CERS6_MOUSE
ID CERS6_MOUSE Reviewed; 384 AA.
AC Q8C172; Q3U817; Q8BV12;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Ceramide synthase 6 {ECO:0000305};
DE Short=CerS6 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:15823095, ECO:0000269|PubMed:18541923, ECO:0000269|PubMed:31150623};
DE AltName: Full=LAG1 longevity assurance homolog 6 {ECO:0000303|PubMed:15823095};
DE AltName: Full=Sphingoid base N-palmitoyltransferase CERS6 {ECO:0000305};
DE EC=2.3.1.291 {ECO:0000269|PubMed:15823095, ECO:0000269|PubMed:18541923, ECO:0000269|PubMed:31150623};
GN Name=Cers6 {ECO:0000312|MGI:MGI:2442564};
GN Synonyms=Lass6 {ECO:0000303|PubMed:15823095};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Head, and Skin;
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].
RC STRAIN=FVB/N; TISSUE=Colon;
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 FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT ASN-18, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND PATHWAY.
RX PubMed=15823095; DOI=10.1042/bj20050291;
RA Mizutani Y., Kihara A., Igarashi Y.;
RT "Mammalian Lass6 and its related family members regulate synthesis of
RT specific ceramides.";
RL Biochem. J. 390:263-271(2005).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=18541923; DOI=10.1194/jlr.m800158-jlr200;
RA Mizutani Y., Kihara A., Chiba H., Tojo H., Igarashi Y.;
RT "2-Hydroxy-ceramide synthesis by ceramide synthase family: enzymatic basis
RT for the preference of FA chain length.";
RL J. Lipid Res. 49:2356-2364(2008).
RN [5]
RP FUNCTION.
RX PubMed=22544924; DOI=10.4049/jimmunol.1103109;
RA Schiffmann S., Ferreiros N., Birod K., Eberle M., Schreiber Y.,
RA Pfeilschifter W., Ziemann U., Pierre S., Scholich K., Groesch S.,
RA Geisslinger G.;
RT "Ceramide synthase 6 plays a critical role in the development of
RT experimental autoimmune encephalomyelitis.";
RL J. Immunol. 188:5723-5733(2012).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, GLYCOSYLATION, AND DISRUPTION PHENOTYPE.
RX PubMed=23760501; DOI=10.1074/jbc.m113.479907;
RA Ebel P., Vom Dorp K., Petrasch-Parwez E., Zlomuzica A., Kinugawa K.,
RA Mariani J., Minich D., Ginkel C., Welcker J., Degen J., Eckhardt M.,
RA Dere E., Doermann P., Willecke K.;
RT "Inactivation of ceramide synthase 6 in mice results in an altered
RT sphingolipid metabolism and behavioral abnormalities.";
RL J. Biol. Chem. 288:21433-21447(2013).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=25295788; DOI=10.1016/j.cmet.2014.08.002;
RA Turpin S.M., Nicholls H.T., Willmes D.M., Mourier A., Brodesser S.,
RA Wunderlich C.M., Mauer J., Xu E., Hammerschmidt P., Broenneke H.S.,
RA Trifunovic A., LoSasso G., Wunderlich F.T., Kornfeld J.W., Blueher M.,
RA Kroenke M., Bruening J.C.;
RT "Obesity-induced CerS6-dependent C16:0 ceramide production promotes weight
RT gain and glucose intolerance.";
RL Cell Metab. 20:678-686(2014).
RN [8]
RP ACETYLATION, AND DEACETYLATION BY SIRT3.
RX PubMed=26620563; DOI=10.1074/jbc.m115.668228;
RA Novgorodov S.A., Riley C.L., Keffler J.A., Yu J., Kindy M.S., Macklin W.B.,
RA Lombard D.B., Gudz T.I.;
RT "SIRT3 deacetylates ceramide synthases: Implications for mitochondrial
RT dysfunction and brain injury.";
RL J. Biol. Chem. 291:1957-1973(2016).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=31150623; DOI=10.1016/j.cell.2019.05.008;
RA Hammerschmidt P., Ostkotte D., Nolte H., Gerl M.J., Jais A., Brunner H.L.,
RA Sprenger H.G., Awazawa M., Nicholls H.T., Turpin-Nolan S.M., Langer T.,
RA Krueger M., Bruegger B., Bruening J.C.;
RT "CerS6-derived sphingolipids interact with Mff and promote mitochondrial
RT fragmentation in obesity.";
RL Cell 177:1536-1552(2019).
