ID PTGR2_MOUSE Reviewed; 351 AA.
AC Q8VDQ1; Q3TG36; Q3ULY3; Q8BZA2; Q9D1W8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 27-MAR-2024, entry version 158.
DE RecName: Full=Prostaglandin reductase 2 {ECO:0000305};
DE Short=PRG-2;
DE EC=1.3.1.48 {ECO:0000269|PubMed:17449869};
DE AltName: Full=15-oxoprostaglandin 13-reductase;
DE AltName: Full=Zinc-binding alcohol dehydrogenase domain-containing protein 1;
GN Name=Ptgr2 {ECO:0000312|MGI:MGI:1916372}; Synonyms=Zadh1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Embryonic heart, Mammary gland, and Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF TYR-259.
RX PubMed=17449869; DOI=10.1074/jbc.m702289200;
RA Chou W.-L., Chuang L.-M., Chou C.-C., Wang A.H.-J., Lawson J.A.,
RA FitzGerald G.A., Chang Z.-F.;
RT "Identification of a novel prostaglandin reductase reveals the involvement
RT of prostaglandin E2 catabolism in regulation of peroxisome proliferator-
RT activated receptor gamma activation.";
RL J. Biol. Chem. 282:18162-18172(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SUBUNIT.
RX PubMed=15229897; DOI=10.1002/prot.20163;
RA Levin I., Schwarzenbacher R., McMullan D., Abdubek P., Ambing E.,
RA Biorac T., Cambell J., Canaves J.M., Chiu H.-J., Dai X., Deacon A.M.,
RA DiDonato M., Elsliger M.-A., Godzik A., Grittini C., Grzechnik S.K.,
RA Hampton E., Jaroszewski L., Karlak C., Klock H.E., Koesema E., Kreusch A.,
RA Kuhn P., Lesley S.A., McPhillips T.M., Miller M.D., Morse A., Moy K.,
RA Ouyang J., Page R., Quijano K., Reyes R., Robb A., Sims E., Spraggon G.,
RA Stevens R.C., van den Bedem H., Velasquez J., Vincent J., von Delft F.,
RA Wang X., West B., Wolf G., Xu Q., Hodgson K.O., Wooley J., Wilson I.A.;
RT "Crystal structure of a putative NADPH-dependent oxidoreductase (GI:
RT 18204011) from mouse at 2.10 A resolution.";
RL Proteins 56:629-633(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NADPH.
RX PubMed=19000823; DOI=10.1016/j.str.2008.09.007;
RA Wu Y.H., Ko T.P., Guo R.T., Hu S.M., Chuang L.M., Wang A.H.;
RT "Structural basis for catalytic and inhibitory mechanisms of human
RT prostaglandin reductase PTGR2.";
RL Structure 16:1714-1723(2008).
CC -!- FUNCTION: Functions as 15-oxo-prostaglandin 13-reductase and acts on
CC 15-keto-PGE1, 15-keto-PGE2, 15-keto-PGE1-alpha and 15-keto-PGE2-alpha
CC with highest activity towards 15-keto-PGE2. Overexpression represses
CC transcriptional activity of PPARG and inhibits adipocyte
CC differentiation. {ECO:0000269|PubMed:17449869}.
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:17449869};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11918;
CC Evidence={ECO:0000305|PubMed:17449869};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13,14-dihydro-15-oxo-prostaglandin E2 + NADP(+) = 15-
CC oxoprostaglandin E2 + H(+) + NADPH; Xref=Rhea:RHEA:11912,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57400, ChEBI:CHEBI:57402,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.48;
CC Evidence={ECO:0000269|PubMed:17449869};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11914;
CC Evidence={ECO:0000305|PubMed:17449869};
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:0000269|PubMed:17449869};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50590;
CC Evidence={ECO:0000305|PubMed:17449869};
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:0000269|PubMed:17449869};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50586;
CC Evidence={ECO:0000305|PubMed:17449869};
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:0000269|PubMed:17449869};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50594;
CC Evidence={ECO:0000305|PubMed:17449869};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=49.6 uM for 15-keto-PGE2 {ECO:0000269|PubMed:17449869};
CC KM=34.4 uM for 15-keto-PGE1 {ECO:0000269|PubMed:17449869};
CC KM=108.8 uM for 15-keto-PGF2-alpha {ECO:0000269|PubMed:17449869};
CC KM=59.2 uM for 15-keto-PGF2-beta {ECO:0000269|PubMed:17449869};
CC KM=94.6 uM for NADPH {ECO:0000269|PubMed:17449869};
CC Vmax=178.4 umol/min/mg enzyme for 15-keto-PGE2
CC {ECO:0000269|PubMed:17449869};
CC Vmax=115.0 umol/min/mg enzyme for 15-keto-PGE1
CC {ECO:0000269|PubMed:17449869};
CC Vmax=230.9 umol/min/mg enzyme for 15-keto-PGF2-alpha
CC {ECO:0000269|PubMed:17449869};
CC Vmax=206.4 umol/min/mg enzyme for 15-keto-PGF2-beta
CC {ECO:0000269|PubMed:17449869};
CC Vmax=144.7 umol/min/mg enzyme for NADPH
CC {ECO:0000269|PubMed:17449869};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15229897,
CC ECO:0000269|PubMed:19000823}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VDQ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VDQ1-2; Sequence=VSP_013528, VSP_013529;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in adipose
CC tissues. {ECO:0000269|PubMed:17449869}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in the late phase of adipocyte
CC differentiation (at protein level). {ECO:0000269|PubMed:17449869}.
