ID   CPT1_YEAST              Reviewed;         393 AA.
AC   P17898; D6W152;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 3.
DT   04-NOV-2026, entry version 187.
DE   RecName: Full=Cholinephosphotransferase 1;
DE            EC=2.7.8.2;
DE   AltName: Full=Aminoalcohol phosphotransferase CPT1;
DE   AltName: Full=Diacylglycerol cholinephosphotransferase 1;
DE   AltName: Full=Sn-1,2-diacylglycerol cholinephosphotransferase;
DE            Short=CHOPT;
GN   Name=CPT1; OrderedLocusNames=YNL130C; ORFNames=N1218, N1867;
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].
RX   PubMed=2153142; DOI=10.1016/s0021-9258(19)40081-1;
RA   Hjelmstad R.H., Bell R.M.;
RT   "The sn-1,2-diacylglycerol cholinephosphotransferase of Saccharomyces
RT   cerevisiae. Nucleotide sequence, transcriptional mapping, and gene product
RT   analysis of the CPT1 gene.";
RL   J. Biol. Chem. 265:1755-1764(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8619318; DOI=10.1002/yea.320111210;
RA   Mallet L., Bussereau F., Jacquet M.;
RT   "A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2,
RT   CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine
RT   deaminase gene and 14 new open reading frames.";
RL   Yeast 11:1195-1209(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873; DOI=10.1038/387s093;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [4]
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   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=3005242; DOI=10.1128/jb.165.3.901-910.1986;
RA   Kuchler K., Daum G., Paltauf F.;
RT   "Subcellular and submitochondrial localization of phospholipid-synthesizing
RT   enzymes in Saccharomyces cerevisiae.";
RL   J. Bacteriol. 165:901-910(1986).
RN   [6]
RP   FUNCTION.
RX   PubMed=3029130; DOI=10.1016/s0021-9258(18)61443-7;
RA   Hjelmstad R.H., Bell R.M.;
RT   "Mutants of Saccharomyces cerevisiae defective in sn-1,2-diacylglycerol
RT   cholinephosphotransferase. Isolation, characterization, and cloning of the
RT   CPT1 gene.";
RL   J. Biol. Chem. 262:3909-3917(1987).
RN   [7]
RP   CATALYTIC ACTIVITY, FUNCTION, COFACTOR, ACTIVITY REGULATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=1847919; DOI=10.1016/s0021-9258(20)64330-7;
RA   Hjelmstad R.H., Bell R.M.;
RT   "sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases in
RT   Saccharomyces cerevisiae. Mixed micellar analysis of the CPT1 and EPT1 gene
RT   products.";
RL   J. Biol. Chem. 266:4357-4365(1991).
RN   [8]
RP   FUNCTION.
RX   PubMed=7961445; DOI=10.1128/jb.176.22.6861-6868.1994;
RA   McGee T.P., Skinner H.B., Bankaitis V.A.;
RT   "Functional redundancy of CDP-ethanolamine and CDP-choline pathway enzymes
RT   in phospholipid biosynthesis: ethanolamine-dependent effects on steady-
RT   state membrane phospholipid composition in Saccharomyces cerevisiae.";
RL   J. Bacteriol. 176:6861-6868(1994).
RN   [9]
RP   FUNCTION.
RX   PubMed=7961735; DOI=10.1016/s0021-9258(18)46888-3;
RA   McMaster C.R., Bell R.M.;
RT   "Phosphatidylcholine biosynthesis in Saccharomyces cerevisiae. Regulatory
RT   insights from studies employing null and chimeric sn-1,2-diacylglycerol
RT   choline- and ethanolaminephosphotransferases.";
RL   J. Biol. Chem. 269:28010-28016(1994).
RN   [10]
RP   INDUCTION.
RX   PubMed=7961831; DOI=10.1016/s0021-9258(19)61972-1;
RA   Morash S.C., McMaster C.R., Hjelmstad R.H., Bell R.M.;
RT   "Studies employing Saccharomyces cerevisiae cpt1 and ept1 null mutants
RT   implicate the CPT1 gene in coordinate regulation of phospholipid
RT   biosynthesis.";
RL   J. Biol. Chem. 269:28769-28776(1994).
RN   [11]
RP   SUBCELLULAR LOCATION.
RX   PubMed=8543066; DOI=10.1016/0014-5793(95)01361-x;
RA   Leber A., Hrastnik C., Daum G.;
RT   "Phospholipid-synthesizing enzymes in Golgi membranes of the yeast,
RT   Saccharomyces cerevisiae.";
RL   FEBS Lett. 377:271-274(1995).
RN   [12]
RP   REVISION OF GENE MODEL.
RX   PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA   Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA   Gates K., Gaffney T.D., Philippsen P.;
RT   "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT   comparison to the genome of a related fungus: Ashbya gossypii.";
RL   Genome Biol. 4:R45.1-R45.13(2003).
