ID   ELO3_YEAST              Reviewed;         345 AA.
AC   P40319; D6VZ09;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 186.
DE   RecName: Full=Fatty acid elongase 3 {ECO:0000305};
DE            EC=2.3.1.199 {ECO:0000269|PubMed:12684876};
DE   AltName: Full=3-keto acyl-CoA synthase ELO3 {ECO:0000305};
DE   AltName: Full=Affecting plasma membrane ATPase activity protein 1 {ECO:0000303|PubMed:8027068};
DE   AltName: Full=Elongation of fatty acids protein 3 {ECO:0000303|PubMed:9211877};
DE   AltName: Full=Suppressor of RAD3 essential function protein 1 {ECO:0000303|PubMed:3323825};
DE   AltName: Full=Suppressor of Rvs161 and Rvs167 mutations protein 4 {ECO:0000303|PubMed:8488727};
DE   AltName: Full=Very-long-chain 3-oxoacyl-CoA synthase 3 {ECO:0000305};
DE   AltName: Full=v-SNARE bypass mutant gene 1 protein {ECO:0000303|PubMed:9832547};
GN   Name=ELO3 {ECO:0000303|PubMed:9211877};
GN   Synonyms=APA1 {ECO:0000303|PubMed:8027068}, SRE1
GN   {ECO:0000303|PubMed:3323825}, SUR4 {ECO:0000303|PubMed:8488727}, VBM1
GN   {ECO:0000303|PubMed:9832547};
GN   OrderedLocusNames=YLR372W {ECO:0000312|SGD:S000004364};
GN   ORFNames=L8039.2;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 44827 / SKQ2N;
RA   Revardel E.;
RL   Thesis (1994), University of Bordeaux II, France.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=8027068; DOI=10.1016/s0021-9258(17)32419-5;
RA   Garcia-Arranz M., Maldonado A.M., Mazon M.J., Portillo F.;
RT   "Transcriptional control of yeast plasma membrane H(+)-ATPase by glucose.
RT   Cloning and characterization of a new gene involved in this regulation.";
RL   J. Biol. Chem. 269:18076-18082(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8649379; DOI=10.1128/mcb.16.6.2719;
RA   Silve S., Leplatois P., Josse A., Dupuy P.-H., Lanau C., Kaghad M.,
RA   Dhers C., Picard C., Rahier A., Taton M., Le Fur G., Caput D., Ferrara P.,
RA   Loison G.;
RT   "The immunosuppressant SR 31747 blocks cell proliferation by inhibiting a
RT   steroid isomerase in Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 16:2719-2727(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX   PubMed=9832547; DOI=10.1083/jcb.143.5.1167;
RA   David D., Sundarababu S., Gerst J.E.;
RT   "Involvement of long chain fatty acid elongation in the trafficking of
RT   secretory vesicles in yeast.";
RL   J. Cell Biol. 143:1167-1182(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [6]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [7]
RP   GENE NAME.
RX   PubMed=3323825; DOI=10.1007/bf00331150;
RA   Naumovski L., Friedberg E.C.;
RT   "The RAD3 gene of Saccharomyces cerevisiae: isolation and characterization
RT   of a temperature-sensitive mutant in the essential function and of
RT   extragenic suppressors of this mutant.";
RL   Mol. Gen. Genet. 209:458-466(1987).
RN   [8]
RP   IDENTIFICATION.
RX   PubMed=8488727; DOI=10.1002/yea.320090306;
RA   Desfarges L., Durrens P., Juguelin H., Cassagne C., Bonneu M., Aigle M.;
RT   "Yeast mutants affected in viability upon starvation have a modified
RT   phospholipid composition.";
RL   Yeast 9:267-277(1993).
RN   [9]
RP   FUNCTION.
RX   PubMed=9211877; DOI=10.1074/jbc.272.28.17376;
RA   Oh C.-S., Toke D.A., Mandala S., Martin C.E.;
RT   "ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene,
RT   function in fatty acid elongation and are required for sphingolipid
RT   formation.";
RL   J. Biol. Chem. 272:17376-17384(1997).
RN   [10]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12087109; DOI=10.1074/jbc.m205620200;
RA   Han G., Gable K., Kohlwein S.D., Beaudoin F., Napier J.A., Dunn T.M.;
RT   "The Saccharomyces cerevisiae YBR159w gene encodes the 3-ketoreductase of
RT   the microsomal fatty acid elongase.";
RL   J. Biol. Chem. 277:35440-35449(2002).
RN   [11]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=12684876; DOI=10.1007/s00438-003-0836-0;
RA   Roessler H., Rieck C., Delong T., Hoja U., Schweizer E.;
RT   "Functional differentiation and selective inactivation of multiple
RT   Saccharomyces cerevisiae genes involved in very-long-chain fatty acid
RT   synthesis.";
RL   Mol. Genet. Genomics 269:290-298(2003).
RN   [12]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [13]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN   [14]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF PHE-262 AND LYS-266.
RX   PubMed=17719544; DOI=10.1016/j.cell.2007.06.031;
RA   Denic V., Weissman J.S.;
RT   "A molecular caliper mechanism for determining very long-chain fatty acid
RT   length.";
RL   Cell 130:663-677(2007).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [16]
RP   FUNCTION.
