ID CEGT_MOUSE Reviewed; 394 AA. AC O88693; A2AN90; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 24-JAN-2024, entry version 153. DE RecName: Full=Ceramide glucosyltransferase {ECO:0000305}; DE EC=2.4.1.80 {ECO:0000269|PubMed:10430909}; DE AltName: Full=GLCT-1; DE AltName: Full=Glucosylceramide synthase; DE Short=GCS {ECO:0000303|PubMed:33361282}; DE AltName: Full=Glycosylceramide synthase; DE AltName: Full=UDP-glucose ceramide glucosyltransferase; DE AltName: Full=UDP-glucose:N-acylsphingosine D-glucosyltransferase; GN Name=Ugcg {ECO:0000312|MGI:MGI:1332243}; 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 [GENOMIC DNA]. RC STRAIN=129/SvJ; RX PubMed=9918791; DOI=10.1006/bbrc.1998.9855; RA Ichikawa S., Ozawa K., Hirabayashi Y.; RT "Molecular cloning and characterization of the mouse ceramide RT glucosyltransferase gene."; RL Biochem. Biophys. Res. Commun. 253:707-711(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain; RX PubMed=9623774; DOI=10.1080/15216549800202282; RA Ichikawa S., Ozawa K., Hirabayashi Y.; RT "Molecular cloning and expression of mouse ceramide glucosyltransferase."; RL Biochem. Mol. Biol. Int. 44:1193-1202(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). 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] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Limb {ECO:0000312|EMBL:AAH50828.1}; 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 FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND DISRUPTION RP PHENOTYPE. RX PubMed=10430909; DOI=10.1073/pnas.96.16.9142; RA Yamashita T., Wada R., Sasaki T., Deng C., Bierfreund U., Sandhoff K., RA Proia R.L.; RT "A vital role for glycosphingolipid synthesis during development and RT differentiation."; RL Proc. Natl. Acad. Sci. U.S.A. 96:9142-9147(1999). RN [7] RP DEVELOPMENTAL STAGE. RX PubMed=12417405; DOI=10.1016/s0304-4165(02)00389-6; RA Yamashita T., Wada R., Proia R.L.; RT "Early developmental expression of the gene encoding glucosylceramide RT synthase, the enzyme controlling the first committed step of RT glycosphingolipid synthesis."; RL Biochim. Biophys. Acta 1573:236-240(2002). RN [8] RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE. RX PubMed=16109770; DOI=10.1073/pnas.0500893102; RA Jennemann R., Sandhoff R., Wang S., Kiss E., Gretz N., Zuliani C., RA Martin-Villalba A., Jaeger R., Schorle H., Kenzelmann M., Bonrouhi M., RA Wiegandt H., Groene H.J.; RT "Cell-specific deletion of glucosylceramide synthase in brain leads to RT severe neural defects after birth."; RL Proc. Natl. Acad. Sci. U.S.A. 102:12459-12464(2005). RN [9] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=17145749; DOI=10.1074/jbc.m610304200; RA Jennemann R., Sandhoff R., Langbein L., Kaden S., Rothermel U., Gallala H., RA Sandhoff K., Wiegandt H., Groene H.J.; RT "Integrity and barrier function of the epidermis critically depend on RT glucosylceramide synthesis."; RL J. Biol. Chem. 282:3083-3094(2007). RN [10] RP DISRUPTION PHENOTYPE. RX PubMed=20544855; DOI=10.1002/glia.20999; RA Watanabe S., Endo S., Oshima E., Hoshi T., Higashi H., Yamada K., RA Tohyama K., Yamashita T., Hirabayashi Y.; RT "Glycosphingolipid synthesis in cerebellar Purkinje neurons: roles in RT myelin formation and axonal homeostasis."; RL Glia 58:1197-1207(2010). RN [11] RP DISRUPTION PHENOTYPE. RX PubMed=20432257; DOI=10.1002/hep.23545; RA Jennemann R., Rothermel U., Wang S., Sandhoff