TPS4_VITAC
ID TPS4_VITAC Reviewed; 789 AA.
AC A0A2K9RFY0;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 25-APR-2018, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Ent-kaurene synthase TSP4, chloroplastic {ECO:0000303|PubMed:29315936};
DE EC=4.2.3.19 {ECO:0000269|PubMed:29315936};
DE AltName: Full=Terpene synthase 4 {ECO:0000303|PubMed:29315936};
DE Short=VacTPS4 {ECO:0000303|PubMed:29315936};
GN Name=TPS4 {ECO:0000303|PubMed:29315936};
OS Vitex agnus-castus (Chaste tree).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Viticoideae; Vitex.
OX NCBI_TaxID=54477;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Fruit, Leaf, and Trichome gland;
RX PubMed=29315936; DOI=10.1111/tpj.13822;
RA Heskes A.M., Sundram T.C.M., Boughton B.A., Jensen N.B., Hansen N.L.,
RA Crocoll C., Cozzi F., Rasmussen S., Hamberger B., Hamberger B., Staerk D.,
RA Moeller B.L., Pateraki I.;
RT "Biosynthesis of bioactive diterpenoids in the medicinal plant Vitex agnus-
RT castus.";
RL Plant J. 93:943-958(2018).
RN [2]
RP REVIEW ON MENSTRUAL CYCLE DISORDERS.
RX PubMed=12809367; DOI=10.1078/094471103322004866;
RA Wuttke W., Jarry H., Christoffel V., Spengler B., Seidlova-Wuttke D.;
RT "Chaste tree (Vitex agnus-castus)--pharmacology and clinical indications.";
RL Phytomedicine 10:348-357(2003).
RN [3]
RP PATHWAY, AND REVIEW.
RX PubMed=30468448; DOI=10.1039/c8np00077h;
RA Liu Y., Jing S.-X., Luo S.-H., Li S.-H.;
RT "Non-volatile natural products in plant glandular trichomes: chemistry,
RT biological activities and biosynthesis.";
RL Nat. Prod. Rep. 36:626-665(2019).
CC -!- FUNCTION: Involved in the biosynthesis of labdane-type diterpenoid
CC including cleroda-dienols, and peregrinol lactones and furan
CC derivatives, dopaminergic diterpenoids that can bind to dopamine
CC receptors in the human pituitary gland, have probably ability to lower
CC prolactin levels, and are used to treat menstrual cycle disorders (e.g.
CC premenstrual syndrome and mastodynia) (Probable). Terpene synthase that
CC produces ent-kaurene from ent-copalyl diphosphate (PubMed:29315936).
CC {ECO:0000269|PubMed:29315936, ECO:0000305|PubMed:12809367,
CC ECO:0000305|PubMed:29315936, ECO:0000305|PubMed:30468448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ent-copalyl diphosphate = diphosphate + ent-kaur-16-ene;
CC Xref=Rhea:RHEA:22220, ChEBI:CHEBI:15415, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58553; EC=4.2.3.19;
CC Evidence={ECO:0000269|PubMed:29315936};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22221;
CC Evidence={ECO:0000269|PubMed:29315936};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};
CC -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC {ECO:0000305|PubMed:29315936, ECO:0000305|PubMed:30468448}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000305|PubMed:29315936}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and fruits, including
CC trichomes. {ECO:0000269|PubMed:29315936}.
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 {ECO:0000250|UniProtKB:G8GJ94}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; MG696751; AUT77123.1; -; mRNA.
DR AlphaFoldDB; A0A2K9RFY0; -.
DR SMR; A0A2K9RFY0; -.
DR UniPathway; UPA00390; -.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009899; F:ent-kaurene synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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 SUPFAM; SSF48239; SSF48239; 2.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Lyase; Magnesium; Membrane; Metal-binding; Plastid;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..789
FT /note="Ent-kaurene synthase TSP4, chloroplastic"
FT /id="PRO_0000449310"
FT TRANSMEM 638..656
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 540..544
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:G8GJ94"
FT BINDING 540
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 540
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 544
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 544
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 684
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 687
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 692
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 789 AA; 90215 MW; E689C527AD1351D4 CRC64;
MSLQLSNSLF FARKESHFRC FSHVSASLDT GVRRVTSAKI ASTCFEETKE RIADLIHKAE
LSVSTYDTAW VAMVPSPNSS QEPCFPDCLS WLLQNQCCDG SWACPHHHPL LKKDVLCSTL
ACVLALKKWG VGEEKINRGV HFIEHNFASA MEKCQISPMG FDIIFPAMLD YARDLLLNLR
LEPTMLNDLI YKRGLELKRN QNHSAEREAY LAYVAEGMGK LQDLGSVMKH QRRNGSLFNS
PSTTAAAFIA FPNSRCLTYL RSALKKFGSA VPAVYPLDIY LQLCTVDNLE RLGISRYFQK
EIQGVLDETY RCWLQGNEEI FMDAPTCALA FRVLRKNGYN VTSDPITKLL EECFSSSFCG
NIKDINTTLG LYRASEFILY PDERDLEKQN LMLKNLLEQE LSSDFIHSSQ LGRNIDAEVK
HALEYPFYAD LDRIVNRRNI EHYNFDNTRI LKTSYCSPNF GNKDFLFLSV KDYNECQAIH
REELRELERW VIENRLDELR FARQKCAYCY FSAAATLFAP ELSNARMSWA KNGVLTTVVD
DFFDLGGSVE ELKNLIQLVE LWDVDVSTEC SSQNVQIIFS ALKCTICDIG DKGSKLQERS
ITNHIIDIWL DLLYSMMKET EWARDKYIPT MDEYISNAYV SFALGPIVLP ALYLVGPKLS
EEMVHHSEYH NLYKLMSTCG RLLNDIRGCE RELKEGKLNA IPLYIINNGG EITKEAAASE
MKSLIETHRR ELLRLVLEGK NSVLPKSCKE LFWHMSKVLH LFYSKDDGFT SQDLIKVVKA
VIYEPIVLK
