ADAS_CAVPO
ID ADAS_CAVPO Reviewed; 658 AA.
AC P97275;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Alkyldihydroxyacetonephosphate synthase, peroxisomal;
DE Short=Alkyl-DHAP synthase;
DE EC=2.5.1.26 {ECO:0000269|PubMed:10692424, ECO:0000269|PubMed:23112191, ECO:0000269|PubMed:8399344, ECO:0000269|PubMed:9989261};
DE AltName: Full=Alkylglycerone-phosphate synthase;
DE Flags: Precursor;
GN Name=AGPS;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 59-83; 92-114; 422-445
RP AND 515-539.
RC TISSUE=Liver;
RX PubMed=8995366; DOI=10.1074/jbc.272.2.798;
RA de Vet E.C.J.M., Zomer A.W.M., Lahaut G.J.H.T.J., van den Bosch H.;
RT "Polymerase chain reaction-based cloning of alkyl-dihydroxyacetonephosphate
RT synthase complementary DNA from guinea pig liver.";
RL J. Biol. Chem. 272:798-803(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF HIS-300;
RP SER-367; ARG-419; HIS-615; HIS-616 AND HIS-617.
RX PubMed=10692424; DOI=10.1074/jbc.275.9.6276;
RA de Vet E.C.J.M., Hilkes Y.H.A., Fraaije M.W., van den Bosch H.;
RT "Alkyl-dihydroxyacetonephosphate synthase. Presence and role of flavin
RT adenine dinucleotide.";
RL J. Biol. Chem. 275:6276-6283(2000).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=8399344; DOI=10.1016/0005-2760(93)90070-p;
RA Zomer A.W., de Weerd W.F., Langeveld J., van den Bosch H.;
RT "Ether lipid synthesis: purification and identification of alkyl
RT dihydroxyacetone phosphate synthase from guinea-pig liver.";
RL Biochim. Biophys. Acta 1170:189-196(1993).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF SER-367; ARG-419; CYS-576 AND
RP HIS-617, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=9989261; DOI=10.1016/s0005-2760(98)00118-0;
RA de Vet E.C., van den Bosch H.;
RT "Characterization of recombinant guinea pig alkyl-dihydroxyacetonephosphate
RT synthase expressed in Escherichia coli. Kinetics, chemical modification and
RT mutagenesis.";
RL Biochim. Biophys. Acta 1436:299-306(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF WILD-TYPE AND MUTANTS HIS-419 AND
RP PHE-578 IN COMPLEX WITH FAD AND SUBSTRATE ANALOG, FUNCTION, CATALYTIC
RP ACTIVITY, SUBUNIT, ACTIVE SITE, COFACTOR, AND MUTAGENESIS OF THR-309;
RP ARG-419; LEU-469; ARG-515 AND TYR-578.
RX PubMed=23112191; DOI=10.1073/pnas.1215128109;
RA Nenci S., Piano V., Rosati S., Aliverti A., Pandini V., Fraaije M.W.,
RA Heck A.J., Edmondson D.E., Mattevi A.;
RT "Precursor of ether phospholipids is synthesized by a flavoenzyme through
RT covalent catalysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:18791-18796(2012).
CC -!- FUNCTION: Catalyzes the exchange of the acyl chain in acyl-
CC dihydroxyacetonephosphate (acyl-DHAP) for a long chain fatty alcohol,
CC yielding the first ether linked intermediate, i.e. alkyl-
CC dihydroxyacetonephosphate (alkyl-DHAP), in the pathway of ether lipid
CC biosynthesis. {ECO:0000269|PubMed:10692424,
CC ECO:0000269|PubMed:23112191, ECO:0000269|PubMed:8399344,
CC ECO:0000269|PubMed:9989261}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acylglycerone 3-phosphate + a long chain fatty alcohol =
CC 1-O-alkylglycerone 3-phosphate + a long-chain fatty acid + H(+);
CC Xref=Rhea:RHEA:36171, ChEBI:CHEBI:15378, ChEBI:CHEBI:17135,
CC ChEBI:CHEBI:57534, ChEBI:CHEBI:57560, ChEBI:CHEBI:73315; EC=2.5.1.26;
CC Evidence={ECO:0000269|PubMed:10692424, ECO:0000269|PubMed:23112191,
CC ECO:0000269|PubMed:8399344, ECO:0000269|PubMed:9989261};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36172;
CC Evidence={ECO:0000305|PubMed:10692424, ECO:0000305|PubMed:23112191,
CC ECO:0000305|PubMed:8399344, ECO:0000305|PubMed:9989261};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoylglycerone 3-phosphate + hexadecan-1-ol = 1-O-
