ID A0A1J1IPB4_9DIPT Unreviewed; 1395 AA.
AC A0A1J1IPB4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Diacylglycerol O-acyltransferase 1 {ECO:0000256|ARBA:ARBA00022158};
DE EC=2.3.1.20 {ECO:0000256|ARBA:ARBA00013244};
DE EC=2.3.1.76 {ECO:0000256|ARBA:ARBA00012977};
DE AltName: Full=Acyl-CoA retinol O-fatty-acyltransferase {ECO:0000256|ARBA:ARBA00033044};
DE AltName: Full=Diglyceride acyltransferase {ECO:0000256|ARBA:ARBA00030205};
GN ORFNames=CLUMA_CG014426 {ECO:0000313|EMBL:CRL01570.1};
OS Clunio marinus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Clunio.
OX NCBI_TaxID=568069 {ECO:0000313|EMBL:CRL01570.1, ECO:0000313|Proteomes:UP000183832};
RN [1] {ECO:0000313|EMBL:CRL01570.1, ECO:0000313|Proteomes:UP000183832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + 1,2-di-(9Z-octadecenoyl)-glycerol + H(+)
CC = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O; Xref=Rhea:RHEA:38379,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:52323, ChEBI:CHEBI:53753;
CC Evidence={ECO:0000256|ARBA:ARBA00000645};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38380;
CC Evidence={ECO:0000256|ARBA:ARBA00000645};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1,2-di-(9Z-octadecenoyl)-sn-glycerol =
CC 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38219,
CC ChEBI:CHEBI:52333, ChEBI:CHEBI:53753, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387; Evidence={ECO:0000256|ARBA:ARBA00000389};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38220;
CC Evidence={ECO:0000256|ARBA:ARBA00000389};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1,3-di-(9Z-octadecenoyl)-glycerol =
CC 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38435,
CC ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:75735; Evidence={ECO:0000256|ARBA:ARBA00000883};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38436;
CC Evidence={ECO:0000256|ARBA:ARBA00000883};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-glycerol = 1,2-di-
CC (9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:37915,
CC ChEBI:CHEBI:52323, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:75342; Evidence={ECO:0000256|ARBA:ARBA00001009};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37916;
CC Evidence={ECO:0000256|ARBA:ARBA00001009};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecenyl)-glycerol = 1-O-
CC (9Z-octadecyl)-3-(9Z-octadecenoyl)-glycerol + CoA;
CC Xref=Rhea:RHEA:55340, ChEBI:CHEBI:34116, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:197429;
CC Evidence={ECO:0000256|ARBA:ARBA00043738};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55341;
CC Evidence={ECO:0000256|ARBA:ARBA00043738};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecyl)-3-(9Z-
CC octadecenoyl)-glycerol = 1-O-(9Z-octadecenyl)-2,3-di-(9Z-
CC octadecenoyl)glycerol + CoA; Xref=Rhea:RHEA:55344, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:138735, ChEBI:CHEBI:197429;
CC Evidence={ECO:0000256|ARBA:ARBA00043821};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55345;
CC Evidence={ECO:0000256|ARBA:ARBA00043821};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycerol = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-3-(9Z)-octadecenoyl-sn-glycerol + CoA;
CC Xref=Rhea:RHEA:38307, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:75728, ChEBI:CHEBI:75729;
CC Evidence={ECO:0000256|ARBA:ARBA00001100};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38308;
CC Evidence={ECO:0000256|ARBA:ARBA00001100};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 2,3-di-(9Z)-octadecenoyl-sn-glycerol =
CC 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:38439,
CC ChEBI:CHEBI:53753, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:75824; Evidence={ECO:0000256|ARBA:ARBA00001338};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38440;
CC Evidence={ECO:0000256|ARBA:ARBA00001338};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 2-(9Z-octadecenoyl)-glycerol = 1,2-di-
CC (9Z-octadecenoyl)-sn-glycerol + CoA; Xref=Rhea:RHEA:37911,
CC ChEBI:CHEBI:52333, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:73990; Evidence={ECO:0000256|ARBA:ARBA00001793};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37912;
CC Evidence={ECO:0000256|ARBA:ARBA00001793};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + hexadecanoyl-CoA = 1,2-
