PLSC_YEAST
ID PLSC_YEAST Reviewed; 303 AA.
AC P33333; D6VRU4; E9P8Y5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase;
DE Short=1-AGP acyltransferase;
DE Short=1-AGPAT;
DE EC=2.3.1.23 {ECO:0000269|PubMed:26643989};
DE EC=2.3.1.51 {ECO:0000269|PubMed:18154737, ECO:0000269|PubMed:26643989, ECO:0000269|PubMed:9401016};
DE EC=2.3.1.n7 {ECO:0000269|PubMed:26643989};
DE AltName: Full=Lysophosphatidic acid acyltransferase;
DE Short=LPAAT;
DE AltName: Full=Sphingolipid compensation protein 1 {ECO:0000303|PubMed:8408076};
GN Name=SLC1 {ECO:0000303|PubMed:8408076}; OrderedLocusNames=YDL052C;
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.
RX PubMed=8408076; DOI=10.1016/s0021-9258(20)80661-9;
RA Nagiec M.M., Wells G.B., Lester R.L., Dickson R.C.;
RT "A suppressor gene that enables Saccharomyces cerevisiae to grow without
RT making sphingolipids encodes a protein that resembles an Escherichia coli
RT fatty acyltransferase.";
RL J. Biol. Chem. 268:22156-22163(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=9401016; DOI=10.1128/jb.179.24.7611-7616.1997;
RA Athenstaedt K., Daum G.;
RT "Biosynthesis of phosphatidic acid in lipid particles and endoplasmic
RT reticulum of Saccharomyces cerevisiae.";
RL J. Bacteriol. 179:7611-7616(1997).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=17675291; DOI=10.1074/jbc.m702719200;
RA Benghezal M., Roubaty C., Veepuri V., Knudsen J., Conzelmann A.;
RT "SLC1 and SLC4 encode partially redundant acyl-coenzyme A 1-acylglycerol-3-
RT phosphate O-acyltransferases of budding yeast.";
RL J. Biol. Chem. 282:30845-30855(2007).
RN [7]
RP FUNCTION.
RX PubMed=17890783; DOI=10.1074/jbc.m704509200;
RA Tamaki H., Shimada A., Itoh Y., Ohya M., Takase J., Miyashita M.,
RA Miyagawa H., Nozaki H., Nakayama R., Kumagai H.;
RT "LPT1 encodes a membrane-bound O-acyltransferase involved in the acylation
RT of lysophospholipids in the yeast Saccharomyces cerevisiae.";
RL J. Biol. Chem. 282:34288-34298(2007).
RN [8]
RP CATALYTIC ACTIVITY.
RX PubMed=18154737; DOI=10.1016/j.febslet.2007.12.020;
RA Stahl U., Stalberg K., Stymne S., Ronne H.;
RT "A family of eukaryotic lysophospholipid acyltransferases with broad
RT specificity.";
RL FEBS Lett. 582:305-309(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [10]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=20694142; DOI=10.1371/journal.pone.0011956;
RA Shui G., Guan X.L., Gopalakrishnan P., Xue Y., Goh J.S., Yang H.,
RA Wenk M.R.;
RT "Characterization of substrate preference for Slc1p and Cst26p in
RT Saccharomyces cerevisiae using lipidomic approaches and an LPAAT activity
RT assay.";
RL PLoS ONE 5:e11956-e11956(2010).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=21820081; DOI=10.1016/j.bbalip.2011.07.015;
RA Grillitsch K., Connerth M., Kofeler H., Arrey T.N., Rietschel B.,
RA Wagner B., Karas M., Daum G.;
RT "Lipid particles/droplets of the yeast Saccharomyces cerevisiae revisited:
RT lipidome meets proteome.";
RL Biochim. Biophys. Acta 1811:1165-1176(2011).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=24868093; DOI=10.1194/jlr.m050229;
RA Currie E., Guo X., Christiano R., Chitraju C., Kory N., Harrison K.,
RA Haas J., Walther T.C., Farese R.V. Jr.;
RT "High-confidence proteomic analysis of yeast lipid droplets identifies
RT additional droplet proteins and reveals connections to dolichol synthesis
RT and sterol acetylation.";
RL J. Lipid Res. 55:1465-1477(2014).
