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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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 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. DR Genevisible; Q9QYJ6; RN. 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 //