000269|PubMed:10583409, ECO:0000269|PubMed:14752115}.
CC -!- INDUCTION: Up-regulated in brain after seizures. Up-regulated in the
CC hippocampus one hour after induction of long-term potentiation.
CC {ECO:0000269|PubMed:14752115}.
CC -!- DOMAIN: The tandem GAF domains bind cAMP, and regulate enzyme activity.
CC The binding of cAMP stimulates enzyme activity.
CC {ECO:0000250|UniProtKB:Q9Y233}.
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:0000250|UniProtKB:Q9Y233}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000305}.
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DR EMBL; AB027155; BAA88996.1; -; mRNA.
DR EMBL; AB027156; BAA88997.1; -; mRNA.
DR EMBL; AY462091; AAS21243.1; -; mRNA.
DR EMBL; AY462092; AAS21244.1; -; mRNA.
DR EMBL; AY462093; AAS21245.1; -; mRNA.
DR EMBL; AY462094; AAS21246.1; -; mRNA.
DR EMBL; AY462095; AAS21247.1; -; mRNA.
DR EMBL; CH474059; EDL83106.1; -; Genomic_DNA.
DR RefSeq; NP_071572.1; NM_022236.1. [Q9QYJ6-1]
DR PDB; 2O8H; X-ray; 1.80 A; A=452-794.
DR PDB; 2OVV; X-ray; 2.00 A; A=452-794.
DR PDB; 2OVY; X-ray; 1.80 A; A=452-794.
DR PDB; 3HQW; X-ray; 1.70 A; A=452-794.
DR PDB; 3HQY; X-ray; 2.00 A; A=452-794.
DR PDB; 3HQZ; X-ray; 1.70 A; A=452-794.
DR PDB; 3HR1; X-ray; 1.53 A; A=452-794.
DR PDB; 3LXG; X-ray; 2.30 A; A=463-770.
DR PDB; 3QPN; X-ray; 2.00 A; A=452-794.
DR PDB; 3QPO; X-ray; 1.80 A; A=452-794.
DR PDB; 3QPP; X-ray; 1.80 A; A=452-794.
DR PDB; 6K9U; X-ray; 2.35 A; A=463-770.
DR PDBsum; 2O8H; -.
DR PDBsum; 2OVV; -.
DR PDBsum; 2OVY; -.
DR PDBsum; 3HQW; -.
DR PDBsum; 3HQY; -.
DR PDBsum; 3HQZ; -.
DR PDBsum; 3HR1; -.
DR PDBsum; 3LXG; -.
DR PDBsum; 3QPN; -.
DR PDBsum; 3QPO; -.
DR PDBsum; 3QPP; -.
DR PDBsum; 6K9U; -.
DR AlphaFoldDB; Q9QYJ6; -.
DR SMR; Q9QYJ6; -.
DR BioGRID; 248919; 1.
DR STRING; 10116.ENSRNOP00000042134; -.
DR BindingDB; Q9QYJ6; -.
DR ChEMBL; CHEMBL6140; -.
DR DrugCentral; Q9QYJ6; -.
DR iPTMnet; Q9QYJ6; -.
DR PhosphoSitePlus; Q9QYJ6; -.
DR SwissPalm; Q9QYJ6; -.
DR PaxDb; 10116-ENSRNOP00000060834; -.
DR Ensembl; ENSRNOT00000043474.4; ENSRNOP00000042134.2; ENSRNOG00000011310.9. [Q9QYJ6-1]
DR Ensembl; ENSRNOT00000067142.5; ENSRNOP00000060834.4; ENSRNOG00000011310.9. [Q9QYJ6-4]
DR Ensembl; ENSRNOT00000111873.1; ENSRNOP00000091632.1; ENSRNOG00000011310.9. [Q9QYJ6-3]
DR Ensembl; ENSRNOT00055049538; ENSRNOP00055040758; ENSRNOG00055028570. [Q9QYJ6-1]
DR Ensembl; ENSRNOT00060017358; ENSRNOP00060013486; ENSRNOG00060010248. [Q9QYJ6-1]
DR Ensembl; ENSRNOT00065051379; ENSRNOP00065042316; ENSRNOG00065029728. [Q9QYJ6-1]
DR GeneID; 63885; -.
