PDE1C_MOUSE
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 03-AUG-2022, entry version 156.
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=1.0 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 RefSeq; XP_017176943.1; XM_017321454.1. [Q64338-2]
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; Q64338; -.
DR PRIDE; Q64338; -.
DR ProteomicsDB; 287986; -. [Q64338-3]
DR ProteomicsDB; 287987; -. [Q64338-1]
DR ProteomicsDB; 287988; -. [Q64338-2]
DR Antibodypedia; 12721; 176 antibodies from 28 providers.
DR DNASU; 18575; -.
DR Ensembl; ENSMUST00000044505; ENSMUSP00000046601; ENSMUSG00000004347. [Q64338-3]
DR Ensembl; ENSMUST00000114327; ENSMUSP00000109966; ENSMUSG00000004347. [Q64338-1]
DR Ensembl; ENSMUST00000164752; ENSMUSP00000129185; ENSMUSG00000004347. [Q64338-2]
DR Ensembl; ENSMUST00000166102; ENSMUSP00000131350; ENSMUSG00000004347. [Q64338-2]
DR Ensembl; ENSMUST00000168944; ENSMUSP00000128364; ENSMUSG00000004347. [Q64338-1]
DR GeneID; 18575; -.
DR KEGG; mmu:18575; -.
DR UCSC; uc009caz.2; mouse. [Q64338-3]
DR UCSC; uc009cbb.2; mouse. [Q64338-1]
DR CTD; 5137; -.
DR MGI; MGI:108413; Pde1c.
DR VEuPathDB; HostDB:ENSMUSG00000004347; -.
DR eggNOG; KOG3688; Eukaryota.
DR GeneTree; ENSGT00940000155331; -.
DR InParanoid; Q64338; -.
DR OMA; HHRWTMQ; -.
DR OrthoDB; 904682at2759; -.
DR PhylomeDB; Q64338; -.
DR TreeFam; TF314638; -.
DR Reactome; R-MMU-111957; Cam-PDE 1 activation.
DR BioGRID-ORCS; 18575; 2 hits in 72 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 134 other tissues.
DR ExpressionAtlas; Q64338; baseline and differential.
DR Genevisible; Q64338; MM.
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:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IBA:GO_Central.
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; -; 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 Pfam; PF00233; PDEase_I; 1.
DR Pfam; PF08499; PDEase_I_N; 1.
DR PRINTS; PR00387; PDIESTERASE1.
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 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
