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CIN2_ARATH
ID   CIN2_ARATH              Reviewed;         600 AA.
AC   P0DI77; 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 77.
DE   RecName: Full=1,8-cineole synthase 2, chloroplastic;
DE            Short=AtTPS-CIN2;
DE            EC=4.2.3.108;
DE   AltName: Full=Limonene cyclase;
DE   AltName: Full=Terpenoid synthase 23;
DE            Short=AtTPS23;
DE   Flags: Precursor;
GN   Name=TPS23; Synonyms=TPS-CIN2; OrderedLocusNames=At3g25830;
GN   ORFNames=K9I22.3;
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   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   [4]
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   [5]
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   [6]
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   [7]
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   [8]
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=P0DI77-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P0DI77-2; Sequence=VSP_044205, VSP_044206;
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; BAB01181.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77075.1; -; Genomic_DNA.
DR   EMBL; AK229712; BAF01550.1; -; mRNA.
DR   EMBL; AK319171; BAH57286.1; -; mRNA.
DR   RefSeq; NP_001326843.1; NM_001338768.1. [P0DI77-2]
DR   RefSeq; NP_001326844.1; NM_001338769.1. [P0DI77-2]
DR   RefSeq; NP_189210.2; NM_113483.5. [P0DI77-1]
DR   RefSeq; NP_189212.1; NM_113485.5. [P0DI77-1]
DR   AlphaFoldDB; P0DI77; -.
DR   SMR; P0DI77; -.
DR   EnsemblPlants; AT3G25820.1; AT3G25820.1; AT3G25820.
DR   EnsemblPlants; AT3G25820.3; AT3G25820.3; AT3G25820.
DR   EnsemblPlants; AT3G25820.4; AT3G25820.4; AT3G25820.
DR   EnsemblPlants; AT3G25830.1; AT3G25830.1; AT3G25830.
DR   GeneID; 822175; -.
DR   GeneID; 822177; -.
DR   Gramene; AT3G25820.1; AT3G25820.1; AT3G25820.
DR   Gramene; AT3G25820.3; AT3G25820.3; AT3G25820.
DR   Gramene; AT3G25820.4; AT3G25820.4; AT3G25820.
DR   Gramene; AT3G25830.1; AT3G25830.1; AT3G25830.
DR   KEGG; ath:AT3G25820; -.
DR   KEGG; ath:AT3G25830; -.
DR   Araport; AT3G25830; -.
DR   HOGENOM; CLU_003125_7_1_1; -.
DR   InParanoid; P0DI77; -.
DR   OMA; VRCAATI; -.
DR   OrthoDB; 401091at2759; -.
DR   PhylomeDB; P0DI77; -.
DR   BRENDA; 4.2.3.108; 399.
DR   BRENDA; 4.2.3.109; 399.
DR   SABIO-RK; P0DI77; -.
DR   UniPathway; UPA00213; -.
DR   PRO; PR:P0DI77; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; P0DI77; baseline and differential.
DR   Genevisible; P0DI77; 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 2, chloroplastic"
FT                   /id="PRO_0000419502"
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.4"
FT                   /id="VSP_044205"
FT   VAR_SEQ         396..600
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:19423640, ECO:0000303|Ref.4"
FT                   /id="VSP_044206"
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
 
 
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