TKPR2_ARATH
ID TKPR2_ARATH Reviewed; 321 AA.
AC Q9CA28;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Tetraketide alpha-pyrone reductase 2;
DE EC=1.1.1.-;
DE AltName: Full=Protein CINNAMOYL-COA REDUCTASE-LIKE 6;
GN Name=TKPR2; Synonyms=CCRL6; OrderedLocusNames=At1g68540;
GN ORFNames=T26J14.11;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: May be involved in the biosynthesis of hydroxylated
CC tetraketide compounds that serve as sporopollenin precursors (the main
CC constituents of exine). Acts on tetraketide alpha-pyrones and reduces
CC the carbonyl function on the tetraketide alkyl chain to a secondary
CC alcohol function. {ECO:0000269|PubMed:21193572}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21193572}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9CA28-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:21193572}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
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DR EMBL; AC011915; AAG52392.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34806.1; -; Genomic_DNA.
DR EMBL; BT028984; ABI93893.1; -; mRNA.
DR PIR; F96709; F96709.
DR RefSeq; NP_177021.1; NM_105525.5. [Q9CA28-1]
DR AlphaFoldDB; Q9CA28; -.
DR SMR; Q9CA28; -.
DR STRING; 3702.AT1G68540.1; -.
DR iPTMnet; Q9CA28; -.
DR PaxDb; Q9CA28; -.
DR PRIDE; Q9CA28; -.
DR ProteomicsDB; 232428; -. [Q9CA28-1]
DR EnsemblPlants; AT1G68540.1; AT1G68540.1; AT1G68540. [Q9CA28-1]
DR GeneID; 843183; -.
DR Gramene; AT1G68540.1; AT1G68540.1; AT1G68540. [Q9CA28-1]
DR KEGG; ath:AT1G68540; -.
DR Araport; AT1G68540; -.
DR TAIR; locus:2201272; AT1G68540.
DR eggNOG; KOG1502; Eukaryota.
DR InParanoid; Q9CA28; -.
DR OMA; YAYAKTT; -.
DR PhylomeDB; Q9CA28; -.
DR BioCyc; ARA:AT1G68540-MON; -.
DR BioCyc; MetaCyc:AT1G68540-MON; -.
DR PRO; PR:Q9CA28; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CA28; baseline and differential.
DR Genevisible; Q9CA28; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
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:0010584; P:pollen exine formation; 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 Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; NADP; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..321
FT /note="Tetraketide alpha-pyrone reductase 2"
FT /id="PRO_0000418215"
FT BINDING 4..28
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT BINDING 40
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT BINDING 160
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 321 AA; 35666 MW; 7D789130AA5802A1 CRC64;
MSEYLVTGGT GFIASYIIKS LLELGHTVRT TVRNPRDEEK VGFLWEFQGA KQRLKILQAD
LTVEGSFDEA VNGVDGVFHT ASPVLVPQDH NIQETLVDPI IKGTTNVMSS CAKSKATLKR
IVLTSSCSSI RYRFDATEAS PLNESHWSDP EYCKRFNLWY GYAKTLGERE AWRIAEEKGL
DLVVVNPSFV VGPLLGPKPT STLLMILAIA KGLAGEYPNF TVGFVHIDDV VAAHVLAMEE
PKASGRIICS SSVAHWSEII ELMRNKYPNY PFENKCSNKE GDNSPHSMDT RKIHELGFGS
FKSLPEMFDD CIISFQKKGL L