CC hexadecylglycerone 3-phosphate + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:40659, ChEBI:CHEBI:7896, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16125, ChEBI:CHEBI:58303, ChEBI:CHEBI:77429;
CC Evidence={ECO:0000269|PubMed:10692424, ECO:0000269|PubMed:8399344,
CC ECO:0000269|PubMed:9989261};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40660;
CC Evidence={ECO:0000305|PubMed:10692424, ECO:0000305|PubMed:8399344,
CC ECO:0000305|PubMed:9989261};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoylglycerone 3-phosphate + a long-chain fatty acid
CC = a 1-acylglycerone 3-phosphate + hexadecanoate;
CC Xref=Rhea:RHEA:40727, ChEBI:CHEBI:7896, ChEBI:CHEBI:57534,
CC ChEBI:CHEBI:57560, ChEBI:CHEBI:58303;
CC Evidence={ECO:0000250|UniProtKB:Q8C0I1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40728;
CC Evidence={ECO:0000250|UniProtKB:Q8C0I1};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:10692424, ECO:0000269|PubMed:23112191};
CC -!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide, p-
CC bromophenacylbromide, 2,4- dinitrofluorobenzene and divalent cations
CC such as such as Mn(2+), Mg(2+) and Zn(2+) (PubMed:9989261). Inhibition
CC by p-bromophenacylbromide is strongly pH dependent and is highest at
CC alkaline conditions (PubMed:9989261). {ECO:0000269|PubMed:9989261}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=68 uM for palmitoyl-dihydroxyacetonephosphate (in the presence of
CC 0.5 mM of hexadecanol) {ECO:0000269|PubMed:8399344};
CC KM=72 uM for hexadecanol (in the presence of 0.3 mM of
CC palmitoyl- dihydroxyacetonephosphate) {ECO:0000269|PubMed:8399344};
CC KM=192 uM for hexadecyl-dihydroxyacetonephosphate (in the presence of
CC 0.05 mM of hexadecanol) {ECO:0000269|PubMed:8399344};
CC KM=115 uM for hexadecyl-dihydroxyacetonephosphate (in the presence of
CC 0.4 mM of hexadecanol) {ECO:0000269|PubMed:8399344};
CC KM=100 uM for hexadecanol (in the presence of 0.4 mM of hexadecyl-
CC dihydroxyacetonephosphate) {ECO:0000269|PubMed:8399344};
CC Vmax=42 nmol/min/mg enzyme toward palmitoyl-dihydroxyacetonephosphate
CC (in the presence of 0.5 mM of hexadecanol)
CC {ECO:0000269|PubMed:8399344};
CC Vmax=50 nmol/min/mg enzyme toward hexadecanol (in the presence of 0.3
CC mM of palmitoyl-dihydroxyacetonephosphate)
CC {ECO:0000269|PubMed:8399344};
CC Vmax=8 nmol/min/mg enzyme toward hexadecyl-dihydroxyacetonephosphate
CC (in the presence of 0.05 mM of hexadecanol)
CC {ECO:0000269|PubMed:8399344};
CC Vmax=7 nmol/min/mg enzyme toward hexadecyl-dihydroxyacetonephosphate
CC (in the presence of 0.4 mM of hexadecanol)
CC {ECO:0000269|PubMed:8399344};
CC Vmax=7 nmol/min/mg enzyme toward hexadecanal (in the presence of 0.4
CC mM of hexadecyl-dihydroxyacetonephosphate)
CC {ECO:0000269|PubMed:8399344};
CC pH dependence:
CC Optimum pH is 7-8. {ECO:0000269|PubMed:8399344};
CC -!- PATHWAY: Glycerolipid metabolism; ether lipid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23112191}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:8399344}.
CC Peroxisome {ECO:0000269|PubMed:9989261}.
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000305}.
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DR EMBL; Y08826; CAA70060.1; -; mRNA.
DR RefSeq; XP_005007711.2; XM_005007654.2.
DR PDB; 4BBY; X-ray; 1.90 A; A/B/C/D=1-658.
DR PDB; 4BC7; X-ray; 2.40 A; A/B/C/D=1-658.
DR PDB; 4BC9; X-ray; 2.41 A; A/B/C/D=1-658.
DR PDB; 4BCA; X-ray; 2.40 A; A/B/C/D=1-658.
DR PDB; 5ADZ; X-ray; 2.20 A; A/B/C/D=1-658.
DR PDB; 5AE1; X-ray; 2.10 A; A/B/C/D=1-658.
DR PDB; 5AE2; X-ray; 2.00 A; A/B/C/D=1-658.
DR PDB; 5AE3; X-ray; 2.18 A; A/B/C/D=1-658.
