DEGS1_HUMAN
ID DEGS1_HUMAN Reviewed; 323 AA.
AC O15121;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Sphingolipid delta(4)-desaturase DES1 {ECO:0000305};
DE EC=1.14.19.17 {ECO:0000269|PubMed:11937514, ECO:0000269|PubMed:30620338};
DE AltName: Full=Cell migration-inducing gene 15 protein;
DE AltName: Full=Degenerative spermatocyte homolog 1;
DE AltName: Full=Dihydroceramide desaturase-1;
DE AltName: Full=Membrane lipid desaturase;
DE AltName: Full=Retinol isomerase;
DE EC=5.2.1.- {ECO:0000269|PubMed:23143414};
GN Name=DEGS1 {ECO:0000312|HGNC:HGNC:13709}; Synonyms=DES1, MLD;
GN ORFNames=MIG15;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=9188692; DOI=10.1021/bi970091l;
RA Cadena D.L., Kurten R.C., Gill G.N.;
RT "The product of the MLD gene is a member of the membrane fatty acid
RT desaturase family: overexpression of MLD inhibits EGF receptor
RT biosynthesis.";
RL Biochemistry 36:6960-6967(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Lung;
RX PubMed=11937514; DOI=10.1074/jbc.m202947200;
RA Ternes P., Franke S., Zaehringer U., Sperling P., Heinz E.;
RT "Identification and characterization of a sphingolipid delta 4-desaturase
RT family.";
RL J. Biol. Chem. 277:25512-25518(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim J.W.;
RT "Identification of a human migration-inducing gene.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP SUBCELLULAR LOCATION, AND MYRISTOYLATION AT GLY-2.
RX PubMed=19647031; DOI=10.1016/j.biochi.2009.07.014;
RA Beauchamp E., Tekpli X., Marteil G., Lagadic-Gossmann D., Legrand P.,
RA Rioux V.;
RT "N-Myristoylation targets dihydroceramide Delta4-desaturase 1 to
RT mitochondria: partial involvement in the apoptotic effect of myristic
RT acid.";
RL Biochimie 91:1411-1419(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP CATALYTIC ACTIVITY.
RX PubMed=23143414; DOI=10.1038/nchembio.1114;
RA Kaylor J.J., Yuan Q., Cook J., Sarfare S., Makshanoff J., Miu A., Kim A.,
RA Kim P., Habib S., Roybal C.N., Xu T., Nusinowitz S., Travis G.H.;
RT "Identification of DES1 as a vitamin A isomerase in Mueller glial cells of
RT the retina.";
RL Nat. Chem. Biol. 9:30-36(2013).
RN [10]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INVOLVEMENT IN HLD18,
RP VARIANT HLD18 VAL-280, AND CHARACTERIZATION OF VARIANT HLD18 VAL-280.
RX PubMed=30620338; DOI=10.1172/jci124159;
RA Karsai G., Kraft F., Haag N., Korenke G.C., Haenisch B., Othman A.,
RA Suriyanarayanan S., Steiner R., Knopp C., Mull M., Bergmann M.,
RA Schroeder J.M., Weis J., Elbracht M., Begemann M., Hornemann T., Kurth I.;
RT "DEGS1-associated aberrant sphingolipid metabolism impairs nervous system
RT function in humans.";
RL J. Clin. Invest. 129:1229-1239(2019).
RN [12]
RP FUNCTION, INVOLVEMENT IN HLD18, VARIANTS HLD18 THR-37; 107-TRP--GLU-323
RP DEL; ASP-113; ARG-132; TRP-133; 173-ARG--GLU-323 DEL; ASP-189; SER-255;
RP 284-TYR--GLU-323 DEL; 293-TRP--GLU-323 DEL AND GLU-323 DEL, AND
RP CHARACTERIZATION OF VARIANTS HLD18 ASP-113 AND SER-255.