RN   [13]
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   [14]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [15]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX   PubMed=15225629; DOI=10.1016/j.febslet.2004.05.043;
RA   Boumann H.A., de Kruijff B., Heck A.J., de Kroon A.I.;
RT   "The selective utilization of substrates in vivo by the
RT   phosphatidylethanolamine and phosphatidylcholine biosynthetic enzymes Ept1p
RT   and Cpt1p in yeast.";
RL   FEBS Lett. 569:173-177(2004).
CC   -!- FUNCTION: Catalyzes the final step in the CDP-choline route leading to
CC       phosphatidylcholin (PC). Preferentially uses CDP-monomethylethanolamine
CC       as aminoalcohol substrate. Shows highest activity toward di- and mono-
CC       unsaturated diacylglycerol species as lipid substrates. The CDP-choline
CC       pathway only contributes to net PC synthesis if exogenous choline is
CC       present. In its absence, this pathway recycles choline from PC turnover
CC       and may contribute to maintaining the proper PC species composition.
CC       {ECO:0000269|PubMed:15225629, ECO:0000269|PubMed:1847919,
CC       ECO:0000269|PubMed:3029130, ECO:0000269|PubMed:7961445,
CC       ECO:0000269|PubMed:7961735}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CDP-choline + a 1,2-diacyl-sn-glycerol = a 1,2-diacyl-sn-
CC         glycero-3-phosphocholine + CMP + H(+); Xref=Rhea:RHEA:32939,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:57643,
CC         ChEBI:CHEBI:58779, ChEBI:CHEBI:60377; EC=2.7.8.2;
CC         Evidence={ECO:0000269|PubMed:15225629, ECO:0000269|PubMed:1847919};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32940;
CC         Evidence={ECO:0000305|PubMed:1847919};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CDP-N,N-dimethylethanolamine + a 1,2-diacyl-sn-glycerol = a
CC         1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + CMP +
CC         H(+); Xref=Rhea:RHEA:33775, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815,
CC         ChEBI:CHEBI:60377, ChEBI:CHEBI:64572, ChEBI:CHEBI:65117;
CC         Evidence={ECO:0000269|PubMed:1847919};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33776;
CC         Evidence={ECO:0000305|PubMed:1847919};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:1847919};
CC   -!- ACTIVITY REGULATION: Requires a divalent cation activator, and is
CC       inhibited by CMP. Activated by phospholipids, especially
CC       phosphatidylcholine. {ECO:0000269|PubMed:1847919}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=100 uM for CDP-choline {ECO:0000269|PubMed:1847919};
CC         KM=137 uM for CDP-dimethylethanolamine {ECO:0000269|PubMed:1847919};
CC         Vmax=0.2 nmol/min/mg enzyme for CDP-choline
CC         {ECO:0000269|PubMed:1847919};
CC         Vmax=0.07 nmol/min/mg enzyme for CDP-dimethylethanolamine
CC         {ECO:0000269|PubMed:1847919};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC       phosphatidylcholine from phosphocholine: step 2/2.
CC   -!- INTERACTION:
CC       P17898; P22140: EPT1; NbExp=5; IntAct=EBI-2050738, EBI-6494;
CC   -!- SUBCELLULAR LOCATION: Microsome membrane; Multi-pass membrane protein.
CC       Endoplasmic reticulum membrane; Multi-pass membrane protein.
CC       Mitochondrion outer membrane; Multi-pass membrane protein.
CC   -!- INDUCTION: Repressed by inositol. {ECO:0000269|PubMed:7961831}.
CC   -!- MISCELLANEOUS: Present with 981 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA63571.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA86895.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA96012.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; J05203; AAA63571.1; ALT_INIT; Genomic_DNA.
DR   EMBL; Z46843; CAA86895.1; ALT_INIT; Genomic_DNA.
DR   EMBL; Z71406; CAA96012.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BK006947; DAA10418.1; -; Genomic_DNA.
DR   PIR; S63075; S63075.
DR   RefSeq; NP_014269.4; NM_001182968.3.
DR   PDB; 8UL9; EM; 3.20 A; A/B=2-388.
DR   PDB; 8URP; EM; 2.90 A; A/B=2-388.
DR   PDB; 8URT; EM; 3.10 A; A/B=2-393.
DR   AlphaFoldDB; P17898; -.
DR   EMDB; EMD-42357; -.
DR   EMDB; EMD-42496; -.
DR   EMDB; EMD-42500; -.
DR   EMDB; EMD-46969; -.
DR   SMR; P17898; -.
DR   BioGRID; 35697; 127.
DR   DIP; DIP-7848N; -.
DR   FunCoup; P17898; 653.
DR   IntAct; P17898; 20.
DR   STRING; 4932.YNL130C; -.
DR   SwissLipids; SLP:000000070; -.