RN [10]
RP FUNCTION.
RX PubMed=30655217; DOI=10.1016/j.molmet.2018.12.008;
RA Raichur S., Brunner B., Bielohuby M., Hansen G., Pfenninger A., Wang B.,
RA Bruning J.C., Larsen P.J., Tennagels N.;
RT "The role of C16:0 ceramide in the development of obesity and type 2
RT diabetes: CerS6 inhibition as a novel therapeutic approach.";
RL Mol. Metab. 21:36-50(2019).
RN [11]
RP STRUCTURE BY NMR OF 76-127.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the homeobox domain of mouse LAG1 longevity
RT assurance homolog 6.";
RL Submitted (OCT-2005) to the PDB data bank.
CC -!- FUNCTION: Ceramide synthase that catalyzes the transfer of the acyl
CC chain from acyl-CoA to a sphingoid base, with high selectivity toward
CC palmitoyl-CoA (hexadecanoyl-CoA; C16:0-CoA) (PubMed:15823095,
CC PubMed:18541923, PubMed:23760501, PubMed:31150623). Can use other acyl
CC donors, but with less efficiency (PubMed:18541923). N-acylates
CC sphinganine and sphingosine bases to form dihydroceramides and
CC ceramides in de novo synthesis and salvage pathways, respectively.
CC Ceramides generated by CERS6 play a role in inflammatory response
CC (PubMed:22544924). Acts as a regulator of metabolism and hepatic lipid
CC accumulation (PubMed:25295788, PubMed:30655217, PubMed:31150623). Under
CC high fat diet, palmitoyl- (C16:0-) ceramides generated by CERS6
CC specifically bind the mitochondrial fission factor MFF, thereby
CC promoting mitochondrial fragmentation and contributing to the
CC development of obesity (PubMed:31150623). {ECO:0000269|PubMed:15823095,
CC ECO:0000269|PubMed:18541923, ECO:0000269|PubMed:22544924,
CC ECO:0000269|PubMed:23760501, ECO:0000269|PubMed:25295788,
CC ECO:0000269|PubMed:30655217, ECO:0000269|PubMed:31150623}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sphingoid base + hexadecanoyl-CoA = an N-hexadecanoyl-
CC sphingoid base + CoA + H(+); Xref=Rhea:RHEA:61472, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:84410,
CC ChEBI:CHEBI:144703; EC=2.3.1.291;
CC Evidence={ECO:0000269|PubMed:15823095, ECO:0000269|PubMed:18541923,
CC ECO:0000269|PubMed:31150623};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61473;
CC Evidence={ECO:0000269|PubMed:15823095, ECO:0000269|PubMed:18541923,
CC ECO:0000269|PubMed:31150623};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + sphinganine = CoA + H(+) + N-
CC hexadecanoylsphinganine; Xref=Rhea:RHEA:36539, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57817,
CC ChEBI:CHEBI:67042; Evidence={ECO:0000269|PubMed:15823095,
CC ECO:0000269|PubMed:18541923, ECO:0000269|PubMed:31150623};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36540;
CC Evidence={ECO:0000269|PubMed:15823095, ECO:0000269|PubMed:18541923,
CC ECO:0000269|PubMed:31150623};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + hexadecasphinganine = CoA + H(+) + N-
CC hexadecanoylhexadecasphinganine; Xref=Rhea:RHEA:43040,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:71009, ChEBI:CHEBI:82810;
CC Evidence={ECO:0000250|UniProtKB:Q6ZMG9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43041;
CC Evidence={ECO:0000250|UniProtKB:Q6ZMG9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + sphing-4-enine = CoA + H(+) + N-
CC hexadecanoylsphing-4-enine; Xref=Rhea:RHEA:36687, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57756,
CC ChEBI:CHEBI:72959; Evidence={ECO:0000250|UniProtKB:Q6ZMG9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36688;
CC Evidence={ECO:0000250|UniProtKB:Q6ZMG9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sphinganine + tetradecanoyl-CoA = CoA + H(+) + N-
CC (tetradecanoyl)-sphinganine; Xref=Rhea:RHEA:36571, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:57817,
CC ChEBI:CHEBI:67045; Evidence={ECO:0000269|PubMed:15823095,
CC ECO:0000269|PubMed:18541923};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36572;
CC Evidence={ECO:0000269|PubMed:15823095, ECO:0000269|PubMed:18541923};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=octadecanoyl-CoA + sphinganine = CoA + H(+) + N-
CC (octadecanoyl)-sphinganine; Xref=Rhea:RHEA:36547, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:57817,
CC ChEBI:CHEBI:67033; Evidence={ECO:0000269|PubMed:15823095,
CC ECO:0000269|PubMed:18541923};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36548;
CC Evidence={ECO:0000269|PubMed:15823095, ECO:0000269|PubMed:18541923};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000269|PubMed:15823095, ECO:0000269|PubMed:18541923,
CC ECO:0000269|PubMed:31150623}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15823095}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15823095}.