DR PDB; 6GOU; X-ray; 2.90 A; A/B/C/D=1-658.
DR PDBsum; 4BBY; -.
DR PDBsum; 4BC7; -.
DR PDBsum; 4BC9; -.
DR PDBsum; 4BCA; -.
DR PDBsum; 5ADZ; -.
DR PDBsum; 5AE1; -.
DR PDBsum; 5AE2; -.
DR PDBsum; 5AE3; -.
DR PDBsum; 6GOU; -.
DR AlphaFoldDB; P97275; -.
DR SMR; P97275; -.
DR STRING; 10141.ENSCPOP00000000601; -.
DR SwissLipids; SLP:000000212; -.
DR PRIDE; P97275; -.
DR Ensembl; ENSCPOT00000000684; ENSCPOP00000000601; ENSCPOG00000000679.
DR GeneID; 100734021; -.
DR KEGG; cpoc:100734021; -.
DR CTD; 8540; -.
DR eggNOG; KOG1233; Eukaryota.
DR GeneTree; ENSGT00940000156112; -.
DR HOGENOM; CLU_017779_2_2_1; -.
DR InParanoid; P97275; -.
DR OMA; PRCHDEV; -.
DR OrthoDB; 824020at2759; -.
DR TreeFam; TF313830; -.
DR BRENDA; 2.5.1.26; 1225.
DR SABIO-RK; P97275; -.
DR UniPathway; UPA00781; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000000679; Expressed in uterine cervix and 12 other tissues.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0008609; F:alkylglycerone-phosphate synthase activity; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0008611; P:ether lipid biosynthetic process; IDA:UniProtKB.
DR Gene3D; 1.10.45.10; -; 1.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR025650; Alkyl-DHAP_Synthase.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR004113; FAD-linked_oxidase_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR46568; PTHR46568; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF55103; SSF55103; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; FAD; Flavoprotein;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Peroxisome; Phosphoprotein;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..58
FT /note="Peroxisome"
FT /evidence="ECO:0000269|PubMed:8995366"
FT CHAIN 59..658
FT /note="Alkyldihydroxyacetonephosphate synthase,
FT peroxisomal"
FT /id="PRO_0000020430"
FT DOMAIN 202..384
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..617
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000269|PubMed:10692424,
FT ECO:0000269|PubMed:9989261"
FT REGION 654..658
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000269|PubMed:9989261"
FT ACT_SITE 578
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000269|PubMed:23112191"
FT BINDING 234..240
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23112191"
FT BINDING 303..309
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23112191"
FT BINDING 316..319
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23112191"
FT BINDING 368..374
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:23112191"
FT BINDING 515
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23112191"
FT SITE 419
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000269|PubMed:10692424,
FT ECO:0000269|PubMed:23112191"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00116"
FT MOD_RES 74
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00116"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00116"
FT MOD_RES 347
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00116"
FT MUTAGEN 300
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10692424"
FT MUTAGEN 309
FT /note="T->I: Impaired FAD binding and protein stability.
FT Loss of activity."
FT /evidence="ECO:0000269|PubMed:23112191"
FT MUTAGEN 367
FT /note="S->A: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:10692424,
FT ECO:0000269|PubMed:9989261"
FT MUTAGEN 419
FT /note="R->H: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10692424,
FT ECO:0000269|PubMed:23112191"
FT MUTAGEN 419
FT /note="R->K: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:10692424,
FT ECO:0000269|PubMed:23112191, ECO:0000269|PubMed:9989261"
FT MUTAGEN 469
FT /note="L->P: Impaired FAD binding and protein stability.
FT Loss of activity."
FT /evidence="ECO:0000269|PubMed:23112191"
FT MUTAGEN 515
FT /note="R->L: Impaired FAD binding and protein stability.
FT Loss of activity."
FT /evidence="ECO:0000269|PubMed:23112191"
FT MUTAGEN 576
FT /note="C->A: No effect on activity."
FT /evidence="ECO:0000269|PubMed:9989261"
FT MUTAGEN 578
FT /note="Y->F: Loss of activity."