CC di-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol + CoA;
CC Xref=Rhea:RHEA:38163, ChEBI:CHEBI:52333, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:75583;
CC Evidence={ECO:0000256|ARBA:ARBA00001349};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38164;
CC Evidence={ECO:0000256|ARBA:ARBA00001349};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13-cis-retinol + hexadecanoyl-CoA = 13-cis-retinyl
CC hexadecanoate + CoA; Xref=Rhea:RHEA:55296, ChEBI:CHEBI:45479,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:138722;
CC Evidence={ECO:0000256|ARBA:ARBA00000895};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55297;
CC Evidence={ECO:0000256|ARBA:ARBA00000895};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-glycerol + hexadecanoyl-CoA = 1-
CC hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CoA;
CC Xref=Rhea:RHEA:38071, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:73990, ChEBI:CHEBI:75466;
CC Evidence={ECO:0000256|ARBA:ARBA00001313};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38072;
CC Evidence={ECO:0000256|ARBA:ARBA00001313};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol
CC + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20;
CC Evidence={ECO:0000256|ARBA:ARBA00001150};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10869;
CC Evidence={ECO:0000256|ARBA:ARBA00001150};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + an acyl-CoA = an all-trans-retinyl ester +
CC CoA; Xref=Rhea:RHEA:11488, ChEBI:CHEBI:17336, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:63410; EC=2.3.1.76;
CC Evidence={ECO:0000256|ARBA:ARBA00000633};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11489;
CC Evidence={ECO:0000256|ARBA:ARBA00000633};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinol + hexadecanoyl-CoA = all-trans-retinyl
CC hexadecanoate + CoA; Xref=Rhea:RHEA:38175, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:17616, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379;
CC Evidence={ECO:0000256|ARBA:ARBA00001764};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38176;
CC Evidence={ECO:0000256|ARBA:ARBA00001764};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecan-1-ol + hexadecanoyl-CoA = CoA + hexadecanyl
CC hexadecanoate; Xref=Rhea:RHEA:38167, ChEBI:CHEBI:16125,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:75584;
CC Evidence={ECO:0000256|ARBA:ARBA00001796};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38168;
CC Evidence={ECO:0000256|ARBA:ARBA00001796};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecane-1,2-diol + 2 hexadecanoyl-CoA = 1,2-O,O-
CC dihexadecanoyl-1,2-hexadecanediol + 2 CoA; Xref=Rhea:RHEA:38211,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:75586,
CC ChEBI:CHEBI:75608; Evidence={ECO:0000256|ARBA:ARBA00001118};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38212;
CC Evidence={ECO:0000256|ARBA:ARBA00001118};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecane-1,2-diol + hexadecanoyl-CoA = 2-hydroxyhexadecyl
CC hexadecanoate + CoA; Xref=Rhea:RHEA:38171, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:75586, ChEBI:CHEBI:75587;
CC Evidence={ECO:0000256|ARBA:ARBA00000174};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38172;
CC Evidence={ECO:0000256|ARBA:ARBA00000174};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000256|ARBA:ARBA00005175}.
CC -!- SUBUNIT: Homodimer or homotetramer; both forms have similar enzymatic
CC activities. {ECO:0000256|ARBA:ARBA00023610}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Endoplasmic
CC reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC Sterol o-acyltransferase subfamily. {ECO:0000256|ARBA:ARBA00009010}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CVRI01000055; CRL01570.1; -; Genomic_DNA.
DR STRING; 568069.A0A1J1IPB4; -.
DR OrthoDB; 9612at2759; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000183832; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0050252; F:retinol O-fatty-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IEA:InterPro.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR027251; Diacylglycerol_acylTrfase1.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR004299; MBOAT_fam.
DR InterPro; IPR014371; Oat_ACAT_DAG_ARE.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR10408:SF7; DIACYLGLYCEROL O-ACYLTRANSFERASE 1; 1.
