ID   LPP60_RAT               Reviewed;         564 AA.
AC   O88202; Q4G088;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-NOV-2023, entry version 151.
DE   RecName: Full=60 kDa lysophospholipase;
DE            EC=3.1.1.5 {ECO:0000269|PubMed:10320809, ECO:0000269|PubMed:8119970, ECO:0000269|PubMed:9575212};
DE   AltName: Full=Lysophospholipase-transacylase {ECO:0000303|PubMed:10320809, ECO:0000303|PubMed:8119970, ECO:0000303|PubMed:9575212};
DE   Includes:
DE     RecName: Full=L-asparaginase;
DE              EC=3.5.1.1 {ECO:0000269|PubMed:9575212};
DE     AltName: Full=L-asparagine amidohydrolase;
DE   Includes:
DE     RecName: Full=1-alkyl-2-acetylglycerophosphocholine esterase;
DE              EC=3.1.1.47 {ECO:0000269|PubMed:9575212};
DE     AltName: Full=Platelet-activating factor acetylhydrolase {ECO:0000303|PubMed:9575212};
DE              Short=PAF acetylhydrolase {ECO:0000303|PubMed:9575212};
GN   Name=Aspg;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000312|EMBL:BAA31197.1};
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAA31197.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 226-233 AND 428-440, TISSUE
RP   SPECIFICITY, FUNCTION, AND CATALYTIC ACTIVITY.
RC   TISSUE=Liver;
RX   PubMed=9575212; DOI=10.1074/jbc.273.20.12536;
RA   Sugimoto H., Odani S., Yamashita S.;
RT   "Cloning and expression of cDNA encoding rat liver 60-kDa lysophospholipase
RT   containing an asparaginase-like region and ankyrin repeat.";
RL   J. Biol. Chem. 273:12536-12542(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   ACTIVITY REGULATION.
RX   PubMed=8119970; DOI=10.1016/s0021-9258(17)37595-6;
RA   Sugimoto H., Yamashita S.;
RT   "Purification, characterization, and inhibition by phosphatidic acid of
RT   lysophospholipase transacylase from rat liver.";
RL   J. Biol. Chem. 269:6252-6258(1994).
RN   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=10320809; DOI=10.1016/s1388-1981(99)00059-1;
RA   Sugimoto H., Yamashita S.;
RT   "Characterization of the transacylase activity of rat liver 60-kDa
RT   lysophospholipase-transacylase. Acyl transfer from the sn-2 to the sn-1
RT   position.";
RL   Biochim. Biophys. Acta 1438:264-272(1999).
CC   -!- FUNCTION: Exhibits lysophospholipase, transacylase, PAF acetylhydrolase
CC       and asparaginase activities (PubMed:9575212, PubMed:8119970,
CC       PubMed:10320809). Can catalyze three types of transacylation reactions:
CC       (1) acyl transfer from 1-acyl-sn-glycero-3-phosphocholine (1-acyl-GPC)
CC       to the sn-1(3) positions of glycerol and 2-acylglycerol (sn-1 to -1(3)
CC       transfer), (2) acyl transfer from 1-acyl-GPC to the sn-2 positions of
CC       1-acyl-GPC, 1-acyl-sn-glycero-3-phosphoethanolamine (1-acyl-GPE), and
CC       other lysophospholipids (sn-1 to -2 transfer) and (3) acyl transfer
CC       from 2-acyl-GPC to the sn-1 position of 2-acyl-GPC and 2-acyl-GPE (sn-2
CC       to -1 transfer) (PubMed:10320809). Mediates the synthesis of 1-
CC       arachidonoyl species of phospholipids by transferring the arachidonoyl
CC       residue from 2-arachidonoyl lysophospholipid to the sn-1 position of 2-
CC       acyl lysophospholipid (PubMed:10320809). {ECO:0000269|PubMed:10320809,
CC       ECO:0000269|PubMed:8119970, ECO:0000269|PubMed:9575212}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC         H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC         Evidence={ECO:0000269|PubMed:10320809, ECO:0000269|PubMed:8119970,
CC         ECO:0000269|PubMed:9575212};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC         Evidence={ECO:0000305|PubMed:10320809, ECO:0000305|PubMed:8119970,
CC         ECO:0000305|PubMed:9575212};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-asparagine = L-aspartate + NH4(+);
CC         Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1;
CC         Evidence={ECO:0000269|PubMed:9575212};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21017;
CC         Evidence={ECO:0000305|PubMed:9575212};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-