FT /evidence="ECO:0000269|PubMed:23112191"
FT MUTAGEN 615
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10692424"
FT MUTAGEN 616
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10692424"
FT MUTAGEN 617
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10692424,
FT ECO:0000269|PubMed:9989261"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:4BBY"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:4BBY"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:4BBY"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:4BBY"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:4BBY"
FT TURN 119..122
FT /evidence="ECO:0007829|PDB:4BC9"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:4BBY"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:5AE2"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:5AE1"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:4BBY"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:4BBY"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:4BBY"
FT HELIX 191..198
FT /evidence="ECO:0007829|PDB:4BBY"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:4BBY"
FT HELIX 215..227
FT /evidence="ECO:0007829|PDB:4BBY"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:4BBY"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:4BBY"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:4BBY"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:4BBY"
FT TURN 271..274
FT /evidence="ECO:0007829|PDB:4BBY"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:4BBY"
FT HELIX 284..293
FT /evidence="ECO:0007829|PDB:4BBY"
FT TURN 303..307
FT /evidence="ECO:0007829|PDB:4BBY"
FT HELIX 310..316
FT /evidence="ECO:0007829|PDB:4BBY"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:4BBY"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:4BBY"
FT STRAND 333..340
FT /evidence="ECO:0007829|PDB:4BBY"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:4BBY"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:4BBY"
FT HELIX 361..364
FT /evidence="ECO:0007829|PDB:4BBY"
FT STRAND 373..380
FT /evidence="ECO:0007829|PDB:4BBY"
FT STRAND 386..397
FT /evidence="ECO:0007829|PDB:4BBY"
FT HELIX 398..410
FT /evidence="ECO:0007829|PDB:4BBY"
FT STRAND 416..421
FT /evidence="ECO:0007829|PDB:4BBY"
FT HELIX 423..431
FT /evidence="ECO:0007829|PDB:4BBY"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:4BCA"
FT HELIX 444..449
FT /evidence="ECO:0007829|PDB:5AE2"
FT TURN 451..457
FT /evidence="ECO:0007829|PDB:5ADZ"
FT TURN 460..462
FT /evidence="ECO:0007829|PDB:4BBY"
FT STRAND 464..472
FT /evidence="ECO:0007829|PDB:4BBY"
FT HELIX 474..489
FT /evidence="ECO:0007829|PDB:4BBY"
FT TURN 490..492
FT /evidence="ECO:0007829|PDB:4BBY"
FT HELIX 498..520
FT /evidence="ECO:0007829|PDB:4BBY"
FT STRAND 523..533
FT /evidence="ECO:0007829|PDB:4BBY"
FT HELIX 534..536
FT /evidence="ECO:0007829|PDB:4BBY"
FT HELIX 537..554
FT /evidence="ECO:0007829|PDB:4BBY"
FT STRAND 562..570
FT /evidence="ECO:0007829|PDB:4BBY"
FT STRAND 572..584
FT /evidence="ECO:0007829|PDB:4BBY"
FT HELIX 591..608
FT /evidence="ECO:0007829|PDB:4BBY"
FT STRAND 615..617
FT /evidence="ECO:0007829|PDB:4BBY"
FT TURN 620..622
FT /evidence="ECO:0007829|PDB:4BBY"
FT HELIX 624..626
FT /evidence="ECO:0007829|PDB:4BBY"
FT HELIX 627..631
FT /evidence="ECO:0007829|PDB:4BBY"
FT HELIX 633..646
FT /evidence="ECO:0007829|PDB:4BBY"
SQ SEQUENCE 658 AA; 72846 MW; B6272EB407EBB5F1 CRC64;
MAEAAAAAAA AAAAGETSAS SGSAAERDPD QDRAGRRLRV LSGHLLGRPQ EALSTNECKA
RRAASAATAA PTATPAAPES GIIPKKRQEL MKWNGWGYND SKFFLNKKGQ LELTGKRYPL
SGVALPTFKD WIQNTFGINL DHKTTSKASL NPSDTPPSIV NEDFLHELKK TNISYSQEAD
DRVFRAHGHC LHEIFLLREG MFERIPDIVL WPTCHDDVVK IVNLACKYNL CIIPIGGGTS
VSYGLMCPAD ETRTIISLDT SQMNRILWVD ENNLTAHVEA GITGQELERQ LKESGYCTGH
EPDSLEFSTV GGWISTRASG MKKNIYGNIE DLVVHMKVVT PRGVIEKSCQ GPRMSTGPDI
HHFIMGSEGT LGVITEATIK IRPTPEYQKY GSVAFPNFEQ GVACLREIAK QRCAPASIRL
MDNQQFQFGH ALKPQVSSIF TSFLDGLKKF YITKFKGFDP NQLSVATLLF EGDREKVLQH
EKQVYDIAAK FGGLAAGEDN GQRGYLLTYV IAYMRDLGLE YYIIGESFET SAPWDRVVDL
CRNVKERIRR ECKEKGVQFP PLSTCRVTQT YDAGACIYFY FAFNYRGISD PLAVFEQTEA
AAREEILANG GSLSHHHGVG KLRKQWLKES ISDVGFGMLK SVKDYVDPTN IFGNRNLL