RN [13]
RP CATALYTIC ACTIVITY.
RX PubMed=26643989; DOI=10.1007/s11745-015-4102-0;
RA Jasieniecka-Gazarkiewicz K., Demski K., Lager I., Stymne S., Banas A.;
RT "Possible role of different yeast and plant lysophospholipid:acyl-CoA
RT acyltransferases (LPLATs) in acyl remodelling of phospholipids.";
RL Lipids 51:15-23(2016).
CC -!- FUNCTION: Acyltransferase that catalyzes the sn-2-specific, acyl-CoA-
CC dependent acylation of lysophosphatidic acid (LPA) to phosphatidic acid
CC (PA) in lipid particles (PubMed:9401016). Together with ALE1, plays a
CC central role in PA biosynthesis. PA is the intermediate, from which all
CC glycerophospholipids are synthesized (PubMed:17890783). Can also
CC acylate lysophosphoinositol (LPI) and lysophosphoserine (LPS)
CC (PubMed:17675291). The fatty acyl substrates include 18:1-acyl-CoA,
CC 14:0-acyl-CoA, 12:0-acyl-CoA and 10:0-acyl-CoA (PubMed:20694142).
CC {ECO:0000269|PubMed:17675291, ECO:0000269|PubMed:17890783,
CC ECO:0000269|PubMed:20694142, ECO:0000269|PubMed:9401016}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000269|PubMed:18154737, ECO:0000269|PubMed:26643989,
CC ECO:0000269|PubMed:9401016};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000269|PubMed:26643989, ECO:0000305|PubMed:18154737,
CC ECO:0000305|PubMed:9401016};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19711;
CC Evidence={ECO:0000269|PubMed:26643989};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:58342; EC=2.3.1.23;
CC Evidence={ECO:0000269|PubMed:26643989};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12938;
CC Evidence={ECO:0000269|PubMed:26643989};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + an acyl-CoA = a
CC 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:32995, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:64612; EC=2.3.1.n7;
CC Evidence={ECO:0000269|PubMed:26643989};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32996;
CC Evidence={ECO:0000269|PubMed:26643989};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:32997;
CC Evidence={ECO:0000269|PubMed:26643989};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate
CC = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:33187, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:64839;
CC Evidence={ECO:0000269|PubMed:17675291};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188;
CC Evidence={ECO:0000305|PubMed:17675291};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-phosphate
CC = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37163, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74560, ChEBI:CHEBI:74565;
CC Evidence={ECO:0000269|PubMed:17675291};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37164;
CC Evidence={ECO:0000305|PubMed:17675291};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-L-serine = 1,2-di-(9Z)-octadecenoyl-sn-glycero-3-phospho-L-
CC serine + CoA; Xref=Rhea:RHEA:37407, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:74617, ChEBI:CHEBI:74905;
CC Evidence={ECO:0000269|PubMed:17675291};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37408;
CC Evidence={ECO:0000305|PubMed:17675291};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + a 1-acyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) = a 1-acyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1D-
CC myo-inositol) + CoA; Xref=Rhea:RHEA:37623, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:64771, ChEBI:CHEBI:75116;
CC Evidence={ECO:0000269|PubMed:17675291};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37624;
CC Evidence={ECO:0000305|PubMed:17675291};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-heptadecanoyl-sn-glycero-3-phosphate
CC = 1-heptadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37151, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74554, ChEBI:CHEBI:74556;
CC Evidence={ECO:0000269|PubMed:20694142};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37152;
CC Evidence={ECO:0000305|PubMed:20694142};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-heptadecanoyl-sn-glycero-3-phosphate + dodecanoyl-CoA = 1-
CC heptadecanoyl-2-dodecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:44384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:74554, ChEBI:CHEBI:84427;
CC Evidence={ECO:0000269|PubMed:20694142};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44385;
CC Evidence={ECO:0000305|PubMed:20694142};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-heptadecanoyl-sn-glycero-3-phosphate + tetradecanoyl-CoA =
CC 1-heptadecanoyl-2-tetradecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:44388, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:74554, ChEBI:CHEBI:84428;
CC Evidence={ECO:0000269|PubMed:20694142};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44389;
CC Evidence={ECO:0000305|PubMed:20694142};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:18154737,
CC ECO:0000269|PubMed:21820081, ECO:0000269|PubMed:24868093}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
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DR EMBL; L13282; AAA16514.1; -; Unassigned_DNA.