RX PubMed=30620337; DOI=10.1172/jci123959;
RA Pant D.C., Dorboz I., Schluter A., Fourcade S., Launay N., Joya J.,
RA Aguilera-Albesa S., Yoldi M.E., Casasnovas C., Willis M.J., Ruiz M.,
RA Ville D., Lesca G., Siquier-Pernet K., Desguerre I., Yan H., Wang J.,
RA Burmeister M., Brady L., Tarnopolsky M., Cornet C., Rubbini D.,
RA Terriente J., James K.N., Musaev D., Zaki M.S., Patterson M.C.,
RA Lanpher B.C., Klee E.W., Pinto e Vairo F., Wohler E., Sobreira N.L.M.,
RA Cohen J.S., Maroofian R., Galehdari H., Mazaheri N., Shariati G.,
RA Colleaux L., Rodriguez D., Gleeson J.G., Pujades C., Fatemi A.,
RA Boespflug-Tanguy O., Pujol A.;
RT "Loss of the sphingolipid desaturase DEGS1 causes hypomyelinating
RT leukodystrophy.";
RL J. Clin. Invest. 129:1240-1256(2019).
RN [13]
RP VARIANT HLD18 SER-255, AND INVOLVEMENT IN HLD18.
RX PubMed=31186544; DOI=10.1038/s41431-019-0444-z;
RA Dolgin V., Straussberg R., Xu R., Mileva I., Yogev Y., Khoury R., Konen O.,
RA Barhum Y., Zvulunov A., Mao C., Birk O.S.;
RT "DEGS1 variant causes neurological disorder.";
RL Eur. J. Hum. Genet. 27:1668-1676(2019).
CC -!- FUNCTION: Has sphingolipid-delta-4-desaturase activity. Converts D-
CC erythro-sphinganine to D-erythro-sphingosine (E-sphing-4-enine)
CC (PubMed:11937514, PubMed:30620337, PubMed:30620338). Catalyzes the
CC equilibrium isomerization of retinols (By similarity).
CC {ECO:0000250|UniProtKB:Q5F3C1, ECO:0000269|PubMed:11937514,
CC ECO:0000269|PubMed:30620337, ECO:0000269|PubMed:30620338}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2
CC = an N-acylsphing-4-enine + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:46544, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:31488,
CC ChEBI:CHEBI:52639; EC=1.14.19.17;
CC Evidence={ECO:0000269|PubMed:11937514, ECO:0000269|PubMed:30620338};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46545;
CC Evidence={ECO:0000305|PubMed:11937514};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol = 11-cis-retinol; Xref=Rhea:RHEA:19141,
CC ChEBI:CHEBI:16302, ChEBI:CHEBI:17336;
CC Evidence={ECO:0000269|PubMed:23143414};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19142;
CC Evidence={ECO:0000305|PubMed:23143414};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19143;
CC Evidence={ECO:0000250|UniProtKB:Q5F3C1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol = 9-cis-retinol; Xref=Rhea:RHEA:55348,
CC ChEBI:CHEBI:17336, ChEBI:CHEBI:78272;
CC Evidence={ECO:0000250|UniProtKB:Q5F3C1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55349;
CC Evidence={ECO:0000250|UniProtKB:Q5F3C1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol = 13-cis-retinol; Xref=Rhea:RHEA:55352,
CC ChEBI:CHEBI:17336, ChEBI:CHEBI:45479;
CC Evidence={ECO:0000250|UniProtKB:Q5F3C1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55353;
CC Evidence={ECO:0000250|UniProtKB:Q5F3C1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-cis-retinol = 13-cis-retinol; Xref=Rhea:RHEA:55356,
CC ChEBI:CHEBI:16302, ChEBI:CHEBI:45479;
CC Evidence={ECO:0000250|UniProtKB:Q5F3C1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55357;
CC Evidence={ECO:0000250|UniProtKB:Q5F3C1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-cis-retinol = 9-cis-retinol; Xref=Rhea:RHEA:55360,
CC ChEBI:CHEBI:16302, ChEBI:CHEBI:78272;
CC Evidence={ECO:0000250|UniProtKB:Q5F3C1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55361;
CC Evidence={ECO:0000250|UniProtKB:Q5F3C1};
CC -!- SUBUNIT: Interacts with RLBP1; the interaction increases synthesis of
CC chromophore-precursors by DEGS1. {ECO:0000250|UniProtKB:Q5F3C1}.
CC -!- INTERACTION:
CC O15121; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-1052713, EBI-12003442;
CC O15121; Q9NTN9-2: SEMA4G; NbExp=3; IntAct=EBI-1052713, EBI-12913124;
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:19647031, ECO:0000269|PubMed:30620338}. Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:19647031,
CC ECO:0000269|PubMed:30620338, ECO:0000269|PubMed:9188692}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:19647031,
CC ECO:0000269|PubMed:9188692}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9188692}.