CC         alkyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC         Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47;
CC         Evidence={ECO:0000269|PubMed:9575212};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778;
CC         Evidence={ECO:0000305|PubMed:9575212};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC         hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC         ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC         Evidence={ECO:0000269|PubMed:8119970, ECO:0000269|PubMed:9575212};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC         Evidence={ECO:0000305|PubMed:8119970, ECO:0000305|PubMed:9575212};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 1-hexadecanoyl-sn-glycero-3-phosphocholine = 1,2-
CC         dihexadecanoyl-sn-glycero-3-phosphocholine + sn-glycerol 3-
CC         phosphocholine; Xref=Rhea:RHEA:40879, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC         Evidence={ECO:0000269|PubMed:10320809, ECO:0000269|PubMed:8119970};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40880;
CC         Evidence={ECO:0000305|PubMed:10320809, ECO:0000305|PubMed:8119970};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-octadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC         octadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40887,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:25629, ChEBI:CHEBI:73858;
CC         Evidence={ECO:0000269|PubMed:8119970};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40888;
CC         Evidence={ECO:0000305|PubMed:8119970};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-
CC         octadecenoate + H(+) + sn-glycerol 3-phosphocholine;
CC         Xref=Rhea:RHEA:40807, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16870, ChEBI:CHEBI:28610, ChEBI:CHEBI:30823;
CC         Evidence={ECO:0000269|PubMed:8119970};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40808;
CC         Evidence={ECO:0000305|PubMed:8119970};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H2O = H(+) +
CC         hexadecanoate + sn-glycero-3-phosphoethanolamine;
CC         Xref=Rhea:RHEA:40891, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:73004, ChEBI:CHEBI:143890;
CC         Evidence={ECO:0000269|PubMed:8119970};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40892;
CC         Evidence={ECO:0000305|PubMed:8119970};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O =
CC         (9Z)-octadecenoate + H(+) + sn-glycero-3-phosphoethanolamine;
CC         Xref=Rhea:RHEA:40895, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:74971, ChEBI:CHEBI:143890;
CC         Evidence={ECO:0000269|PubMed:8119970};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40896;
CC         Evidence={ECO:0000305|PubMed:8119970};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + 1-hexadecanoyl-
CC         sn-glycero-3-phosphoethanolamine = 1,2-dihexadecanoyl-sn-glycero-3-
CC         phosphoethanolamine + sn-glycerol 3-phosphocholine;
CC         Xref=Rhea:RHEA:40899, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998,
CC         ChEBI:CHEBI:73004, ChEBI:CHEBI:73005;
CC         Evidence={ECO:0000269|PubMed:10320809};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40900;
CC         Evidence={ECO:0000305|PubMed:10320809};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine
CC         + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + sn-glycerol 3-
CC         phosphocholine; Xref=Rhea:RHEA:40827, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:32395,
CC         ChEBI:CHEBI:76079; Evidence={ECO:0000269|PubMed:10320809};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40828;
CC         Evidence={ECO:0000305|PubMed:10320809};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC         hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40903,
CC         ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16870, ChEBI:CHEBI:76078;
CC         Evidence={ECO:0000269|PubMed:10320809};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40904;
