ID   RER2_ENCCU              Reviewed;         270 AA.
AC   Q8SQJ8;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Dehydrodolichyl diphosphate synthase;
DE            Short=DEDOL-PP synthase;
DE            EC=2.5.1.-;
GN   Name=RER2; OrderedLocusNames=ECU09_1870;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
CC   -!- FUNCTION: Cis-prenyl transferase that adds multiple copies of
CC       isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to
CC       produce dehydrodolichyl diphosphate (Dedol-PP). {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
CC   -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}.
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DR   EMBL; AL590451; CAD27160.1; -; Genomic_DNA.
DR   RefSeq; XP_955741.1; XM_950648.1.
DR   AlphaFoldDB; Q8SQJ8; -.
DR   SMR; Q8SQJ8; -.
DR   STRING; 284813.Q8SQJ8; -.
DR   PRIDE; Q8SQJ8; -.
DR   GeneID; 860529; -.
DR   KEGG; ecu:ECU09_1870; -.
DR   VEuPathDB; MicrosporidiaDB:ECU09_1870; -.
DR   HOGENOM; CLU_086428_0_0_1; -.
DR   InParanoid; Q8SQJ8; -.
DR   OMA; ICIAYNS; -.
DR   OrthoDB; 1362420at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000000819; Chromosome IX.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR   GO; GO:0019408; P:dolichol biosynthetic process; IEA:UniProt.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd00475; Cis_IPPS; 1.
DR   Gene3D; 3.40.1180.10; -; 2.
DR   InterPro; IPR001441; UPP_synth-like.
DR   InterPro; IPR036424; UPP_synth-like_sf.
DR   PANTHER; PTHR10291; PTHR10291; 2.
DR   Pfam; PF01255; Prenyltransf; 2.
DR   SUPFAM; SSF64005; SSF64005; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Transferase.
FT   CHAIN           1..270
FT                   /note="Dehydrodolichyl diphosphate synthase"
FT                   /id="PRO_0000382907"
SQ   SEQUENCE   270 AA;  31180 MW;  14303A4D03567B53 CRC64;
     MIEGLKVKAL ICVVEIIENG INSIHAMGIL LFALNILKKA SVLVSRILCA WNGKLSSEYP
     RDPRSRLGIF KNMNIAFICD GNRRYARKLG LEDSFIKDKG LQKIYEFIEF GCFYGIKEIS
     FFCFALSNFK RSPEEVNKLM GLVKQKIERP KEIGIRPKFR VYGRLDLLEE DVRKRLMDIE
     EESKNNTSII VNIFFAYSAE DEITRGIQFN SHVDILIRTS NTKRLSNFMI RQVAKGTSVF
     FAKALWPELT TAHLFLILLK HRLENKYLLG