SMS2_MOUSE
ID SMS2_MOUSE Reviewed; 365 AA.
AC Q9D4B1; Q149I0;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Phosphatidylcholine:ceramide cholinephosphotransferase 2;
DE EC=2.7.8.27 {ECO:0000269|PubMed:22580896};
DE AltName: Full=Sphingomyelin synthase 2;
GN Name=Sgms2;
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 {ECO:0000312|EMBL:BAB30364.2};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP IDENTIFICATION.
RX PubMed=14685263; DOI=10.1038/sj.emboj.7600034;
RA Huitema K., Van Den Dikkenberg J., Brouwers J.F.H.M., Holthuis J.C.;
RT "Identification of a family of animal sphingomyelin synthases.";
RL EMBO J. 23:33-44(2004).
RN [4]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=19590047; DOI=10.1161/circresaha.109.194613;
RA Liu J., Huan C., Chakraborty M., Zhang H., Lu D., Kuo M.S., Cao G.,
RA Jiang X.C.;
RT "Macrophage sphingomyelin synthase 2 deficiency decreases atherosclerosis
RT in mice.";
RL Circ. Res. 105:295-303(2009).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=21844222; DOI=10.1128/mcb.05893-11;
RA Li Z., Zhang H., Liu J., Liang C.P., Li Y., Li Y., Teitelman G., Beyer T.,
RA Bui H.H., Peake D.A., Zhang Y., Sanders P.E., Kuo M.S., Park T.S., Cao G.,
RA Jiang X.C.;
RT "Reducing plasma membrane sphingomyelin increases insulin sensitivity.";
RL Mol. Cell. Biol. 31:4205-4218(2011).
RN [6]
RP DISRUPTION PHENOTYPE, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22580896; DOI=10.1161/atvbaha.112.251538;
RA Li Z., Fan Y., Liu J., Li Y., Huan C., Bui H.H., Kuo M.S., Park T.S.,
RA Cao G., Jiang X.C.;
RT "Impact of sphingomyelin synthase 1 deficiency on sphingolipid metabolism
RT and atherosclerosis in mice.";
RL Arterioscler. Thromb. Vasc. Biol. 32:1577-1584(2012).
RN [7]
RP REVIEW.
RX PubMed=22849442; DOI=10.1186/1743-7075-9-71;
RA Hussain M.M., Jin W., Jiang X.C.;
RT "Mechanisms involved in cellular ceramide homeostasis.";
RL Nutr. Metab. 9:71-71(2012).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=30779713; DOI=10.1172/jci.insight.126180;
RA Pekkinen M., Terhal P.A., Botto L.D., Henning P., Maekitie R.E.,
RA Roschger P., Jain A., Kol M., Kjellberg M.A., Paschalis E.P.,
RA van Gassen K., Murray M., Bayrak-Toydemir P., Magnusson M.K., Jans J.,
RA Kausar M., Carey J.C., Somerharju P., Lerner U.H., Olkkonen V.M.,
RA Klaushofer K., Holthuis J.C., Maekitie O.;
RT "Osteoporosis and skeletal dysplasia caused by pathogenic variants in
RT SGMS2.";
RL JCI Insight 4:0-0(2019).
CC -!- FUNCTION: Sphingomyelin synthase that primarily contributes to
CC sphingomyelin synthesis and homeostasis at the plasma membrane
CC (PubMed:19590047, PubMed:21844222, PubMed:22580896). Catalyzes the
CC reversible transfer of phosphocholine moiety in sphingomyelin
CC biosynthesis: in the forward reaction transfers phosphocholine head
CC group of phosphatidylcholine (PC) on to ceramide (CER) to form ceramide
CC phosphocholine (sphingomyelin, SM) and diacylglycerol (DAG) as by-
CC product, and in the reverse reaction transfers phosphocholine from SM
CC to DAG to form PC and CER. The direction of the reaction appears to
CC depend on the levels of CER and DAG in the plasma membrane. Does not
CC use free phosphorylcholine or CDP-choline as donors (By similarity).
