ID   PDE1C_MOUSE             Reviewed;         706 AA.
AC   Q64338; Q62045; Q8BSV6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C {ECO:0000305|PubMed:8810348};
DE            Short=Cam-PDE 1C;
DE            EC=3.1.4.17 {ECO:0000269|PubMed:8810348};
GN   Name=Pde1c {ECO:0000312|MGI:MGI:108413};
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] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC
RP   ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ; TISSUE=Brain;
RX   PubMed=8810348; DOI=10.1074/jbc.271.41.25699;
RA   Yan C., Zhao A.Z., Bentley J.K., Beavo J.A.;
RT   "The calmodulin-dependent phosphodiesterase gene PDE1C encodes several
RT   functionally different splice variants in a tissue-specific manner.";
RL   J. Biol. Chem. 271:25699-25706(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Pituitary;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, 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   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=29860631; DOI=10.1007/s00439-018-1895-y;
RA   Wang L., Feng Y., Yan D., Qin L., Grati M., Mittal R., Li T.,
RA   Sundhari A.K., Liu Y., Chapagain P., Blanton S.H., Liao S., Liu X.;
RT   "A dominant variant in the PDE1C gene is associated with nonsyndromic
RT   hearing loss.";
RL   Hum. Genet. 137:437-446(2018).
CC   -!- FUNCTION: Calmodulin-dependent cyclic nucleotide phosphodiesterase with
CC       a dual specificity for cAMP and cGMP, which are key regulators of many
CC       important physiological processes (PubMed:8810348). Exhibits high
CC       affinity for both cAMP and cGMP (By similarity). Modulates the
CC       amplitude and duration of the cAMP signal in sensory cilia in response
CC       to odorant stimulation, hence contributing to the generation of action
CC       potentials. Regulates smooth muscle cell proliferation. Regulates the
CC       stability of growth factor receptors, including PDGFRB (Probable).
CC       {ECO:0000250|UniProtKB:Q14123, ECO:0000269|PubMed:8810348,
CC       ECO:0000305|PubMed:29860631}.
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:8810348};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14654;
CC         Evidence={ECO:0000305|PubMed:8810348};
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:8810348};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958;
CC         Evidence={ECO:0000305|PubMed:8810348};
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:8810348};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278;
CC         Evidence={ECO:0000305|PubMed:8810348};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q01064};
CC       Note=Binds 2 divalent metal cations per subunit. Site 1 may
CC       preferentially bind zinc ions. {ECO:0000250|UniProtKB:Q01064};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q01064};
CC       Note=Binds 2 divalent metal cations per subunit. Site 2 has a
CC       preference for magnesium ions. {ECO:0000250|UniProtKB:Q01064};
CC   -!- ACTIVITY REGULATION: Type I PDE are activated by the binding of
CC       calmodulin in the presence of Ca(2+) (PubMed:8810348). Different splice
CC       variants may have different sensitivities to Ca(2+) (PubMed:8810348).
CC       {ECO:0000269|PubMed:8810348}.
CC   -!- ACTIVITY REGULATION: [Isoform 3]: Exhibits a higher sensitivity to
CC       Ca(2+) stimulation than isoforms 1 and 2 (PubMed:8810348).
CC       {ECO:0000269|PubMed:8810348}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 1]:
CC       Kinetic parameters:
CC         KM=1.1 uM for 3',5'-cyclic AMP (isoform 1)
CC         {ECO:0000269|PubMed:8810348};
CC         KM=1 uM for 3',5'-cyclic GMP (isoform 1)
CC         {ECO:0000269|PubMed:8810348};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 2]:
CC       Kinetic parameters:
CC         KM=3.5 uM for 3',5'-cyclic AMP (isoform 2)
CC         {ECO:0000269|PubMed:8810348};
CC         KM=2.2 uM for 3',5'-cyclic GMP (isoform 2)
CC         {ECO:0000269|PubMed:8810348};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P14100}.
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:29860631}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=3; Synonyms=PDE1C2 {ECO:0000303|PubMed:8810348};
CC         IsoId=Q64338-3; Sequence=Displayed;
CC       Name=1; Synonyms=PDE1C4 {ECO:0000303|PubMed:8810348}, PDE1C5
CC       {ECO:0000303|PubMed:8810348};
CC         IsoId=Q64338-1; Sequence=VSP_012381, VSP_012382;
CC       Name=2; Synonyms=PDE1C1 {ECO:0000303|PubMed:8810348};
CC         IsoId=Q64338-2; Sequence=VSP_004554, VSP_012380;
CC   -!- TISSUE SPECIFICITY: [Isoform 1]: Highly expressed in testis and at
CC       moderate levels in heart. {ECO:0000269|PubMed:8810348}.
CC   -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed at a moderate level in
CC       brain, the cerebellum, testis, heart and olfactory epithelium.
