CPT3_SOLLC
ID CPT3_SOLLC Reviewed; 290 AA.
AC K7WCI9;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Dehydrodolichyl diphosphate synthase CPT3 {ECO:0000305};
DE EC=2.5.1.87 {ECO:0000305|PubMed:23134568};
DE AltName: Full=Cis-prenyltransferase 3 {ECO:0000303|PubMed:23134568};
DE Short=SlCPT3 {ECO:0000303|PubMed:23134568};
GN Name=CPT3 {ECO:0000303|PubMed:23134568};
GN OrderedLocusNames=Solyc03g025560 {ECO:0000305};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23134568; DOI=10.1111/tpj.12063;
RA Akhtar T.A., Matsuba Y., Schauvinhold I., Yu G., Lees H.A., Klein S.E.,
RA Pichersky E.;
RT "The tomato cis-prenyltransferase gene family.";
RL Plant J. 73:640-652(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
CC -!- FUNCTION: Catalyzes cis-prenyl chain elongation to produce the
CC polyprenyl backbone of dolichol, a glycosyl carrier-lipid required for
CC the biosynthesis of several classes of glycoprotein.
CC {ECO:0000305|PubMed:23134568}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = di-
CC trans,poly-cis-polyprenyl diphosphate + n diphosphate;
CC Xref=Rhea:RHEA:53008, Rhea:RHEA-COMP:13431, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:136960, ChEBI:CHEBI:175763;
CC EC=2.5.1.87; Evidence={ECO:0000305|PubMed:23134568};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53009;
CC Evidence={ECO:0000305|PubMed:23134568};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:23134568};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23134568}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf trichomes and stem trichomes
CC (PubMed:23134568). Expressed at low levels in young leaves, stems and
CC old leaves (PubMed:23134568). {ECO:0000269|PubMed:23134568}.
CC -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}.
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DR EMBL; JX943885; AFW98427.1; -; Genomic_DNA.
DR EMBL; CM001066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001307121.1; NM_001320192.1.
DR AlphaFoldDB; K7WCI9; -.
DR SMR; K7WCI9; -.
DR STRING; 4081.Solyc03g025560.2.1; -.
DR EnsemblPlants; Solyc03g025560.3.1; Solyc03g025560.3.1.1; Solyc03g025560.3.
DR GeneID; 101253666; -.
DR Gramene; Solyc03g025560.3.1; Solyc03g025560.3.1.1; Solyc03g025560.3.
DR KEGG; sly:101253666; -.
DR OMA; TKGQPDP; -.
DR OrthoDB; 1362420at2759; -.
DR BRENDA; 2.5.1.87; 3101.
DR Proteomes; UP000004994; Chromosome 3.
DR ExpressionAtlas; K7WCI9; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0002094; F:polyprenyltransferase activity; IBA:GO_Central.
DR GO; GO:0004659; F:prenyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016094; P:polyprenol biosynthetic process; IBA:GO_Central.
DR CDD; cd00475; Cis_IPPS; 1.
DR Gene3D; 3.40.1180.10; -; 1.
DR HAMAP; MF_01139; ISPT; 1.
DR InterPro; IPR001441; UPP_synth-like.
DR InterPro; IPR018520; UPP_synth-like_CS.
DR InterPro; IPR036424; UPP_synth-like_sf.
DR PANTHER; PTHR10291; PTHR10291; 1.
DR Pfam; PF01255; Prenyltransf; 1.
DR SUPFAM; SSF64005; SSF64005; 1.
DR TIGRFAMs; TIGR00055; uppS; 1.
DR PROSITE; PS01066; UPP_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Magnesium; Metal-binding; Reference proteome; Transferase.
FT CHAIN 1..290
FT /note="Dehydrodolichyl diphosphate synthase CPT3"
FT /id="PRO_0000450934"
FT ACT_SITE 42
FT /evidence="ECO:0000250|UniProtKB:P60472"
SQ SEQUENCE 290 AA; 33271 MW; 7AC42C46D7AC64B1 CRC64;
MEGVNGKKVG HLCENISSFV RQCIFSILSV GPVPSHIAFI MDGNRRYSKK QNLLDGNGHR
AGFSALINML KYCYELGVKY ITVYAFSIDN FKRRPEEVVS LMKLMQEKID ELTKEESIVN
RLGIRIYFQG NLKLLSDHVR LAAERAMVKT SGNSKAILSI CVAYTSTDEI VHAVQESCEE
KWDEIRKLDV NNDGSNLIRL EENVKDKNEH RIGVTNVDRH MYMSVCPDPD IIIRTSGATR
LSNFLLWQSS HCLLYSPAAL WPEIGLRHLI WVILDFQRNY LYLKEKKKQS
