MBOA2_ARATH
ID MBOA2_ARATH Reviewed; 465 AA.
AC Q9CAN8;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Lysophospholipid acyltransferase 2 {ECO:0000303|PubMed:18154737};
DE Short=AtLPLAT2 {ECO:0000303|PubMed:18154737};
DE EC=2.3.1.- {ECO:0000269|PubMed:18154737};
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase {ECO:0000305};
DE EC=2.3.1.23 {ECO:0000269|PubMed:18154737};
DE AltName: Full=1-acylglycerophosphoethanolamine O-acyltransferase {ECO:0000305};
DE EC=2.3.1.n7 {ECO:0000269|PubMed:18154737};
DE AltName: Full=1-acylglycerophosphoserine O-acyltransferase {ECO:0000305};
DE EC=2.3.1.n6 {ECO:0000269|PubMed:18154737};
DE AltName: Full=Lysophosphatidylcholine acyltransferase 2 {ECO:0000303|PubMed:23150634};
DE Short=LPCAT2 {ECO:0000303|PubMed:23150634};
DE AltName: Full=Lysophosphatidylethanolamine acyltransferase {ECO:0000303|PubMed:18154737};
DE Short=LPEAT {ECO:0000303|PubMed:18154737};
DE AltName: Full=Lysophosphatidylglycerol acyltransferase {ECO:0000303|PubMed:18154737};
DE Short=LPGAT {ECO:0000303|PubMed:18154737};
DE AltName: Full=Lysophosphatidylserine acyltransferase {ECO:0000303|PubMed:18154737};
DE Short=LPSAT {ECO:0000303|PubMed:18154737};
GN Name=LPCAT2 {ECO:0000303|PubMed:23150634};
GN Synonyms=LPLAT2 {ECO:0000303|PubMed:18154737};
GN OrderedLocusNames=At1g63050 {ECO:0000312|Araport:AT1G63050};
GN ORFNames=F16M19.14 {ECO:0000312|EMBL:AAG51612.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, AND 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 [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=22233193; DOI=10.1186/1471-2229-12-4;
RA Xu J., Carlsson A.S., Francis T., Zhang M., Hoffman T., Giblin M.E.,
RA Taylor D.C.;
RT "Triacylglycerol synthesis by PDAT1 in the absence of DGAT1 activity is
RT dependent on re-acylation of LPC by LPCAT2.";
RL BMC Plant Biol. 12:4-4(2012).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23150634; DOI=10.1105/tpc.112.104604;
RA Wang L., Shen W., Kazachkov M., Chen G., Chen Q., Carlsson A.S., Stymne S.,
RA Weselake R.J., Zou J.;
RT "Metabolic interactions between the Lands cycle and the Kennedy pathway of
RT glycerolipid synthesis in Arabidopsis developing seeds.";
RL Plant Cell 24:4652-4669(2012).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=22923678; DOI=10.1104/pp.112.204263;
RA Nikolovski N., Rubtsov D., Segura M.P., Miles G.P., Stevens T.J.,
RA Dunkley T.P., Munro S., Lilley K.S., Dupree P.;
RT "Putative glycosyltransferases and other plant Golgi apparatus proteins are
RT revealed by LOPIT proteomics.";
RL Plant Physiol. 160:1037-1051(2012).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22932756; DOI=10.1104/pp.112.204438;
RA Bates P.D., Fatihi A., Snapp A.R., Carlsson A.S., Browse J., Lu C.;
RT "Acyl editing and headgroup exchange are the major mechanisms that direct
RT polyunsaturated fatty acid flux into triacylglycerols.";
RL Plant Physiol. 160:1530-1539(2012).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24189065; DOI=10.1074/jbc.m113.521815;
RA Lager I., Yilmaz J.L., Zhou X.R., Jasieniecka K., Kazachkov M., Wang P.,
RA Zou J., Weselake R., Smith M.A., Bayon S., Dyer J.M., Shockey J.M.,
RA Heinz E., Green A., Banas A., Stymne S.;
RT "Plant acyl-CoA:lysophosphatidylcholine acyltransferases (LPCATs) have
RT different specificities in their forward and reverse reactions.";
RL J. Biol. Chem. 288:36902-36914(2013).
RN [10]
RP FUNCTION.
RX PubMed=25268378; DOI=10.1111/tpj.12683;
RA Wang L., Kazachkov M., Shen W., Bai M., Wu H., Zou J.;
RT "Deciphering the roles of Arabidopsis LPCAT and PAH in phosphatidylcholine
RT homeostasis and pathway coordination for chloroplast lipid synthesis.";
RL Plant J. 80:965-976(2014).