CC -!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in kidney
CC and brain (at protein level). {ECO:0000269|PubMed:15823095,
CC ECO:0000269|PubMed:23760501}.
CC -!- INDUCTION: Up-regulated in liver in response to high-fat diet.
CC {ECO:0000269|PubMed:25295788}.
CC -!- PTM: N-glycosylated (PubMed:15823095, PubMed:23760501). Glycosylation
CC on Asn-18 is not necessary for function (PubMed:15823095).
CC {ECO:0000269|PubMed:15823095, ECO:0000269|PubMed:23760501}.
CC -!- PTM: Acetylated (PubMed:26620563). Deacetylation by SIRT3 increases
CC enzyme activity and promotes mitochondrial ceramide accumulation
CC (PubMed:26620563). {ECO:0000269|PubMed:26620563}.
CC -!- PTM: Phosphorylated at the C-terminus by CK2.
CC {ECO:0000250|UniProtKB:Q6ZMG9}.
CC -!- DISRUPTION PHENOTYPE: Mice show behavioral abnormalities including a
CC clasping abnormality of their hind limbs and a habituation deficit
CC (PubMed:23760501). Knockout mice are protected against high fat diet-
CC induced obesity and glucose intolerance (PubMed:25295788,
CC PubMed:31150623). Mice show decreased palmitoyl (C16:0) ceramide pools
CC and increased energy expenditure (PubMed:25295788, PubMed:31150623).
CC Conditional deletion in brown adipose tissue or liver also protects
CC mice against high fat diet-induced obesity, while it is not the case
CC with specific deletion in myeloid cells (PubMed:25295788).
CC {ECO:0000269|PubMed:23760501, ECO:0000269|PubMed:25295788,
CC ECO:0000269|PubMed:31150623}.
CC -!- CAUTION: Some prediction bioinformatics tools predict the presence of a
CC homeobox domain (By similarity). However, the domain is degenerate and
CC residues that are important for DNA-binding are absent (By similarity).
CC Moreover, the protein localizes in the endoplasmic reticulum and not in
CC the nucleus, strongly suggesting that it does not constitute a
CC canonical homeobox domain (PubMed:15823095). {ECO:0000255,
CC ECO:0000269|PubMed:15823095}.
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DR EMBL; AK028849; BAC26153.1; -; mRNA.
DR EMBL; AK081354; BAC38204.1; ALT_SEQ; mRNA.
DR EMBL; AK151848; BAE30739.1; -; mRNA.
DR EMBL; AK152417; BAE31202.1; -; mRNA.
DR EMBL; BC057629; AAH57629.1; -; mRNA.
DR CCDS; CCDS16086.1; -.
DR RefSeq; NP_766444.1; NM_172856.4.
DR PDB; 1X2M; NMR; -; A=76-126.
DR PDBsum; 1X2M; -.
DR AlphaFoldDB; Q8C172; -.
DR SMR; Q8C172; -.
DR STRING; 10090.ENSMUSP00000028426; -.
