KCR1_ARATH
ID KCR1_ARATH Reviewed; 318 AA.
AC Q8L9C4; O24481; Q8H1N9; Q9AST7;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Very-long-chain 3-oxoacyl-CoA reductase 1;
DE EC=1.1.1.330;
DE AltName: Full=Beta-ketoacyl reductase 1;
DE Short=AtKCR1;
DE AltName: Full=Protein GLOSSY 8;
DE Short=gl8At;
GN Name=KCR1; Synonyms=At-YBR159, GL8; OrderedLocusNames=At1g67730;
GN ORFNames=F12A21.31;
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 57-318.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 71-318, AND FUNCTION.
RX PubMed=9342868; DOI=10.1104/pp.115.2.501;
RA Xu X., Dietrich C.R., Delledonne M., Xia Y., Wen T.J., Robertson D.S.,
RA Nikolau B.J., Schnable P.S.;
RT "Sequence analysis of the cloned glossy8 gene of maize suggests that it may
RT code for a beta-ketoacyl reductase required for the biosynthesis of
RT cuticular waxes.";
RL Plant Physiol. 115:501-510(1997).
RN [6]
RP FUNCTION.
RX PubMed=11792704; DOI=10.1074/jbc.m111441200;
RA Beaudoin F., Gable K., Sayanova O., Dunn T., Napier J.A.;
RT "A Saccharomyces cerevisiae gene required for heterologous fatty acid
RT elongase activity encodes a microsomal beta-keto-reductase.";
RL J. Biol. Chem. 277:11481-11488(2002).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=19439572; DOI=10.1104/pp.109.137497;
RA Beaudoin F., Wu X., Li F., Haslam R.P., Markham J.E., Zheng H.,
RA Napier J.A., Kunst L.;
RT "Functional characterization of the Arabidopsis beta-ketoacyl-coenzyme A
RT reductase candidates of the fatty acid elongase.";
RL Plant Physiol. 150:1174-1191(2009).
CC -!- FUNCTION: Beta-ketoacyl-coenzyme A reductase required for the
CC elongation of fatty acids precursors of sphingolipids,
CC triacylglycerols, cuticular waxes and suberin. Responsible for the
CC first reduction step in very long-chain fatty acids (VLCFAs) synthesis.
CC Decreased expression of KCR1 (RNAi) leads to plants with fused
CC vegetative and reproductive organs, and abnormal trichome, epidermal
CC cell and root morphology. Cannot be complemented by KCR2.
CC {ECO:0000269|PubMed:11792704, ECO:0000269|PubMed:19439572,
CC ECO:0000269|PubMed:9342868}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP(+) = a very-
CC long-chain 3-oxoacyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:48680,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:85440, ChEBI:CHEBI:90725; EC=1.1.1.330;
CC Evidence={ECO:0000269|PubMed:19439572};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000269|PubMed:19439572}.
CC -!- SUBUNIT: Part of the fatty acid elongase complex which contains a beta-
CC ketoacyl-CoA synthase (KCS), a beta-ketoacyl-CoA reductase (KCR), a
CC beta-hydroxyacyl-CoA dehydratase (HCD) and an enoyl-CoA reductase
CC (ECR). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19439572}; Single-pass membrane protein
CC {ECO:0000269|PubMed:19439572}.
CC -!- TISSUE SPECIFICITY: Expressed in green siliques, flowers, inflorescence
CC stems, leaves and roots. {ECO:0000269|PubMed:19439572}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos of different stages and young
CC developing seedlings, but absent from mature seeds.
CC {ECO:0000269|PubMed:19439572}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethal when homozygote.
CC {ECO:0000269|PubMed:19439572}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK32856.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC008113; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE34688.1; -; Genomic_DNA.
DR EMBL; AY088517; AAM66051.1; -; mRNA.
DR EMBL; AF361844; AAK32856.1; ALT_INIT; mRNA.
DR EMBL; AY143811; AAN28750.1; -; mRNA.
DR EMBL; U89512; AAB82765.1; -; mRNA.
DR RefSeq; NP_564905.1; NM_105441.3.
DR AlphaFoldDB; Q8L9C4; -.
DR SMR; Q8L9C4; -.
DR BioGRID; 28319; 12.
DR STRING; 3702.AT1G67730.1; -.
DR SwissPalm; Q8L9C4; -.
DR PaxDb; Q8L9C4; -.
DR PRIDE; Q8L9C4; -.
DR ProteomicsDB; 247312; -.
DR EnsemblPlants; AT1G67730.1; AT1G67730.1; AT1G67730.
DR GeneID; 843098; -.
DR Gramene; AT1G67730.1; AT1G67730.1; AT1G67730.
DR KEGG; ath:AT1G67730; -.
DR Araport; AT1G67730; -.
DR TAIR; locus:2008630; AT1G67730.
DR eggNOG; ENOG502QRPU; Eukaryota.
DR HOGENOM; CLU_010194_38_3_1; -.
DR InParanoid; Q8L9C4; -.
DR OMA; FLQHWSS; -.
DR OrthoDB; 895581at2759; -.
DR PhylomeDB; Q8L9C4; -.
DR BioCyc; ARA:AT1G67730-MON; -.
DR BioCyc; MetaCyc:AT1G67730-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q8L9C4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L9C4; baseline and differential.
DR Genevisible; Q8L9C4; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0102339; F:3-oxo-arachidoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0102340; F:3-oxo-behenoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0102342; F:3-oxo-cerotoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0102341; F:3-oxo-lignoceroyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0018454; F:acetoacetyl-CoA reductase activity; IMP:TAIR.
DR GO; GO:0045703; F:ketoreductase activity; IDA:TAIR.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IMP:TAIR.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..318
FT /note="Very-long-chain 3-oxoacyl-CoA reductase 1"
FT /id="PRO_0000420421"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 206
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 51..80
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 122
FT /note="I -> T (in Ref. 4; AAK32856/AAN28750)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="R -> S (in Ref. 4; AAK32856/AAN28750)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="T -> I (in Ref. 4; AAN28750)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 318 AA; 35762 MW; 005C48C7D3447031 CRC64;
MEICTYFKSQ PTWLLILFVL GSISIFKFIF TLLRSFYIYF LRPSKNLRRY GSWAIITGPT
DGIGKAFAFQ LAQKGLNLIL VARNPDKLKD VSDSIRSKYS QTQILTVVMD FSGDIDEGVK
RIKESIEGLD VGILINNAGM SYPYAKYFHE VDEELINNLI KINVEGTTKV TQAVLPNMLK
RKKGAIINMG SGAAALIPSY PFYSVYAGAK TYVDQFTKCL HVEYKKSGID VQCQVPLYVA
TKMTKIRRAS FLVASPEGYA KAALRFVGYE AQCTPYWPHA LMGAVVSALP ESVFESFNIK
RCLQIRKKGL QKDSMKKE