CC         Evidence={ECO:0000305|PubMed:10320809};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 2-hexadecanoyl-sn-glycero-3-phosphocholine = 1,2-
CC         dihexadecanoyl-sn-glycero-3-phosphocholine + sn-glycerol 3-
CC         phosphocholine; Xref=Rhea:RHEA:40907, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:72999, ChEBI:CHEBI:76078;
CC         Evidence={ECO:0000269|PubMed:10320809};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40908;
CC         Evidence={ECO:0000305|PubMed:10320809};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-(9Z)-octadecenoyl-2-O-acetyl-sn-glycero-3-phosphocholine +
CC         H2O = (9Z)-octadecenoate + 2-acetyl-sn-glycero-3-phosphocholine +
CC         H(+); Xref=Rhea:RHEA:41320, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:78044, ChEBI:CHEBI:78045;
CC         Evidence={ECO:0000269|PubMed:8119970};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41321;
CC         Evidence={ECO:0000305|PubMed:8119970};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + a 1-acyl-sn-
CC         glycero-3-phospho-(1D-myo-inositol) = a 1-acyl-2-hexadecanoyl-sn-
CC         glycero-3-phospho-(1D-myo-inositol) + sn-glycerol 3-phosphocholine;
CC         Xref=Rhea:RHEA:41352, ChEBI:CHEBI:16870, ChEBI:CHEBI:64771,
CC         ChEBI:CHEBI:64874, ChEBI:CHEBI:72998;
CC         Evidence={ECO:0000269|PubMed:10320809};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41353;
CC         Evidence={ECO:0000305|PubMed:10320809};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-
CC         phosphocholine = 1,2-di-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC         3-phosphocholine + sn-glycerol 3-phosphocholine;
CC         Xref=Rhea:RHEA:40959, ChEBI:CHEBI:16870, ChEBI:CHEBI:60657,
CC         ChEBI:CHEBI:76079; Evidence={ECO:0000269|PubMed:10320809};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40960;
CC         Evidence={ECO:0000305|PubMed:10320809};
CC   -!- ACTIVITY REGULATION: Inhibited by phosphatidic acid.
CC       {ECO:0000269|PubMed:8119970}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=91 uM for 1-palmitoyl-glycerophosphocholine
CC         {ECO:0000269|PubMed:8119970};
CC         Vmax=12.9 nmol/min/mg enzyme for 1-palmitoyl-glycerophosphocholine
CC         {ECO:0000269|PubMed:8119970};
CC       pH dependence:
CC         Optimum pH is 6. {ECO:0000269|PubMed:8119970};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8119970}.
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in liver and kidney and at
CC       a low level in stomach. Barely detectable in lung, heart, spleen and
CC       brain. {ECO:0000269|PubMed:9575212}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the asparaginase 1
CC       family. {ECO:0000305}.
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DR   EMBL; AB009372; BAA31197.1; -; mRNA.
DR   EMBL; BC098655; AAH98655.1; -; mRNA.
DR   RefSeq; NP_653351.1; NM_144750.2.
DR   AlphaFoldDB; O88202; -.
DR   SMR; O88202; -.
DR   STRING; 10116.ENSRNOP00000017454; -.
DR   SwissLipids; SLP:000000623; -.
DR   iPTMnet; O88202; -.
DR   PhosphoSitePlus; O88202; -.
DR   PaxDb; 10116-ENSRNOP00000017454; -.
DR   GeneID; 246266; -.
DR   KEGG; rno:246266; -.
DR   UCSC; RGD:708388; rat.
DR   AGR; RGD:708388; -.
DR   CTD; 374569; -.
DR   RGD; 708388; Aspg.
DR   eggNOG; KOG0503; Eukaryota.
DR   InParanoid; O88202; -.
DR   OrthoDB; 1421816at2759; -.
DR   PhylomeDB; O88202; -.
DR   TreeFam; TF315247; -.
DR   Reactome; R-RNO-8963693; Aspartate and asparagine metabolism.
DR   PRO; PR:O88202; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IMP:RGD.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA:UniProtKB.
DR   GO; GO:0004067; F:asparaginase activity; IDA:UniProtKB.
DR   GO; GO:0004622; F:lysophospholipase activity; IDA:UniProtKB.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0006528; P:asparagine metabolic process; IDA:UniProtKB.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006644; P:phospholipid metabolic process; IDA:UniProtKB.
DR   CDD; cd08963; L-asparaginase_I; 1.
