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 27-MAR-2024, entry version 182. 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}. 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; 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; 68. DR IntAct; O15121; 20. DR MINT; O15121; -. 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; 9606-ENSP00000316476; -. DR PeptideAtlas; O15121; -. DR ProteomicsDB; 48459; -. DR Pumba; O15121; -. DR Antibodypedia; 20751; 191 antibodies from 25 providers. DR DNASU; 8560; -. DR Ensembl; ENST00000323699.9; ENSP00000316476.4; ENSG00000143753.14. 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 AGR; HGNC:13709; -. 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; IWIITMM; -. DR OrthoDB; 5485164at2759; -. DR PhylomeDB; O15121; -. DR TreeFam; TF313582; -. DR BioCyc; MetaCyc:ENSG00000143753-MONOMER; -. 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 1162 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 204 other cell types or tissues. DR ExpressionAtlas; O15121; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. 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; IPR011388; DES1/DES2. DR InterPro; IPR005804; FA_desaturase_dom. DR InterPro; IPR013866; Sphingolipid_d4-desaturase_N. DR PANTHER; PTHR12879; SPHINGOLIPID DELTA 4 DESATURASE/C-4 HYDROXYLASE PROTEIN DES2; 1. DR PANTHER; PTHR12879:SF2; SPHINGOLIPID DELTA(4)-DESATURASE DES1; 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. DR Genevisible; O15121; HS. 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; uncertain 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; uncertain 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; uncertain 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; uncertain 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 //