R., Kaden S., Out R., RA van Berkel T.J., Aerts J.M., Ghauharali K., Sticht C., Groene H.J.; RT "Hepatic glycosphingolipid deficiency and liver function in mice."; RL Hepatology 51:1799-1809(2010). RN [12] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=22851168; DOI=10.1074/jbc.m112.371005; RA Jennemann R., Kaden S., Sandhoff R., Nordstroem V., Wang S., Volz M., RA Robine S., Amen N., Rothermel U., Wiegandt H., Groene H.J.; RT "Glycosphingolipids are essential for intestinal endocytic function."; RL J. Biol. Chem. 287:32598-32616(2012). RN [13] RP FUNCTION. RX PubMed=23748427; DOI=10.1093/hmg/ddt264; RA Amen N., Mathow D., Rabionet M., Sandhoff R., Langbein L., Gretz N., RA Jaeckel C., Groene H.J., Jennemann R.; RT "Differentiation of epidermal keratinocytes is dependent on RT glucosylceramide:ceramide processing."; RL Hum. Mol. Genet. 22:4164-4179(2013). RN [14] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=23554574; DOI=10.1371/journal.pbio.1001506; RA Nordstroem V., Willershaeuser M., Herzer S., Rozman J., RA von Bohlen Und Halbach O., Meldner S., Rothermel U., Kaden S., Roth F.C., RA Waldeck C., Gretz N., de Angelis M.H., Draguhn A., Klingenspor M., RA Groene H.J., Jennemann R.; RT "Neuronal expression of glucosylceramide synthase in central nervous system RT regulates body weight and energy homeostasis."; RL PLoS Biol. 11:E1001506-E1001506(2013). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-117, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria RT identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). RN [16] RP FUNCTION, AND PATHWAY. RX PubMed=28373486; DOI=10.1194/jlr.d076190; RA von Gerichten J., Schlosser K., Lamprecht D., Morace I., Eckhardt M., RA Wachten D., Jennemann R., Groene H.J., Mack M., Sandhoff R.; RT "Diastereomer-specific quantification of bioactive hexosylceramides from RT bacteria and mammals."; RL J. Lipid Res. 58:1247-1258(2017). RN [17] RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=33361282; DOI=10.1194/jlr.ra120001043; RA Boer D.E., Mirzaian M., Ferraz M.J., Zwiers K.C., Baks M.V., Hazeu M.D., RA Ottenhoff R., Marques A.R.A., Meijer R., Roos J.C.P., Cox T.M., Boot R.G., RA Pannu N., Overkleeft H.S., Artola M., Aerts J.M.; RT "Human glucocerebrosidase mediates formation of xylosyl-cholesterol by RT beta-xylosidase and transxylosidase reactions."; RL J. Lipid Res. 62:100018-100018(2021). CC -!- FUNCTION: Participates in the initial step of the glucosylceramide- CC based glycosphingolipid/GSL synthetic pathway at the cytosolic surface CC of the Golgi. Catalyzes the transfer of glucose from UDP-glucose to CC ceramide to produce glucosylceramide/GlcCer (such as beta-D-glucosyl- CC (1<->1')-N-acylsphing-4-enine) (PubMed:10430909, PubMed:16109770, CC PubMed:28373486). Glucosylceramide is the core component of CC glycosphingolipids/GSLs, amphipathic molecules consisting of a ceramide CC lipid moiety embedded in the outer leaflet of the membrane, linked to CC one of hundreds of different externally oriented oligosaccharide CC structures (PubMed:10430909). Glycosphingolipids are essential CC components of membrane microdomains that mediate membrane trafficking CC and signal transduction (PubMed:10430909). They are implicated in many CC fundamental cellular processes, including growth, differentiation, CC migration, morphogenesis, cell-to-cell and cell-to-matrix interactions CC (PubMed:10430909). They are required for instance in the proper CC development and functioning of the nervous system (PubMed:16109770). As CC an example of their role in signal transduction, they regulate the CC leptin receptor/LEPR in the leptin-mediated signaling pathway CC (PubMed:23554574). They also play an important role in the CC establishment of the skin barrier regulating keratinocyte CC differentiation and the proper assembly of the cornified envelope CC (PubMed:17145749, PubMed:23748427). The biosynthesis of GSLs is also CC required for the proper intestinal endocytic uptake of nutritional CC lipids (PubMed:22851168). Catalyzes the synthesis of CC xylosylceramide/XylCer (such as beta-D-xylosyl-(1<->1')-N-acylsphing-4- CC enine) using UDP-Xyl as xylose donor (PubMed:33361282). CC {ECO:0000269|PubMed:10430909, ECO:0000269|PubMed:16109770, CC ECO:0000269|PubMed:17145749, ECO:0000269|PubMed:22851168, CC ECO:0000269|PubMed:23554574, ECO:0000269|PubMed:23748427, CC ECO:0000269|PubMed:28373486, ECO:0000269|PubMed:33361282, CC ECO:0000303|PubMed:10430909}. CC -!- CATALYTIC ACTIVITY: CC Reaction=an N-acylsphing-4-enine + UDP-alpha-D-glucose = a beta-D- CC glucosyl-(1<->1')-N-acylsphing-4-enine + H(+) + UDP; CC Xref=Rhea:RHEA:12088, ChEBI:CHEBI:15378, ChEBI:CHEBI:22801, CC ChEBI:CHEBI:52639, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.80; CC Evidence={ECO:0000269|PubMed:10430909}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12089; CC Evidence={ECO:0000269|PubMed:10430909}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an N-acylsphing-4-enine + UDP-alpha-D-xylose = a beta-D- CC xylosyl-(1<->1')-N-acylsphing-4-enine + H(+) + UDP; CC Xref=Rhea:RHEA:70243, ChEBI:CHEBI:15378, ChEBI:CHEBI:52639, CC ChEBI:CHEBI:57632, ChEBI:CHEBI:58223, ChEBI:CHEBI:189068; CC Evidence={ECO:0000269|PubMed:33361282}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70244; CC Evidence={ECO:0000269|PubMed:33361282}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N-(9Z-octadecenoyl)-sphing-4-enine + UDP-alpha-D-xylose = CC beta-D-xylosyl-(1<->1')-N-(9Z-octadecenoyl)-sphing-4-enine + H(+) + CC UDP; Xref=Rhea:RHEA:70247, ChEBI:CHEBI:15378, ChEBI:CHEBI:57632, CC ChEBI:CHEBI:58223, ChEBI:CHEBI:77996, ChEBI:CHEBI:189081; CC Evidence={ECO:0000269|PubMed:33361282}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70248; CC Evidence={ECO:0000269|PubMed:33361282}; CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism. CC {ECO:0000269|PubMed:10430909, ECO:0000269|PubMed:16109770, CC ECO:0000269|PubMed:28373486, ECO:0000269|PubMed:33361282}. CC -!- SUBUNIT: Interacts with RTN1; regulates the ceramide CC glucosyltransferase activity of UGCG. {ECO:0000250|UniProtKB:Q16739}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000305|PubMed:10430909}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:Q9R0E0}. CC -!- DEVELOPMENTAL STAGE: Expressed early in preimplantation development, CC being already detected in eight-cell-stage embryos. CC {ECO:0000269|PubMed:12417405}. CC -!- DOMAIN: The D1, D2, D3, (Q/R)XXRW motif is a critical part of the GCS CC active site, involved in catalysis and UDP-sugar binding. CC {ECO:0000250|UniProtKB:Q9R0E0}. CC -!