DR KEGG; rno:63885; -.
DR AGR; RGD:68434; -.
DR CTD; 10846; -.
DR RGD; 68434; Pde10a.
DR eggNOG; KOG3689; Eukaryota.
DR GeneTree; ENSGT00940000156543; -.
DR InParanoid; Q9QYJ6; -.
DR OMA; HNWAHGW; -.
DR OrthoDB; 5479253at2759; -.
DR TreeFam; TF316499; -.
DR Reactome; R-RNO-418457; cGMP effects.
DR Reactome; R-RNO-418555; G alpha (s) signalling events.
DR SABIO-RK; Q9QYJ6; -.
DR UniPathway; UPA00762; UER00747.
DR UniPathway; UPA00763; UER00748.
DR EvolutionaryTrace; Q9QYJ6; -.
DR PRO; PR:Q9QYJ6; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000011310; Expressed in Ammon's horn and 15 other cell types or tissues.
DR ExpressionAtlas; Q9QYJ6; baseline and differential.
DR Genevisible; Q9QYJ6; RN.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0030552; F:cAMP binding; ISO:RGD.
DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR GO; GO:0004118; F:cGMP-stimulated cyclic-nucleotide phosphodiesterase activity; ISS:UniProtKB.
DR GO; GO:0004112; F:cyclic-nucleotide phosphodiesterase activity; IDA:RGD.
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:0043951; P:negative regulation of cAMP-mediated signaling; IDA:RGD.
DR GO; GO:0010754; P:negative regulation of cGMP-mediated signaling; IDA:RGD.
DR GO; GO:0106070; P:regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; ISO:RGD.
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 splicing; cAMP; cAMP-binding;
KW cGMP; cGMP-binding; Cytoplasm; Hydrolase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..794
FT /note="cAMP and cAMP-inhibited cGMP 3',5'-cyclic
FT phosphodiesterase 10A"
FT /id="PRO_0000355559"
FT DOMAIN 452..769
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT ACT_SITE 525
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O76083"
FT BINDING 296..297
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250|UniProtKB:Q9Y233"
FT BINDING 340..341
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250|UniProtKB:Q9Y233"
FT BINDING 374
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250|UniProtKB:Q9Y233"
FT BINDING 393
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250|UniProtKB:Q9Y233"
FT BINDING 525
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250|UniProtKB:Q9Y233"
FT BINDING 525
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000250|UniProtKB:Q9Y233"
FT BINDING 529
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17228859"
FT BINDING 563
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17228859"
FT BINDING 564
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17228859"
FT BINDING 564
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17228859"
FT BINDING 674
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17228859"
FT BINDING 726
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250|UniProtKB:Q9Y233"
FT BINDING 726
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000250|UniProtKB:Q9Y233"
FT VAR_SEQ 1..141
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14752115"
FT /id="VSP_035919"
FT VAR_SEQ 1..80
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14752115"
