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Dehydrodolichyl diphosphate synthase complex subunit DHDDS (EC 2.5.1.87) (Cis-isoprenyltransferase) (CIT) (Cis-IPTase) (Epididymis tissue protein Li 189m)

 DHDDS_HUMAN             Reviewed;         333 AA.
Q86SQ9; B7Z4B9; B7ZB20; D3DPK7; D3DPK8; D3DPK9; E9KL43; Q5T0A4;
Q8NE90; Q9BTG5; Q9BTK3; Q9H905;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
23-MAY-2018, entry version 139.
RecName: Full=Dehydrodolichyl diphosphate synthase complex subunit DHDDS {ECO:0000305};
EC=2.5.1.87 {ECO:0000269|PubMed:25066056};
AltName: Full=Cis-isoprenyltransferase;
Short=CIT;
Short=Cis-IPTase;
AltName: Full=Epididymis tissue protein Li 189m;
Name=DHDDS; Synonyms=HDS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=12591616; DOI=10.1016/S0167-4781(02)00628-0;
Endo S., Zhang Y.-W., Takahashi S., Koyama T.;
"Identification of human dehydrodolichyl diphosphate synthase gene.";
Biochim. Biophys. Acta 1625:291-295(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-253, AND TISSUE
SPECIFICITY.
TISSUE=Epididymis;
PubMed=20736409; DOI=10.1074/mcp.M110.001719;
Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W.,
Zhang C., Jin S., Liu J., Zhu P., Liu Y.;
"Systematic mapping and functional analysis of a family of human
epididymal secretory sperm-located proteins.";
Mol. Cell. Proteomics 9:2517-2528(2010).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), AND VARIANT
MET-253.
TISSUE=Teratocarcinoma, and Thyroid;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
MET-253.
TISSUE=Lung, Muscle, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=14652022; DOI=10.1016/j.bbrc.2003.11.065;
Shridas P., Rush J.S., Waechter C.J.;
"Identification and characterization of a cDNA encoding a long-chain
cis-isoprenyltransferase involved in dolichyl monophosphate
biosynthesis in the ER of brain cells.";
Biochem. Biophys. Res. Commun. 312:1349-1356(2003).
[8]
INTERACTION WITH NUS1.
PubMed=21572394; DOI=10.1038/emboj.2011.147;
Harrison K.D., Park E.J., Gao N., Kuo A., Rush J.S., Waechter C.J.,
Lehrman M.A., Sessa W.C.;
"Nogo-B receptor is necessary for cellular dolichol biosynthesis and
protein N-glycosylation.";
EMBO J. 30:2490-2500(2011).
[9]
CATALYTIC ACTIVITY, FUNCTION, AND SUBUNIT.
PubMed=25066056; DOI=10.1016/j.cmet.2014.06.016;
Park E.J., Grabinska K.A., Guan Z., Stranecky V., Hartmannova H.,
Hodanova K., Baresova V., Sovova J., Jozsef L., Ondruskova N.,
Hansikova H., Honzik T., Zeman J., Hulkova H., Wen R., Kmoch S.,
Sessa W.C.;
"Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase,
causes a congenital disorder of glycosylation.";
Cell Metab. 20:448-457(2014).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[11]
VARIANT RP59 GLU-42.
PubMed=21295283; DOI=10.1016/j.ajhg.2011.01.001;
Zuchner S., Dallman J., Wen R., Beecham G., Naj A., Farooq A.,
Kohli M.A., Whitehead P.L., Hulme W., Konidari I., Edwards Y.J.,
Cai G., Peter I., Seo D., Buxbaum J.D., Haines J.L., Blanton S.,
Young J., Alfonso E., Vance J.M., Lam B.L., Pericak-Vance M.A.;
"Whole-exome sequencing links a variant in DHDDS to retinitis
pigmentosa.";
Am. J. Hum. Genet. 88:201-206(2011).
-!- FUNCTION: With DHDDS, forms the dehydrodolichyl diphosphate
synthase (DDS) complex, an essential component of the dolichol
monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies
of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP)
to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of
dolichol which is utilized as a sugar carrier in protein
glycosylation in the endoplasmic reticulum (ER). Regulates the
glycosylation and stability of nascent NPC2, thereby promoting
trafficking of LDL-derived cholesterol.
{ECO:0000269|PubMed:25066056, ECO:0000303|PubMed:21572394}.
-!- CATALYTIC ACTIVITY: (2E,6E)-farnesyl diphosphate + n isopentenyl
diphosphate = n diphosphate + ditrans,polycis-polyprenyl
diphosphate (n = 10-55). {ECO:0000303|PubMed:25066056}.
-!- PATHWAY: Protein modification; protein glycosylation.
{ECO:0000305}.
-!- SUBUNIT: Forms an active dehydrodolichyl diphosphate synthase
complex with NUS1. Interacts with NPC2.
