PTGR1_MOUSE
ID PTGR1_MOUSE Reviewed; 329 AA.
AC Q91YR9; Q3TKT6; Q9CPS1;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Prostaglandin reductase 1;
DE Short=PRG-1;
DE AltName: Full=15-oxoprostaglandin 13-reductase {ECO:0000250|UniProtKB:Q14914};
DE EC=1.3.1.48 {ECO:0000250|UniProtKB:Q14914};
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:0000250|UniProtKB:Q14914};
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 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].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Liver, Testis, and Urinary bladder;
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].
RC STRAIN=FVB/N; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, 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 [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-178, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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). Catalyzes with high
CC efficiency the reduction of the 13,14 double bond of 15-oxoPGs,
CC including 15-oxo-PGE1, 15-oxo-PGE2, 15-oxo-PGF1-alpha and 15-oxo-PGF2-
CC alpha (By similarity). Catalyzes with lower efficiency the oxidation of
CC the hydroxyl group at C12 of LTB4 and its derivatives, converting them
CC into biologically less active 12-oxo-LTB4 metabolites (By similarity).
CC Reduces 15-oxo-LXA4 to 13,14 dihydro-15-oxo-LXA4, enhancing neutrophil
CC recruitment at the inflammatory site (By similarity). Plays a role in
CC metabolic detoxification of alkenals and ketones. Reduces alpha,beta-
CC unsaturated alkenals and ketones, particularly those with medium-chain
CC length, showing highest affinity toward (2E)-decenal and (3E)-3-nonen-
CC 2-one (By similarity). May inactivate 4-hydroxy-2-nonenal, a cytotoxic
CC lipid constituent of oxidized low-density lipoprotein particles (By
CC similarity). {ECO:0000250|UniProtKB:P97584,
CC ECO:0000250|UniProtKB:Q14914, ECO:0000250|UniProtKB:Q29073}.
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 + 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:0000250|UniProtKB:Q14914};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11914;
CC Evidence={ECO:0000250|UniProtKB:Q14914};
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:0000250|UniProtKB:Q29073,
CC ECO:0000250|UniProtKB:Q9EQZ5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50609;
CC Evidence={ECO:0000250|UniProtKB:Q29073,
CC ECO:0000250|UniProtKB:Q9EQZ5};
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 -!- SUBUNIT: Monomer or homodimer. {ECO:0000250|UniProtKB:Q9EQZ5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q29073}.
CC -!- SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD family.
CC {ECO:0000305}.
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DR EMBL; AK010888; BAB27248.1; -; mRNA.
DR EMBL; AK011962; BAB27941.1; -; mRNA.
DR EMBL; AK035425; BAC29060.1; -; mRNA.
DR EMBL; AK134440; BAE22145.1; -; mRNA.
DR EMBL; AK166835; BAE39057.1; -; mRNA.
DR EMBL; BC014865; AAH14865.1; -; mRNA.
DR CCDS; CCDS18215.1; -.
DR RefSeq; NP_080244.1; NM_025968.3.
DR AlphaFoldDB; Q91YR9; -.
DR SMR; Q91YR9; -.
DR BioGRID; 211942; 2.
DR IntAct; Q91YR9; 1.
DR STRING; 10090.ENSMUSP00000030069; -.
DR iPTMnet; Q91YR9; -.
DR PhosphoSitePlus; Q91YR9; -.
DR REPRODUCTION-2DPAGE; Q91YR9; -.
DR EPD; Q91YR9; -.
DR jPOST; Q91YR9; -.
DR MaxQB; Q91YR9; -.
DR PaxDb; Q91YR9; -.
DR PeptideAtlas; Q91YR9; -.
DR PRIDE; Q91YR9; -.
DR ProteomicsDB; 291619; -.
DR Antibodypedia; 29578; 221 antibodies from 28 providers.
DR DNASU; 67103; -.
DR Ensembl; ENSMUST00000030069; ENSMUSP00000030069; ENSMUSG00000028378.
DR GeneID; 67103; -.
DR KEGG; mmu:67103; -.
DR UCSC; uc008szm.1; mouse.
DR CTD; 22949; -.
DR MGI; MGI:1914353; Ptgr1.
DR VEuPathDB; HostDB:ENSMUSG00000028378; -.
DR eggNOG; KOG1196; Eukaryota.
DR GeneTree; ENSGT00940000154810; -.
DR HOGENOM; CLU_026673_29_3_1; -.
DR InParanoid; Q91YR9; -.
DR OMA; GKDKCDY; -.
DR OrthoDB; 884151at2759; -.
DR PhylomeDB; Q91YR9; -.
DR TreeFam; TF324201; -.
DR BioGRID-ORCS; 67103; 2 hits in 75 CRISPR screens.
DR PRO; PR:Q91YR9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q91YR9; protein.
DR Bgee; ENSMUSG00000028378; Expressed in epithelium of stomach and 232 other tissues.
DR Genevisible; Q91YR9; MM.
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; ISS:UniProtKB.
DR GO; GO:0047522; F:15-oxoprostaglandin 13-oxidase activity; IBA:GO_Central.
DR GO; GO:0035798; F:2-alkenal reductase (NADP+) activity; ISS:UniProtKB.
DR GO; GO:0097257; F:leukotriene B4 12-hydroxy dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0036102; P:leukotriene B4 metabolic process; ISS:UniProtKB.
DR GO; GO:2001302; P:lipoxin A4 metabolic process; ISS:UniProtKB.
DR GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB.
DR GO; GO:0097327; P:response to antineoplastic agent; IEA:Ensembl.
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 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_0000218066"
FT BINDING 152..155
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q14914"
FT BINDING 178
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q14914"
FT BINDING 193
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q14914"
FT BINDING 217
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q14914"
FT BINDING 239..245
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q14914"
FT BINDING 270..272
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q14914"
FT BINDING 321
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q14914"
FT MOD_RES 18
FT /note="Phosphothreonine"
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:Q14914"
FT CONFLICT 298
FT /note="C -> Y (in Ref. 2; AAH14865)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="Y -> H (in Ref. 2; AAH14865)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 329 AA; 35560 MW; FD0CA4682DB493D8 CRC64;
MVQAKSWTLK KHFEGFPTDG NFELKTTELP PLNNGEVLLE ALFLSVDPYM RVAAKKLKEG
DRMMGEQVAR VVESKNSAFP KGTIVAALLG WTSHSISDGN GLTKLPVEWP DKLPLSLALG
TVGMPGLTAY FGLLDICGVK GGETVMVSAA AGAVGSVVGQ IAKLKGCKVV GTAGSDEKVA
YLKKLGFDVA FNYKTVKSLE EALRTASPDG YDCYFDNVGG EFSNAVILQM KTFGRIAICG
AISQYNRTGP CPQGPAPEVV IYQQLRMEGF IVNRWQGEVR QKALTELMNW VSEGKVQCHE
YVTEGFEKMP AAFMGMLKGE NLGKTIVKA
