LIPY_MYCTU
ID LIPY_MYCTU Reviewed; 437 AA.
AC I6Y2J4;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Triacylglycerol lipase {ECO:0000303|PubMed:16354661};
DE EC=3.1.1.3 {ECO:0000269|PubMed:16354661};
DE AltName: Full=Esterase/lipase {ECO:0000303|PubMed:16354661};
DE AltName: Full=Triolein hydrolase {ECO:0000305|PubMed:16354661};
DE Contains:
DE RecName: Full=Cytosolic triacylglycerol lipase {ECO:0000305};
DE Contains:
DE RecName: Full=Extracellular triacylglycerol lipase {ECO:0000305};
GN Name=lipY {ECO:0000303|PubMed:16354661};
GN Synonyms=PE-PGRS63 {ECO:0000303|PubMed:16354661};
GN OrderedLocusNames=Rv3097c;
GN ORFNames=LH57_16905 {ECO:0000312|EMBL:AIR15878.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RA Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J.,
RA Monaco A., King S., Sohrabi A.;
RT "Phylogenetic analysis of Mycobacterial species using whole genome
RT sequences.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, DISRUPTION PHENOTYPE, AND ACTIVE SITE.
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RX PubMed=16354661; DOI=10.1074/jbc.m505556200;
RA Deb C., Daniel J., Sirakova T.D., Abomoelak B., Dubey V.S.,
RA Kolattukudy P.E.;
RT "A novel lipase belonging to the hormone-sensitive lipase family induced
RT under starvation to utilize stored triacylglycerol in Mycobacterium
RT tuberculosis.";
RL J. Biol. Chem. 281:3866-3875(2006).
RN [4]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=17938218; DOI=10.1128/iai.00410-07;
RA Mishra K.C., de Chastellier C., Narayana Y., Bifani P., Brown A.K.,
RA Besra G.S., Katoch V.M., Joshi B., Balaji K.N., Kremer L.;
RT "Functional role of the PE domain and immunogenicity of the Mycobacterium
RT tuberculosis triacylglycerol hydrolase LipY.";
RL Infect. Immun. 76:127-140(2008).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=21471225; DOI=10.1074/jbc.m110.204966;
RA Daleke M.H., Cascioferro A., de Punder K., Ummels R., Abdallah A.M.,
RA van der Wel N., Peters P.J., Luirink J., Manganelli R., Bitter W.;
RT "Conserved Pro-Glu (PE) and Pro-Pro-Glu (PPE) protein domains target LipY
RT lipases of pathogenic mycobacteria to the cell surface via the ESX-5
RT pathway.";
RL J. Biol. Chem. 286:19024-19034(2011).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC STRAIN=H37Rv;
RX PubMed=23684389; DOI=10.1016/j.ijantimicag.2013.03.007;
RA Saxena A.K., Roy K.K., Singh S., Vishnoi S.P., Kumar A., Kashyap V.K.,
RA Kremer L., Srivastava R., Srivastava B.S.;
RT "Identification and characterisation of small-molecule inhibitors of
RT Rv3097c-encoded lipase (LipY) of Mycobacterium tuberculosis that
RT selectively inhibit growth of bacilli in hypoxia.";
RL Int. J. Antimicrob. Agents 42:27-35(2013).
RN [7]
RP FUNCTION IN VIRULENCE, AND OVEREXPRESSION.
RX PubMed=24631199; DOI=10.1016/j.tube.2014.02.001;
RA Singh V.K., Srivastava M., Dasgupta A., Singh M.P., Srivastava R.,
RA Srivastava B.S.;
RT "Increased virulence of Mycobacterium tuberculosis H37Rv overexpressing
RT LipY in a murine model.";
RL Tuberculosis 94:252-261(2014).
RN [8]
RP ACTIVITY REGULATION, SUBUNIT, AND DOMAIN.