CC Can also transfer phosphoethanolamine head group of
CC phosphatidylethanolamine (PE) on to ceramide (CER) to form ceramide
CC phosphoethanolamine (CPE) (By similarity). Regulates receptor-mediated
CC signal transduction via mitogenic DAG and proapoptotic CER, as well as
CC via SM, a structural component of membrane rafts that serve as
CC platforms for signal transduction and protein sorting (PubMed:19590047,
CC PubMed:21844222). To a lesser extent, plays a role in secretory
CC transport via regulation of DAG pool at the Golgi apparatus and its
CC downstream effects on PRKD1. Required for normal bone matrix
CC mineralization (By similarity). {ECO:0000250|UniProtKB:Q8NHU3,
CC ECO:0000269|PubMed:19590047, ECO:0000269|PubMed:21844222,
CC ECO:0000269|PubMed:22580896}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + an N-acylsphing-4-
CC enine = a 1,2-diacyl-sn-glycerol + a sphingomyelin;
CC Xref=Rhea:RHEA:18765, ChEBI:CHEBI:17636, ChEBI:CHEBI:17815,
CC ChEBI:CHEBI:52639, ChEBI:CHEBI:57643; EC=2.7.8.27;
CC Evidence={ECO:0000269|PubMed:22580896};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18766;
CC Evidence={ECO:0000305|PubMed:22580896};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18767;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + an N-
CC acylsphing-4-enine = 1,2-dihexadecanoyl-sn-glycerol + a
CC sphingomyelin; Xref=Rhea:RHEA:43324, ChEBI:CHEBI:17636,
CC ChEBI:CHEBI:52639, ChEBI:CHEBI:72999, ChEBI:CHEBI:82929;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43325;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43326;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-2-acyl-sn-3-glycerol + a sphingomyelin = a
CC 1-(9Z-octadecenoyl)-2-acyl-sn-glycero-3-phosphocholine + an N-
CC acylsphing-4-enine; Xref=Rhea:RHEA:43320, ChEBI:CHEBI:17636,
CC ChEBI:CHEBI:52639, ChEBI:CHEBI:78421, ChEBI:CHEBI:82983;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43321;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43322;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + N-
CC hexadecanoylsphinganine = a 1,2-diacyl-sn-glycerol + N-hexadecanoyl-
CC sphinganine-1-phosphocholine; Xref=Rhea:RHEA:41796,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:57643, ChEBI:CHEBI:67042,
CC ChEBI:CHEBI:78647; Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41797;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:41798;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + N-hexadecanoyl-
CC (4R)-hydroxysphinganine = a 1,2-diacyl-sn-glycerol + N-hexadecanoyl-
CC (4R)-hydroxysphinganine-phosphocholine; Xref=Rhea:RHEA:42140,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:57643, ChEBI:CHEBI:65107,
CC ChEBI:CHEBI:78650; Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42141;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42142;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + N-
CC hexadecanoylsphinganine = a 1,2-diacyl-sn-glycerol + N-hexadecanoyl-
CC sphinganine-1-phosphoethanolamine; Xref=Rhea:RHEA:42128,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:64612, ChEBI:CHEBI:67042,
CC ChEBI:CHEBI:78654; Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42129;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + N-
CC hexadecanoyl-(4R)-hydroxysphinganine = a 1,2-diacyl-sn-glycerol + N-
CC hexadecanoyl-(4R)-hydroxysphinganine-1-phosphoethanolamine;
CC Xref=Rhea:RHEA:42144, ChEBI:CHEBI:17815, ChEBI:CHEBI:64612,
CC ChEBI:CHEBI:65107, ChEBI:CHEBI:78656;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42145;
CC Evidence={ECO:0000250|UniProtKB:Q8NHU3};
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000250|UniProtKB:Q8NHU3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8NHU3};
CC Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8NHU3}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Primarily localized at the plasma membrane with a
CC small fraction at the Golgi apparatus. {ECO:0000250|UniProtKB:Q8NHU3}.
CC -!- TISSUE SPECIFICITY: Highest expression is detected in cortical bone,
CC followed by vertebrae, kidney and liver. Expression levels are very low
CC in spleen, muscle, heart, brown fat and thymus (PubMed:30779713).
CC Expressed in macrophages. {ECO:0000269|PubMed:19590047,
CC ECO:0000269|PubMed:30779713}.
CC -!- PTM: Palmitoylated on Cys-331, Cys-332, Cys-343 and Cys-348; which
CC plays an important role in plasma membrane localization. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Null mice are viable but exhibit increased cell
CC membrane ceramide and decreased sphingomyelin levels. In both skeletal
CC muscle and adipose tissue, there is a significant increase in glucose
CC uptake. This leads to increased insulin sensitivity and ameliorated
CC high-fat diet-induced obesity. There is blunted NFKB1- and MAP kinase-
CC mediated responses to inflammatory stimuli and macrophages display
CC increased cholesterol efflux into blood circulation. Liver SMS activity
CC is markedly reduced (by about 80%) but only small change in macrophage
CC SMS2 activity (16%). No change in glycosphingolipid levels in plasma.
CC Atherosclerosis in SMS2(-/-)/LDLR(-/-) mice is significantly decreased.
CC {ECO:0000269|PubMed:19590047, ECO:0000269|PubMed:21844222,
CC ECO:0000269|PubMed:22580896}.
CC -!- SIMILARITY: Belongs to the sphingomyelin synthase family.
CC {ECO:0000305}.
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DR EMBL; AK016659; BAB30364.2; -; mRNA.
DR EMBL; BC117782; AAI17783.1; -; mRNA.
