PDE10_MOUSE
ID PDE10_MOUSE Reviewed; 790 AA.
AC Q8CA95; Q3TLU6; Q3TRG6; Q69C21; Q9WVI1;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A;
DE EC=3.1.4.17 {ECO:0000269|PubMed:10359840};
GN Name=Pde10a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=10359840; DOI=10.1073/pnas.96.12.7071;
RA Soderling S.H., Bayuga S.J., Beavo J.A.;
RT "Isolation and characterization of a dual-substrate phosphodiesterase gene
RT family: PDE10A.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:7071-7076(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INDUCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6 X CBA; TISSUE=Corpus striatum;
RX PubMed=14751289; DOI=10.1016/j.neuroscience.2003.11.009;
RA Hebb A.L., Robertson H.A., Denovan-Wright E.M.;
RT "Striatal phosphodiesterase mRNA and protein levels are reduced in
RT Huntington's disease transgenic mice prior to the onset of motor
RT symptoms.";
RL Neuroscience 123:967-981(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Mammary gland, Spinal cord, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF TYR-101.
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).
CC -!- FUNCTION: Plays a role in signal transduction by regulating the
CC intracellular concentration of cyclic nucleotides (PubMed:10359840).
CC Can hydrolyze both cAMP and cGMP, but has higher affinity for cAMP and
CC is more efficient with cAMP as substrate (PubMed:10359840). May play a
CC critical role in regulating cAMP and cGMP levels in the striatum, a
CC region of the brain that contributes to the control of movement and
CC cognition (PubMed:10359840, PubMed:14751289, PubMed:27058446).
CC {ECO:0000269|PubMed:10359840, ECO:0000269|PubMed:14751289,
CC ECO:0000269|PubMed:27058446}.
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:10359840};
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:10359840};
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:10359840};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:Q9Y233};
CC Note=Binds 2 divalent metal cations per subunit. Site 1 may
CC preferentially bind zinc ions, while site 2 has a preference for
CC magnesium and/or manganese ions. {ECO:0000250|UniProtKB:Q9Y233};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.05 uM for cAMP {ECO:0000269|PubMed:10359840};
CC KM=3 uM for cGMP {ECO:0000269|PubMed:10359840};
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC 3',5'-cyclic AMP: step 1/1. {ECO:0000269|PubMed:10359840}.
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic GMP degradation; GMP from
CC 3',5'-cyclic GMP: step 1/1. {ECO:0000269|PubMed:10359840}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9Y233}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9Y233}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8CA95-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CA95-2; Sequence=VSP_035917;
CC Name=3;
CC IsoId=Q8CA95-3; Sequence=VSP_035916;
CC Name=4;
CC IsoId=Q8CA95-4; Sequence=VSP_035915, VSP_035918;
CC -!- TISSUE SPECIFICITY: Detected in striatum (at protein level). Detected
CC in testis and brain. {ECO:0000269|PubMed:10359840,
CC ECO:0000269|PubMed:14751289}.
CC -!- INDUCTION: Down-regulated by the expression of a huntingtin (HD) gene
CC with an expanded polyglutamine repeat prior to the onset of
CC neurological symptoms related to Huntington disease.
CC {ECO:0000269|PubMed:14751289}.
CC -!- DOMAIN: The tandem GAF domains bind cAMP, and regulate enzyme activity.
CC The binding of cAMP stimulates enzyme activity (By similarity).
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; AF110507; AAD31544.1; -; mRNA.
DR EMBL; AY360383; AAR12579.1; -; mRNA.
DR EMBL; AK039249; BAC30292.1; -; mRNA.
DR EMBL; AK162804; BAE37063.1; -; mRNA.
DR EMBL; AK166310; BAE38696.1; -; mRNA.
DR EMBL; CH466619; EDL02097.1; -; Genomic_DNA.
DR EMBL; CH466619; EDL02099.1; -; Genomic_DNA.
DR EMBL; BC113201; AAI13202.1; -; mRNA.
DR CCDS; CCDS28384.1; -. [Q8CA95-3]
DR CCDS; CCDS84274.1; -. [Q8CA95-2]
DR RefSeq; NP_001277636.1; NM_001290707.1.
DR RefSeq; NP_001334250.1; NM_001347321.1. [Q8CA95-2]
DR RefSeq; NP_035996.2; NM_011866.2. [Q8CA95-3]
DR RefSeq; XP_017172950.1; XM_017317461.1.
DR AlphaFoldDB; Q8CA95; -.
DR SMR; Q8CA95; -.
DR BioGRID; 204836; 18.
DR STRING; 10090.ENSMUSP00000086485; -.
DR BindingDB; Q8CA95; -.
DR ChEMBL; CHEMBL1795126; -.
DR iPTMnet; Q8CA95; -.
DR PhosphoSitePlus; Q8CA95; -.
DR SwissPalm; Q8CA95; -.
DR MaxQB; Q8CA95; -.
DR PaxDb; Q8CA95; -.
DR PeptideAtlas; Q8CA95; -.
DR PRIDE; Q8CA95; -.
DR ProteomicsDB; 287982; -. [Q8CA95-1]
DR ProteomicsDB; 287983; -. [Q8CA95-2]
DR ProteomicsDB; 287984; -. [Q8CA95-3]
DR ProteomicsDB; 287985; -. [Q8CA95-4]
DR Antibodypedia; 33512; 232 antibodies from 27 providers.
DR DNASU; 23984; -.
DR Ensembl; ENSMUST00000089085; ENSMUSP00000086485; ENSMUSG00000023868. [Q8CA95-3]
DR Ensembl; ENSMUST00000115720; ENSMUSP00000111385; ENSMUSG00000023868. [Q8CA95-2]
DR Ensembl; ENSMUST00000149440; ENSMUSP00000123216; ENSMUSG00000023868. [Q8CA95-4]
DR GeneID; 23984; -.