DR   Gene3D; 3.40.50.40; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 3.40.50.1170; L-asparaginase, N-terminal domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR006033; AsnA_fam.
DR   InterPro; IPR036152; Asp/glu_Ase-like_sf.
DR   InterPro; IPR006034; Asparaginase/glutaminase-like.
DR   InterPro; IPR027475; Asparaginase/glutaminase_AS2.
DR   InterPro; IPR040919; Asparaginase_C.
DR   InterPro; IPR027473; L-asparaginase_C.
DR   InterPro; IPR041725; L-asparaginase_I.
DR   InterPro; IPR027474; L-asparaginase_N.
DR   InterPro; IPR037152; L-asparaginase_N_sf.
DR   NCBIfam; TIGR00519; asnASE_I; 1.
DR   PANTHER; PTHR11707:SF28; 60 KDA LYSOPHOSPHOLIPASE; 1.
DR   PANTHER; PTHR11707; L-ASPARAGINASE; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF00710; Asparaginase; 1.
DR   Pfam; PF17763; Asparaginase_C; 1.
DR   PIRSF; PIRSF001220; L-ASNase_gatD; 1.
DR   PIRSF; PIRSF500176; L_ASNase; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   PRINTS; PR00139; ASNGLNASE.
DR   SFLD; SFLDS00057; Glutaminase/Asparaginase; 1.
DR   SMART; SM00248; ANK; 4.
DR   SMART; SM00870; Asparaginase; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF53774; Glutaminase/Asparaginase; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS00917; ASN_GLN_ASE_2; 1.
DR   PROSITE; PS51732; ASN_GLN_ASE_3; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; ANK repeat; Direct protein sequencing; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Phosphoprotein; Reference proteome;
KW   Repeat; Transferase.
FT   CHAIN           1..564
FT                   /note="60 kDa lysophospholipase"
FT                   /id="PRO_0000171092"
FT   DOMAIN          9..355
FT                   /note="Asparaginase/glutaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT   REPEAT          141..170
FT                   /note="ANK 1"
FT   REPEAT          396..426
FT                   /note="ANK 2"
FT   REPEAT          430..459
FT                   /note="ANK 3"
FT   REPEAT          463..492
FT                   /note="ANK 4"
FT   REPEAT          530..559
FT                   /note="ANK 5"
FT   REGION          41..350
FT                   /note="Asparaginase"
FT   ACT_SITE        19
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10100"
FT   BINDING         84..86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         116..117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         478
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A0JNU3"
FT   CONFLICT        280
FT                   /note="I -> L (in Ref. 2; AAH98655)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   564 AA;  60795 MW;  9DBB2F8FA8B1C477 CRC64;
     MARATGPEQR LLAIYTGGTI GMRSEGGVLV PGRGLAAVLR TLHMLHDEEY ARAHSLPEDT
     LVLPPASSDQ RIIYKVLECQ PLFDSSDMTI TEWVQIAQTI ERHYTQYQGF VVIHGTDTMA
     FAASVLSFML ENLQKPVILT GAQVPIHELW SDGRENLLGA LLMAGQYVIP EVCLFFQNQL
     FRGNRTTKVD ARRFAAFCSP NLPPLATVGA DVTINRELVR KASWKSHLVV HSNMEPDVGL
     LRLYPGIPAS LVRTFLQPPL KGVVMETFGS GNGPTKPDLI QELRAAAERG LIIVNCTHCL
     QGAVTSDYAP GMAMAGAGII SGFDMTSEAA LAKLSYVLGQ PGLSLSDRKK LLAKDLRGEM
     TLPTTDDLLG DDMLGCRATW LLSMNGSQDA DAMKDVLLPG LALAAAHAGD LDTLQAFVEL
     GRDLNLKDYS GQTPLHVAAR RGHASVVAML LQKGVDVDAC NEDGQSPLLL AVRGRHQSVI
     RLLRAAGAHL SPQELEDVGT ELCRLASRAD SEGLRAWWQA GADLGQPDYD GHCALQVAEA
     AGNADVVALL QSLEDRVSAQ PQPH
//