DR CCDS; CCDS17843.1; -.
DR RefSeq; NP_083219.2; NM_028943.5.
DR RefSeq; XP_006502256.1; XM_006502193.2.
DR RefSeq; XP_006502257.1; XM_006502194.3.
DR RefSeq; XP_006502259.1; XM_006502196.3.
DR RefSeq; XP_006502260.1; XM_006502197.3.
DR RefSeq; XP_006502262.1; XM_006502199.3.
DR RefSeq; XP_011238551.1; XM_011240249.2.
DR RefSeq; XP_011238552.1; XM_011240250.2.
DR AlphaFoldDB; Q9D4B1; -.
DR STRING; 10090.ENSMUSP00000087713; -.
DR BindingDB; Q9D4B1; -.
DR ChEMBL; CHEMBL4523444; -.
DR iPTMnet; Q9D4B1; -.
DR PhosphoSitePlus; Q9D4B1; -.
DR MaxQB; Q9D4B1; -.
DR PaxDb; Q9D4B1; -.
DR PRIDE; Q9D4B1; -.
DR ProteomicsDB; 261462; -.
DR Antibodypedia; 15282; 255 antibodies from 25 providers.
DR DNASU; 74442; -.
DR Ensembl; ENSMUST00000090246; ENSMUSP00000087713; ENSMUSG00000050931.
DR GeneID; 74442; -.
DR KEGG; mmu:74442; -.
DR UCSC; uc008rjq.2; mouse.
DR CTD; 166929; -.
DR MGI; MGI:1921692; Sgms2.
DR VEuPathDB; HostDB:ENSMUSG00000050931; -.
DR eggNOG; KOG3058; Eukaryota.
DR GeneTree; ENSGT00940000157370; -.
DR HOGENOM; CLU_027104_0_1_1; -.
DR InParanoid; Q9D4B1; -.
DR OMA; VNWAFTV; -.
DR OrthoDB; 599210at2759; -.
DR PhylomeDB; Q9D4B1; -.
DR TreeFam; TF314547; -.
DR BRENDA; 2.7.8.27; 3474.
DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR BioGRID-ORCS; 74442; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Sgms2; mouse.
DR PRO; PR:Q9D4B1; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9D4B1; protein.
DR Bgee; ENSMUSG00000050931; Expressed in granulocyte and 89 other tissues.
DR ExpressionAtlas; Q9D4B1; baseline and differential.
DR Genevisible; Q9D4B1; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030173; C:integral component of Golgi membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0047493; F:ceramide cholinephosphotransferase activity; ISS:UniProtKB.
DR GO; GO:0002950; F:ceramide phosphoethanolamine synthase activity; IMP:MGI.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0033188; F:sphingomyelin synthase activity; IDA:UniProtKB.
DR GO; GO:0046513; P:ceramide biosynthetic process; IMP:MGI.
DR GO; GO:1905373; P:ceramide phosphoethanolamine biosynthetic process; IMP:MGI.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0030500; P:regulation of bone mineralization; ISS:UniProtKB.
DR GO; GO:0006686; P:sphingomyelin biosynthetic process; IMP:UniProtKB.
DR InterPro; IPR045221; Sphingomyelin_synth-like.
DR InterPro; IPR025749; Sphingomyelin_synth-like_dom.
DR PANTHER; PTHR21290; PTHR21290; 1.
DR Pfam; PF14360; PAP2_C; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Golgi apparatus; Kinase; Lipid metabolism; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Sphingolipid metabolism;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..365
FT /note="Phosphatidylcholine:ceramide
FT cholinephosphotransferase 2"
FT /id="PRO_0000221073"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 9..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 229
FT /evidence="ECO:0000250"
FT ACT_SITE 272
FT /evidence="ECO:0000250"
FT ACT_SITE 276
FT /evidence="ECO:0000250"
FT LIPID 331
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 332
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 343
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 348
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 365 AA; 42248 MW; 7DDC667F74CA4824 CRC64;
MDIIETAKLE GHLESQTNDS TNTYTSPTEA VEEEGKNGKG KPKTLSNGLR KGAKKYPDYI
QISMPNDSKN KFPLEWWKTG IAFVYALFNL ILTTVMITVV HERVPPKELS PPLPDKFFDY
FDRVKWAFSV SEINGMVLVG LWITQWLFLR YKSIVGRRFF FIMGTLYLYR CITMYVTTLP
VPGMHFQCAP KLNGDSQAKI QRILRLISGG GLSITGSHIL CGDFLFSGHT VVLTLTYLFI
KEYSPRHFWW YHLVCWLLSA AGIICILVAH EHYTVDVIIA YYITTRLFWW YHSMANEKNL
KVSSQTNFLS RAWWFPIFYF FEKNVQGSIP CCFSWPLSWP PGCFKSSCRK YSRVQKIGED
NEKST