RX PubMed=26270534; DOI=10.1371/journal.pone.0135447;
RA Garrett C.K., Broadwell L.J., Hayne C.K., Neher S.B.;
RT "Modulation of the activity of Mycobacterium tuberculosis LipY by its PE
RT domain.";
RL PLoS ONE 10:e0135447-e0135447(2015).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26398213; DOI=10.1371/journal.pone.0138151;
RA Cao J., Dang G., Li H., Li T., Yue Z., Li N., Liu Y., Liu S., Chen L.;
RT "Identification and characterization of lipase activity and immunogenicity
RT of LipL from Mycobacterium tuberculosis.";
RL PLoS ONE 10:E0138151-E0138151(2015).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=29986895; DOI=10.1128/iai.00394-18;
RA Santucci P., Diomande S., Poncin I., Alibaud L., Viljoen A., Kremer L.,
RA de Chastellier C., Canaan S.;
RT "Delineating the physiological roles of the PE and catalytic domains of
RT LipY in lipid consumption in Mycobacterium-infected foamy macrophages.";
RL Infect. Immun. 86:E00394-E00394(2018).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=31034693; DOI=10.1111/febs.14864;
RA Santucci P., Smichi N., Diomande S., Poncin I., Point V., Gaussier H.,
RA Cavalier J.F., Kremer L., Canaan S.;
RT "Dissecting the membrane lipid binding properties and lipase activity of
RT Mycobacterium tuberculosis LipY domains.";
RL FEBS J. 286:3164-3181(2019).
RN [12]
RP PROTEOLYTIC CLEAVAGE, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=31662454; DOI=10.1128/mbio.01951-19;
RA Burggraaf M.J., Speer A., Meijers A.S., Ummels R., van der Sar A.M.,
RA Korotkov K.V., Bitter W., Kuijl C.;
RT "Type VII secretion substrates of pathogenic Mycobacteria are processed by
RT a surface protease.";
RL MBio 10:E01951-E01951(2019).
CC -!- FUNCTION: Catalyzes the hydrolysis of both intracellular and
CC extracellular triacylglycerol (TAG) (PubMed:16354661, PubMed:17938218,
CC PubMed:21471225, PubMed:29986895, PubMed:31034693). In vitro, can also
CC hydrolyze p-nitrophenyl (pNP) esters with various chain lengths,
CC including pNP-acetate (C2), pNP-butyrate (C4), pNP-caproate (C6), pNP-
CC caprylate (C8), pNP-laurate (C12), pNP-myristate (C14), pNP-palmitate
CC (C16) and pNP-stearate (C18) (PubMed:23684389, PubMed:26398213). Also
CC hydrolyzes monobutyrin, tributyrin and trioctanoin (PubMed:29986895).
CC Overexpression results in increase of virulence characterized by
CC reduced survival of infected mouse and increased burden of bacilli in
CC the lungs (PubMed:24631199). Hydrolyzes internal or host-derived TAG
CC depending on its localization (PubMed:29986895).
CC {ECO:0000269|PubMed:16354661, ECO:0000269|PubMed:17938218,
CC ECO:0000269|PubMed:21471225, ECO:0000269|PubMed:23684389,
CC ECO:0000269|PubMed:24631199, ECO:0000269|PubMed:26398213,
CC ECO:0000269|PubMed:29986895, ECO:0000269|PubMed:31034693}.
CC -!- FUNCTION: [Cytosolic triacylglycerol lipase]: Hydrolyzes TAG that
CC accumulates within mycobacterial intracytosolic lipid inclusions (ILI)
CC (PubMed:29986895). Probably responsible for the utilization of stored
CC long-chain TAG during the dormancy and reactivation stages of the
CC pathogen (PubMed:16354661). {ECO:0000269|PubMed:16354661,
CC ECO:0000269|PubMed:29986895}.
