PTGR1_CAVPO
ID PTGR1_CAVPO Reviewed; 329 AA.
AC Q9EQZ5;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Prostaglandin reductase 1;
DE Short=PRG-1;
DE AltName: Full=15-oxoprostaglandin 13-reductase {ECO:0000303|PubMed:11733004};
DE EC=1.3.1.48 {ECO:0000269|PubMed:11733004};
DE AltName: Full=Dithiolethione-inducible gene 1 protein {ECO:0000250|UniProtKB:P97584};
DE Short=D3T-inducible gene 1 protein {ECO:0000250|UniProtKB:P97584};
DE Short=DIG-1 {ECO:0000250|UniProtKB:P97584};
DE AltName: Full=Leukotriene B4 12-hydroxydehydrogenase {ECO:0000303|PubMed:11733004};
DE AltName: Full=NAD(P)H-dependent alkenal/one oxidoreductase {ECO:0000250|UniProtKB:Q14914};
DE EC=1.3.1.74 {ECO:0000250|UniProtKB:Q14914};
GN Name=Ptgr1; Synonyms=Ltb4dh;
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], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=11733004; DOI=10.1046/j.0014-2956.2001.02462.x;
RA Yamamoto T., Yokomizo T., Nakao A., Izumi T., Shimizu T.;
RT "Immunohistochemical localization of guinea-pig leukotriene B4 12-
RT hydroxydehydrogenase/15-ketoprostaglandin 13-reductase.";
RL Eur. J. Biochem. 268:6105-6113(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH NADP
RP AND SUBSTRATE.
RX PubMed=15007077; DOI=10.1074/jbc.m312655200;
RA Hori T., Yokomizo T., Ago H., Sugahara M., Ueno G., Yamamoto M.,
RA Kumasaka T., Shimizu T., Miyano M.;
RT "Structural basis of leukotriene B4 12-hydroxydehydrogenase/15-oxo-
RT prostaglandin 13-reductase catalytic mechanism and a possible Src homology
RT 3 domain binding loop.";
RL J. Biol. Chem. 279:22615-22623(2004).
CC -!- FUNCTION: NAD(P)H-dependent oxidoreductase involved in metabolic
CC inactivation of pro- and anti-inflammatory eicosanoids: prostaglandins
CC (PG), leukotrienes (LT) and lipoxins (LX) (PubMed:11733004). Catalyzes
CC with high efficiency the reduction of the 13,14 double bond of 15-
CC oxoPGs, including 15-oxo-PGE1, 15-oxo-PGE2, 15-oxo-PGF1-alpha and 15-
CC oxo-PGF2-alpha (PubMed:11733004) (By similarity). Catalyzes with lower
CC efficiency the oxidation of the hydroxyl group at C12 of LTB4 and its
CC derivatives, converting them into biologically less active 12-oxo-LTB4
CC metabolites (PubMed:11733004) (By similarity). Reduces 15-oxo-LXA4 to
CC 13,14 dihydro-15-oxo-LXA4, enhancing neutrophil recruitment at the
CC inflammatory site (By similarity). Plays a role in metabolic
CC detoxification of alkenals and ketones. Reduces alpha,beta-unsaturated
CC alkenals and ketones, particularly those with medium-chain length,
CC showing highest affinity toward (2E)-decenal and (3E)-3-nonen-2-one (By
CC similarity). May inactivate 4-hydroxy-2-nonenal, a cytotoxic lipid
CC constituent of oxidized low-density lipoprotein particles (By
CC similarity). {ECO:0000250|UniProtKB:P97584,
CC ECO:0000250|UniProtKB:Q14914, ECO:0000250|UniProtKB:Q29073,
CC ECO:0000269|PubMed:11733004}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13,14-dihydro-15-oxo-prostaglandin E1 + NADP(+) = 15-
CC oxoprostaglandin E1 + H(+) + NADPH; Xref=Rhea:RHEA:50584,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57401, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:133408;
CC Evidence={ECO:0000250|UniProtKB:Q14914};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50586;
CC Evidence={ECO:0000250|UniProtKB:Q14914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13,14-dihydro-15-oxo-prostaglandin E2 + NAD(+) = 15-
CC oxoprostaglandin E2 + H(+) + NADH; Xref=Rhea:RHEA:11916,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57400, ChEBI:CHEBI:57402,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.48;
