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Dehydrodolichyl diphosphate synthase complex subunit nus1 (EC 2.5.1.87) (Di-trans,poly-cis-decaprenylcistransferase) (Undecaprenyl diphosphate synthase) (UDS)

 UPPS_SCHPO              Reviewed;         258 AA.
Q9Y7K8;
04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
28-FEB-2018, entry version 103.
RecName: Full=Dehydrodolichyl diphosphate synthase complex subunit nus1 {ECO:0000305};
EC=2.5.1.87 {ECO:0000269|PubMed:25066056};
AltName: Full=Di-trans,poly-cis-decaprenylcistransferase;
AltName: Full=Undecaprenyl diphosphate synthase {ECO:0000303|PubMed:25066056};
Short=UDS {ECO:0000305};
Name=nus1; ORFNames=SPBC2A9.06c;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, AND MUTAGENESIS OF ARG-255.
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).
-!- FUNCTION: With SPAC4D7.04c, 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).
{ECO:0000269|PubMed:25066056}.
-!- CATALYTIC ACTIVITY: (2E,6E)-farnesyl diphosphate + n isopentenyl
diphosphate = n diphosphate + ditrans,polycis-polyprenyl
diphosphate (n = 10-55). {ECO:0000269|PubMed:25066056}.
-!- PATHWAY: Protein modification; protein glycosylation.
{ECO:0000305}.
-!- SUBUNIT: Forms an active dehydrodolichyl diphosphate synthase
complex with SPAC4D7.04c. {ECO:0000303|PubMed:25066056}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
-!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}.
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EMBL; CU329671; CAB39848.1; -; Genomic_DNA.
PIR; T40097; T40097.
RefSeq; NP_596215.1; NM_001022134.2.
ProteinModelPortal; Q9Y7K8; -.
BioGrid; 276927; 1.
STRING; 4896.SPBC2A9.06c.1; -.
MaxQB; Q9Y7K8; -.
PaxDb; Q9Y7K8; -.
PRIDE; Q9Y7K8; -.
EnsemblFungi; SPBC2A9.06c.1; SPBC2A9.06c.1:pep; SPBC2A9.06c.
GeneID; 2540399; -.
KEGG; spo:SPBC2A9.06c; -.
EuPathDB; FungiDB:SPBC2A9.06c; -.
PomBase; SPBC2A9.06c; nus1.
InParanoid; Q9Y7K8; -.
KO; K19177; -.
OMA; HIRLTEF; -.
OrthoDB; EOG092C50UF; -.
PhylomeDB; Q9Y7K8; -.
Reactome; R-SPO-446199; Synthesis of Dolichyl-phosphate.
UniPathway; UPA00378; -.
PRO; PR:Q9Y7K8; -.
Proteomes; UP000002485; Chromosome II.
GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
GO; GO:0019408; P:dolichol biosynthetic process; IDA:PomBase.
GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
Gene3D; 3.40.1180.10; -; 1.
InterPro; IPR036424; UPP_synth-like_sf.
SUPFAM; SSF64005; SSF64005; 1.
1: Evidence at protein level;
Complete proteome; Endoplasmic reticulum; Membrane;
Reference proteome; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 258 Dehydrodolichyl diphosphate synthase
complex subunit nus1.
/FTId=PRO_0000353827.
TRANSMEM 5 21 Helical. {ECO:0000255}.
MUTAGEN 255 255 R->H: Loss of function.
SEQUENCE 258 AA; 29863 MW; B6979D3C8B932AC0 CRC64;
MYDDIFFYLA LWVIQSVYGA WDWAKNWVFW TCSYLLNFLY HHHCSRDLIR RDTKKLKKKP
KHIAVIIECV EDGGIEGLIH DACELSAWCV CSNIRELTIY ERKGFLKQSP EAVEKAIYSH
LPFYLGGDKC TVHVTNPCSP DEKNQNDCVD LKVHLIAKED GRDAIIDLTR GLADLCTKKV
ISSTQVTLEL IDKELKESVI PEPDLLIIFA PLLKLQGFPP WQLRLCEIFH DPILYTTNYL
TFFKALVHYS NAEMRLGH


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