ID   UPPS_SCHPO              Reviewed;         258 AA.
AC   Q9Y7K8;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Dehydrodolichyl diphosphate synthase complex subunit nus1 {ECO:0000305};
DE            EC=2.5.1.87 {ECO:0000269|PubMed:25066056};
GN   Name=nus1; ORFNames=SPBC2A9.06c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, AND MUTAGENESIS OF ARG-255.
RX   PubMed=25066056; DOI=10.1016/j.cmet.2014.06.016;
RA   Park E.J., Grabinska K.A., Guan Z., Stranecky V., Hartmannova H.,
RA   Hodanova K., Baresova V., Sovova J., Jozsef L., Ondruskova N.,
RA   Hansikova H., Honzik T., Zeman J., Hulkova H., Wen R., Kmoch S.,
RA   Sessa W.C.;
RT   "Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a
RT   congenital disorder of glycosylation.";
RL   Cell Metab. 20:448-457(2014).
CC   -!- FUNCTION: With SPAC4D7.04c, forms the dehydrodolichyl diphosphate
CC       synthase (DDS) complex, an essential component of the dolichol
CC       monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of
CC       isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to
CC       produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol
CC       which is utilized as a sugar carrier in protein glycosylation in the
CC       endoplasmic reticulum (ER). {ECO:0000269|PubMed:25066056}.
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:0000269|PubMed:25066056};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q96E22};
CC   -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC   -!- SUBUNIT: Forms an active dehydrodolichyl diphosphate synthase complex
CC       with SPAC4D7.04c. {ECO:0000303|PubMed:25066056}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Single-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}.
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DR   EMBL; CU329671; CAB39848.1; -; Genomic_DNA.
DR   PIR; T40097; T40097.
DR   RefSeq; NP_596215.1; NM_001022134.2.
DR   AlphaFoldDB; Q9Y7K8; -.
DR   SMR; Q9Y7K8; -.
DR   BioGRID; 276927; 1.
DR   STRING; 4896.SPBC2A9.06c.1; -.
DR   MaxQB; Q9Y7K8; -.
DR   PaxDb; Q9Y7K8; -.
DR   EnsemblFungi; SPBC2A9.06c.1; SPBC2A9.06c.1:pep; SPBC2A9.06c.
DR   GeneID; 2540399; -.
DR   KEGG; spo:SPBC2A9.06c; -.
DR   PomBase; SPBC2A9.06c; nus1.
DR   VEuPathDB; FungiDB:SPBC2A9.06c; -.
DR   eggNOG; KOG2818; Eukaryota.
DR   HOGENOM; CLU_051870_1_0_1; -.
DR   InParanoid; Q9Y7K8; -.
DR   OMA; MPRVYEA; -.
DR   PhylomeDB; Q9Y7K8; -.
DR   BRENDA; 2.5.1.87; 5613.
DR   Reactome; R-SPO-446199; Synthesis of Dolichyl-phosphate.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q9Y7K8; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:1904423; C:dehydrodolichyl diphosphate synthase complex; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IDA:PomBase.
DR   GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR   Gene3D; 3.40.1180.10; -; 1.
DR   InterPro; IPR038887; Nus1/NgBR.
DR   InterPro; IPR036424; UPP_synth-like_sf.
DR   PANTHER; PTHR21528; PTHR21528; 1.
DR   SUPFAM; SSF64005; SSF64005; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Magnesium; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..258
FT                   /note="Dehydrodolichyl diphosphate synthase complex subunit
FT                   nus1"
FT                   /id="PRO_0000353827"
FT   TRANSMEM        5..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         255
FT                   /note="R->H: Loss of function."
SQ   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