MBOA6_DROME
ID MBOA6_DROME Reviewed; 722 AA.
AC Q6NN55; A0A0B4LG01;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Lysophospholipid acyltransferase 6;
DE Short=LPLAT 6;
DE EC=2.3.1.- {ECO:0000269|PubMed:19864461};
DE EC=2.3.1.23 {ECO:0000269|PubMed:19864461};
DE EC=2.3.1.n6 {ECO:0000269|PubMed:19864461};
DE EC=2.3.1.n7 {ECO:0000269|PubMed:19864461};
DE AltName: Full=Membrane-bound acyltransferase 6;
DE Short=MBOA 6;
DE AltName: Full=Oysgedart {ECO:0000303|PubMed:19864461};
DE Short=Oys {ECO:0000303|PubMed:19864461};
GN Name=oys {ECO:0000303|PubMed:19864461, ECO:0000312|EMBL:AAF58858.1,
GN ECO:0000312|FlyBase:FBgn0033476};
GN ORFNames=CG18445 {ECO:0000312|EMBL:AAR99097.1,
GN ECO:0000312|FlyBase:FBgn0033476};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAR99097.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAR99097.1};
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K., Yu C., Rubin G.M., Celniker S.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBCELLULAR LOCATION.
RX PubMed=19864461; DOI=10.1091/mbc.e09-05-0382;
RA Steinhauer J., Gijon M.A., Riekhof W.R., Voelker D.R., Murphy R.C.,
RA Treisman J.E.;
RT "Drosophila lysophospholipid acyltransferases are specifically required for
RT germ cell development.";
RL Mol. Biol. Cell 20:5224-5235(2009).
CC -!- FUNCTION: Acyltransferase with broad-specificity, that mediates the
CC acylation of lysophospholipids to produce phospholipids
CC (glycerophospholipids). Converts lysophosphatidylserine (1-acyl-2-
CC hydroxy-sn-glycero-3-phospho-L-serine or LPS) to phosphatidylserine
CC (1,2-diacyl-sn-glycero-3-phospho-L-serine or PS) (LPSAT activity),
CC lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) to
CC phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC)
CC (LPCAT activity), also lysophosphatidylethanolamine (1-acyl-sn-glycero-
CC 3-phosphochethanolamine or LPE) to phosphatidylchethanolamine (LPEAT
CC activity) and lysophosphatidylglycerol (1-acyl-2-hydroxy-sn-glycero-3-
CC phospho-(1'-sn-glycerol) or LPG) to phosphatidylglycerol (1,2-diacyl-
CC sn-glycero-3-phospho-(1'-sn-glycerol) or PG) (LPGAT activity). Has a
CC preference for unsaturated fatty acids of at least 16 carbons such as
CC oleoyl-CoA ((9Z)-octadecenoyl-CoA) and palmitoleoyl-CoA ((9Z)-
CC hexadecenoyl-CoA). Glycerophospholipids are important structural and
CC functional components of cellular membrane, acyl-chain remodeling
CC regulates the molecular species distribution of glycerophospholipids
CC which can affect membrane fluidity and curvature. Essential for
CC fertility and viability together with Nessy protein (Nes).
CC {ECO:0000269|PubMed:19864461}.
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:19864461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33192;
CC Evidence={ECO:0000269|PubMed:19864461};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-L-serine = 1-(9Z-octadecenoyl)-2-(9Z-hexadecenoyl)-sn-
CC glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:37399,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:61540, ChEBI:CHEBI:74617,
CC ChEBI:CHEBI:74901; Evidence={ECO:0000269|PubMed:19864461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37400;
CC Evidence={ECO:0000269|PubMed:19864461};
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:19864461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37408;
CC Evidence={ECO:0000269|PubMed:19864461};
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:19864461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12938;
CC Evidence={ECO:0000269|PubMed:19864461};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:35991, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001;
CC Evidence={ECO:0000269|PubMed:19864461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35992;
CC Evidence={ECO:0000269|PubMed:19864461};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z-hexadecenoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37207, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:61540, ChEBI:CHEBI:72998, ChEBI:CHEBI:74000;
CC Evidence={ECO:0000269|PubMed:19864461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37208;
CC Evidence={ECO:0000269|PubMed:19864461};
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:19864461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32996;
CC Evidence={ECO:0000269|PubMed:19864461};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphoethanolamine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:36015, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:73004, ChEBI:CHEBI:73007;
CC Evidence={ECO:0000269|PubMed:19864461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36016;
CC Evidence={ECO:0000269|PubMed:19864461};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:36019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:73004,
CC ChEBI:CHEBI:73008; Evidence={ECO:0000269|PubMed:19864461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36020;
CC Evidence={ECO:0000269|PubMed:19864461};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphoethanolamine = 1-hexadecanoyl-2-(9Z)-hexadecenoyl-sn-glycero-
CC 3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:37419, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:61540, ChEBI:CHEBI:73004, ChEBI:CHEBI:73999;
CC Evidence={ECO:0000269|PubMed:19864461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37420;
CC Evidence={ECO:0000269|PubMed:19864461};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-(1'-sn-glycerol) = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-(1'-sn-glycerol) + CoA; Xref=Rhea:RHEA:37651,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:72828,
CC ChEBI:CHEBI:75163; Evidence={ECO:0000269|PubMed:19864461};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37652;
CC Evidence={ECO:0000269|PubMed:19864461};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000269|PubMed:19864461}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:19864461}. Membrane {ECO:0000269|PubMed:19864461};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=A,B,E;
CC IsoId=Q6NN55-1; Sequence=Displayed;
CC Name=D;
CC IsoId=Q6NN55-2; Sequence=VSP_061130;
CC -!- MISCELLANEOUS: 'Oysgedart' is a Yiddish word meaning skinny, chosen
CC because of this protein's role in phospholipid synthesis.