CC       {ECO:0000269|PubMed:8810348}.
CC   -!- TISSUE SPECIFICITY: [Isoform 3]: Highly expressed in olfactory
CC       epithelium and at very low levels, if any, in other tissues
CC       (PubMed:8810348). In the cochlea, expressed in the inner and outer hair
CC       cells (at protein level) (PubMed:29860631). In the brain, highly
CC       expressed in the neurons of the granule layer of the cerebellum, some
CC       Purkinje cells, the central amygdaloid nucleus, and the interpolar
CC       spinal trigem nucleus and, at moderate levels, in the glomerular and
CC       external plexiform layer of the olfactory bulb as well as in parts of
CC       the caudate-putamen and olfactory tubercle (PubMed:8810348).
CC       {ECO:0000269|PubMed:29860631, ECO:0000269|PubMed:8810348}.
CC   -!- MISCELLANEOUS: [Isoform 1]: PDE1C4 and PDE1C5 isoforms differ at the
CC       level of the 3'-UTR. {ECO:0000305|PubMed:8810348}.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC       PDE1 subfamily. {ECO:0000305}.
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DR   EMBL; L76947; AAC37702.1; -; mRNA.
DR   EMBL; L76946; AAC37703.1; -; mRNA.
DR   EMBL; L76944; AAC37701.1; -; mRNA.
DR   EMBL; AK030423; BAC26956.1; -; mRNA.
DR   CCDS; CCDS20170.1; -. [Q64338-1]
DR   CCDS; CCDS51784.1; -. [Q64338-3]
DR   CCDS; CCDS51785.1; -. [Q64338-2]
DR   RefSeq; NP_001020739.1; NM_001025568.2. [Q64338-2]
DR   RefSeq; NP_001153424.1; NM_001159952.1.
DR   RefSeq; NP_001153425.1; NM_001159953.1. [Q64338-3]
DR   RefSeq; NP_001153427.1; NM_001159955.1. [Q64338-1]
DR   RefSeq; NP_001153432.1; NM_001159960.1. [Q64338-2]
DR   RefSeq; NP_035184.1; NM_011054.4. [Q64338-1]
DR   RefSeq; XP_011239552.1; XM_011241250.2.
DR   RefSeq; XP_017176942.1; XM_017321453.1.
DR   AlphaFoldDB; Q64338; -.
DR   SMR; Q64338; -.
DR   BioGRID; 202076; 2.
DR   STRING; 10090.ENSMUSP00000046601; -.
DR   iPTMnet; Q64338; -.
DR   PhosphoSitePlus; Q64338; -.
DR   MaxQB; Q64338; -.
DR   PaxDb; 10090-ENSMUSP00000046601; -.
DR   ProteomicsDB; 287986; -. [Q64338-3]
DR   ProteomicsDB; 287987; -. [Q64338-1]
DR   ProteomicsDB; 287988; -. [Q64338-2]
DR   Antibodypedia; 12721; 195 antibodies from 28 providers.
DR   DNASU; 18575; -.
DR   Ensembl; ENSMUST00000044505.14; ENSMUSP00000046601.8; ENSMUSG00000004347.18. [Q64338-3]
DR   Ensembl; ENSMUST00000114327.9; ENSMUSP00000109966.3; ENSMUSG00000004347.18. [Q64338-1]
DR   Ensembl; ENSMUST00000164752.8; ENSMUSP00000129185.2; ENSMUSG00000004347.18. [Q64338-2]
DR   Ensembl; ENSMUST00000166102.8; ENSMUSP00000131350.2; ENSMUSG00000004347.18. [Q64338-2]
DR   Ensembl; ENSMUST00000168944.8; ENSMUSP00000128364.2; ENSMUSG00000004347.18. [Q64338-1]
DR   GeneID; 18575; -.
DR   KEGG; mmu:18575; -.
DR   UCSC; uc009caz.2; mouse. [Q64338-3]
DR   UCSC; uc009cbb.2; mouse. [Q64338-1]
DR   AGR; MGI:108413; -.
DR   CTD; 5137; -.
DR   MGI; MGI:108413; Pde1c.
DR   VEuPathDB; HostDB:ENSMUSG00000004347; -.
DR   eggNOG; KOG3688; Eukaryota.
DR   GeneTree; ENSGT00940000155331; -.
DR   InParanoid; Q64338; -.
DR   OMA; NLHERWT; -.
DR   OrthoDB; 240889at2759; -.
DR   PhylomeDB; Q64338; -.
DR   TreeFam; TF314638; -.
DR   Reactome; R-MMU-111957; Cam-PDE 1 activation.
DR   BioGRID-ORCS; 18575; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Pde1c; mouse.
DR   PRO; PR:Q64338; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q64338; Protein.