RX   PubMed=29458843; DOI=10.1016/j.micres.2017.11.001;
RA   Wang Q., Du X., Ma K., Shi P., Liu W., Sun J., Peng M., Huang Z.;
RT   "A critical role for very long-chain fatty acid elongases in oleic acid-
RT   mediated Saccharomyces cerevisiae cytotoxicity.";
RL   Microbiol. Res. 207:1-7(2018).
CC   -!- FUNCTION: Component of a microsomal membrane bound long-chain fatty
CC       acid elongation system, which produces the 20-26-carbon very long-chain
CC       fatty acids (VLCFA) from long-chain fatty acid precursors and is
CC       involved ceramide and inositol sphingolipid biosynthesis. Component of
CC       elongase III, which synthesizes 20-26-carbon fatty acids from 18-
CC       carbon-fatty acyl-CoA primers such as stearoyl-CoA by incorporation of
CC       malonyl-CoA (PubMed:9211877, PubMed:12684876). The enzymes active site
CC       faces the cytosol, whereas VLCFA length is determined by a lysine near
CC       the luminal end of transmembrane helix 6 (PubMed:17719544). Plays an
CC       important role in lipotoxic cell death induced by oleic acid through
CC       maintaining a balanced fatty acid composition in thr plasma membrane
CC       (PubMed:29458843). Affects plasma membrane H(+)-ATPase activity. May
CC       act on a glucose-signaling pathway that controls the expression of
CC       several genes that are transcriptionally regulated by glucose such as
CC       PMA1, HXT3 and SNF3 (PubMed:8027068). {ECO:0000269|PubMed:12684876,
CC       ECO:0000269|PubMed:17719544, ECO:0000269|PubMed:29458843,
CC       ECO:0000269|PubMed:8027068, ECO:0000269|PubMed:9211877}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-
CC         chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736;
CC         EC=2.3.1.199; Evidence={ECO:0000269|PubMed:12684876};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + malonyl-CoA + octadecanoyl-CoA = 3-oxoeicosanoyl-CoA +
CC         CO2 + CoA; Xref=Rhea:RHEA:35319, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:57394, ChEBI:CHEBI:65115;
CC         Evidence={ECO:0000269|PubMed:17719544};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35320;
CC         Evidence={ECO:0000269|PubMed:17719544};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hexadecanoyl-CoA + malonyl-CoA = 3-oxooctadecanoyl-CoA
CC         + CO2 + CoA; Xref=Rhea:RHEA:35315, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:71407;
CC         Evidence={ECO:0000269|PubMed:17719544};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35316;
CC         Evidence={ECO:0000269|PubMed:17719544};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=eicosanoyl-CoA + H(+) + malonyl-CoA = 3-oxodocosanoyl-CoA +
CC         CO2 + CoA; Xref=Rhea:RHEA:35327, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:71451;
CC         Evidence={ECO:0000269|PubMed:17719544};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35328;
CC         Evidence={ECO:0000269|PubMed:17719544};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=docosanoyl-CoA + H(+) + malonyl-CoA = 3-oxotetracosanoyl-CoA +
CC         CO2 + CoA; Xref=Rhea:RHEA:36507, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:65059, ChEBI:CHEBI:73977;
CC         Evidence={ECO:0000269|PubMed:17719544};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36508;
CC         Evidence={ECO:0000269|PubMed:17719544};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:12087109, ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:9832547}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- DOMAIN: The HxxHH motif is essential for ELOp function in vivo and 3-
CC       keto acyl-CoA synthase activity in vitro.
CC       {ECO:0000269|PubMed:17719544}.
CC   -!- DOMAIN: The C-terminal di-lysine motifs may confer endoplasmic
CC       reticulum localization. {ECO:0000303|PubMed:9832547}.
CC   -!- SIMILARITY: Belongs to the ELO family. {ECO:0000305}.
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DR   EMBL; L28723; AAA35134.1; -; Genomic_DNA.
DR   EMBL; X78326; CAA55129.1; -; Genomic_DNA.
DR   EMBL; X82033; CAA57553.1; -; Genomic_DNA.
DR   EMBL; U19103; AAB67563.1; -; Genomic_DNA.
DR   EMBL; AF011409; AAC28398.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09675.1; -; Genomic_DNA.
DR   PIR; S48517; S48517.
DR   RefSeq; NP_013476.3; NM_001182261.3.
DR   AlphaFoldDB; P40319; -.
DR   SMR; P40319; -.
DR   BioGRID; 31632; 634.
DR   DIP; DIP-4024N; -.
DR   IntAct; P40319; 56.
DR   MINT; P40319; -.
DR   STRING; 4932.YLR372W; -.
DR   SwissLipids; SLP:000000494; -.
DR   GlyCosmos; P40319; 3 sites, No reported glycans.
DR   GlyGen; P40319; 3 sites.
DR   iPTMnet; P40319; -.
DR   MaxQB; P40319; -.
DR   PaxDb; 4932-YLR372W; -.