CC -!- SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD family.
CC {ECO:0000305}.
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DR EMBL; AK036168; BAC29329.1; -; mRNA.
DR EMBL; AK021033; BAB32284.1; -; mRNA.
DR EMBL; AK145232; BAE26315.1; -; mRNA.
DR EMBL; AK159932; BAE35493.1; -; mRNA.
DR EMBL; AK168895; BAE40712.1; -; mRNA.
DR EMBL; BC021466; AAH21466.1; -; mRNA.
DR CCDS; CCDS36490.1; -. [Q8VDQ1-1]
DR RefSeq; NP_001239554.1; NM_001252625.1. [Q8VDQ1-1]
DR RefSeq; NP_001239555.1; NM_001252626.1.
DR RefSeq; NP_084156.2; NM_029880.3. [Q8VDQ1-1]
DR PDB; 1VJ1; X-ray; 2.10 A; A=1-351.
DR PDB; 2ZB3; X-ray; 2.00 A; A=1-351.
DR PDBsum; 1VJ1; -.
DR PDBsum; 2ZB3; -.
DR AlphaFoldDB; Q8VDQ1; -.
DR SMR; Q8VDQ1; -.
DR BioGRID; 218562; 2.
DR IntAct; Q8VDQ1; 2.
DR MINT; Q8VDQ1; -.
DR STRING; 10090.ENSMUSP00000115704; -.
DR SwissLipids; SLP:000001623; -.
DR GlyGen; Q8VDQ1; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q8VDQ1; -.
DR PhosphoSitePlus; Q8VDQ1; -.
DR SwissPalm; Q8VDQ1; -.
DR EPD; Q8VDQ1; -.
DR jPOST; Q8VDQ1; -.
DR MaxQB; Q8VDQ1; -.
DR PaxDb; 10090-ENSMUSP00000115704; -.
DR PeptideAtlas; Q8VDQ1; -.
DR ProteomicsDB; 302006; -. [Q8VDQ1-1]
DR ProteomicsDB; 302007; -. [Q8VDQ1-2]
DR Pumba; Q8VDQ1; -.
DR DNASU; 77219; -.
DR Ensembl; ENSMUST00000123614.8; ENSMUSP00000115704.2; ENSMUSG00000072946.13. [Q8VDQ1-1]
DR Ensembl; ENSMUST00000146377.8; ENSMUSP00000119981.2; ENSMUSG00000072946.13. [Q8VDQ1-1]
DR Ensembl; ENSMUST00000147363.8; ENSMUSP00000114766.2; ENSMUSG00000072946.13. [Q8VDQ1-2]
DR GeneID; 77219; -.
DR KEGG; mmu:77219; -.
DR UCSC; uc007oep.2; mouse. [Q8VDQ1-1]
DR AGR; MGI:1916372; -.
DR CTD; 145482; -.
DR MGI; MGI:1916372; Ptgr2.
DR VEuPathDB; HostDB:ENSMUSG00000072946; -.
DR eggNOG; KOG1196; Eukaryota.
DR GeneTree; ENSGT00940000156793; -.
DR InParanoid; Q8VDQ1; -.
DR OMA; EEKCRYA; -.
DR OrthoDB; 179761at2759; -.
DR PhylomeDB; Q8VDQ1; -.
DR TreeFam; TF324201; -.
DR BRENDA; 1.3.1.48; 3474.
DR SABIO-RK; Q8VDQ1; -.
DR BioGRID-ORCS; 77219; 2 hits in 79 CRISPR screens.
DR ChiTaRS; Ptgr2; mouse.
DR EvolutionaryTrace; Q8VDQ1; -.
DR PRO; PR:Q8VDQ1; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8VDQ1; Protein.
DR Bgee; ENSMUSG00000072946; Expressed in interventricular septum and 248 other cell types or tissues.
DR ExpressionAtlas; Q8VDQ1; baseline and differential.