DR   iPTMnet; P17898; -.
DR   PaxDb; 4932-YNL130C; -.
DR   PeptideAtlas; P17898; -.
DR   EnsemblFungi; YNL130C_mRNA; YNL130C; YNL130C.
DR   GeneID; 855593; -.
DR   KEGG; sce:YNL130C; -.
DR   AGR; SGD:S000005074; -.
DR   SGD; S000005074; CPT1.
DR   VEuPathDB; FungiDB:YNL130C; -.
DR   eggNOG; KOG2877; Eukaryota.
DR   HOGENOM; CLU_035066_5_2_1; -.
DR   InParanoid; P17898; -.
DR   OMA; AAHLEIY; -.
DR   OrthoDB; 196717at2759; -.
DR   BioCyc; MetaCyc:YNL130C-MONOMER; -.
DR   BioCyc; YEAST:YNL130C-MONOMER; -.
DR   BRENDA; 2.7.8.2; 984.
DR   Reactome; R-SCE-1483191; Synthesis of PC.
DR   Reactome; R-SCE-1483213; Synthesis of PE.
DR   SABIO-RK; P17898; -.
DR   UniPathway; UPA00753; UER00740.
DR   BioGRID-ORCS; 855593; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P17898; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P17898; protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
DR   GO; GO:0004142; F:diacylglycerol cholinephosphotransferase activity; IDA:SGD.
DR   GO; GO:0006657; P:CDP-choline pathway; IDA:SGD.
DR   FunFam; 1.20.120.1760:FF:000012; sn-1,2-diacylglycerol cholinephosphotransferase; 1.
DR   Gene3D; 1.20.120.1760; -; 1.
DR   InterPro; IPR000462; CDP-OH_P_trans.
DR   InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR   InterPro; IPR048254; CDP_ALCOHOL_P_TRANSF_CS.
DR   InterPro; IPR014472; CHOPT.
DR   PANTHER; PTHR10414:SF37; BB IN A BOXCAR, ISOFORM C; 1.
DR   PANTHER; PTHR10414; ETHANOLAMINEPHOSPHOTRANSFERASE; 1.
DR   Pfam; PF01066; CDP-OH_P_transf; 1.
DR   PIRSF; PIRSF015665; CHOPT; 1.
DR   PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism;
KW   Magnesium; Membrane; Metal-binding; Microsome; Mitochondrion;
KW   Mitochondrion outer membrane; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..393
FT                   /note="Cholinephosphotransferase 1"
FT                   /id="PRO_0000056808"
FT   TOPO_DOM        1..40
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        62..172
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        194..210
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        232..263
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        285
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        307..320
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        321..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        342..348
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        370..393
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   HELIX           8..14
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   STRAND          20..22
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   HELIX           25..29
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   HELIX           32..39
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:8URT"
FT   HELIX           48..69
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   HELIX           80..105
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   HELIX           111..127
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   HELIX           129..136
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   HELIX           142..165
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   STRAND          166..170
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   HELIX           175..179
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   HELIX           180..192
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   HELIX           195..199
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   STRAND          202..204
FT                   /evidence="ECO:0007829|PDB:8URT"
FT   STRAND          208..211
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   HELIX           217..247
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   HELIX           248..250
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   STRAND          254..256
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   HELIX           257..265
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   HELIX           266..268
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   HELIX           269..284
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   HELIX           286..288
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   HELIX           291..314
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   HELIX           316..319
FT                   /evidence="ECO:0007829|PDB:8UL9"
FT   HELIX           323..326
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   HELIX           327..336
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   HELIX           337..341
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   TURN            346..348
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   HELIX           349..380
FT                   /evidence="ECO:0007829|PDB:8URP"
FT   STRAND          384..386
FT                   /evidence="ECO:0007829|PDB:8URP"
SQ   SEQUENCE   393 AA;  44829 MW;  320845FE9A79C5D6 CRC64;
     MGFFIPQSSL GNLKLYKYQS DDRSFLSNHV LRPFWRKFAT IFPLWMAPNL VTLLGFCFII
     FNVLTTLYYD PYFDQESPRW TYFSYAIGLF LYQTFDACDG MHARRTGQQG PLGELFDHCI
     DSINTTLSMI PVCSMTGMGY TYMTIFSQFA ILCSFYLSTW EEYHTHKLYL AEFCGPVEGI
     IVLCISFIAV GIYGPQTIWH TKVAQFSWQD FVFDVETVHL MYAFCTGALI FNIVTAHTNV
     VRYYESQSTK SATPSKTAEN ISKAVNGLLP FFAYFSSIFT LVLIQPSFIS LALILSIGFS
     VAFVVGRMII AHLTMQPFPM VNFPFLIPTI QLVLYAFMVY VLDYQKGSIV SALVWMGLGL
     TLAIHGMFIN DIIYDITTFL DIYALSIKHP KEI
//