UPPS_YEAST
ID UPPS_YEAST Reviewed; 375 AA.
AC Q12063; D6VRG0;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Dehydrodolichyl diphosphate synthase complex subunit NUS1 {ECO:0000305};
DE EC=2.5.1.87 {ECO:0000269|PubMed:25066056};
DE AltName: Full=Nuclear undecaprenyl pyrophosphate synthase 1 {ECO:0000312|SGD:S000002352};
GN Name=NUS1; OrderedLocusNames=YDL193W {ECO:0000312|SGD:S000002352};
GN ORFNames=D1239 {ECO:0000303|PubMed:8533471};
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8533471; DOI=10.1002/yea.320111007;
RA Verhasselt P., Voet M., Volckaert G.;
RT "New open reading frames, one of which is similar to the nifV gene of
RT Azotobacter vinelandii, found on a 12.5 kbp fragment of chromosome IV of
RT Saccharomyces cerevisiae.";
RL Yeast 11:961-966(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10515935; DOI=10.1128/jb.181.20.6441-6448.1999;
RA Athenstaedt K., Zweytick D., Jandrositz A., Kohlwein S.D., Daum G.;
RT "Identification and characterization of major lipid particle proteins of
RT the yeast Saccharomyces cerevisiae.";
RL J. Bacteriol. 181:6441-6448(1999).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=11086160; DOI=10.1016/s0014-5793(00)02179-7;
RA Prein B., Natter K., Kohlwein S.D.;
RT "A novel strategy for constructing N-terminal chromosomal fusions to green
RT fluorescent protein in the yeast Saccharomyces cerevisiae.";
RL FEBS Lett. 485:29-34(2000).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, AND MUTAGENESIS OF ASN-372.
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 SRT1 or RER2, 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 either SRT1 or RER2. {ECO:0000303|PubMed:25066056}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000305}. Lipid droplet
CC {ECO:0000269|PubMed:10515935, ECO:0000269|PubMed:11086160,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14690591}. Nucleus
CC membrane {ECO:0000269|PubMed:14690591}; Single-pass membrane protein
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}.
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DR EMBL; X83276; CAA58254.1; -; Genomic_DNA.
DR EMBL; Z74241; CAA98770.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11670.1; -; Genomic_DNA.
DR PIR; S58784; S58784.
DR RefSeq; NP_010088.1; NM_001180253.1.
DR PDB; 6JCN; X-ray; 2.00 A; A/B=148-375.
DR PDBsum; 6JCN; -.
DR AlphaFoldDB; Q12063; -.
DR SMR; Q12063; -.
DR BioGRID; 31852; 286.
DR ComplexPortal; CPX-162; Dehydrodolichyl diphosphate synthase complex variant RER2.
DR ComplexPortal; CPX-166; Dehydrodolichyl diphosphate synthase complex variant SRT1.
DR DIP; DIP-1220N; -.
DR IntAct; Q12063; 13.
DR STRING; 4932.YDL193W; -.
DR iPTMnet; Q12063; -.
DR MaxQB; Q12063; -.
DR PaxDb; Q12063; -.
DR PRIDE; Q12063; -.
DR EnsemblFungi; YDL193W_mRNA; YDL193W; YDL193W.
DR GeneID; 851334; -.
DR KEGG; sce:YDL193W; -.
DR SGD; S000002352; NUS1.
DR VEuPathDB; FungiDB:YDL193W; -.
DR eggNOG; KOG2818; Eukaryota.
DR GeneTree; ENSGT00390000003223; -.
DR HOGENOM; CLU_051870_0_0_1; -.
DR InParanoid; Q12063; -.
DR OMA; MPRVYEA; -.
DR BioCyc; MetaCyc:G3O-29578-MON; -.
DR BioCyc; YEAST:G3O-29578-MON; -.
DR BRENDA; 2.5.1.87; 984.
DR Reactome; R-SCE-446199; Synthesis of Dolichyl-phosphate.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q12063; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12063; protein.
DR GO; GO:1904423; C:dehydrodolichyl diphosphate synthase complex; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
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:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; HDA:SGD.
DR GO; GO:0031965; C:nuclear 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; IDA:SGD.
DR GO; GO:0006486; P:protein glycosylation; IMP:SGD.
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 3D-structure; Endoplasmic reticulum; Lipid droplet; Magnesium; Membrane;
KW Nucleus; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..375
FT /note="Dehydrodolichyl diphosphate synthase complex subunit
FT NUS1"
FT /id="PRO_0000242134"
FT TRANSMEM 97..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 372
FT /note="N->H: Loss of function."
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:6JCN"
FT HELIX 171..188
FT /evidence="ECO:0007829|PDB:6JCN"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:6JCN"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:6JCN"
FT HELIX 207..222
FT /evidence="ECO:0007829|PDB:6JCN"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:6JCN"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:6JCN"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:6JCN"
FT TURN 243..247
FT /evidence="ECO:0007829|PDB:6JCN"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:6JCN"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:6JCN"
FT HELIX 279..294
FT /evidence="ECO:0007829|PDB:6JCN"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:6JCN"
FT HELIX 305..315
FT /evidence="ECO:0007829|PDB:6JCN"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:6JCN"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:6JCN"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:6JCN"
FT HELIX 356..367
FT /evidence="ECO:0007829|PDB:6JCN"
SQ SEQUENCE 375 AA; 42557 MW; AFB4A55F242C94D0 CRC64;
MPTMIKKDDK AMEPPNEKPH RKIERDDVPE SSNHIPPPES GVLKGGKVNS KTRALKAVTS
IIADADENPQ KKVNNETNGV QKQKTEDLSK RIGKFEYLFY KFLLVLLYIC FGLFRYGQYQ
YNKMKLRIFS IIYNHAYTPQ LIRQDVIPLK KIPKRLAAIL EVKPVGDVGG GVTGLLNDAS
EIVCWTVSAG IKHLMLYDYD GILQRNVPEL RMEIHSNLAK YFGPAHVPNY AVKIPHSNKI
FYNLDGIETE TDVGNEIEAN QEKDKIAIEI SLLSNRDGRE TIVDLTKTMA ELCAVNELSV
SDITMDLVDS ELKQLVGPEP DLLLYFGPSL DLQGFPPWHI RLTEFYWEKD NNEVIYSVFI
RGLRQYAGCK VNVGK
