ID   DDPS4_ARATH             Reviewed;         289 AA.
AC   Q8GY03; Q8LFW9; Q9LUY2;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=Dehydrodolichyl diphosphate synthase 4;
DE            Short=Dedol-PP synthase 4;
DE            EC=2.5.1.-;
GN   OrderedLocusNames=At5g58782; ORFNames=MZN1.23;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(2000).
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=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA97347.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB020755; BAA97347.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED97098.1; -; Genomic_DNA.
DR   EMBL; AK117939; BAC42577.1; -; mRNA.
DR   EMBL; BT005285; AAO63349.1; -; mRNA.
DR   EMBL; AY084601; AAM67372.1; -; mRNA.
DR   RefSeq; NP_568883.1; NM_125266.4.
DR   AlphaFoldDB; Q8GY03; -.
DR   SMR; Q8GY03; -.
DR   BioGRID; 21237; 1.
DR   IntAct; Q8GY03; 1.
DR   STRING; 3702.AT5G58782.1; -.
DR   PaxDb; Q8GY03; -.
DR   PRIDE; Q8GY03; -.
DR   ProteomicsDB; 224043; -.
DR   EnsemblPlants; AT5G58782.1; AT5G58782.1; AT5G58782.
DR   GeneID; 835993; -.
DR   Gramene; AT5G58782.1; AT5G58782.1; AT5G58782.
DR   KEGG; ath:AT5G58782; -.
DR   Araport; AT5G58782; -.
DR   TAIR; locus:505006701; AT5G58782.
DR   eggNOG; KOG1602; Eukaryota.
DR   HOGENOM; CLU_038505_1_0_1; -.
DR   InParanoid; Q8GY03; -.
DR   OMA; MIAVNYG; -.
DR   PhylomeDB; Q8GY03; -.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q8GY03; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8GY03; baseline and differential.
DR   Genevisible; Q8GY03; AT.
DR   GO; GO:0009570; C:chloroplast stroma; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045547; F:dehydrodolichyl diphosphate synthase activity; IBA:GO_Central.
DR   GO; GO:0002094; F:polyprenyltransferase activity; IBA:GO_Central.
DR   GO; GO:0009668; P:plastid membrane organization; IBA:GO_Central.
DR   GO; GO:0016094; P:polyprenol biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009409; P:response to cold; 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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..289
FT                   /note="Dehydrodolichyl diphosphate synthase 4"
FT                   /id="PRO_0000123754"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        216
FT                   /note="L -> F (in Ref. 5; AAM67372)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   289 AA;  33710 MW;  4ED6ED5B63F9C244 CRC64;
     MLSMLWFLLS LLSLLLLPCL RPCFPAKGSL KNKKKIDKGT YVVGEEETPK ELQRELMPRH
     VAVIMDGNRR WAKQTGLLTS QGYEAGAKRL LEFADLCFKL GINTVSAFAF STENWGRHKI
     EVKCLMYLFQ RYLKSKIQFF QSKEIRVSVI GNLAKIPESL LRTVHELEEA TKSYKKKHLI
     LAIDYSGRFD ILGACKNIVK KSEQGLIREE DVDETLFERE LQTRCTEFPS PDLLIRTSGE
     QRISNFFLWQ LAYTEFFFSP VLWPDFDKQK FIEALVSYQR RDRRFGSRL