CC -!- PTM: Myristoylation can target the enzyme to the mitochondria leading
CC to an increase in ceramide levels. {ECO:0000269|PubMed:19647031}.
CC -!- DISEASE: Leukodystrophy, hypomyelinating, 18 (HLD18) [MIM:618404]: An
CC autosomal recessive disorder characterized by hypomyelinating
CC leukodystrophy with progressive atrophy of the corpus callosum, thalami
CC and cerebellum, and peripheral neuropathy. Clinical features include
CC very poor psychomotor development, dystonia, severe spasticity,
CC seizures, and failure to thrive. {ECO:0000269|PubMed:30620337,
CC ECO:0000269|PubMed:30620338, ECO:0000269|PubMed:31186544}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. DEGS
CC subfamily. {ECO:0000305}.
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DR EMBL; AF002668; AAB62238.1; -; mRNA.
DR EMBL; AF466375; AAM12531.1; -; mRNA.
DR EMBL; AY423730; AAS00493.1; -; mRNA.
DR EMBL; CH471098; EAW69711.1; -; Genomic_DNA.
DR EMBL; BC000961; AAH00961.1; -; mRNA.
DR CCDS; CCDS1540.1; -.
DR RefSeq; NP_003667.1; NM_003676.3.
DR AlphaFoldDB; O15121; -.
DR BioGRID; 114130; 56.
DR IntAct; O15121; 19.
DR STRING; 9606.ENSP00000316476; -.
DR BindingDB; O15121; -.
DR ChEMBL; CHEMBL2021749; -.
DR GuidetoPHARMACOLOGY; 2484; -.
DR SwissLipids; SLP:000000166; -.
DR GlyGen; O15121; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O15121; -.
DR PhosphoSitePlus; O15121; -.
DR SwissPalm; O15121; -.
DR BioMuta; DEGS1; -.
DR EPD; O15121; -.
DR jPOST; O15121; -.
DR MassIVE; O15121; -.
DR MaxQB; O15121; -.
DR PaxDb; O15121; -.
DR PeptideAtlas; O15121; -.
DR PRIDE; O15121; -.
DR ProteomicsDB; 48459; -.
DR Antibodypedia; 20751; 170 antibodies from 25 providers.
DR DNASU; 8560; -.
DR Ensembl; ENST00000323699.9; ENSP00000316476.4; ENSG00000143753.13.
DR Ensembl; ENST00000391877.3; ENSP00000375749.3; ENSG00000143753.13.
DR GeneID; 8560; -.
DR KEGG; hsa:8560; -.
DR MANE-Select; ENST00000323699.9; ENSP00000316476.4; NM_003676.4; NP_003667.1.
DR UCSC; uc001hoj.4; human.
DR CTD; 8560; -.
DR DisGeNET; 8560; -.
DR GeneCards; DEGS1; -.
DR HGNC; HGNC:13709; DEGS1.
DR HPA; ENSG00000143753; Tissue enriched (skin).
DR MalaCards; DEGS1; -.
DR MIM; 615843; gene.
DR MIM; 618404; phenotype.
DR neXtProt; NX_O15121; -.
DR OpenTargets; ENSG00000143753; -.
DR PharmGKB; PA27250; -.
DR VEuPathDB; HostDB:ENSG00000143753; -.
DR eggNOG; KOG2987; Eukaryota.
DR GeneTree; ENSGT00390000013448; -.
DR InParanoid; O15121; -.
DR OMA; VYYVFGI; -.
DR OrthoDB; 1255438at2759; -.
DR PhylomeDB; O15121; -.
DR TreeFam; TF313582; -.
DR BioCyc; MetaCyc:ENSG00000143753-MON; -.
DR BRENDA; 1.14.19.17; 2681.
DR PathwayCommons; O15121; -.
DR Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; O15121; -.
DR BioGRID-ORCS; 8560; 16 hits in 1082 CRISPR screens.
DR ChiTaRS; DEGS1; human.
DR GenomeRNAi; 8560; -.
DR Pharos; O15121; Tchem.