- DISRUPTION PHENOTYPE: Embryonic lethal (PubMed:10430909). Homozygous CC knockout embryos initiate gastrulation with clear differentiation into CC embryonic germ layers, mesoderm, endoderm and ectoderm as well as the CC regional expression of critical genes (PubMed:10430909). However, a CC major apoptotic process leads to their resorption that starts at 7.5 CC dpc and is completed at 9.5 dpc (PubMed:10430909). Neural cell-specific CC conditional knockout does not affect early brain development but mice CC die between postnatal days 11 and 24 (PubMed:16109770). Dysfunction of CC cerebellum and peripheral nerves associated with some structural CC defects are observed (PubMed:16109770, PubMed:20544855). Peripheral CC nerves display increased surface area for both axon and myelin CC (PubMed:16109770). Purkinje cells undergo axonal degeneration CC associated with a disruption of myelin sheaths (PubMed:20544855). CC Forebrain neuron-specific conditional knockout leads to development of CC progressive obesity, hyperleptinemia, and glucose intolerance CC (PubMed:23554574). Epidermal-specific conditional knockout leads to a CC significant decrease of the total glucosylceramide content in the CC epidermis, a failure of the skin water barrier and a detachment of the CC stratum corneum (PubMed:17145749). Enterocyte-specific conditional CC knockout mice display deficient absorption of nutritional lipids CC (PubMed:22851168). Severe defects in intestinal epithelial CC differentiation also appear between postnatal days 5 and 7 but not CC before (PubMed:22851168). Hepatocyte-specific conditional knockout does CC not change basic liver functions with respect to sterol, glucose, and CC lipoprotein homeostasis (PubMed:20432257). CC {ECO:0000269|PubMed:10430909, ECO:0000269|PubMed:16109770, CC ECO:0000269|PubMed:17145749, ECO:0000269|PubMed:20432257, CC ECO:0000269|PubMed:20544855, ECO:0000269|PubMed:22851168, CC ECO:0000269|PubMed:23554574}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 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; AB012807; BAA33558.1; -; Genomic_DNA. DR EMBL; D89866; BAA28782.1; -; mRNA. DR EMBL; AL808112; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466565; EDL02214.1; -; Genomic_DNA. DR EMBL; BC050828; AAH50828.1; -; mRNA. DR CCDS; CCDS18219.1; -. DR RefSeq; NP_035803.1; NM_011673.3. DR AlphaFoldDB; O88693; -. DR SMR; O88693; -. DR BioGRID; 204432; 13. DR STRING; 10090.ENSMUSP00000030074; -. DR BindingDB; O88693; -. DR ChEMBL; CHEMBL6013; -. DR DrugCentral; O88693; -. DR CAZy; GT21; Glycosyltransferase Family 21. DR iPTMnet; O88693; -. DR PhosphoSitePlus; O88693; -. DR SwissPalm; O88693; -. DR EPD; O88693; -. DR MaxQB; O88693; -. DR PaxDb; 10090-ENSMUSP00000030074; -. DR PeptideAtlas; O88693; -. DR ProteomicsDB; 281529; -. DR Pumba; O88693; -. DR Antibodypedia; 15178; 252 antibodies from 30 providers. DR DNASU; 22234; -. DR Ensembl; ENSMUST00000030074.8; ENSMUSP00000030074.8; ENSMUSG00000028381.9. DR GeneID; 22234; -. DR KEGG; mmu:22234; -. DR UCSC; uc008szr.1; mouse. DR AGR; MGI:1332243; -. DR CTD; 7357; -. DR MGI; MGI:1332243; Ugcg. DR VEuPathDB; HostDB:ENSMUSG00000028381; -. DR eggNOG; KOG2547; Eukaryota. DR GeneTree; ENSGT00390000012898; -. DR HOGENOM; CLU_030898_0_0_1; -. DR InParanoid; O88693; -. DR OMA; HGSMPFH; -. DR OrthoDB; 2786173at2759; -. DR PhylomeDB; O88693; -. DR TreeFam; TF314564; -. DR BRENDA; 2.4.1.80; 3474. DR Reactome; R-MMU-9840309; Glycosphingolipid biosynthesis. DR UniPathway; UPA00222; -. DR BioGRID-ORCS; 22234; 2 hits in 81 CRISPR screens. DR ChiTaRS; Ugcg; mouse. DR