CCR1_ARATH
ID CCR1_ARATH Reviewed; 344 AA.
AC Q9S9N9; Q9FPM0;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Cinnamoyl-CoA reductase 1 {ECO:0000303|PubMed:11430991};
DE Short=AtCCR1 {ECO:0000303|PubMed:11430991};
DE EC=1.2.1.44 {ECO:0000269|PubMed:11430991};
DE AltName: Full=Protein IRREGULAR XYLEM 4 {ECO:0000303|PubMed:16153410};
GN Name=CCR1 {ECO:0000303|PubMed:11430991};
GN Synonyms=IRX4 {ECO:0000303|PubMed:16153410};
GN OrderedLocusNames=At1g15950 {ECO:0000312|Araport:AT1G15950};
GN ORFNames=T24D18.5 {ECO:0000312|EMBL:AAF18492.1};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Seedling;
RX PubMed=11430991; DOI=10.1016/s0031-9422(01)00053-x;
RA Lauvergeat V., Lacomme C., Lacombe E., Lasserre E., Roby D.,
RA Grima-Pettenati J.;
RT "Two cinnamoyl-CoA reductase (CCR) genes from Arabidopsis thaliana are
RT differentially expressed during development and in response to infection
RT with pathogenic bacteria.";
RL Phytochemistry 57:1187-1195(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=16153410; DOI=10.1016/j.phytochem.2004.12.016;
RA Patten A.M., Cardenas C.L., Cochrane F.C., Laskar D.D., Bedgar D.L.,
RA Davin L.B., Lewis N.G.;
RT "Reassessment of effects on lignification and vascular development in the
RT irx4 Arabidopsis mutant.";
RL Phytochemistry 66:2092-2107(2005).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=11389761; DOI=10.1046/j.1365-313x.2001.01021.x;
RA Jones L., Ennos A.R., Turner S.R.;
RT "Cloning and characterization of irregular xylem4 (irx4): a severely
RT lignin-deficient mutant of Arabidopsis.";
RL Plant J. 26:205-216(2001).
RN [9]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16122934; DOI=10.1016/j.plaphy.2005.06.003;
RA Baltas M., Lapeyre C., Bedos-Belval F., Maturano M., Saint-Aguet P.,
RA Roussel L., Duran H., Grima-Pettenati J.;
RT "Kinetic and inhibition studies of cinnamoyl-CoA reductase 1 from
RT Arabidopsis thaliana.";
RL Plant Physiol. Biochem. 43:746-753(2005).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=18046574; DOI=10.1007/s00425-007-0669-x;
RA Mir Derikvand M., Sierra J.B., Ruel K., Pollet B., Do C.T., Thevenin J.,
RA Buffard D., Jouanin L., Lapierre C.;
RT "Redirection of the phenylpropanoid pathway to feruloyl malate in
RT Arabidopsis mutants deficient for cinnamoyl-CoA reductase 1.";
RL Planta 227:943-956(2008).
RN [11]
RP FUNCTION.
RX PubMed=19674336; DOI=10.1111/j.1469-8137.2009.02951.x;
RA Ruel K., Berrio-Sierra J., Derikvand M.M., Pollet B., Thevenin J.,
RA Lapierre C., Jouanin L., Joseleau J.P.;
RT "Impact of CCR1 silencing on the assembly of lignified secondary walls in
RT Arabidopsis thaliana.";
RL New Phytol. 184:99-113(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [13]
RP FUNCTION.
RX PubMed=20829305; DOI=10.1093/mp/ssq045;
RA Thevenin J., Pollet B., Letarnec B., Saulnier L., Gissot L.,
RA Maia-Grondard A., Lapierre C., Jouanin L.;
RT "The simultaneous repression of CCR and CAD, two enzymes of the lignin
RT biosynthetic pathway, results in sterility and dwarfism in Arabidopsis
RT thaliana.";
RL Mol. Plant 4:70-82(2011).
CC -!- FUNCTION: Involved in the latter stages of lignin biosynthesis.
CC Catalyzes one of the last steps of monolignol biosynthesis, the
CC conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes.
CC {ECO:0000269|PubMed:11389761, ECO:0000269|PubMed:11430991,
CC ECO:0000269|PubMed:16122934, ECO:0000269|PubMed:16153410,
CC ECO:0000269|PubMed:18046574, ECO:0000269|PubMed:19674336,
CC ECO:0000269|PubMed:20829305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-cinnamaldehyde + CoA + NADP(+) = (E)-cinnamoyl-CoA + H(+)
CC + NADPH; Xref=Rhea:RHEA:10620, ChEBI:CHEBI:15378, ChEBI:CHEBI:16731,
CC ChEBI:CHEBI:57252, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.44;
CC Evidence={ECO:0000269|PubMed:11430991};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.96 uM for feruloyl-CoA {ECO:0000269|PubMed:11430991,
CC ECO:0000269|PubMed:16122934, ECO:0000269|PubMed:16153410};
CC KM=2.27 uM for p-coumaroyl-CoA {ECO:0000269|PubMed:11430991,
CC ECO:0000269|PubMed:16122934, ECO:0000269|PubMed:16153410};
CC KM=6.32 uM for sinapoyl-CoA {ECO:0000269|PubMed:11430991,
CC ECO:0000269|PubMed:16122934, ECO:0000269|PubMed:16153410};
CC KM=12.5 uM for caffeoyl-CoA {ECO:0000269|PubMed:11430991,
CC ECO:0000269|PubMed:16122934, ECO:0000269|PubMed:16153410};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
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=Q9S9N9-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and flowers.