CC Evidence={ECO:0000269|PubMed:11733004};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11918;
CC Evidence={ECO:0000305|PubMed:11733004};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13,14-dihydro-15-oxo-prostaglandin F1alpha + NADP(+) = 15-
CC oxoprostaglandin F1alpha + H(+) + NADPH; Xref=Rhea:RHEA:50592,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:79072, ChEBI:CHEBI:133411;
CC Evidence={ECO:0000250|UniProtKB:Q14914};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50594;
CC Evidence={ECO:0000250|UniProtKB:Q14914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13,14-dihydro-15-oxo-PGF2alpha + NADP(+) = 15-oxoprostaglandin
CC F2alpha + H(+) + NADPH; Xref=Rhea:RHEA:50588, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133374,
CC ChEBI:CHEBI:133409; Evidence={ECO:0000250|UniProtKB:Q14914};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50590;
CC Evidence={ECO:0000250|UniProtKB:Q14914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=leukotriene B4 + NADP(+) = 12-oxo-leukotriene B4 + H(+) +
CC NADPH; Xref=Rhea:RHEA:50608, ChEBI:CHEBI:15378, ChEBI:CHEBI:57461,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133309;
CC Evidence={ECO:0000269|PubMed:11733004};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50609;
CC Evidence={ECO:0000305|PubMed:11733004};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=20-hydroxy-leukotriene B4 + NADP(+) = 12-oxo-20-hydroxy-
CC leukotriene B4 + H(+) + NADPH; Xref=Rhea:RHEA:51208,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57460, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:133346;
CC Evidence={ECO:0000250|UniProtKB:Q29073};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51209;
CC Evidence={ECO:0000250|UniProtKB:Q29073};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-trans-leukotriene B4 + NADP(+) = 12-oxo-(5S)-hydroxy-
CC (6E,8E,10E,14Z)-eicosatetraenoate + H(+) + NADPH;
CC Xref=Rhea:RHEA:51204, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:90723, ChEBI:CHEBI:133974;
CC Evidence={ECO:0000250|UniProtKB:Q29073};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51205;
CC Evidence={ECO:0000250|UniProtKB:Q29073};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5S,12S)-dihydroxy-(6E,10E,12E,14Z)-eicosatetraenoate +
CC NADP(+) = 12-oxo-(5S)-hydroxy-(6E,8E,10E,14Z)-eicosatetraenoate +
CC H(+) + NADPH; Xref=Rhea:RHEA:51212, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133974,
CC ChEBI:CHEBI:133975; Evidence={ECO:0000250|UniProtKB:Q29073};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51213;
CC Evidence={ECO:0000250|UniProtKB:Q29073};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an n-alkanal + NADP(+) = an alk-2-enal + H(+) + NADPH;
CC Xref=Rhea:RHEA:13737, ChEBI:CHEBI:12834, ChEBI:CHEBI:13757,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.74;
CC Evidence={ECO:0000250|UniProtKB:Q14914};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13739;
CC Evidence={ECO:0000250|UniProtKB:Q14914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexanal + NADP(+) = (E)-hex-2-enal + H(+) + NADPH;
CC Xref=Rhea:RHEA:50776, ChEBI:CHEBI:15378, ChEBI:CHEBI:28913,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:88528;
CC Evidence={ECO:0000250|UniProtKB:Q14914};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50778;
CC Evidence={ECO:0000250|UniProtKB:Q14914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + octanal = (2E)-octenal + H(+) + NADPH;
