SEC59_YEAST
ID SEC59_YEAST Reviewed; 519 AA.
AC P20048; D6VZI7;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Dolichol kinase;
DE EC=2.7.1.108 {ECO:0000305|PubMed:1323123, ECO:0000305|PubMed:2657387};
GN Name=SEC59; OrderedLocusNames=YMR013C; ORFNames=YM8270.17C;
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], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=2657387; DOI=10.1128/mcb.9.3.1191-1199.1989;
RA Bernstein M., Kepes F., Schekman R.;
RT "Sec59 encodes a membrane protein required for core glycosylation in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 9:1191-1199(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1323123; DOI=10.1073/pnas.89.15.7013;
RA Heller L., Orlean P., Adair W.L. Jr.;
RT "Saccharomyces cerevisiae sec59 cells are deficient in dolichol kinase
RT activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:7013-7016(1992).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: Involved in the synthesis of the sugar donor Dol-P-Man which
CC is required in the synthesis of N-linked and O-linked oligosaccharides
CC and for that of GPI anchors. It is required for spore germination. Has
CC an essential role in cellular metabolism. {ECO:0000269|PubMed:2657387,
CC ECO:0000269|PubMed:9169872}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + di-trans,poly-cis-dolichol = a dolichyl phosphate + CDP
CC + H(+); Xref=Rhea:RHEA:13133, Rhea:RHEA-COMP:9517, Rhea:RHEA-
CC COMP:9521, ChEBI:CHEBI:15378, ChEBI:CHEBI:16091, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:57683, ChEBI:CHEBI:58069; EC=2.7.1.108;
CC Evidence={ECO:0000305|PubMed:1323123, ECO:0000305|PubMed:2657387};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13134;
CC Evidence={ECO:0000305|PubMed:1323123, ECO:0000305|PubMed:2657387};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the polyprenol kinase family. {ECO:0000305}.
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DR EMBL; M25779; AAA35033.1; -; Genomic_DNA.
DR EMBL; Z48613; CAA88530.1; -; Genomic_DNA.
DR EMBL; AY692829; AAT92848.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09911.1; -; Genomic_DNA.
DR PIR; JQ0124; JQ0124.
DR RefSeq; NP_013726.1; NM_001182509.1.
DR AlphaFoldDB; P20048; -.
DR BioGRID; 35183; 172.
DR DIP; DIP-8198N; -.
DR STRING; 4932.YMR013C; -.
DR iPTMnet; P20048; -.
DR MaxQB; P20048; -.
DR PaxDb; P20048; -.
DR PRIDE; P20048; -.
DR EnsemblFungi; YMR013C_mRNA; YMR013C; YMR013C.
DR GeneID; 855026; -.
DR KEGG; sce:YMR013C; -.
DR SGD; S000004615; SEC59.
DR VEuPathDB; FungiDB:YMR013C; -.
DR eggNOG; KOG2468; Eukaryota.
DR GeneTree; ENSGT00390000004067; -.
DR HOGENOM; CLU_031307_0_0_1; -.
DR InParanoid; P20048; -.
DR OMA; KNWENTF; -.
DR BioCyc; MetaCyc:YMR013C-MON; -.
DR BioCyc; YEAST:YMR013C-MON; -.
DR BRENDA; 2.7.1.108; 984.
DR Reactome; R-SCE-446199; Synthesis of Dolichyl-phosphate.
DR UniPathway; UPA00378; -.
DR PRO; PR:P20048; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P20048; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0004168; F:dolichol kinase activity; IMP:SGD.
DR GO; GO:0043048; P:dolichyl monophosphate biosynthetic process; IMP:SGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR026566; DOLK.
DR InterPro; IPR032974; Polypren_kinase.
DR PANTHER; PTHR13205; PTHR13205; 1.
DR PANTHER; PTHR13205:SF15; PTHR13205:SF15; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Kinase; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..519
FT /note="Dolichol kinase"
FT /id="PRO_0000097662"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..88
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..151
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..223
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..294
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..349
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..417
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..472
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 494..519
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 519 AA; 58906 MW; 2C75B6F175BBFF06 CRC64;
MVAIIPHASF TTIKLTQKTE GSQMPTEEIC KINMRTRKFD VGGNSRDFEC FYSNFVQTVI
LLGTFFYCVE RLQPWSIVTA DISYKQIFVN VFVVCLIMVG LIFTKYWQHG YKSLPKFDTI
YSLYLPFMVS LLFDTSSTVI NTILILSVLN SYRWRTQLVV IILQLCLIFF NFEAGDRLKN
IISIVINSLL SLILKYIGQL KSLDNIDSNL FSILLTNILY VSEAGTVHFR ILKGIILALT
TIISINYVLK KVMHFKPFML SISFAIGLPL FANTFIHLED GENPLLWLVK YILESTIRQK
ILFAWSSILI LSIPSILIEK DSLSLNTSRK LWHFIIFLLI IPSFQMDSNF VKIALSGTIP
VFLSIEYIRF QNLPPLGSAI ELQLRRFADD RDHSGPLIIS YLYLLFGIST PLLMNNSPMG
LIGLGIGDSL ASIIGKRYGR IRWKGTQKTL EGTLAFIVTS FIVCLVLLRF DKAAIFNHLT
TLQLLTLCTL SGVLEGNSVL NDNILIPAFM MICEKLITL