CC -!- DISRUPTION PHENOTYPE: Dwarf phenotype, delayed senescence, collapsed
CC xylem and significant reduction of lignin content in ecotype Columbia
CC (PubMed:19674336). Retarded growth, impaired upright growth, altered
CC leaf morphology, dark green leaves, collapsed xylem and strong decrease
CC in lignin content in ecotype Landsberg erecta (PubMed:11389761).
CC {ECO:0000269|PubMed:11389761, ECO:0000269|PubMed:16153410,
CC ECO:0000269|PubMed:18046574, ECO:0000269|PubMed:19674336}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
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DR EMBL; AF320624; AAG46037.1; -; mRNA.
DR EMBL; AY743921; AAU45042.1; -; mRNA.
DR EMBL; AC010924; AAF18492.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29388.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59759.1; -; Genomic_DNA.
DR EMBL; AF332459; AAG48822.1; -; mRNA.
DR EMBL; AF321114; AAL37194.1; -; mRNA.
DR EMBL; AK228419; BAF00353.1; -; mRNA.
DR EMBL; AY087316; AAM64866.1; -; mRNA.
DR PIR; A86294; A86294.
DR RefSeq; NP_001319013.1; NM_001332191.1. [Q9S9N9-1]
DR RefSeq; NP_173047.1; NM_101463.4. [Q9S9N9-1]
DR AlphaFoldDB; Q9S9N9; -.
DR SMR; Q9S9N9; -.
DR STRING; 3702.AT1G15950.1; -.
DR iPTMnet; Q9S9N9; -.
DR PaxDb; Q9S9N9; -.
DR PRIDE; Q9S9N9; -.
DR ProteomicsDB; 224447; -. [Q9S9N9-1]
DR EnsemblPlants; AT1G15950.1; AT1G15950.1; AT1G15950. [Q9S9N9-1]
DR EnsemblPlants; AT1G15950.3; AT1G15950.3; AT1G15950. [Q9S9N9-1]
DR GeneID; 838165; -.
DR Gramene; AT1G15950.1; AT1G15950.1; AT1G15950. [Q9S9N9-1]
DR Gramene; AT1G15950.3; AT1G15950.3; AT1G15950. [Q9S9N9-1]
DR KEGG; ath:AT1G15950; -.
DR Araport; AT1G15950; -.
DR TAIR; locus:2200427; AT1G15950.
DR eggNOG; KOG1502; Eukaryota.
DR HOGENOM; CLU_007383_9_0_1; -.
DR PhylomeDB; Q9S9N9; -.
DR BioCyc; MetaCyc:AT1G15950-MON; -.
DR BRENDA; 1.2.1.44; 399.
DR SABIO-RK; Q9S9N9; -.
DR UniPathway; UPA00711; -.
DR PRO; PR:Q9S9N9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S9N9; baseline and differential.
DR Genevisible; Q9S9N9; AT.
DR GO; GO:0016621; F:cinnamoyl-CoA reductase activity; 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:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0009809; P:lignin biosynthetic process; IDA:TAIR.
DR GO; GO:0009409; P:response to cold; IEP: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 Alternative splicing; Disulfide bond; Lignin biosynthesis; NADP;
KW Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..344
FT /note="Cinnamoyl-CoA reductase 1"
FT /id="PRO_0000418212"
FT REGION 317..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 165
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q12068"
FT BINDING 17..23
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P51110"
FT BINDING 42
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P51110"
FT BINDING 48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT BINDING 68..69
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P51110"
FT BINDING 88..90
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P51110"
FT BINDING 161
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT BINDING 165
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P51110"
FT BINDING 188..191
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P51110"
FT BINDING 203
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P51110"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT DISULFID 154..162
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT CONFLICT 302
FT /note="F -> L (in Ref. 1; AAG46037)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="L -> F (in Ref. 1; AAG46037)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 37489 MW; F6580F3D849B5A46 CRC64;
MPVDVASPAG KTVCVTGAGG YIASWIVKIL LERGYTVKGT VRNPDDPKNT HLRELEGGKE
RLILCKADLQ DYEALKAAID GCDGVFHTAS PVTDDPEQMV EPAVNGAKFV INAAAEAKVK
RVVITSSIGA VYMDPNRDPE AVVDESCWSD LDFCKNTKNW YCYGKMVAEQ AAWETAKEKG
VDLVVLNPVL VLGPPLQPTI NASLYHVLKY LTGSAKTYAN LTQAYVDVRD VALAHVLVYE
APSASGRYLL AESARHRGEV VEILAKLFPE YPLPTKCKDE KNPRAKPYKF TNQKIKDLGL
EFTSTKQSLY DTVKSLQEKG HLAPPPPPPS ASQESVENGI KIGS
