TKPR1_ARATH
ID TKPR1_ARATH Reviewed; 326 AA.
AC Q500U8; O65487;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Tetraketide alpha-pyrone reductase 1;
DE EC=1.1.1.-;
DE AltName: Full=Protein DIHYDROFLAVONOL 4-REDUCTASE-LIKE 1;
GN Name=TKPR1; Synonyms=DRL1; OrderedLocusNames=At4g35420; ORFNames=F23E12.20;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19054337; DOI=10.1111/j.1469-8137.2008.02692.x;
RA Tang L.K., Chu H., Yip W.K., Yeung E.C., Lo C.;
RT "An anther-specific dihydroflavonol 4-reductase-like gene (DRL1) is
RT essential for male fertility in Arabidopsis.";
RL New Phytol. 181:576-587(2009).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21193572; DOI=10.1105/tpc.110.080036;
RA Grienenberger E., Kim S.S., Lallemand B., Geoffroy P., Heintz D.,
RA de Azevedo Souza C., Heitz T., Douglas C.J., Legrand M.;
RT "Analysis of TETRAKETIDE ?-PYRONE REDUCTASE function in Arabidopsis
RT thaliana reveals a previously unknown, but conserved, biochemical pathway
RT in sporopollenin monomer biosynthesis.";
RL Plant Cell 22:4067-4083(2010).
RN [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH 4CLL1/ACOS5;
RP PKSA AND PKSB.
RX PubMed=23632852; DOI=10.1104/pp.112.213124;
RA Lallemand B., Erhardt M., Heitz T., Legrand M.;
RT "Sporopollenin biosynthetic enzymes interact and constitute a metabolon
RT localized to the endoplasmic reticulum of tapetum cells.";
RL Plant Physiol. 162:616-625(2013).
CC -!- FUNCTION: Involved in the biosynthesis of hydroxylated tetraketide
CC compounds that serve as sporopollenin precursors (the main constituents
CC of exine). Is essential for pollen wall development. Acts on
CC tetraketide alpha-pyrones and reduces the carbonyl function on the
CC tetraketide alkyl chain to a secondary alcohol function.
CC {ECO:0000269|PubMed:19054337, ECO:0000269|PubMed:21193572}.
CC -!- SUBUNIT: Interacts with 4CLL1/ACOS5, PKSA and PKSB.
CC {ECO:0000269|PubMed:23632852}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Endoplasmic reticulum
CC {ECO:0000269|PubMed:23632852}. Note=According to PubMed:21193572, TKPR1
CC is associated with the endoplasmic reticulum.
CC -!- TISSUE SPECIFICITY: Specifically expressed in anther tapetal cells
CC during microspores development. {ECO:0000269|PubMed:19054337,
CC ECO:0000269|PubMed:21193572, ECO:0000269|PubMed:23632852}.
CC -!- DISRUPTION PHENOTYPE: Male sterility due to distorted pollen grains
CC lacking reticulate exine pattern. {ECO:0000269|PubMed:19054337,
CC ECO:0000269|PubMed:21193572}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18727.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80259.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL022604; CAA18727.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161587; CAB80259.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86509.1; -; Genomic_DNA.
DR EMBL; BT022119; AAY34180.1; -; mRNA.
DR EMBL; BT025661; ABF74722.1; -; mRNA.
DR PIR; T06115; T06115.
DR RefSeq; NP_195268.2; NM_119708.3.
DR AlphaFoldDB; Q500U8; -.
DR SMR; Q500U8; -.
DR BioGRID; 14977; 1.
DR IntAct; Q500U8; 1.
DR STRING; 3702.AT4G35420.1; -.
DR PaxDb; Q500U8; -.
DR PRIDE; Q500U8; -.
DR ProteomicsDB; 234281; -.
DR EnsemblPlants; AT4G35420.1; AT4G35420.1; AT4G35420.
DR GeneID; 829695; -.
DR Gramene; AT4G35420.1; AT4G35420.1; AT4G35420.
DR KEGG; ath:AT4G35420; -.
DR Araport; AT4G35420; -.
DR TAIR; locus:2122093; AT4G35420.
DR eggNOG; KOG1502; Eukaryota.
DR HOGENOM; CLU_007383_9_0_1; -.
DR InParanoid; Q500U8; -.
DR OMA; WDSCQAN; -.
DR OrthoDB; 992332at2759; -.
DR PhylomeDB; Q500U8; -.
DR BioCyc; ARA:AT4G35420-MON; -.
DR BioCyc; MetaCyc:AT4G35420-MON; -.
DR PRO; PR:Q500U8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q500U8; baseline and differential.
DR Genevisible; Q500U8; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0010584; P:pollen exine formation; IMP:TAIR.
DR GO; GO:0048316; P:seed development; IMP:TAIR.
DR GO; GO:0080110; P:sporopollenin biosynthetic process; IMP:TAIR.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR033267; TKPR1.
DR PANTHER; PTHR10366:SF684; PTHR10366:SF684; 1.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endoplasmic reticulum; NADP; Nucleus; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..326
FT /note="Tetraketide alpha-pyrone reductase 1"
FT /id="PRO_0000418214"
FT BINDING 8..32
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT BINDING 44
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT BINDING 162
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
SQ SEQUENCE 326 AA; 36463 MW; 568FF7CC6D5C861E CRC64;
MDQAKGKVCV TGASGFLASW LVKRLLLEGY EVIGTVRDPG NEKKLAHLWK LEGAKERLRL
VKADLMEEGS FDNAIMGCQG VFHTASPVLK PTSNPEEEIL RPAIEGTLNV LRSCRKNPSL
KRVVLTSSSS TVRIRDDFDP KIPLDESIWT SVELCKRFQV WYALSKTLAE QAAWKFSEEN
GIDLVTVLPS FLVGPSLPPD LCSTASDVLG LLKGETEKFQ WHGQMGYVHI DDVARTHIVV
FEHEAAQGRY ICSSNVISLE ELVSFLSARY PSLPIPKRFE KLNRLHYDFD TSKIQSLGLK
FKSLEEMFDD CIASLVEQGY LSTVLP