PRO; PR:O88693; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; O88693; Protein. DR Bgee; ENSMUSG00000028381; Expressed in ectoplacental cone and 265 other cell types or tissues. DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; ISO:MGI. DR GO; GO:0008120; F:ceramide glucosyltransferase activity; IMP:UniProtKB. DR GO; GO:0102769; F:dihydroceramide glucosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0030154; P:cell differentiation; IMP:UniProtKB. DR GO; GO:1903575; P:cornified envelope assembly; IMP:UniProtKB. DR GO; GO:0061436; P:establishment of skin barrier; IMP:UniProtKB. DR GO; GO:0006679; P:glucosylceramide biosynthetic process; IMP:UniProtKB. DR GO; GO:0098856; P:intestinal lipid absorption; IMP:UniProtKB. DR GO; GO:0030216; P:keratinocyte differentiation; IMP:UniProtKB. DR GO; GO:0033210; P:leptin-mediated signaling pathway; IMP:UniProtKB. DR GO; GO:0048666; P:neuron development; IMP:UniProtKB. DR GO; GO:0006497; P:protein lipidation; IMP:UniProtKB. DR GO; GO:0009966; P:regulation of signal transduction; IMP:UniProtKB. DR CDD; cd02520; Glucosylceramide_synthase; 1. DR InterPro; IPR025993; Ceramide_glucosylTrfase. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR PANTHER; PTHR12726; CERAMIDE GLUCOSYLTRANSFERASE; 1. DR PANTHER; PTHR12726:SF0; CERAMIDE GLUCOSYLTRANSFERASE; 1. DR Pfam; PF13506; Glyco_transf_21; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. DR Genevisible; O88693; MM. PE 1: Evidence at protein level; KW Acetylation; Glycosyltransferase; Golgi apparatus; Lipid biosynthesis; KW Lipid metabolism; Membrane; Reference proteome; Sphingolipid metabolism; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..394 FT /note="Ceramide glucosyltransferase" FT /id="PRO_0000059177" FT TOPO_DOM 1..10 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 11..32 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 33..195 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 196..215 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 216..287 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 288..304 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 305..309 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 310..328 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 329..348 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 349..369 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 370..394 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT MOTIF 92 FT /note="D1" FT /evidence="ECO:0000305" FT MOTIF 144 FT /note="D2" FT /evidence="ECO:0000305" FT MOTIF 236 FT /note="D3" FT /evidence="ECO:0000305" FT MOTIF 272..276 FT /note="(Q/R)XXRW" FT /evidence="ECO:0000305" FT ACT_SITE 236 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:Q9R0E0" FT SITE 193 FT /note="May play an important role in binding to the FT inhibitors DEPC and PDMP" FT /evidence="ECO:0000250" FT MOD_RES 117 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" SQ SEQUENCE 394 AA; 44839 MW; 8B18D09437CACE0E CRC64; MALLDLAQEG MALFGFVLFV VLWLMHFMSI IYTRLHLNKK ATDKQPYSKL PGVSLLKPLK GVDPNLINNL ETFFELDYPK YEVLLCVQDH DDPAIDVCKK LLGKYPNVDA RLFIGGKKVG INPKINNLMP AYEVAKYDLI WICDSGIRVI PDTLTDMVNQ MTEKVGLVHG LPYVADRQGF AATLEQVYFG TSHPRSYISA NVTGFKCVTG MSCLMRKDVL DQAGGLIAFA QYIAEDYFMA KAIADRGWRF SMSTQVAMQN SGSYSISQFQ SRMIRWTKLR INMLPATIIC EPISECFVAS LIIGWAAHHV FRWDIMVFFM CHCLAWFIFD YIQLRGVQGG TLCFSKLDYA VAWFIRESMT IYIFLSALWD PTISWRTGRY RLRCGGTAEE ILDV //