{ECO:0000269|PubMed:21572394, ECO:0000269|PubMed:25066056}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:14652022}; Peripheral membrane protein
{ECO:0000269|PubMed:14652022}. Note=colocalizes with calnexin.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q86SQ9-1; Sequence=Displayed;
Name=2;
IsoId=Q86SQ9-2; Sequence=VSP_010031;
Name=3;
IsoId=Q86SQ9-3; Sequence=VSP_010030;
Note=May be due to exon skipping.;
Name=4;
IsoId=Q86SQ9-4; Sequence=VSP_045007;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed at high levels in testis and kidney.
Expressed in epididymis (at protein level). Slightly expressed in
heart, spleen and thymus. {ECO:0000269|PubMed:20736409}.
-!- DISEASE: Retinitis pigmentosa 59 (RP59) [MIM:613861]: A retinal
dystrophy belonging to the group of pigmentary retinopathies.
Retinitis pigmentosa is characterized by retinal pigment deposits
visible on fundus examination and primary loss of rod
photoreceptor cells followed by secondary loss of cone
photoreceptors. Patients typically have night vision blindness and
loss of midperipheral visual field. As their condition progresses,
they lose their far peripheral visual field and eventually central
vision as well. {ECO:0000269|PubMed:21295283}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}.
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EMBL; AB090852; BAC57588.1; -; mRNA.
EMBL; GU727641; ADU87642.1; -; mRNA.
EMBL; AK023164; BAB14439.1; -; mRNA.
EMBL; AK297134; BAH12505.1; -; mRNA.
EMBL; AK316485; BAH14856.1; -; mRNA.
EMBL; AL513365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX07806.1; -; Genomic_DNA.
EMBL; CH471059; EAX07808.1; -; Genomic_DNA.
EMBL; CH471059; EAX07809.1; -; Genomic_DNA.
EMBL; CH471059; EAX07810.1; -; Genomic_DNA.
EMBL; CH471059; EAX07811.1; -; Genomic_DNA.
EMBL; CH471059; EAX07812.1; -; Genomic_DNA.
EMBL; BC003643; AAH03643.1; -; mRNA.
EMBL; BC004117; AAH04117.1; -; mRNA.
EMBL; BC034152; AAH34152.1; -; mRNA.
CCDS; CCDS281.1; -. [Q86SQ9-2]
CCDS; CCDS282.1; -. [Q86SQ9-1]
CCDS; CCDS57983.1; -. [Q86SQ9-4]
CCDS; CCDS57984.1; -. [Q86SQ9-3]
RefSeq; NP_001230493.1; NM_001243564.1. [Q86SQ9-4]
RefSeq; NP_001230494.1; NM_001243565.1. [Q86SQ9-3]
RefSeq; NP_079163.2; NM_024887.3. [Q86SQ9-2]
RefSeq; NP_995583.1; NM_205861.2. [Q86SQ9-1]
RefSeq; XP_006710975.1; XM_006710912.2. [Q86SQ9-2]
RefSeq; XP_006710976.1; XM_006710913.2. [Q86SQ9-2]
RefSeq; XP_006710977.1; XM_006710914.2. [Q86SQ9-2]
RefSeq; XP_011540485.1; XM_011542183.2. [Q86SQ9-2]
RefSeq; XP_011540486.1; XM_011542184.2. [Q86SQ9-1]
RefSeq; XP_011540488.1; XM_011542186.2. [Q86SQ9-4]
RefSeq; XP_016857868.1; XM_017002379.1. [Q86SQ9-1]
RefSeq; XP_016857869.1; XM_017002380.1. [Q86SQ9-1]
UniGene; Hs.369385; -.
ProteinModelPortal; Q86SQ9; -.
SMR; Q86SQ9; -.
BioGrid; 123018; 6.
CORUM; Q86SQ9; -.
STRING; 9606.ENSP00000353104; -.
iPTMnet; Q86SQ9; -.
PhosphoSitePlus; Q86SQ9; -.
BioMuta; DHDDS; -.
DMDM; 116241329; -.
MaxQB; Q86SQ9; -.
PaxDb; Q86SQ9; -.
PeptideAtlas; Q86SQ9; -.
PRIDE; Q86SQ9; -.
DNASU; 79947; -.
Ensembl; ENST00000236342; ENSP00000236342; ENSG00000117682. [Q86SQ9-1]
Ensembl; ENST00000360009; ENSP00000353104; ENSG00000117682. [Q86SQ9-2]
Ensembl; ENST00000525682; ENSP00000434984; ENSG00000117682. [Q86SQ9-4]
Ensembl; ENST00000526219; ENSP00000434219; ENSG00000117682. [Q86SQ9-3]
GeneID; 79947; -.
KEGG; hsa:79947; -.
UCSC; uc001bmk.4; human. [Q86SQ9-1]
CTD; 79947; -.
DisGeNET; 79947; -.
EuPathDB; HostDB:ENSG00000117682.16; -.
GeneCards; DHDDS; -.
GeneReviews; DHDDS; -.
HGNC; HGNC:20603; DHDDS.
