CIN1_ARATH
ID CIN1_ARATH Reviewed; 600 AA.
AC P0DI76; A0A1I9LQI2; C0Z3K7; Q0WMV0; Q9LDF1;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=1,8-cineole synthase 1, chloroplastic;
DE Short=AtTPS-CIN1;
DE EC=4.2.3.108;
DE AltName: Full=Limonene cyclase;
DE AltName: Full=Terpenoid synthase 27;
DE Short=AtTPS27;
DE Flags: Precursor;
GN Name=TPS27; Synonyms=TPS-CIN1; OrderedLocusNames=At3g25820;
GN ORFNames=K13N2.19;
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP TISSUE SPECIFICITY, INDUCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15299125; DOI=10.1104/pp.104.044388;
RA Chen F., Ro D.K., Petri J., Gershenzon J., Bohlmann J., Pichersky E.,
RA Tholl D.;
RT "Characterization of a root-specific Arabidopsis terpene synthase
RT responsible for the formation of the volatile monoterpene 1,8-cineole.";
RL Plant Physiol. 135:1956-1966(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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] (ISOFORM 2).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [7]
RP IDENTIFICATION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12207221; DOI=10.1007/s00438-002-0709-y;
RA Aubourg S., Lecharny A., Bohlmann J.;
RT "Genomic analysis of the terpenoid synthase (AtTPS) gene family of
RT Arabidopsis thaliana.";
RL Mol. Genet. Genomics 267:730-745(2002).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=12566586; DOI=10.1105/tpc.007989;
RA Chen F., Tholl D., D'Auria J.C., Farooq A., Pichersky E., Gershenzon J.;
RT "Biosynthesis and emission of terpenoid volatiles from Arabidopsis
RT flowers.";
RL Plant Cell 15:481-494(2003).
RN [9]
RP GENE FAMILY.
RX PubMed=12777052; DOI=10.1023/a:1023005504702;
RA Lange B.M., Ghassemian M.;
RT "Genome organization in Arabidopsis thaliana: a survey for genes involved
RT in isoprenoid and chlorophyll metabolism.";
RL Plant Mol. Biol. 51:925-948(2003).
CC -!- FUNCTION: Involved in monoterpene (C10) biosynthesis. The major product
CC is 1,8-cineole (52%) followed by minor amounts of sabinene (14.5%),
CC myrcene (13.3%), (-)-(1S)-beta-pinene (7.8%), (-)-(4S)-limonene (4.0%),
CC (E)-beta-ocimene (2.7%), alpha-terpineol (2.4%), (-)-(1S)-alpha-pinene
CC (1.9%), terpinolene (0.8%), and (+)-alpha-thujene (0.6%).
CC {ECO:0000269|PubMed:15299125}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = 1,8-cineole + diphosphate;
CC Xref=Rhea:RHEA:32543, ChEBI:CHEBI:15377, ChEBI:CHEBI:27961,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.108;
CC Evidence={ECO:0000269|PubMed:15299125};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 uM for geranyl diphosphate {ECO:0000269|PubMed:15299125};
CC Vmax=10.9 pmol/sec/mg enzyme toward geranyl diphosphate
CC {ECO:0000269|PubMed:15299125};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:15299125};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P0DI76-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P0DI76-2; Sequence=VSP_035149, VSP_035150;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in roots and at much lower
CC levels in siliques. Not found in leaves, flowers or stems. Also
CC detected in flowers in cv. Landsberg erecta. Not expressed in root
CC apical meristem and elongation zone. Found in the vascular system of
CC young roots and additionally in the cortex and epidermal cell layer of
CC older roots. {ECO:0000269|PubMed:12566586,
CC ECO:0000269|PubMed:15299125}.
CC -!- INDUCTION: Not induces in aerial parts by treatments with jasmonic
CC acid, 6-ethyl indanoyl-L-Ile, fungal peptaibol elicitor alamethicin or
CC herbivory. {ECO:0000269|PubMed:15299125}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC the catalytic activity, presumably through binding to Mg(2+).
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; AY691947; AAU01970.1; -; mRNA.
DR EMBL; AP000599; BAB01180.1; -; Genomic_DNA.
DR EMBL; AB028607; BAB01180.1; JOINED; Genomic_DNA.
DR EMBL; CP002686; AEE77073.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64839.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64840.1; -; Genomic_DNA.
DR EMBL; AK229712; BAF01550.1; -; mRNA.
DR EMBL; AK319171; BAH57286.1; -; mRNA.
DR RefSeq; NP_001326843.1; NM_001338768.1. [P0DI76-2]
DR RefSeq; NP_001326844.1; NM_001338769.1. [P0DI76-2]
DR RefSeq; NP_189210.2; NM_113483.5. [P0DI76-1]
DR RefSeq; NP_189212.1; NM_113485.5. [P0DI76-1]
DR AlphaFoldDB; P0DI76; -.