DR PRO; PR:O15121; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O15121; protein.
DR Bgee; ENSG00000143753; Expressed in skin of hip and 202 other tissues.
DR ExpressionAtlas; O15121; baseline and differential.
DR Genevisible; O15121; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
DR GO; GO:0050251; F:retinol isomerase activity; IDA:UniProtKB.
DR GO; GO:0042284; F:sphingolipid delta-4 desaturase activity; IMP:UniProtKB.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0043217; P:myelin maintenance; IMP:UniProtKB.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; TAS:Reactome.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; TAS:ProtInc.
DR CDD; cd03508; Delta4-sphingolipid-FADS-like; 1.
DR InterPro; IPR031196; DES1.
DR InterPro; IPR011388; DES1/DES2.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR013866; Sphingolipid_d4-desaturase_N.
DR PANTHER; PTHR12879:SF2; PTHR12879:SF2; 1.
DR Pfam; PF00487; FA_desaturase; 1.
DR Pfam; PF08557; Lipid_DES; 1.
DR PIRSF; PIRSF017228; Sphnglp_dlt4_des; 1.
DR SMART; SM01269; Lipid_DES; 1.
PE 1: Evidence at protein level;
KW Disease variant; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Isomerase; Leukodystrophy; Lipid biosynthesis;
KW Lipid metabolism; Lipoprotein; Membrane; Mitochondrion; Myristate;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805"
FT CHAIN 2..323
FT /note="Sphingolipid delta(4)-desaturase DES1"
FT /id="PRO_0000312727"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 89..93
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 128..132
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 259..263
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:19647031,
FT ECO:0000269|PubMed:25255805"
FT VARIANT 37
FT /note="M -> T (in HLD18; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30620337"
FT /id="VAR_082594"
FT VARIANT 107..323
FT /note="Missing (in HLD18)"
FT /evidence="ECO:0000269|PubMed:30620337"
FT /id="VAR_082595"
FT VARIANT 113
FT /note="N -> D (in HLD18; decreased function in sphingolipid
FT biosynthetic process)"
FT /evidence="ECO:0000269|PubMed:30620337"
FT /id="VAR_082596"
FT VARIANT 132
FT /note="H -> R (in HLD18; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30620337"
FT /id="VAR_082597"
FT VARIANT 133
FT /note="R -> W (in HLD18)"
FT /evidence="ECO:0000269|PubMed:30620337"
FT /id="VAR_082598"
FT VARIANT 173..323
FT /note="Missing (in HLD18)"
FT /evidence="ECO:0000269|PubMed:30620337"
FT /id="VAR_082599"
FT VARIANT 189
FT /note="N -> D (in HLD18; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30620337"
FT /id="VAR_082600"
FT VARIANT 255
FT /note="N -> S (in HLD18; decreased function in sphingolipid
FT biosynthetic process)"
FT /evidence="ECO:0000269|PubMed:30620337,
FT ECO:0000269|PubMed:31186544"
FT /id="VAR_082601"
FT VARIANT 280
FT /note="A -> V (in HLD18; decreased function in sphingolipid
FT biosynthetic process; reduced protein levels; increased
FT protein degradation)"
FT /evidence="ECO:0000269|PubMed:30620338"
FT /id="VAR_082602"
FT VARIANT 293..323
FT /note="Missing (in HLD18; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30620337"
FT /id="VAR_082603"
SQ SEQUENCE 323 AA; 37866 MW; 9FF2E4A0B87EA71C CRC64;
MGSRVSREDF EWVYTDQPHA DRRREILAKY PEIKSLMKPD PNLIWIIIMM VLTQLGAFYI
VKDLDWKWVI FGAYAFGSCI NHSMTLAIHE IAHNAAFGNC KAMWNRWFGM FANLPIGIPY
SISFKRYHMD HHRYLGADGV DVDIPTDFEG WFFCTAFRKF IWVILQPLFY AFRPLFINPK
PITYLEVINT VAQVTFDILI YYFLGIKSLV YMLAASLLGL GLHPISGHFI AEHYMFLKGH
ETYSYYGPLN LLTFNVGYHN EHHDFPNIPG KSLPLVRKIA AEYYDNLPHY NSWIKVLYDF
VMDDTISPYS RMKRHQKGEM VLE