DR SwissLipids; SLP:000000119; -.
DR GlyConnect; 2204; 5 N-Linked glycans (1 site).
DR GlyGen; Q8C172; 1 site, 5 N-linked glycans (1 site).
DR iPTMnet; Q8C172; -.
DR PhosphoSitePlus; Q8C172; -.
DR SwissPalm; Q8C172; -.
DR EPD; Q8C172; -.
DR jPOST; Q8C172; -.
DR MaxQB; Q8C172; -.
DR PaxDb; Q8C172; -.
DR PRIDE; Q8C172; -.
DR ProteomicsDB; 281384; -.
DR Antibodypedia; 33795; 235 antibodies from 26 providers.
DR DNASU; 241447; -.
DR Ensembl; ENSMUST00000028426; ENSMUSP00000028426; ENSMUSG00000027035.
DR GeneID; 241447; -.
DR KEGG; mmu:241447; -.
DR UCSC; uc008jxs.1; mouse.
DR CTD; 253782; -.
DR MGI; MGI:2442564; Cers6.
DR VEuPathDB; HostDB:ENSMUSG00000027035; -.
DR eggNOG; KOG1607; Eukaryota.
DR GeneTree; ENSGT01030000234515; -.
DR InParanoid; Q8C172; -.
DR OMA; YLIGAPY; -.
DR PhylomeDB; Q8C172; -.
DR TreeFam; TF314319; -.
DR BRENDA; 2.3.1.24; 3474.
DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00222; -.
DR BioGRID-ORCS; 241447; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Cers6; mouse.
DR EvolutionaryTrace; Q8C172; -.
DR PRO; PR:Q8C172; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8C172; protein.
DR Bgee; ENSMUSG00000027035; Expressed in animal zygote and 220 other tissues.
DR ExpressionAtlas; Q8C172; baseline and differential.
DR Genevisible; Q8C172; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016410; F:N-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0050291; F:sphingosine N-acyltransferase activity; IDA:MGI.
DR GO; GO:0046513; P:ceramide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IDA:MGI.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR016439; Lag1/Lac1-like.
DR InterPro; IPR006634; TLC-dom.
DR PANTHER; PTHR12560; PTHR12560; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF03798; TRAM_LAG1_CLN8; 1.
DR PIRSF; PIRSF005225; LAG1_LAC1; 1.
DR SMART; SM00724; TLC; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS50922; TLC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Endoplasmic reticulum; Glycoprotein;
KW Inflammatory response; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..384
FT /note="Ceramide synthase 6"
FT /id="PRO_0000185517"
FT TOPO_DOM 1..34
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:15823095"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q6ZMG9"
FT DOMAIN 130..331
FT /note="TLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
FT REGION 66..127
FT /note="Homeobox-like"
FT /evidence="ECO:0000305"
FT REGION 335..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 285
FT /note="Not glycosylated"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15823095"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:1X2M"
FT HELIX 96..106
FT /evidence="ECO:0007829|PDB:1X2M"
FT HELIX 110..123
FT /evidence="ECO:0007829|PDB:1X2M"
SQ SEQUENCE 384 AA; 44813 MW; 9D43AF6CA06A335A CRC64;
MAGILAWFWN ERFWLPHNVT WADLKNTEEA TFPQAEDLYL AFPLAFCIFM VRLIFERFIA
KPCAIALNIQ ANGPQTAQPN AILEKVFTAI TKHPDEKRLE GLSKQLDWDV RSIQRWFRQR
RNQEKPSTLT RFCESMWRFS FYLYVFSYGV RFLKQTPWLW NTRHCWYNYP YQPLTADLHY
YYILELSFYW SLMVSQFTDI KRKDFGIMFL HHLATIFLIT FSYVNNMARV GTLVLCLHDS
ADALLEAAKM ANYAKFQKMC DLLFVMFAVV FITTRLGIFP LWVLNTTLFE SWEIVGPYPS
WWVFNLLLLL LQGLNCFWSY LIVKIACKTV SKGKVSKDDR SDIESSSDDE DSEPPGKKPH
SSTTTNGTSG TNGYLLTGPC SVDD