DR PANTHER; PTHR10408; STEROL O-ACYLTRANSFERASE; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF03062; MBOAT; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PIRSF; PIRSF000439; Oat_ACAT_DAG_ARE; 1.
DR PIRSF; PIRSF500231; Oat_dag; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000183832};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT TRANSMEM 60..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 399..416
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 428..445
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 457..478
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 547..729
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 776..987
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 1058..1349
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 417
FT /evidence="ECO:0000256|PIRSR:PIRSR000439-1"
FT BINDING 839
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
SQ SEQUENCE 1395 AA; 161972 MW; 7180F2B1F2CE6CF1 CRC64;
MGNDNDDHHV RLRRTQSVTR AEEITTSEQK QRKSQPDKPI HKPRDSLFSW SSNFNDFSGL
VNWGFLLLTM GGIRLLLENF IKYGIRVDPM QWFNVLTGKD EGDASYPSIV LGMYATVPIV
ICLIIEKGLS VEIIAETSGR MAHVFNLVVL LMIPIVVIYL RGTSFALIGS VGICVLYSIL
FMKLWSYVQV NLWCRMSQKQ HKNSISGKRR ESFSIDRRRE SEDFNGNALP NGYTEHHQPP
TLVKYPDNLS LKDLFYFLCA PTLCYELNFP RTTRIRKRFL IKRLVEFVVG VNIVMALFQQ
WMIPSVKNSL VPFSNMEFTK ATERLLKLAI PNHFIWLCLF YLTFHSFLNL LGEILHFADR
NFYCDWWNSN NVDVFWRTWN MPVHRWCVRH LYIPIVDMGY NKTVASIIVF FVSAFFHEYL
VSVPLKTFKI WAFMGMMAQI PLSFISKFLE TNMGERWGNV LVWASLILGQ PLCILVYYHD
YVIQNFNHIE KEFSNFNSML EKENSFDFSK YLKGNLNVNH LKGKIFKSED SEKIFERNLR
LPNDTIPLHY NLRLRTNIHN NDPDYHGDVR IKFQVLEPTD TITIHSTNVI RWIDLFNGPD
IEIFNLPFTM NHFFNLLIIR IPRLLNPQEE RTLRIEFSGQ ITDSIRGFYR TSYRRQSGEL
APLASTFLHP IFARNVFPCY DEIRYRTSFD LAIEHHVTYN AVSNMPVLSR VPTDFGFITT
TFETTPMMPI SALAFTISDF TSVTNENENL PMSVWANPFL IGDGRADNGL LLHEQTWNTL
EGIFNISFSL PKSDVILIPT SFIDSVNWGL IGLPENWVIT GSFEDPPELG IIFANKNAHQ
YFGNLVSQSS WAYSWLSTGV SKLYENIVID IINPERHQWE HFLIDFLDIM FQLDTFNFLP
PLNRYPESDQ EIIRKFDVPD EVKGAIILRM LKEALGDEIF TEGVREYLLD MQYKSASPDD
LFRNVQKVYD VLSPGNNVDL GLMMTPWLEV SGFPLLTVQR TENGLKLKQE TFQQVHNELF
NIPISFTTSK ALDFDNTTTN LWMTAEEMDL NVDNDIDWGI FNLRDTSFYL TNYDDQLWRG
INNALNNDHE AIHFLNRGTL FADFSRFFQE DFHISSVVFL EMMRSLRLEF HPHVWNRATS
GMILKQLRLR GSEFDEDHTN FMKNLMTTVY GRFPVEWSSP WNDIIAAQSV TFFSCFSGVE
LCREDAMNAL IQYLETGVTS VPYEFQCSAL MGANETIWTM VLDNALETGN TSVIQSNLAR
LSCSQDKLLI ETLINIILDP TIDLIQDQFR HFMFSSVLLN SNLASYEAVI DTVETRYEEL
EAVGVNILTV LFNAAFVTNT EQQAERFLNI LSQHSPWPIE QEQIEFVINR NIEYVQRNAE
ELREWYASLA EIQNS
//