CC -!- FUNCTION: [Extracellular triacylglycerol lipase]: Hydrolyzes host-
CC derived TAG. {ECO:0000269|PubMed:29986895}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC Evidence={ECO:0000269|PubMed:16354661};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-
CC octadecenoate + di-(9Z)-octadecenoylglycerol + H(+);
CC Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945;
CC Evidence={ECO:0000269|PubMed:16354661, ECO:0000269|PubMed:31034693};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+);
CC Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622;
CC Evidence={ECO:0000269|PubMed:26398213};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate +
CC H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477;
CC Evidence={ECO:0000269|PubMed:26398213};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a hexanoate ester + H2O = an aliphatic alcohol + H(+) +
CC hexanoate; Xref=Rhea:RHEA:47352, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:87656;
CC Evidence={ECO:0000269|PubMed:26398213};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) +
CC octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657;
CC Evidence={ECO:0000269|PubMed:26398213};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dodecanoate ester + H2O = an aliphatic alcohol + dodecanoate
CC + H(+); Xref=Rhea:RHEA:47364, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:87659;
CC Evidence={ECO:0000269|PubMed:26398213};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tetradecanoate ester + H2O = an aliphatic alcohol + H(+) +
CC tetradecanoate; Xref=Rhea:RHEA:47388, ChEBI:CHEBI:2571,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807,
CC ChEBI:CHEBI:87691; Evidence={ECO:0000269|PubMed:26398213};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoate ester = an aliphatic alcohol + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:47392, ChEBI:CHEBI:2571,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25835; Evidence={ECO:0000269|PubMed:26398213};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + octadecanoate ester = an aliphatic alcohol + H(+) +
CC octadecanoate; Xref=Rhea:RHEA:47396, ChEBI:CHEBI:2571,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629,
CC ChEBI:CHEBI:75925; Evidence={ECO:0000269|PubMed:23684389,
CC ECO:0000269|PubMed:26398213};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-butyrylglycerol + H2O = butanoate + glycerol + H(+);
CC Xref=Rhea:RHEA:44324, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:17968, ChEBI:CHEBI:76503;
CC Evidence={ECO:0000269|PubMed:29986895};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tributanoylglycerol + H2O = butanoate +
CC dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020,
CC ChEBI:CHEBI:76478; Evidence={ECO:0000269|PubMed:29986895,
CC ECO:0000269|PubMed:31034693};
CC -!- ACTIVITY REGULATION: [Cytosolic triacylglycerol lipase]: PE domain
CC down-regulates lipase activity. {ECO:0000269|PubMed:17938218,
CC ECO:0000269|PubMed:26270534, ECO:0000269|PubMed:29986895,
CC ECO:0000269|PubMed:31034693}.
CC -!- ACTIVITY REGULATION: [Extracellular triacylglycerol lipase]: Cleavage
CC by PecA does not affect surface localization and lipase activity.
CC {ECO:0000269|PubMed:31662454}.
CC -!- ACTIVITY REGULATION: Inhibited by diethyl-p-nitrophenyl phosphate (E-
CC 600) at 0.5 uM, by phenylmethanesulfonyl fluoride at 5 mM and by
CC polyethylene glycol sorbitan monolaurate (Tween 20). Also inhibited by
CC CaCl(2), CoCl(2), MnCl(2), ZnCl(2) and MgCl(2) (PubMed:16354661).
CC Inhibited by several hydrazides compounds (PubMed:23684389). Stimulated
CC slightly by SDS at concentrations up to 2 mM, above which the activity
CC is severely inhibited (PubMed:16354661). {ECO:0000269|PubMed:16354661,
CC ECO:0000269|PubMed:23684389}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.57 mM for triolein (glyceryl trioleate)
CC {ECO:0000269|PubMed:16354661};
CC Vmax=653.3 nmol/min/mg enzyme with triolein (glyceryl trioleate) as
CC substrate {ECO:0000269|PubMed:16354661};
CC pH dependence:
CC Optimum pH is between 8 and 9. {ECO:0000269|PubMed:16354661};
CC -!- SUBUNIT: [Cytosolic triacylglycerol lipase]: Forms aggregates via its
CC PE domain. {ECO:0000269|PubMed:26270534}.
CC -!- SUBCELLULAR LOCATION: [Cytosolic triacylglycerol lipase]: Cytoplasm
CC {ECO:0000269|PubMed:29986895}.
CC -!- SUBCELLULAR LOCATION: [Extracellular triacylglycerol lipase]: Secreted
CC {ECO:0000269|PubMed:21471225, ECO:0000269|PubMed:29986895,
CC ECO:0000269|PubMed:31034693, ECO:0000269|PubMed:31662454}. Secreted,
CC cell wall {ECO:0000269|PubMed:17938218, ECO:0000269|PubMed:29986895,
CC ECO:0000269|PubMed:31034693}. Cell surface
CC {ECO:0000269|PubMed:17938218, ECO:0000269|PubMed:21471225,
CC ECO:0000269|PubMed:29986895, ECO:0000269|PubMed:31034693,
CC ECO:0000269|PubMed:31662454}. Note=Exported to the cell surface via the
CC ESX-5 / type VII secretion system (T7SS). {ECO:0000269|PubMed:21471225,
CC ECO:0000269|PubMed:31034693, ECO:0000269|PubMed:31662454}.
CC -!- DOMAIN: Contains an N-terminal PE domain and a C-terminal catalytic
CC domain, which are connected by a linker region (PubMed:17938218). The
CC PE domain is involved in aggregation and activity regulation
CC (PubMed:26270534). It is also required for ESX-5-dependent secretion
CC (PubMed:21471225). After transport, the PE domain is removed by
CC proteolytic cleavage (PubMed:21471225). {ECO:0000269|PubMed:17938218,
CC ECO:0000269|PubMed:21471225, ECO:0000269|PubMed:26270534}.