DR Genevisible; Q8VDQ1; MM.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0036132; F:13-prostaglandin reductase activity; TAS:Reactome.
DR GO; GO:0047522; F:15-oxoprostaglandin 13-oxidase activity; ISS:UniProtKB.
DR GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB.
DR CDD; cd08293; PTGR2; 1.
DR DisProt; DP02579; -.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR037399; PTGR2.
DR PANTHER; PTHR43205; PROSTAGLANDIN REDUCTASE; 1.
DR PANTHER; PTHR43205:SF5; PROSTAGLANDIN REDUCTASE 2; 1.
DR Pfam; PF16884; ADH_N_2; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Lipid metabolism; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..351
FT /note="Prostaglandin reductase 2"
FT /id="PRO_0000218071"
FT BINDING 99..100
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 165..168
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19000823"
FT BINDING 192
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19000823"
FT BINDING 208
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19000823"
FT BINDING 231
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19000823"
FT BINDING 253..259
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19000823"
FT BINDING 287..289
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19000823"
FT BINDING 288..290
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:19000823"
FT VAR_SEQ 314..316
FT /note="VKE -> FLF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013528"
FT VAR_SEQ 317..351
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013529"
FT MUTAGEN 259
FT /note="Y->F: Significant reduction in catalytic
FT efficiency."
FT /evidence="ECO:0000269|PubMed:17449869"
FT CONFLICT 18
FT /note="P -> T (in Ref. 1; BAB32284)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="P -> L (in Ref. 2; AAH21466)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="V -> I (in Ref. 1; BAE26315 and 2; AAH21466)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="T -> A (in Ref. 1; BAE26315 and 2; AAH21466)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="A -> T (in Ref. 1; BAE26315 and 2; AAH21466)"
FT /evidence="ECO:0000305"
FT CONFLICT 260..261
FT /note="SN -> NK (in Ref. 1; BAE26315 and 2; AAH21466)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="M -> V (in Ref. 1; BAE26315 and 2; AAH21466)"
FT /evidence="ECO:0000305"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:2ZB3"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:2ZB3"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:2ZB3"
FT STRAND 38..47
FT /evidence="ECO:0007829|PDB:2ZB3"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:2ZB3"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2ZB3"
FT STRAND 75..85
FT /evidence="ECO:0007829|PDB:2ZB3"
FT STRAND 95..110
FT /evidence="ECO:0007829|PDB:2ZB3"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2ZB3"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1VJ1"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:2ZB3"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:2ZB3"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:2ZB3"
FT HELIX 135..147
FT /evidence="ECO:0007829|PDB:2ZB3"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:2ZB3"
FT HELIX 166..177
FT /evidence="ECO:0007829|PDB:2ZB3"
FT STRAND 181..189
FT /evidence="ECO:0007829|PDB:2ZB3"
FT HELIX 190..198
FT /evidence="ECO:0007829|PDB:2ZB3"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:2ZB3"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:2ZB3"
FT HELIX 213..220
FT /evidence="ECO:0007829|PDB:2ZB3"
FT STRAND 225..232
FT /evidence="ECO:0007829|PDB:2ZB3"
FT HELIX 234..242
FT /evidence="ECO:0007829|PDB:2ZB3"
FT STRAND 244..252
FT /evidence="ECO:0007829|PDB:2ZB3"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:2ZB3"
FT HELIX 271..280
FT /evidence="ECO:0007829|PDB:2ZB3"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:2ZB3"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:2ZB3"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:2ZB3"
FT HELIX 296..308
FT /evidence="ECO:0007829|PDB:2ZB3"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:2ZB3"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:2ZB3"
FT HELIX 325..333
FT /evidence="ECO:0007829|PDB:2ZB3"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:2ZB3"
SQ SEQUENCE 351 AA; 38015 MW; 2766871577A8022F CRC64;
MIIQRVVLNS RPGKNGNPVA ENFRVEEFSL PDALNEGQVQ VRTLYLSVDP YMRCKMNEDT
GTDYLAPWQL AQVADGGGIG VVEESKHQKL TKGDFVTSFY WPWQTKAILD GNGLEKVDPQ
LVDGHLSYFL GAIGMPGLTS LIGVQEKGHI SAGSNQTMVV SGAAGACGSL AGQIGHLLGC
SRVVGICGTQ EKCLFLTSEL GFDAAVNYKT GNVAEQLREA CPGGVDVYFD NVGGDISNAV
ISQMNENSHI ILCGQISQYS NDVPYPPPLP PAVEAIRKER NITRERFTVL NYKDKFEPGI
LQLSQWFKEG KLKVKETMAK GLENMGVAFQ SMMTGGNVGK QIVCISEDSS L
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