RN [11]
RP INTERACTION WITH GPAT9 AND DGAT1.
RC STRAIN=cv. Columbia;
RX PubMed=26586834; DOI=10.1104/pp.15.01563;
RA Shockey J., Regmi A., Cotton K., Adhikari N., Browse J., Bates P.D.;
RT "Identification of Arabidopsis GPAT9 (At5g60620) as an essential gene
RT involved in triacylglycerol biosynthesis.";
RL Plant Physiol. 170:163-179(2016).
RN [12]
RP FUNCTION.
RX PubMed=31511316; DOI=10.1105/tpc.19.00121;
RA Karki N., Johnson B.S., Bates P.D.;
RT "Metabolically distinct pools of phosphatidylcholine are involved in
RT trafficking of fatty acids out of and into the chloroplast for membrane
RT production.";
RL Plant Cell 31:2768-2788(2019).
CC -!- FUNCTION: Lysophospholipid acyltransferase with broad specificity
CC (PubMed:18154737). Mediates the conversion of
CC lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine
CC or LPE) into phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-
CC phosphoethanolamine or PE) (LPEAT activity) (PubMed:18154737).
CC Catalyzes the acylation of lysophosphatidylserine (1-acyl-2-hydroxy-sn-
CC glycero-3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-
CC sn-glycero-3-phospho-L-serine or PS) (LPSAT activity)
CC (PubMed:18154737). Can convert lysophosphatidylcholine (1-acyl-sn-
CC glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-
CC sn-glycero-3-phosphocholine or PC) (LPCAT activity) (PubMed:18154737,
CC PubMed:24189065, PubMed:25268378). Exhibits preference for C18-
CC unsaturated acyl-CoA when transferring an acyl group to
CC lysophosphatidylcholine (PubMed:24189065, PubMed:25268378). Can also
CC utilize lysophosphatidylglycerol (LPG) as substrate in vitro
CC (PubMed:18154737). Has neither activity towards lysophosphatidic acid
CC (LPA) nor lysophosphatidylinositol (LPI) (PubMed:18154737).
CC Lysophospholipid acyltransferases catalyze the reacylation step of the
CC phospholipid remodeling pathway also known as the Lands cycle
CC (PubMed:18154737). The primary function of the Lands cycle is to
CC provide a route for acyl remodeling to modify fatty acid (FA)
CC composition of phospholipids derived from the Kennedy pathway
CC (PubMed:23150634, PubMed:22932756). Is involved in PC acyl editing and
CC phosphocholine headgroup exchange between PC and diacylglycerols. This
CC processes control the majority of acyl fluxes through PC to provide
CC polyunsaturated fatty acids for triacylglycerols synthesis in seeds
CC (PubMed:22932756, PubMed:24189065). Involved with LPCAT1 in the direct
CC incorporation of newly synthesized fatty acids exported form the
CC chloroplast into PC through acyl editing (PubMed:31511316).
CC {ECO:0000269|PubMed:18154737, ECO:0000269|PubMed:22932756,
CC ECO:0000269|PubMed:23150634, ECO:0000269|PubMed:24189065,
CC ECO:0000269|PubMed:25268378, ECO:0000269|PubMed:31511316}.
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:18154737, ECO:0000269|PubMed:24189065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12938;
CC Evidence={ECO:0000269|PubMed:18154737, ECO:0000269|PubMed:24189065};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + CoA; Xref=Rhea:RHEA:37387, ChEBI:CHEBI:28610, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:74669;
CC Evidence={ECO:0000269|PubMed:24189065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37388;
CC Evidence={ECO:0000269|PubMed:24189065};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphocholine = 1-(9Z)-octadecenoyl-2-(9Z,12Z)-octadecadienoyl-sn-
CC glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:37391,
CC ChEBI:CHEBI:28610, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:74670; Evidence={ECO:0000269|PubMed:24189065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37392;
CC Evidence={ECO:0000269|PubMed:24189065};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphocholine = 1-(9Z-octadecaenoyl)-2-(9Z,12Z,15Z-
CC octadecatrienoyl)-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:56408, ChEBI:CHEBI:28610, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:74034, ChEBI:CHEBI:86133;
CC Evidence={ECO:0000269|PubMed:24189065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56409;
CC Evidence={ECO:0000269|PubMed:24189065};
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:18154737};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32996;
CC Evidence={ECO:0000269|PubMed:18154737};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phospho-L-serine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:33191,
CC ChEBI:CHEBI:57262, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64379; EC=2.3.1.n6;
CC Evidence={ECO:0000269|PubMed:18154737};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33192;
CC Evidence={ECO:0000269|PubMed:18154737};
CC -!- SUBUNIT: Interacts with GPAT9 and DGAT1. {ECO:0000269|PubMed:26586834}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:22923678}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:22923678}.