CC Xref=Rhea:RHEA:50780, ChEBI:CHEBI:15378, ChEBI:CHEBI:17935,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:61748;
CC Evidence={ECO:0000250|UniProtKB:Q14914};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50782;
CC Evidence={ECO:0000250|UniProtKB:Q14914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanal + NADP(+) = (2E)-decenal + H(+) + NADPH;
CC Xref=Rhea:RHEA:50612, ChEBI:CHEBI:15378, ChEBI:CHEBI:31457,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133455;
CC Evidence={ECO:0000250|UniProtKB:Q14914};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50614;
CC Evidence={ECO:0000250|UniProtKB:Q14914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanal + NADP(+) = (2E)-dodecenal + H(+) + NADPH;
CC Xref=Rhea:RHEA:50784, ChEBI:CHEBI:15378, ChEBI:CHEBI:27836,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133741;
CC Evidence={ECO:0000250|UniProtKB:Q14914};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50786;
CC Evidence={ECO:0000250|UniProtKB:Q14914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxynonanal + NADP(+) = (E)-4-hydroxynon-2-enal + H(+) +
CC NADPH; Xref=Rhea:RHEA:64736, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:58968, ChEBI:CHEBI:156112;
CC Evidence={ECO:0000250|UniProtKB:P97584};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64738;
CC Evidence={ECO:0000250|UniProtKB:P97584};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + pentan-2-one = (E)-pent-3-en-2-one + H(+) + NADPH;
CC Xref=Rhea:RHEA:50788, ChEBI:CHEBI:15378, ChEBI:CHEBI:16472,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:145276;
CC Evidence={ECO:0000250|UniProtKB:Q14914};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50790;
CC Evidence={ECO:0000250|UniProtKB:Q14914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + nonan-2-one = (3E)-nonen-2-one + H(+) + NADPH;
CC Xref=Rhea:RHEA:50616, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:77927, ChEBI:CHEBI:133457;
CC Evidence={ECO:0000250|UniProtKB:Q14914};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50618;
CC Evidence={ECO:0000250|UniProtKB:Q14914};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=93 uM for LTB4 {ECO:0000269|PubMed:11733004};
CC KM=35 uM for 15-keto-PGE2 {ECO:0000269|PubMed:11733004};
CC Vmax=1.7 nmol/min/mg enzyme with LTB4 as substrate
CC {ECO:0000269|PubMed:11733004};
CC Vmax=345 nmol/min/mg enzyme with 15-keto-PGE2 as substrate
CC {ECO:0000269|PubMed:11733004};
CC -!- SUBUNIT: Monomer or homodimer. {ECO:0000269|PubMed:15007077}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11733004}.
CC -!- TISSUE SPECIFICITY: Detected in small intestine, kidney, liver, spleen
CC and stomach (at protein level). Detected in small intestine, kidney and
CC liver. {ECO:0000269|PubMed:11733004}.
CC -!- SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD family.
CC {ECO:0000305}.
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DR EMBL; AB021219; BAB20289.1; -; mRNA.
DR RefSeq; NP_001166451.1; NM_001172980.1.
DR PDB; 1V3T; X-ray; 2.30 A; A/B=1-329.
DR PDB; 1V3U; X-ray; 2.00 A; A/B=1-329.
DR PDB; 1V3V; X-ray; 2.00 A; A/B=1-329.
DR PDB; 2DM6; X-ray; 2.00 A; A/B=1-329.
DR PDBsum; 1V3T; -.
DR PDBsum; 1V3U; -.
DR PDBsum; 1V3V; -.
DR PDBsum; 2DM6; -.
DR AlphaFoldDB; Q9EQZ5; -.
DR SMR; Q9EQZ5; -.
DR GeneID; 100135572; -.
DR KEGG; cpoc:100135572; -.
DR CTD; 22949; -.
DR InParanoid; Q9EQZ5; -.
DR OrthoDB; 884151at2759; -.
DR EvolutionaryTrace; Q9EQZ5; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0036185; F:13-lipoxin reductase activity; ISS:UniProtKB.
DR GO; GO:0036132; F:13-prostaglandin reductase activity; IDA:UniProtKB.
