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TPS20_ARATH
ID   TPS20_ARATH             Reviewed;         575 AA.
AC   Q9FI27; F4K067; Q8RXC7;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2017, sequence version 3.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Inactive terpenoid synthase 20, chloroplastic {ECO:0000305};
DE            Short=AtTPS20 {ECO:0000303|PubMed:12207221};
DE   Flags: Precursor;
GN   Name=TPS20 {ECO:0000303|PubMed:12207221};
GN   OrderedLocusNames=At5g48110 {ECO:0000312|Araport:AT5G48110};
GN   ORFNames=MDN11.20 {ECO:0000312|EMBL:BAB11075.1};
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT   features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT   clones.";
RL   DNA Res. 6:183-195(1999).
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   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   [5]
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   [6]
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).
RN   [7]
RP   FUNCTION, AND LACK OF CATALYTIC ACTIVITY.
RX   PubMed=27933080; DOI=10.3389/fpls.2016.01761;
RA   Wang Q., Jia M., Huh J.H., Muchlinski A., Peters R.J., Tholl D.;
RT   "Identification of a dolabellane type diterpene synthase and other root-
RT   expressed diterpene synthases in Arabidopsis.";
RL   Front. Plant Sci. 7:1761-1761(2016).
CC   -!- FUNCTION: Does not possess diterpene synthase activity.
CC       {ECO:0000269|PubMed:27933080}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in roots but also in leaves
CC       and stems. {ECO:0000269|PubMed:12566586}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: TPS20 in Arabidopsis ecotype Columbia lacks dolabellane-type
CC       diterpene synthase activity because of a 17 amino acid deletion and
CC       several mutations in its sequence. TPS20 protein in ecotype Cvi is
CC       functional and possesses dolabellane-type diterpene synthase activity.
CC       {ECO:0000269|PubMed:27933080}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL91230.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAL91230.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; AB017064; BAB11075.1; -; Genomic_DNA.
DR   EMBL; CP002688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY081341; AAL91230.1; ALT_SEQ; mRNA.
DR   EMBL; BT000253; AAN15572.1; -; mRNA.
DR   RefSeq; NP_001318758.1; NM_001344758.1.
DR   AlphaFoldDB; Q9FI27; -.
DR   SMR; Q9FI27; -.
DR   STRING; 3702.AT5G48110.1; -.
DR   iPTMnet; Q9FI27; -.
DR   PeptideAtlas; Q9FI27; -.
DR   PRIDE; Q9FI27; -.
DR   EnsemblPlants; AT5G48110.1; AT5G48110.1; AT5G48110.
DR   GeneID; 834863; -.
DR   Gramene; AT5G48110.1; AT5G48110.1; AT5G48110.
DR   KEGG; ath:AT5G48110; -.
DR   Araport; AT5G48110; -.
DR   eggNOG; ENOG502QUCN; Eukaryota.
DR   InParanoid; Q9FI27; -.
DR   OrthoDB; 360509at2759; -.
DR   PhylomeDB; Q9FI27; -.
DR   BioCyc; ARA:AT5G48110-MON; -.
DR   PRO; PR:Q9FI27; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FI27; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009975; F:cyclase activity; IBA:GO_Central.
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   GO; GO:0051762; P:sesquiterpene biosynthetic process; IBA:GO_Central.
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   Chloroplast; Lyase; Magnesium; Manganese; Metal-binding; Plastid;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..52
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           53..575
FT                   /note="Inactive terpenoid synthase 20, chloroplastic"
FT                   /id="PRO_0000403711"
FT   MOTIF           332..336
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000305"
FT   BINDING         332
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         332
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         336
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         336
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         474
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         478
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         482
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
SQ   SEQUENCE   575 AA;  66946 MW;  81D73E8461ABA4E4 CRC64;
     MEAITKNGSL SQTLVHCGPK SLSSFIPVRC LRFSKNPFPK KLVVTRARTS INSDHEAANR
     PLFQFPPSLL DDRFLSISAN QSEIDSLGRD IEALKAKVSE KLVCMDVKER IHLIHLLVSL
     GVAYHFEKQI EEFLKVDFEN VEDMNLGEED MYSISVIFRV FRLYRHKLSS DVFNRFKEEN
     GDFKKCLLDD KKSLTKQWAS RGNTWNYFVG GSNEEHLSGH IKNVLYLSQQ ENAEVVMSRE
     YIQFYEQETH HDETLLKFAK INFKFMQLHY VQELQTIVKW WKELDLESKI PNYYRVRAVE
     CLYWAMAVYM EPQYSVARII LSKSLVLWTI IDDLYDAYCT LPEAIAFTEN MERWETDAID
     MPDHMKVLLR SLIDLMEDFK GEVRSEGRLY SVEYGIDEWK RLFRADLTIS KWARTGYIPN
     YDEYMEVGIV TGGVDVTVAF AFIGMGEAGK EAFDWIRSRP KFIQTIDLKS RLRDDVATYK
     DEMARGEIAT GINCYMKQYK VTEEEAFLEF HRRIKHTSKL VNEEYFKTTV PLKLVRIAFN
     VGRVIDTNYK HGDGLTYTGI VGGQITSLFL DLITI
 
 
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