CC -!- TISSUE SPECIFICITY: Expressed in rosette leaves, pollen grains,
CC developing embryos and developing seeds. {ECO:0000269|PubMed:23150634}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the double mutants lpcat1 and lpcat2-2 show increased
CC contents of very-long-chain fatty acids and decreased polyunsaturated
CC fatty acids in seed triacylglycerols. {ECO:0000269|PubMed:22233193,
CC ECO:0000269|PubMed:22932756, ECO:0000269|PubMed:23150634}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AC010795; AAG51612.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34045.1; -; Genomic_DNA.
DR EMBL; AY072080; AAL59903.1; -; mRNA.
DR EMBL; AY122979; AAM67512.1; -; mRNA.
DR PIR; G96655; G96655.
DR RefSeq; NP_176493.1; NM_104983.5.
DR AlphaFoldDB; Q9CAN8; -.
DR SMR; Q9CAN8; -.
DR BioGRID; 27829; 1.
DR IntAct; Q9CAN8; 1.
DR STRING; 3702.AT1G63050.1; -.
DR SwissLipids; SLP:000001898; -.
DR PaxDb; Q9CAN8; -.
DR PRIDE; Q9CAN8; -.
DR ProteomicsDB; 238690; -.
DR EnsemblPlants; AT1G63050.1; AT1G63050.1; AT1G63050.
DR GeneID; 842608; -.
DR Gramene; AT1G63050.1; AT1G63050.1; AT1G63050.
DR KEGG; ath:AT1G63050; -.
DR Araport; AT1G63050; -.
DR TAIR; locus:2015188; AT1G63050.
DR eggNOG; KOG2704; Eukaryota.
DR HOGENOM; CLU_011340_2_0_1; -.
DR InParanoid; Q9CAN8; -.
DR OMA; WAISIFE; -.
DR OrthoDB; 881262at2759; -.
DR PhylomeDB; Q9CAN8; -.
DR BioCyc; ARA:AT1G63050-MON; -.
DR BRENDA; 2.3.1.23; 399.
DR PRO; PR:Q9CAN8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CAN8; baseline and differential.
DR Genevisible; Q9CAN8; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IMP:TAIR.
DR GO; GO:0106262; F:1-acylglycerophosphoethanolamine O-acyltransferase activity; IEA:RHEA.
DR GO; GO:0106263; F:1-acylglycerophosphoserine O-acyltransferase activity; IEA:RHEA.
DR GO; GO:0016746; F:acyltransferase activity; IDA:TAIR.
DR GO; GO:0071617; F:lysophospholipid acyltransferase activity; IGI:TAIR.
DR GO; GO:0019375; P:galactolipid biosynthetic process; IGI:TAIR.
DR GO; GO:0045017; P:glycerolipid biosynthetic process; IMP:TAIR.
DR GO; GO:0030258; P:lipid modification; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IGI:TAIR.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IGI:TAIR.
DR GO; GO:0006641; P:triglyceride metabolic process; IMP:TAIR.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..465
FT /note="Lysophospholipid acyltransferase 2"
FT /id="PRO_0000425533"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 359
FT /evidence="ECO:0000250"
SQ SEQUENCE 465 AA; 52769 MW; 9A35E91B8277DCB3 CRC64;
MELLDMNSMA ASIGVSVAVL RFLLCFVATI PISFLWRFIP SRLGKHIYSA ASGAFLSYLS
FGFSSNLHFL VPMTIGYASM AIYRPLSGFI TFFLGFAYLI GCHVFYMSGD AWKEGGIDST
GALMVLTLKV ISCSINYNDG MLKEEGLREA QKKNRLIQMP SLIEYFGYCL CCGSHFAGPV
FEMKDYLEWT EEKGIWAVSE KGKRPSPYGA MIRAVFQAAI CMALYLYLVP QFPLTRFTEP
VYQEWGFLKR FGYQYMAGFT ARWKYYFIWS ISEASIIISG LGFSGWTDET QTKAKWDRAK
NVDILGVELA KSAVQIPLFW NIQVSTWLRH YVYERIVKPG KKAGFFQLLA TQTVSAVWHG
LYPGYIIFFV QSALMIDGSK AIYRWQQAIP PKMAMLRNVL VLINFLYTVV VLNYSSVGFM
VLSLHETLVA FKSVYYIGTV IPIAVLLLSY LVPVKPVRPK TRKEE