CC {ECO:0000303|PubMed:19864461}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AE013599; AAF58858.1; -; Genomic_DNA.
DR EMBL; AE013599; AHN56063.1; -; Genomic_DNA.
DR EMBL; AE013599; AHN56065.1; -; Genomic_DNA.
DR EMBL; AE013599; AHN56064.1; -; Genomic_DNA.
DR EMBL; BT011439; AAR99097.1; -; mRNA.
DR RefSeq; NP_001286265.1; NM_001299336.1. [Q6NN55-1]
DR RefSeq; NP_001286266.1; NM_001299337.1. [Q6NN55-2]
DR RefSeq; NP_001286267.1; NM_001299338.1. [Q6NN55-1]
DR RefSeq; NP_610546.1; NM_136702.3. [Q6NN55-1]
DR AlphaFoldDB; Q6NN55; -.
DR SMR; Q6NN55; -.
DR STRING; 7227.FBpp0087520; -.
DR SwissLipids; SLP:000001063; -.
DR PaxDb; Q6NN55; -.
DR PRIDE; Q6NN55; -.
DR DNASU; 36045; -.
DR EnsemblMetazoa; FBtr0088434; FBpp0087520; FBgn0033476. [Q6NN55-1]
DR EnsemblMetazoa; FBtr0339416; FBpp0308504; FBgn0033476. [Q6NN55-1]
DR EnsemblMetazoa; FBtr0345629; FBpp0311693; FBgn0033476. [Q6NN55-2]
DR EnsemblMetazoa; FBtr0345630; FBpp0311694; FBgn0033476. [Q6NN55-1]
DR GeneID; 36045; -.
DR KEGG; dme:Dmel_CG18445; -.
DR UCSC; CG18445-RA; d. melanogaster. [Q6NN55-1]
DR CTD; 36045; -.
DR FlyBase; FBgn0033476; oys.
DR VEuPathDB; VectorBase:FBgn0033476; -.
DR eggNOG; KOG2704; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_011340_4_0_1; -.
DR InParanoid; Q6NN55; -.
DR OMA; WHGTRPG; -.
DR OrthoDB; 881262at2759; -.
DR PhylomeDB; Q6NN55; -.
DR Reactome; R-DME-1482788; Acyl chain remodelling of PC.
DR Reactome; R-DME-1482801; Acyl chain remodelling of PS.
DR Reactome; R-DME-1482839; Acyl chain remodelling of PE.
DR UniPathway; UPA00085; -.
DR BioGRID-ORCS; 36045; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36045; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033476; Expressed in embryonic/larval hemocyte (Drosophila) and 28 other tissues.
DR ExpressionAtlas; Q6NN55; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:FlyBase.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0071617; F:lysophospholipid acyltransferase activity; IDA:FlyBase.
DR GO; GO:0008354; P:germ cell migration; IGI:FlyBase.
DR GO; GO:0030258; P:lipid modification; IMP:FlyBase.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0007009; P:plasma membrane organization; IGI:FlyBase.
DR GO; GO:0007291; P:sperm individualization; IGI:FlyBase.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative initiation; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..722
FT /note="Lysophospholipid acyltransferase 6"
FT /id="PRO_0000453372"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 485..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 349
FT /evidence="ECO:0000250|UniProtKB:P0C7A3"
FT ACT_SITE 381
FT /evidence="ECO:0000250|UniProtKB:P0C7A3"
FT VAR_SEQ 1..30
FT /note="MLEPPKFIENDCYNGSRTFTWLADMVGLSV -> MCSASADGSK (in
FT isoform D)"
FT /id="VSP_061130"
SQ SEQUENCE 722 AA; 81221 MW; CB4E84FA6720E367 CRC64;
MLEPPKFIEN DCYNGSRTFT WLADMVGLSV DLVNFLICQI SALFLASLFR SMLHPSKVSS
KLRHTFALSI GLAFGYFCFG QQAIHIAGLP AICYIVIRTQ DPRIVQRAVL LVAMSYLLCV
HLMRQLYDYG SYALDITGPL MIITQKVTSL AFSIHDGFVR GDEELTKAQQ YHAIRKMPSA
LEYFSYVWHF QSILAGPLVF YKDYIEFVEG YNLLSTPPGN GNLDSSKREV VLEPSPTKAV
IRKVVGSLVC AFIFMKFVKI YPVKDMKEDD FMNNTSMVYK YWYAMMATTC IRFKYYHAWL
LADAICNNSG LGFTGYDKDG NSKWDLISNI NVLSFEFSTN MRDAINNWNC GTNRWLRTLV
YERVPQQYGT LLTFALSAVW HGFYPGYYLT FATGAVVVTA ARTGRRLFRH RFQSTQVTRM
FYDILTCLIT RVVLGYATFP FVLLEFMGSI KLYLRFYLCL HIISLVTIFI LPKFIRGERR
LRTSNGNGNV RLSGSGNTKD AVTTSVESTA ALTAGNDLNE DKEEDKHAQC KVHTPTQQQP
AAGPHKTTVE QPTEQPNNVN LRSRPQQQQP HLEKKAMPPT CARDAVSVPH DQCEMDQLSS
KLKEKIEAET KNIEEFIDKT VTETVSGIVE FKNDLMRDIE FPKLKLPGSN GAISLDSSNG
GGLRKRNISS VHDNGTDPGH ATADLHPPLE ENGAAFLKKE IEVINAVVQQ AVPAVLSNGH
AK