DR GO; GO:0047522; F:15-oxoprostaglandin 13-oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0035798; F:2-alkenal reductase (NADP+) activity; ISS:UniProtKB.
DR GO; GO:0097257; F:leukotriene B4 12-hydroxy dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0036102; P:leukotriene B4 metabolic process; IDA:UniProtKB.
DR GO; GO:2001302; P:lipoxin A4 metabolic process; ISS:UniProtKB.
DR GO; GO:0006693; P:prostaglandin metabolic process; IDA:UniProtKB.
DR CDD; cd08294; leukotriene_B4_DH_like; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR041694; ADH_N_2.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR045010; MDR_fam.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR014190; PTGR1.
DR PANTHER; PTHR43205; PTHR43205; 1.
DR Pfam; PF16884; ADH_N_2; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR02825; B4_12hDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Fatty acid metabolism; Hydroxylation;
KW Lipid metabolism; NADP; Oxidoreductase; Phosphoprotein;
KW Prostaglandin metabolism; Reference proteome.
FT CHAIN 1..329
FT /note="Prostaglandin reductase 1"
FT /id="PRO_0000218064"
FT BINDING 152..155
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15007077"
FT BINDING 178
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15007077"
FT BINDING 193
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15007077"
FT BINDING 217
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15007077"
FT BINDING 239..245
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15007077"
FT BINDING 270..272
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15007077"
FT BINDING 321
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15007077"
FT MOD_RES 18
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14914"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14914"
FT MOD_RES 178
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14914"
FT MOD_RES 178
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91YR9"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:1V3U"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1V3T"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:1V3U"
FT STRAND 22..28
FT /evidence="ECO:0007829|PDB:1V3U"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:1V3U"
FT HELIX 49..53
FT /evidence="ECO:0007829|PDB:1V3U"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1V3U"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:1V3U"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:1V3U"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:1V3U"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1V3U"
FT HELIX 115..119
FT /evidence="ECO:0007829|PDB:1V3U"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:1V3U"
FT HELIX 124..134
FT /evidence="ECO:0007829|PDB:1V3U"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:1V3V"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:1V3U"
FT HELIX 153..164
FT /evidence="ECO:0007829|PDB:1V3U"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:1V3U"
FT HELIX 176..184
FT /evidence="ECO:0007829|PDB:1V3U"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:1V3U"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:1V3T"
FT HELIX 199..206
FT /evidence="ECO:0007829|PDB:1V3U"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:1V3U"
FT HELIX 220..227
FT /evidence="ECO:0007829|PDB:1V3U"
FT STRAND 230..238
FT /evidence="ECO:0007829|PDB:1V3U"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:1V3U"
FT HELIX 257..262
FT /evidence="ECO:0007829|PDB:1V3U"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:1V3U"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:1V3U"
FT HELIX 278..292
FT /evidence="ECO:0007829|PDB:1V3U"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:1V3U"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:1V3U"
FT HELIX 309..317
FT /evidence="ECO:0007829|PDB:1V3U"
FT STRAND 322..328
FT /evidence="ECO:0007829|PDB:1V3U"
SQ SEQUENCE 329 AA; 35730 MW; 8C5D86D9D2C9FEA1 CRC64;
MVKAKSWTLK KHFQGKPTQS DFELKTVELP PLKNGEVLLE ALFLSVDPYM RIASKRLKEG
AVMMGQQVAR VVESKNSAFP AGSIVLAQSG WTTHFISDGK GLEKLLTEWP DKLPLSLALG
TIGMPGLTAY FGLLEVCGVK GGETVLVSAA AGAVGSVVGQ IAKLKGCKVV GAAGSDEKIA
YLKQIGFDAA FNYKTVNSLE EALKKASPDG YDCYFDNVGG EFLNTVLSQM KDFGKIAICG
AISVYNRMDQ LPPGPSPESI IYKQLRIEGF IVYRWQGDVR EKALRDLMKW VLEGKIQYHE
HVTKGFENMP AAFIEMLNGA NLGKAVVTA