DR   Bgee; ENSMUSG00000004347; Expressed in lumbar dorsal root ganglion and 136 other cell types or tissues.
DR   ExpressionAtlas; Q64338; baseline and differential.
DR   GO; GO:0005929; C:cilium; IDA:MGI.
DR   GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:UniProtKB.
DR   GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IDA:UniProtKB.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0048101; F:calmodulin-activated 3',5'-cyclic-GMP phosphodiesterase activity; ISO:MGI.
DR   GO; GO:0004117; F:calmodulin-activated dual specificity 3',5'-cyclic-GMP, 3',5'-cyclic-AMP phosphodiesterase activity; ISO:MGI.
DR   GO; GO:0030552; F:cAMP binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI.
DR   GO; GO:0051592; P:response to calcium ion; ISO:MGI.
DR   GO; GO:0007608; P:sensory perception of smell; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   CDD; cd00077; HDc; 1.
DR   Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR   InterPro; IPR023174; PDEase_CS.
DR   InterPro; IPR013706; PDEase_N.
DR   PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR   PANTHER; PTHR11347:SF32; DUAL SPECIFICITY CALCIUM_CALMODULIN-DEPENDENT 3',5'-CYCLIC NUCLEOTIDE PHOSPHODIESTERASE 1C; 1.
DR   Pfam; PF00233; PDEase_I; 1.
DR   Pfam; PF08499; PDEase_I_N; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00471; HDc; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS00126; PDEASE_I_1; 1.
DR   PROSITE; PS51845; PDEASE_I_2; 1.
DR   Genevisible; Q64338; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Calmodulin-binding; cAMP; cGMP;
KW   Hydrolase; Lysosome; Magnesium; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..706
FT                   /note="Dual specificity calcium/calmodulin-dependent 3',5'-
FT                   cyclic nucleotide phosphodiesterase 1C"
FT                   /id="PRO_0000198793"
FT   DOMAIN          151..528
FT                   /note="PDEase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT   REGION          123..146
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P14100"
FT   REGION          453..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        524..553
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..632
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        633..649
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        228
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O76083"
FT   BINDING         232
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q01064"
FT   BINDING         268
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q01064"
FT   BINDING         269
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q01064"
FT   BINDING         269
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q01064"
FT   BINDING         376
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q01064"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14123"
FT   VAR_SEQ         628..631
FT                   /note="GTKK -> DPEE (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8810348"
FT                   /id="VSP_004554"
FT   VAR_SEQ         632..706
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8810348"
FT                   /id="VSP_012380"
FT   VAR_SEQ         651..654
FT                   /note="VIKP -> GDYG (in isoform 1)"
FT                   /evidence="ECO:0000303|PubMed:8810348"
FT                   /id="VSP_012381"
FT   VAR_SEQ         655..706
FT                   /note="Missing (in isoform 1)"
FT                   /evidence="ECO:0000303|PubMed:8810348"
FT                   /id="VSP_012382"
SQ   SEQUENCE   706 AA;  80290 MW;  1F58533E1259801F CRC64;
     MESPTKEIEE FESNSLKHLQ PEQIEKIWLR LRGLRKYKKT SQRLRSLVKQ LERGEASVVD
     LKKNLEYAAT VLESVYIDET RRLLDTEDEL SDIQSDAVPS EVRDWLASTF TRQMGMMLRR
     SDEKPRFKSI VHAVQAGIFV ERMYRRTSNM VGLSYPPAVI DALKDVDTWS FDVFSLNEAS
     GDHALKFIFY ELLTRYDLIS RFKIPISALV SFVEALEVGY SKHKNPYHNL MHAADVTQTV
     HYLLYKTGVA NWLTELEIFA IIFSAAIHDY EHTGTTNNFH IQTRSDPAIL YNDRSVLENH
     HLSAAYRLLQ EDEEMNILVN LSKDDWREFR TLVIEMVMAT DMSCHFQQIK AMKTALQQPE
     AIEKPKALSL MLHTADISHP AKAWDLHHRW TMSLLEEFFR QGDREAELGL PFSPLCDRKS
     TMVAQSQVGF IDFIVEPTFT VLTDMTEKIV SPLIDESSQT GGTGQRRSSL NSINSSDAKR
     SGVKSSGSDG SAPINNSVIP VDYKSFKATW TEVVQINRER WRAKVPKEEK AKKEAEEKAR
     LAAEEKQKEM EAKSQAEQGT TSKGEKKTSG EAKSQVNGTR KGDNPRGKNS KGEKAGEKQQ
     NGDLKDGKNK ADKKDHSNTG NESKKTDGTK KRSHGSPAPS TSSTSRITLP VIKPPLRHFK
     RPAYASSSYA PSVPKKTDDH PVRYKMLDQR IKMKKIQNIS HHWNKK
//