CEGT_MOUSE
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 03-AUG-2022, entry version 146.
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; O88693; -.
DR PeptideAtlas; O88693; -.
DR PRIDE; O88693; -.
DR ProteomicsDB; 281529; -.
DR Antibodypedia; 15178; 191 antibodies from 30 providers.
DR DNASU; 22234; -.
DR Ensembl; ENSMUST00000030074; ENSMUSP00000030074; ENSMUSG00000028381.
DR GeneID; 22234; -.
DR KEGG; mmu:22234; -.
DR UCSC; uc008szr.1; mouse.
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; 793389at2759; -.
DR PhylomeDB; O88693; -.
DR TreeFam; TF314564; -.
DR BRENDA; 2.4.1.80; 3474.
DR Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
DR UniPathway; UPA00222; -.
DR BioGRID-ORCS; 22234; 2 hits in 76 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 261 other tissues.
DR Genevisible; O88693; MM.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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 Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR025993; Ceramide_glucosylTrfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR12726; PTHR12726; 1.
DR Pfam; PF13506; Glyco_transf_21; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
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
