KCR2_ARATH
ID KCR2_ARATH Reviewed; 312 AA.
AC Q9FYL6;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Very-long-chain 3-oxoacyl-CoA reductase-like protein At1g24470;
DE EC=1.-.-.-;
DE AltName: Full=Beta-ketoacyl reductase 2;
DE Short=AtKCR2;
GN Name=KCR2; OrderedLocusNames=At1g24470; ORFNames=F21J9.13;
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;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim C.J., Bautista V.R., Chen H., De Los Reyes C., Wu S.Y., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION.
RX PubMed=15941398; DOI=10.1111/j.1365-313x.2005.02418.x;
RA Dietrich C.R., Perera M.A., Yandeau-Nelson M.D., Meeley R.B., Nikolau B.J.,
RA Schnable P.S.;
RT "Characterization of two GL8 paralogs reveals that the 3-ketoacyl reductase
RT component of fatty acid elongase is essential for maize (Zea mays L.)
RT development.";
RL Plant J. 42:844-861(2005).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP 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: Probable reductase, but unlike KCR1, has no beta-ketoacyl-
CC coenzyme A reductase activity. {ECO:0000269|PubMed:19439572}.
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 and leaves. Not detected in 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: No visible phenotype.
CC {ECO:0000269|PubMed:19439572}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AC000103; AAF97959.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30534.1; -; Genomic_DNA.
DR EMBL; BT030066; ABN04804.1; -; mRNA.
DR RefSeq; NP_173856.1; NM_102292.3.
DR AlphaFoldDB; Q9FYL6; -.
DR SMR; Q9FYL6; -.
DR STRING; 3702.AT1G24470.1; -.
DR PaxDb; Q9FYL6; -.
DR PRIDE; Q9FYL6; -.
DR ProteomicsDB; 247313; -.
DR EnsemblPlants; AT1G24470.1; AT1G24470.1; AT1G24470.
DR GeneID; 839063; -.
DR Gramene; AT1G24470.1; AT1G24470.1; AT1G24470.
DR KEGG; ath:AT1G24470; -.
DR Araport; AT1G24470; -.
DR TAIR; locus:2023996; AT1G24470.
DR eggNOG; ENOG502QS3T; Eukaryota.
DR HOGENOM; CLU_010194_38_3_1; -.
DR InParanoid; Q9FYL6; -.
DR OMA; TIAPMMV; -.
DR OrthoDB; 895581at2759; -.
DR PhylomeDB; Q9FYL6; -.
DR BioCyc; ARA:AT1G24470-MON; -.
DR PRO; PR:Q9FYL6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FYL6; baseline and differential.
DR Genevisible; Q9FYL6; 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:0045703; F:ketoreductase activity; IDA:TAIR.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; NADP; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..312
FT /note="Very-long-chain 3-oxoacyl-CoA reductase-like protein
FT At1g24470"
FT /id="PRO_0000420422"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 205
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 52..81
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 312 AA; 35012 MW; 621E3EBF186EDD54 CRC64;
MQGACISESQ PWYLHFVCFI GFLFLLRVLF IPLLKWFTTR FLLTPKRLKR YGSWAMVTGA
TEGIGRAFAH ELAKHGLNLI LVSRNLSKLE SVSDDFQQEF PHIKIKIIPF DFSSEGGYGA
IEEGIKGLEV GILINNVGIT YPRAMFFHEV DQLTWTKILR VNLEATTWVT RSLIGPMLHR
RRGAIVNISS GAAVVVPSHP LYAIYAATKA YVDALSRSLH VEYKQFGIDV QCQVPLYVST
RMVSEVAAID KPSLFVPSPE VYAKAAVAQI GIGSRCSPFW AHSLQWFLVG LVPDNLVDTW
RLSIGLRRRS LS