CC -!- PTM: Upon export, the PE domain is removed by proteolytic cleavage
CC (PubMed:21471225, PubMed:31662454). Cleavage occurs at the cell surface
CC and is not required for secretion (PubMed:31662454). Cleaved after Gly-
CC 149 by the aspartic protease PecA. May also be cleaved before Leu-98
CC and after Ala-136 (PubMed:31662454). {ECO:0000269|PubMed:21471225,
CC ECO:0000269|PubMed:31662454}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a drastically
CC diminished ability to hydrolyze stored long-chain triacylglycerol.
CC {ECO:0000269|PubMed:16354661}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the mycobacterial PE
CC family. PGRS subfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the 'GDXG' lipolytic
CC enzyme family. {ECO:0000305}.
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; CP009480; AIR15878.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP45906.1; -; Genomic_DNA.
DR RefSeq; WP_003912072.1; NZ_NVQJ01000011.1.
DR RefSeq; YP_177924.1; NC_000962.3.
DR AlphaFoldDB; I6Y2J4; -.
DR SMR; I6Y2J4; -.
DR STRING; 83332.Rv3097c; -.
DR SwissLipids; SLP:000001333; -.
DR ESTHER; myctu-Rv3097c; Hormone-sensitive_lipase_like.
DR PaxDb; I6Y2J4; -.
DR DNASU; 888677; -.
DR GeneID; 888677; -.
DR KEGG; mtu:Rv3097c; -.
DR PATRIC; fig|83332.111.peg.3450; -.
DR TubercuList; Rv3097c; -.
DR eggNOG; COG0657; Bacteria.
DR HOGENOM; CLU_036802_0_0_11; -.
DR OMA; FHWINYS; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008126; F:acetylesterase activity; IEA:RHEA.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR000084; PE-PGRS_N.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR Pfam; PF00934; PE; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Cell wall; Cytoplasm; Hydrolase; Lipid degradation; Lipid metabolism;
KW Reference proteome; Secreted; Virulence.
FT CHAIN 1..437
FT /note="Cytosolic triacylglycerol lipase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000449879"
FT CHAIN 150..437
FT /note="Extracellular triacylglycerol lipase"
FT /evidence="ECO:0000305|PubMed:21471225"
FT /id="PRO_0000438268"
FT DOMAIN 1..100
FT /note="PE"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:17938218"
FT REGION 101..206
FT /note="Linker"
FT /evidence="ECO:0000305|PubMed:17938218"
FT REGION 207..437
FT /note="Lipase"
FT /evidence="ECO:0000305|PubMed:17938218"
FT MOTIF 239..241
FT /note="Involved in the stabilization of the negatively
FT charged intermediate by the formation of the oxyanion hole"
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 309
FT /evidence="ECO:0000305|PubMed:16354661"
FT ACT_SITE 383
FT /evidence="ECO:0000250|UniProtKB:O06350"
FT ACT_SITE 413
FT /evidence="ECO:0000250|UniProtKB:O06350"
FT SITE 149..150
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:21471225"
SQ SEQUENCE 437 AA; 45023 MW; BE37EA4F33E95243 CRC64;
MVSYVVALPE VMSAAATDVA SIGSVVATAS QGVAGATTTV LAAAEDEVSA AIAALFSGHG
QDYQALSAQL AVFHERFVQA LTGAAKGYAA AELANASLLQ SEFASGIGNG FATIHQEIQR
APTALAAGFT QVPPFAAAQA GIFTGTPSGA AGFDIASLWP VKPLLSLSAL ETHFAIPNNP
LLALIASDIP PLSWFLGNSP PPLLNSLLGQ TVQYTTYDGM SVVQITPAHP TGEYVVAIHG
GAFILPPSIF HWLNYSVTAY QTGATVQVPI YPLVQEGGTA GTVVPAMAGL ISTQIAQHGV
SNVSVVGDSA GGNLALAAAQ YMVSQGNPVP SSMVLLSPWL DVGTWQISQA WAGNLAVNDP
LVSPLYGSLN GLPPTYVYSG SLDPLAQQAV VLEHTAVVQG APFSFVLAPW QIHDWILLTP
WGLLSWPQIN QQLGIAA
