ID CDS2_MOUSE Reviewed; 444 AA. AC Q99L43; Q3TMD1; Q6NSU1; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 24-JAN-2024, entry version 161. DE RecName: Full=Phosphatidate cytidylyltransferase 2 {ECO:0000305}; DE EC=2.7.7.41 {ECO:0000250|UniProtKB:O95674}; DE AltName: Full=CDP-DAG synthase 2; DE AltName: Full=CDP-DG synthase 2; DE AltName: Full=CDP-diacylglycerol synthase 2; DE Short=CDS 2; DE AltName: Full=CDP-diglyceride pyrophosphorylase 2; DE AltName: Full=CDP-diglyceride synthase 2; DE AltName: Full=CTP:phosphatidate cytidylyltransferase 2; GN Name=Cds2 {ECO:0000312|MGI:MGI:1332236}; 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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6J; RX PubMed=16023307; DOI=10.1016/j.gene.2005.04.037; RA Inglis-Broadgate S.L., Ocaka L., Banerjee R., Gaasenbeek M., Chapple J.P., RA Cheetham M.E., Clark B.J., Hunt D.M., Halford S.; RT "Isolation and characterization of murine Cds (CDP-diacylglycerol synthase) RT 1 and 2."; RL Gene 356:19-31(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryonic stem cell, and Lung; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Embryo, and Mammary tumor; 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 [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200; RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.; RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and RT MS/MS/MS."; RL Mol. Cell. Proteomics 6:669-676(2007). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18630941; DOI=10.1021/pr800223m; RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity RT chromatography adsorbent for phosphoproteome analysis."; RL J. Proteome Res. 7:3957-3967(2008). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-36 AND THR-50, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, 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 [9] RP FUNCTION. RX PubMed=26946540; DOI=10.1194/jlr.m060574; RA Qi Y., Kapterian T.S., Du X., Ma Q., Fei W., Zhang Y., Huang X., RA Dawes I.W., Yang H.; RT "CDP-diacylglycerol synthases regulate the growth of lipid droplets and RT adipocyte development."; RL J. Lipid Res. 57:767-780(2016). CC -!- FUNCTION: Catalyzes the conversion of phosphatidic acid (PA) to CDP- CC diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of CC phosphatidylglycerol, cardiolipin and phosphatidylinositol (By CC similarity). Exhibits specificity for the nature of the acyl chains at CC the sn-1 and sn-2 positions in the substrate, PA and the preferred acyl CC chain composition is 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid (By CC similarity). Plays an important role in regulating the growth and CC maturation of lipid droplets which are storage organelles at the center CC of lipid and energy homeostasis (PubMed:26946540). CC {ECO:0000250|UniProtKB:O95674, ECO:0000269|PubMed:26946540}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2- CC diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, CC ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41; CC Evidence={ECO:0000250|UniProtKB:O95674}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16230; CC Evidence={ECO:0000250|UniProtKB:O95674}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- CC 3-phosphate + CTP + H(+) = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z- CC eicosatetraenoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphate; CC Xref=Rhea:RHEA:45648, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:37563, ChEBI:CHEBI:77091, ChEBI:CHEBI:85349; CC Evidence={ECO:0000250|UniProtKB:O95674}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45649; CC Evidence={ECO:0000250|UniProtKB:O95674}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3- CC phosphate + CTP + H(+) = 1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)- CC sn-glycero-3-cytidine-5'-diphosphate + diphosphate; CC Xref=Rhea:RHEA:45660, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:37563, ChEBI:CHEBI:77098, ChEBI:CHEBI:85352; CC