DR SMR; P0DI76; -.
DR STRING; 3702.AT3G25820.1; -.
DR PaxDb; P0DI76; -.
DR PRIDE; P0DI76; -.
DR EnsemblPlants; AT3G25820.1; AT3G25820.1; AT3G25820. [P0DI76-1]
DR EnsemblPlants; AT3G25820.3; AT3G25820.3; AT3G25820. [P0DI76-2]
DR EnsemblPlants; AT3G25820.4; AT3G25820.4; AT3G25820. [P0DI76-2]
DR EnsemblPlants; AT3G25830.1; AT3G25830.1; AT3G25830. [P0DI76-1]
DR GeneID; 822175; -.
DR GeneID; 822177; -.
DR Gramene; AT3G25820.1; AT3G25820.1; AT3G25820. [P0DI76-1]
DR Gramene; AT3G25820.3; AT3G25820.3; AT3G25820. [P0DI76-2]
DR Gramene; AT3G25820.4; AT3G25820.4; AT3G25820. [P0DI76-2]
DR Gramene; AT3G25830.1; AT3G25830.1; AT3G25830. [P0DI76-1]
DR KEGG; ath:AT3G25820; -.
DR KEGG; ath:AT3G25830; -.
DR Araport; AT3G25820; -.
DR eggNOG; ENOG502QUH3; Eukaryota.
DR HOGENOM; CLU_003125_7_1_1; -.
DR InParanoid; P0DI76; -.
DR OMA; VRCAATI; -.
DR OrthoDB; 401091at2759; -.
DR PhylomeDB; P0DI76; -.
DR BRENDA; 4.2.3.108; 399.
DR BRENDA; 4.2.3.109; 399.
DR SABIO-RK; P0DI76; -.
DR UniPathway; UPA00213; -.
DR PRO; PR:P0DI76; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P0DI76; baseline and differential.
DR Genevisible; P0DI76; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0102313; F:1,8-cineole synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034741; Terpene_cyclase-like_1_C.
DR InterPro; IPR044814; Terpene_cyclase_plant_C1.
DR InterPro; IPR001906; Terpene_synth_N.
DR InterPro; IPR036965; Terpene_synth_N_sf.
DR InterPro; IPR005630; Terpene_synthase_metal-bd.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF01397; Terpene_synth; 1.
DR Pfam; PF03936; Terpene_synth_C; 1.
DR SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Lyase; Magnesium; Manganese;
KW Metal-binding; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..31
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 32..600
FT /note="1,8-cineole synthase 1, chloroplastic"
FT /id="PRO_0000348419"
FT MOTIF 342..346
FT /note="DDXXD motif"
FT BINDING 342
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 487
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 491
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT VAR_SEQ 363..395
FT /note="NWDVNRLGELPEYMRLCFLILYNEINGIGCDIL -> KLRNILPFFGQSIGY
FT FAAVPWSTTRPLLQKSST (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640, ECO:0000303|Ref.5"
FT /id="VSP_035149"
FT VAR_SEQ 396..600
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640, ECO:0000303|Ref.5"
FT /id="VSP_035150"
SQ SEQUENCE 600 AA; 70455 MW; B3E331C207556B72 CRC64;
MATLRISSAL IYQNTLTHHF RLRRPHRFVC KSMTKTTPDT TLVELSRRSG NYQPSPWNHC
YLLSIENKYA SETEVITRDV LKKKVKSMLD DEKKSRLEQL ELIDDLQKLG VSYHFEIEIN
DTLTDLHLKM GRNCWKCDKE EDLHATSLEF RLLRQHGFDV SENIFDVIID QIESNTFKTN
NINGIISLYE ASYLSTKSDT KLHKVIRPFA TEQIRKFVDD EDTKNIEVRE KAYHALEMPY
HWRMRRLDTR WYIDAYEKKH DMNLVLIEFA KIDFNIVQAA HQEDLKYVSR WWKDTCLTNQ
LPFVRDRIVE NYFWTVGLIY EPQFGYIRRI MTIVNALVTT IDDIYDIYGT LEELELFTSM
VENWDVNRLG ELPEYMRLCF LILYNEINGI GCDILKYKKI DVIPYLKKSW ADLCRTYLVE
AKWYKRGYKP SLEEYMQNAW ISISAPTILI HFYCVFSDQI SVQNLETLSQ HRQHIVRCSA
TVLRLANDLG TSPTELARGD VLKSVQCYMH ETGASEERAR DHVHQMISDM WDDMNSETKT
ACNSSSRSRG FKEAAMNLAR MSQCMYQYGD GHGCPEKAKT IDRVQSLLVD PIPLDVNRLG
