YE54_SCHPO
ID YE54_SCHPO Reviewed; 264 AA.
AC O14171;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Dehydrodolichyl diphosphate synthase complex subunit SPAC4D7.04c {ECO:0000305};
DE EC=2.5.1.87 {ECO:0000303|PubMed:25066056};
DE AltName: Full=Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific) {ECO:0000305};
GN ORFNames=SPAC4D7.04c;
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, AND SUBUNIT.
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 nus1, forms the dehydrodolichyl diphosphate synthase
CC (DDS) complex, an essential component of the dolichol monophosphate
CC (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl
CC pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce
CC dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol which
CC 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:Q86SQ9};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBUNIT: Forms an active dehydrodolichyl diphosphate synthase complex
CC with nus1. {ECO:0000303|PubMed:25066056}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P35196}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P35196}.
CC -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11276.1; -; Genomic_DNA.
DR PIR; T38795; T38795.
DR RefSeq; NP_594957.1; NM_001020388.2.
DR AlphaFoldDB; O14171; -.
DR SMR; O14171; -.
DR BioGRID; 280034; 1.
DR STRING; 4896.SPAC4D7.04c.1; -.
DR MaxQB; O14171; -.
DR PaxDb; O14171; -.
DR EnsemblFungi; SPAC4D7.04c.1; SPAC4D7.04c.1:pep; SPAC4D7.04c.
DR GeneID; 2543620; -.
DR KEGG; spo:SPAC4D7.04c; -.
DR PomBase; SPAC4D7.04c; -.
DR VEuPathDB; FungiDB:SPAC4D7.04c; -.
DR eggNOG; KOG1602; Eukaryota.
DR HOGENOM; CLU_038505_0_4_1; -.
DR InParanoid; O14171; -.
DR OMA; PRTEGHK; -.
DR PhylomeDB; O14171; -.
DR Reactome; R-SPO-446199; Synthesis of Dolichyl-phosphate.
DR UniPathway; UPA00378; -.
DR PRO; PR:O14171; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:1904423; C:dehydrodolichyl diphosphate synthase complex; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031224; C:intrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR GO; GO:0002094; F:polyprenyltransferase activity; IBA:GO_Central.
DR GO; GO:0019408; P:dolichol biosynthetic process; IDA:PomBase.
DR GO; GO:0016094; P:polyprenol biosynthetic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; NAS:PomBase.
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 1: Evidence at protein level;
KW Endoplasmic reticulum; Magnesium; Membrane; Reference proteome;
KW Transferase.
FT CHAIN 1..264
FT /note="Dehydrodolichyl diphosphate synthase complex subunit
FT SPAC4D7.04c"
FT /id="PRO_0000123761"
SQ SEQUENCE 264 AA; 30543 MW; 7DCC6094B114D29D CRC64;
MGNLSGWFIH CPPLQWTLDQ LETMMINTIK RGKVPQHIAF VMDGNRRWAR QRRMETIEGH
SSGFEALKSL LKVCLKLGVK EVSAFTFSIE NFKRSKYEVD MLMEIAKNSL TQITAHGDLV
DQYGIRIRIV GDLSRLQPDV LETALKAVEI TKHNTKATLN VCFPYTSRHE IATSVQSIVK
MAEDGTITPE DIDEDIFEKN LLIKDSLPLD LLIRTSGVER LSDFMLWQCH KNTEIKFIDF
YWPDFSIWKF FPMLIQYQLQ NQPA