Evidence={ECO:0000250|UniProtKB:O95674}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45661; CC Evidence={ECO:0000250|UniProtKB:O95674}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- CC 3-phosphate + CTP + H(+) = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z- CC eicosatetraenoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphate; CC Xref=Rhea:RHEA:45652, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:37563, ChEBI:CHEBI:72864, ChEBI:CHEBI:85350; CC Evidence={ECO:0000250|UniProtKB:O95674}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45653; CC Evidence={ECO:0000250|UniProtKB:O95674}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-di-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate CC + CTP + H(+) = 1,2-di-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3- CC cytidine-5'-diphosphate + diphosphate; Xref=Rhea:RHEA:45656, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, CC ChEBI:CHEBI:77126, ChEBI:CHEBI:85351; CC Evidence={ECO:0000250|UniProtKB:O95674}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45657; CC Evidence={ECO:0000250|UniProtKB:O95674}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CC CTP + H(+) = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3- CC cytidine-5'-diphosphate + diphosphate; Xref=Rhea:RHEA:45664, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, CC ChEBI:CHEBI:74560, ChEBI:CHEBI:85353; CC Evidence={ECO:0000250|UniProtKB:O95674}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45665; CC Evidence={ECO:0000250|UniProtKB:O95674}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn- CC glycero-3-phosphate + CTP + H(+) = 1-octadecanoyl-2- CC (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-cytidine-5'- CC diphosphate + diphosphate; Xref=Rhea:RHEA:45668, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:77130, CC ChEBI:CHEBI:85354; Evidence={ECO:0000250|UniProtKB:O95674}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45669; CC Evidence={ECO:0000250|UniProtKB:O95674}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + CTP + CC H(+) = 1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-cytidine-5'- CC diphosphate + diphosphate; Xref=Rhea:RHEA:45672, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:77128, CC ChEBI:CHEBI:85355; Evidence={ECO:0000250|UniProtKB:O95674}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45673; CC Evidence={ECO:0000250|UniProtKB:O95674}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CTP + H(+) = CC 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-cytidine-5'-diphosphate + CC diphosphate; Xref=Rhea:RHEA:45676, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:74546, CC ChEBI:CHEBI:85356; Evidence={ECO:0000250|UniProtKB:O95674}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45677; CC Evidence={ECO:0000250|UniProtKB:O95674}; CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP- CC diacylglycerol from sn-glycerol 3-phosphate: step 3/3. CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q91XU8}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:16023307}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in the ganglion cell layer CC and inner nuclear layer of the retina. {ECO:0000269|PubMed:16023307}. CC -!- SIMILARITY: Belongs to the CDS family. {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; AY159802; AAO17790.1; -; mRNA. DR EMBL; AK036328; BAC29384.1; -; mRNA. DR EMBL; AK147541; BAE27984.1; -; mRNA. DR EMBL; AK166001; BAE38511.1; -; mRNA. DR EMBL; BC003852; AAH03852.1; -; mRNA. DR EMBL; BC069879; AAH69879.1; -; mRNA. DR CCDS; CCDS16772.1; -. DR RefSeq; NP_001277968.1; NM_001291039.1. DR RefSeq; NP_619592.1; NM_138651.7. DR AlphaFoldDB; Q99L43; -. DR BioGRID; 226008; 11. DR IntAct; Q99L43; 1. DR MINT; Q99L43; -. DR STRING; 10090.ENSMUSP00000099470; -. DR GlyConnect; 2581; 1 N-Linked glycan (1 site). DR GlyCosmos; Q99L43; 1 