HPA; HPA026721; -.
HPA; HPA026727; -.
MalaCards; DHDDS; -.
MIM; 608172; gene.
MIM; 613861; phenotype.
neXtProt; NX_Q86SQ9; -.
OpenTargets; ENSG00000117682; -.
Orphanet; 791; Retinitis pigmentosa.
PharmGKB; PA134867119; -.
eggNOG; KOG1602; Eukaryota.
eggNOG; COG0020; LUCA.
GeneTree; ENSGT00390000007879; -.
HOVERGEN; HBG051350; -.
InParanoid; Q86SQ9; -.
KO; K11778; -.
OMA; FDRRDLW; -.
OrthoDB; EOG091G0K4O; -.
PhylomeDB; Q86SQ9; -.
TreeFam; TF323753; -.
BRENDA; 2.5.1.87; 2681.
Reactome; R-HSA-446199; Synthesis of Dolichyl-phosphate.
Reactome; R-HSA-4755609; Defective DHDDS causes retinitis pigmentosa 59.
UniPathway; UPA00378; -.
ChiTaRS; DHDDS; human.
GeneWiki; Dehydrodolichyl_diphosphate_synthase; -.
GeneWiki; DHDDS; -.
GenomeRNAi; 79947; -.
PRO; PR:Q86SQ9; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000117682; -.
CleanEx; HS_DHDDS; -.
ExpressionAtlas; Q86SQ9; baseline and differential.
Genevisible; Q86SQ9; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
GO; GO:0016094; P:polyprenol biosynthetic process; IBA:GO_Central.
GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
CDD; cd00475; Cis_IPPS; 1.
Gene3D; 3.40.1180.10; -; 1.
HAMAP; MF_01139; ISPT; 1.
InterPro; IPR001441; UPP_synth-like.
InterPro; IPR018520; UPP_synth-like_CS.
InterPro; IPR036424; UPP_synth-like_sf.
PANTHER; PTHR10291; PTHR10291; 1.
Pfam; PF01255; Prenyltransf; 1.
SUPFAM; SSF64005; SSF64005; 1.
TIGRFAMs; TIGR00055; uppS; 1.
PROSITE; PS01066; UPP_SYNTHASE; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disease mutation;
Endoplasmic reticulum; Membrane; Polymorphism; Reference proteome;
Retinitis pigmentosa; Transferase.
CHAIN 1 333 Dehydrodolichyl diphosphate synthase
complex subunit DHDDS.
/FTId=PRO_0000123749.
VAR_SEQ 109 147 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_010030.
VAR_SEQ 147 181 KCFLNVCFAYTSRHEISNAVREMAWGVEQGLLDPS -> N
(in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045007.
VAR_SEQ 255 255 Q -> QQ (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_010031.
VARIANT 42 42 K -> E (in RP59; dbSNP:rs147394623).
{ECO:0000269|PubMed:21295283}.
/FTId=VAR_065356.
VARIANT 253 253 V -> M (in dbSNP:rs3816539).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:20736409}.
/FTId=VAR_028088.
CONFLICT 151 151 N -> Y (in Ref. 3; BAB14439).
{ECO:0000305}.
CONFLICT 277 277 V -> E (in Ref. 6; AAH34152).
{ECO:0000305}.
SEQUENCE 333 AA; 38657 MW; 12EF3A15437A2583 CRC64;
MSWIKEGELS LWERFCANII KAGPMPKHIA FIMDGNRRYA KKCQVERQEG HSQGFNKLAE
TLRWCLNLGI LEVTVYAFSI ENFKRSKSEV DGLMDLARQK FSRLMEEKEK LQKHGVCIRV
LGDLHLLPLD LQELIAQAVQ ATKNYNKCFL NVCFAYTSRH EISNAVREMA WGVEQGLLDP
SDISESLLDK CLYTNRSPHP DILIRTSGEV RLSDFLLWQT SHSCLVFQPV LWPEYTFWNL
FEAILQFQMN HSVLQKARDM YAEERKRQQL ERDQATVTEQ LLREGLQASG DAQLRRTRLH
KLSARREERV QGFLQALELK RADWLARLGT ASA


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YF-PA20968 Mouse polyclonal to Anti-Dehydrodolichyl Diphosphate Synthase, Host Mouse 50 ug
YF-PA20967 Mouse polyclonal to Anti-Dehydrodolichyl Diphosphate Synthase, Host Mouse 50 uL
YF-PA20969 anti-anti-Dehydrodolichyl Diphosphate Synthase type: Primary antibodies host: Rabbit 100 ul
YF-PA20967 anti-anti-Dehydrodolichyl Diphosphate Synthase type: Primary antibodies host: Mouse 50 ul
26-361 Dehydrodolichyl diphosphate (dedol-PP) synthase catalyzes cis-prenyl chain elongation to produce the polyprenyl backbone of dolichol, a glycosyl carrier lipid required for the biosynthesis of several 0.05 mg


 

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