DR KEGG; mmu:23984; -.
DR UCSC; uc008ajr.1; mouse. [Q8CA95-1]
DR UCSC; uc008ajs.1; mouse. [Q8CA95-3]
DR UCSC; uc008aju.1; mouse. [Q8CA95-2]
DR CTD; 10846; -.
DR MGI; MGI:1345143; Pde10a.
DR VEuPathDB; HostDB:ENSMUSG00000023868; -.
DR eggNOG; KOG3689; Eukaryota.
DR GeneTree; ENSGT00940000156543; -.
DR InParanoid; Q8CA95; -.
DR OMA; VAYHNWA; -.
DR OrthoDB; 904682at2759; -.
DR TreeFam; TF316499; -.
DR Reactome; R-MMU-418457; cGMP effects.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR SABIO-RK; Q8CA95; -.
DR UniPathway; UPA00762; UER00747.
DR UniPathway; UPA00763; UER00748.
DR BioGRID-ORCS; 23984; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Pde10a; mouse.
DR PRO; PR:Q8CA95; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8CA95; protein.
DR Bgee; ENSMUSG00000023868; Expressed in caudate-putamen and 233 other tissues.
DR ExpressionAtlas; Q8CA95; baseline and differential.
DR Genevisible; Q8CA95; MM.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0030552; F:cAMP binding; ISS:UniProtKB.
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; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0010754; P:negative regulation of cGMP-mediated signaling; ISO:MGI.
DR GO; GO:0106070; P:regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:MGI.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 1.10.1300.10; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
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 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 PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Alternative splicing; cAMP; cAMP-binding; cGMP;
KW cGMP-binding; Cytoplasm; Hydrolase; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..790
FT /note="cAMP and cAMP-inhibited cGMP 3',5'-cyclic
FT phosphodiesterase 10A"
FT /id="PRO_0000355558"
FT DOMAIN 446..763
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 768..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 519
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O76083"
FT BINDING 290..291
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250|UniProtKB:Q9Y233"
FT BINDING 334..335
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250|UniProtKB:Q9Y233"
FT BINDING 368
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250|UniProtKB:Q9Y233"
FT BINDING 387
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250|UniProtKB:Q9Y233"
FT BINDING 519
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250|UniProtKB:Q9Y233"
FT BINDING 519
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000250|UniProtKB:Q9Y233"
FT BINDING 523
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y233"
FT BINDING 557
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y233"
FT BINDING 558
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y233"
FT BINDING 558
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y233"
FT BINDING 668
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y233"
FT BINDING 720
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250|UniProtKB:Q9Y233"
FT BINDING 720
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000250|UniProtKB:Q9Y233"
FT VAR_SEQ 1..60
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035915"
FT VAR_SEQ 1..17
FT /note="MSNDSTEGTVGSCNATG -> MEDGPSNNASCFRRLTECFLSPS (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14751289"
FT /id="VSP_035916"
FT VAR_SEQ 1..16
FT /note="MSNDSTEGTVGSCNAT -> MEKLY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10359840"
FT /id="VSP_035917"
FT VAR_SEQ 61..69
FT /note="EPSPKEVSR -> MPGPGQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035918"
FT MUTAGEN 101
FT /note="Y->C: Decreased protein abundance; decreased 3',5'-
FT cyclic-nucleotide phosphodiesterase activity."
FT /evidence="ECO:0000269|PubMed:27058446"
FT CONFLICT 774
FT /note="P -> Q (in Ref. 3; BAC30292)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 790 AA; 89408 MW; 1B1D8111A5AD7B92 CRC64;
MSNDSTEGTV GSCNATGLTD EKVKAYLSLH PQVLDEFVSE SVSAETVEKW LKRKTNKAKD
EPSPKEVSRY QDTNMQGVVY ELNSYIEQRL DTGGDNHLLL YELSSIIRIA TKADGFALYF
LGECNNSLCV FIPPGMKEGQ PRLIPAGPIT QGTTISAYVA KSRKTLLVED ILGDERFPRG
TGLESGTRIQ SVLCLPIVTA IGDLIGILEL YRHWGKEAFC LSHQEVATAN LAWASVAIHQ
VQVCRGLAKQ TELNDFLLDV SKTYFDNIVA IDSLLEHIMI YAKNLVNADR CALFQVDHKN
KELYSDLFDI GEEKEGKPIF KKTKEIRFSI EKGIAGQVAR TGEVLNIPDA YADPRFNREV
DLYTGYTTRN ILCMPIVSRG SVIGVVQMVN KISGSAFSKT DENNFKMFAV FCALALHCAN
MYHRIRHSEC IYRVTMEKLS YHSICTSEEW QGLMRFNLPA RICRDIELFH FDIGPFENMW
PGIFVYMIHR SCGTSCFELE KLCRFIMSVK KNYRRVPYHN WKHAVTVAHC MYAILQNNNG
LFTDLERKGL LIACLCHDLD HRGFSNSYLQ KFDHPLAALY STSTMEQHHF SQTVSILQLE
GHNIFSTLSS SEYEQVLEII RKAIIATDLA LYFGNRKQLE EMYQTGSLNL HNQSHRDRVI
GLMMTACDLC SVTKLWPVTK LTANDIYAEF WAEGDEMKKL GIQPIPMMDR DKRDEVPQGQ
LGFYNAVAIP CYTTLTQILP PTEPLLKACR DNLNQWEKVI RGEETAMWIS GPGPAPSKST
PEKLNVKVED