DR EMBL; Z74100; CAA98614.1; -; Genomic_DNA.
DR EMBL; AY692892; AAT92911.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11804.1; -; Genomic_DNA.
DR PIR; A48600; A48600.
DR RefSeq; NP_010231.1; NM_001180111.1.
DR AlphaFoldDB; P33333; -.
DR SMR; P33333; -.
DR BioGRID; 32007; 111.
DR DIP; DIP-5136N; -.
DR IntAct; P33333; 43.
DR MINT; P33333; -.
DR STRING; 4932.YDL052C; -.
DR SwissLipids; SLP:000000049; -.
DR MaxQB; P33333; -.
DR PaxDb; P33333; -.
DR PRIDE; P33333; -.
DR EnsemblFungi; YDL052C_mRNA; YDL052C; YDL052C.
DR GeneID; 851508; -.
DR KEGG; sce:YDL052C; -.
DR SGD; S000002210; SLC1.
DR VEuPathDB; FungiDB:YDL052C; -.
DR eggNOG; KOG2848; Eukaryota.
DR GeneTree; ENSGT00390000008726; -.
DR HOGENOM; CLU_027938_10_0_1; -.
DR InParanoid; P33333; -.
DR OMA; RLMGITM; -.
DR BioCyc; MetaCyc:YDL052C-MON; -.
DR BioCyc; YEAST:YDL052C-MON; -.
DR BRENDA; 2.3.1.51; 984.
DR Reactome; R-SCE-1483166; Synthesis of PA.
DR Reactome; R-SCE-163765; ChREBP activates metabolic gene expression.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR UniPathway; UPA00557; UER00613.
DR PRO; PR:P33333; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P33333; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IDA:SGD.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0106262; F:1-acylglycerophosphoethanolamine O-acyltransferase activity; IEA:RHEA.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IGI:SGD.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central.
DR InterPro; IPR004552; AGP_acyltrans.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR TIGRFAMs; TIGR00530; AGP_acyltrn; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Lipid biosynthesis; Lipid droplet; Lipid metabolism;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..303
FT /note="1-acyl-sn-glycerol-3-phosphate acyltransferase"
FT /id="PRO_0000208189"
FT REGION 278..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 82..87
FT /note="HXXXXD motif"
FT COMPBIAS 280..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 44
FT /note="Q -> L (in allele suppressor SLC1-1)"
FT CONFLICT 115
FT /note="W -> R (in Ref. 4; AAT92911)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 303 AA; 33887 MW; 36ECBBC2659655EB CRC64;
MSVIGRFLYY LRSVLVVLAL AGCGFYGVIA SILCTLIGKQ HLAQWITARC FYHVMKLMLG
LDVKVVGEEN LAKKPYIMIA NHQSTLDIFM LGRIFPPGCT VTAKKSLKYV PFLGWFMALS
GTYFLDRSKR QEAIDTLNKG LENVKKNKRA LWVFPEGTRS YTSELTMLPF KKGAFHLAQQ
GKIPIVPVVV SNTSTLVSPK YGVFNRGCMI VRILKPISTE NLTKDKIGEF AEKVRDQMVD
TLKEIGYSPA INDTTLPPQA IEYAALQHDK KVNKKIKNEP VPSVSISNDV NTHNEGSSVK
KMH