DR   PeptideAtlas; P40319; -.
DR   EnsemblFungi; YLR372W_mRNA; YLR372W; YLR372W.
DR   GeneID; 851087; -.
DR   KEGG; sce:YLR372W; -.
DR   AGR; SGD:S000004364; -.
DR   SGD; S000004364; ELO3.
DR   VEuPathDB; FungiDB:YLR372W; -.
DR   eggNOG; KOG3071; Eukaryota.
DR   GeneTree; ENSGT01050000244965; -.
DR   HOGENOM; CLU_048483_6_1_1; -.
DR   InParanoid; P40319; -.
DR   OMA; EWVPISL; -.
DR   OrthoDB; 2312411at2759; -.
DR   BioCyc; MetaCyc:MONOMER3O-70; -.
DR   BioCyc; YEAST:MONOMER3O-70; -.
DR   BioGRID-ORCS; 851087; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P40319; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P40319; Protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009922; F:fatty acid elongase activity; IMP:SGD.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IMP:SGD.
DR   GO; GO:0030497; P:fatty acid elongation; IMP:SGD.
DR   GO; GO:0034625; P:fatty acid elongation, monounsaturated fatty acid; IBA:GO_Central.
DR   GO; GO:0034626; P:fatty acid elongation, polyunsaturated fatty acid; IBA:GO_Central.
DR   GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IBA:GO_Central.
DR   GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IGI:SGD.
DR   GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IMP:SGD.
DR   GO; GO:0030148; P:sphingolipid biosynthetic process; IMP:SGD.
DR   GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IMP:SGD.
DR   InterPro; IPR030457; ELO_CS.
DR   InterPro; IPR002076; ELO_fam.
DR   PANTHER; PTHR11157:SF157; ELONGATION OF FATTY ACIDS PROTEIN 3; 1.
DR   PANTHER; PTHR11157; FATTY ACID ACYL TRANSFERASE-RELATED; 1.
DR   Pfam; PF01151; ELO; 1.
DR   PROSITE; PS01188; ELO; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Glycoprotein; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..345
FT                   /note="Fatty acid elongase 3"
FT                   /id="PRO_0000207550"
FT   TOPO_DOM        1..73
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:16847258"
FT   TRANSMEM        74..94
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        95..105
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:16847258"
FT   TRANSMEM        106..126
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        127..155
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:16847258"
FT   TRANSMEM        156..176
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        177..180
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:16847258"
FT   TRANSMEM        181..201
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        202..207
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:16847258"
FT   TRANSMEM        208..228
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        229..242
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:16847258"
FT   TRANSMEM        243..263
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        264..283
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:16847258"
FT   TRANSMEM        284..304
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        305..345
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:16847258"
FT   REGION          318..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           185..189
FT                   /note="HxxHH motif"
FT                   /evidence="ECO:0000305|PubMed:17719544"
FT   MOTIF           308..311
FT                   /note="Di-lysine motif 1"
FT                   /evidence="ECO:0000303|PubMed:9832547"
FT   MOTIF           312..315
FT                   /note="Di-lysine motif 2"
FT                   /evidence="ECO:0000303|PubMed:9832547"
FT   MOTIF           316..319
FT                   /note="Di-lysine motif 3"
FT                   /evidence="ECO:0000303|PubMed:9832547"
FT   COMPBIAS        320..339
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            266
FT                   /note="Determines the chain length of the elongated VLCFA"
FT                   /evidence="ECO:0000305|PubMed:17719544"
FT   CARBOHYD        2
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        20
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   MUTAGEN         262
FT                   /note="F->K: Terminates elongation following the production
FT                   of C22 instead of C-26; when associated with L-266."
FT                   /evidence="ECO:0000269|PubMed:17719544"
FT   MUTAGEN         266
FT                   /note="K->L: Terminates elongation following the production
FT                   of C22 instead of C-26; when associated with K-262."
FT                   /evidence="ECO:0000269|PubMed:17719544"
FT   CONFLICT        35
FT                   /note="E -> D (in Ref. 2; CAA55129)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        208
FT                   /note="W -> R (in Ref. 2; CAA55129)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        330..331
FT                   /note="ST -> FY (in Ref. 2; CAA55129)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   345 AA;  39465 MW;  1303A9AC54BFFCC5 CRC64;
     MNTTTSTVIA AVADQFQSLN SSSSCFLKVH VPSIENPFGI ELWPIFSKVF EYFSGYPAEQ
     FEFIHNKTFL ANGYHAVSII IVYYIIIFGG QAILRALNAS PLKFKLLFEI HNLFLTSISL
     VLWLLMLEQL VPMVYHNGLF WSICSKEAFA PKLVTLYYLN YLTKFVELID TVFLVLRRKK
     LLFLHTYHHG ATALLCYTQL IGRTSVEWVV ILLNLGVHVI MYWYYFLSSC GIRVWWKQWV
     TRFQIIQFLI DLVFVYFATY TFYAHKYLDG ILPNKGTCYG TQAAAAYGYL ILTSYLLLFI
     SFYIQSYKKG GKKTVKKESE VSGSVASGSS TGVKTSNTKV SSRKA
//