FT /id="VSP_035920"
FT VAR_SEQ 1..23
FT /note="MEDGPSNNASCFRRLTECFLSPS -> MSNDSPEGAVGSCNATG (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:10583409,
FT ECO:0000303|PubMed:14752115"
FT /id="VSP_035921"
FT VAR_SEQ 1..23
FT /note="MEDGPSNNASCFRRLTECFLSPS -> MSKKRKALEGGGGGGEPQLPEEEPT
FT AWFGGSSEEPAGCLPITFKGGSKGPALLALRNRTDSRGQMSNDSPEGAVGSCNATG
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14752115"
FT /id="VSP_035922"
FT VAR_SEQ 1..23
FT /note="MEDGPSNNASCFRRLTECFLSPS -> MSKKRKALEGGGGGGEPQLPEEEPT
FT AWFGGSSEEPAGCLPITFKGGSKGPALLALRNRTDSRGQMSNDSPEGAVGSCNATGSTG
FT STGELGKEFHTPPRRKSASDSRLALCMG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14752115"
FT /id="VSP_035923"
FT HELIX 466..471
FT /evidence="ECO:0007829|PDB:3HR1"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:3HR1"
FT HELIX 486..498
FT /evidence="ECO:0007829|PDB:3HR1"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:3HQW"
FT HELIX 505..517
FT /evidence="ECO:0007829|PDB:3HR1"
FT STRAND 523..526
FT /evidence="ECO:0007829|PDB:3HR1"
FT HELIX 527..542
FT /evidence="ECO:0007829|PDB:3HR1"
FT TURN 545..547
FT /evidence="ECO:0007829|PDB:3HR1"
FT HELIX 550..562
FT /evidence="ECO:0007829|PDB:3HR1"
FT TURN 563..566
FT /evidence="ECO:0007829|PDB:3HR1"
FT HELIX 572..578
FT /evidence="ECO:0007829|PDB:3HR1"
FT HELIX 581..585
FT /evidence="ECO:0007829|PDB:3HR1"
FT STRAND 587..589
FT /evidence="ECO:0007829|PDB:3HR1"
FT HELIX 590..603
FT /evidence="ECO:0007829|PDB:3HR1"
FT TURN 610..613
FT /evidence="ECO:0007829|PDB:3HR1"
FT HELIX 616..632
FT /evidence="ECO:0007829|PDB:3HR1"
FT HELIX 635..650
FT /evidence="ECO:0007829|PDB:3HR1"
FT HELIX 659..674
FT /evidence="ECO:0007829|PDB:3HR1"
FT HELIX 676..679
FT /evidence="ECO:0007829|PDB:3HR1"
FT HELIX 682..705
FT /evidence="ECO:0007829|PDB:3HR1"
FT HELIX 712..714
FT /evidence="ECO:0007829|PDB:3HR1"
FT HELIX 716..721
FT /evidence="ECO:0007829|PDB:3HR1"
FT HELIX 722..732
FT /evidence="ECO:0007829|PDB:3HR1"
FT HELIX 734..744
FT /evidence="ECO:0007829|PDB:3HR1"
FT HELIX 746..748
FT /evidence="ECO:0007829|PDB:3HR1"
FT HELIX 749..766
FT /evidence="ECO:0007829|PDB:3HR1"
SQ SEQUENCE 794 AA; 90161 MW; A36C4678B385846E CRC64;
MEDGPSNNAS CFRRLTECFL SPSLTDEKVK AYLSLHPQVL DEFVSESVSA ETVEKWLKRK
NNKAEDEPSP KEVSRYQDTN MQGVVYELNS YIEQRLDTGG DNHLLLYELS SIIRIATKAD
GFALYFLGEC NNSLCVFTPP GMKEGQPRLI PAGPITQGTT ISAYVAKSRK TLLVEDILGD
ERFPRGTGLE SGTRIQSVLC LPIVTAIGDL IGILELYRHW GKEAFCLSHQ EVATANLAWA
SVAIHQVQVC RGLAKQTELN DFLLDVSKTY FDNIVAIDSL LEHIMIYAKN LVNADRCALF
QVDHKNKELY SDLFDIGEEK EGKPVFKKTK EIRFSIEKGI AGQVARTGEV LNIPDAYADP
RFNREVDLYT GYTTRNILCM PIVSRGSVIG VVQMVNKISG SAFSKTDENN FKMFAVFCAL
ALHCANMYHR IRHSECIYRV TMEKLSYHSI CTSEEWQGLM HFNLPARICR DIELFHFDIG
PFENMWPGIF VYMIHRSCGT SCFELEKLCR FIMSVKKNYR RVPYHNWKHA VTVAHCMYAI
LQNNNGLFTD LERKGLLIAC LCHDLDHRGF SNSYLQKFDH PLAALYSTST MEQHHFSQTV
SILQLEGHNI FSTLSSSEYE QVLEIIRKAI IATDLALYFG NRKQLEEMYQ TGSLNLHNQS
HRDRVIGLMM TACDLCSVTK LWPVTKLTAN DIYAEFWAEG DEMKKLGIQP IPMMDRDKRD
EVPQGQLGFY NAVAIPCYTT LTQILPPTEP LLKACRDNLN QWEKVIRGEE TAMWISGPAT
SKSTSEKPTR KVDD
//