site, 1 glycan. DR GlyGen; Q99L43; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site). DR iPTMnet; Q99L43; -. DR PhosphoSitePlus; Q99L43; -. DR SwissPalm; Q99L43; -. DR EPD; Q99L43; -. DR jPOST; Q99L43; -. DR MaxQB; Q99L43; -. DR PaxDb; 10090-ENSMUSP00000099470; -. DR PeptideAtlas; Q99L43; -. DR ProteomicsDB; 281301; -. DR Pumba; Q99L43; -. DR Antibodypedia; 8142; 163 antibodies from 23 providers. DR DNASU; 110911; -. DR Ensembl; ENSMUST00000103181.11; ENSMUSP00000099470.5; ENSMUSG00000058793.15. DR GeneID; 110911; -. DR KEGG; mmu:110911; -. DR UCSC; uc008mmo.2; mouse. DR AGR; MGI:1332236; -. DR CTD; 8760; -. DR MGI; MGI:1332236; Cds2. DR VEuPathDB; HostDB:ENSMUSG00000058793; -. DR eggNOG; KOG1440; Eukaryota. DR GeneTree; ENSGT00940000158877; -. DR InParanoid; Q99L43; -. DR OMA; MPIQWHA; -. DR OrthoDB; 5481516at2759; -. DR PhylomeDB; Q99L43; -. DR TreeFam; TF313464; -. DR BRENDA; 2.7.7.41; 3474. DR Reactome; R-MMU-1483148; Synthesis of PG. DR UniPathway; UPA00557; UER00614. DR BioGRID-ORCS; 110911; 27 hits in 82 CRISPR screens. DR ChiTaRS; Cds2; mouse. DR PRO; PR:Q99L43; -. DR Proteomes; UP000000589; Chromosome 2. DR RNAct; Q99L43; Protein. DR Bgee; ENSMUSG00000058793; Expressed in motor neuron and 259 other cell types or tissues. DR ExpressionAtlas; Q99L43; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; ISS:UniProtKB. DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; ISS:UniProtKB. DR GO; GO:0070085; P:glycosylation; NAS:BHF-UCL. DR GO; GO:0140042; P:lipid droplet formation; IMP:UniProtKB. DR GO; GO:0007602; P:phototransduction; TAS:BHF-UCL. DR InterPro; IPR000374; PC_trans. DR InterPro; IPR016720; PC_Trfase_euk. DR PANTHER; PTHR13773; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 1. DR PANTHER; PTHR13773:SF4; PHOSPHATIDATE CYTIDYLYLTRANSFERASE 2; 1. DR Pfam; PF01148; CTP_transf_1; 1. DR PIRSF; PIRSF018269; PC_trans_euk; 1. DR PROSITE; PS01315; CDS; 1. DR Genevisible; Q99L43; MM. PE 1: Evidence at protein level; KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane; KW Nucleotidyltransferase; Phospholipid biosynthesis; Phospholipid metabolism; KW Phosphoprotein; Reference proteome; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1..444 FT /note="Phosphatidate cytidylyltransferase 2" FT /id="PRO_0000090717" FT TRANSMEM 78..98 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 129..149 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 165..185 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 212..232 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 261..281 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 339..359 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 1..48 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..34 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 20 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O95674" FT MOD_RES 30 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:O95674" FT MOD_RES 32 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17208939, FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:18630941, FT ECO:0007744|PubMed:21183079" FT MOD_RES 34 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O95674" FT MOD_RES 36 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 50 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT CONFLICT 43 FT /note="L -> P (in Ref. 3; AAH69879)" FT /evidence="ECO:0000305" SQ SEQUENCE 444 AA; 51314 MW; 6A3568A7E90A6C53 CRC64; MTELRQRVVR EDAPPEDKES ESEAKLDGET ASDSESRAET APLPTSVDDT PEVLNRALSN LSSRWKNWWV RGILTLAMIA FFFIIIYLGP MVLMMIVMCV QIKCFHEIIT IGYNVYHSYD LPWFRTLSWY FLLCVNYFFY GETVTDYFFT LVQREEPLRI LSKYHRFISF ALYLTGFCMF VLSLVKKHYR LQFYMFGWTH VTLLIVVTQS HLVIHNLFEG MIWFIVPISC VICNDIMAYM FGFFFGRTPL IKLSPKKTWE GFIGGFFATV VFGLLLSYVM SGYRCFVCPV EYNNDTNSFT VDCEPSDLFR LQEYNIPGVI QSAIGWKTVR MYPFQIHSIA LSTFASLIGP FGGFFASGFK RAFKIKDFAN TIPGHGGIMD RFDCQYLMAT FVNVYIASFI RGPNPSKLIQ QFLTLRPDQQ LHIFNTLKSH LTDKGILTSA LEDE //