ID   DOLK_HUMAN              Reviewed;         538 AA.
AC   Q9UPQ8; Q5SRE6;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 170.
DE   RecName: Full=Dolichol kinase;
DE            EC=2.7.1.108 {ECO:0000269|PubMed:12213788, ECO:0000269|PubMed:16923818, ECO:0000269|PubMed:17273964};
DE   AltName: Full=Transmembrane protein 15;
GN   Name=DOLK; Synonyms=KIAA1094, TMEM15; ORFNames=UNQ2422/PRO4980;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND FUNCTION.
RC   TISSUE=Brain;
RX   PubMed=12213788; DOI=10.1093/glycob/cwf068;
RA   Fernandez F., Shridas P., Jiang S., Aebi M., Waechter C.J.;
RT   "Expression and characterization of a human cDNA that complements the
RT   temperature-sensitive defect in dolichol kinase activity in the yeast
RT   sec59-1 mutant: the enzymatic phosphorylation of dolichol and
RT   diacylglycerol are catalyzed by separate CTP-mediated kinase activities in
RT   Saccharomyces cerevisiae.";
RL   Glycobiology 12:555-562(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA   Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA   Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIV. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:197-205(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas, and Spleen;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   SUBCELLULAR LOCATION, TOPOLOGY, FUNCTION, CATALYTIC ACTIVITY, CTP-BINDING,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF GLY-443; ASP-451;
RP   LYS-470; LYS-471; THR-472; GLU-474 AND GLY-475.
RX   PubMed=16923818; DOI=10.1074/jbc.m604087200;
RA   Shridas P., Waechter C.J.;
RT   "Human dolichol kinase, a polytopic endoplasmic reticulum membrane protein
RT   with a cytoplasmically oriented CTP-binding site.";
RL   J. Biol. Chem. 281:31696-31704(2006).
RN   [7]
RP   VARIANTS CDG1M SER-99 AND SER-441, CHARACTERIZATION OF VARIANTS CDG1M
RP   SER-99 AND SER-441, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=17273964; DOI=10.1086/512130;
RA   Kranz C., Jungeblut C., Denecke J., Erlekotte A., Sohlbach C., Debus V.,
RA   Kehl H.G., Harms E., Reith A., Reichel S., Groebe H., Hammersen G.,
RA   Schwarzer U., Marquardt T.;
RT   "A defect in dolichol phosphate biosynthesis causes a new inherited
RT   disorder with death in early infancy.";
RL   Am. J. Hum. Genet. 80:433-440(2007).
CC   -!- FUNCTION: Catalyzes CTP-mediated phosphorylation of dolichol, the
CC       terminal step in de novo dolichyl monophosphate (Dol-P) biosynthesis
CC       (PubMed:12213788, PubMed:16923818, PubMed:17273964). Dol-P is a lipid
CC       carrier essential for the synthesis of N-linked and O-linked
CC       oligosaccharides and for GPI anchors (PubMed:12213788).
CC       {ECO:0000269|PubMed:12213788, ECO:0000269|PubMed:16923818,
CC       ECO:0000269|PubMed:17273964}.
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:0000269|PubMed:12213788, ECO:0000269|PubMed:16923818,
CC         ECO:0000269|PubMed:17273964};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13134;
CC         Evidence={ECO:0000305|PubMed:16923818};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=22.8 uM for dolichol {ECO:0000269|PubMed:16923818};
CC         KM=3.5 uM for CTP {ECO:0000269|PubMed:16923818};
CC   -!- INTERACTION:
CC       Q9UPQ8; Q92624: APPBP2; NbExp=3; IntAct=EBI-8645574, EBI-743771;
CC       Q9UPQ8; P11912: CD79A; NbExp=3; IntAct=EBI-8645574, EBI-7797864;
CC       Q9UPQ8; Q9H9P2: CHODL; NbExp=3; IntAct=EBI-8645574, EBI-17447707;
CC       Q9UPQ8; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-8645574, EBI-6942903;
CC       Q9UPQ8; Q92838: EDA; NbExp=6; IntAct=EBI-8645574, EBI-529425;
CC       Q9UPQ8; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-8645574, EBI-18304435;
CC       Q9UPQ8; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-8645574, EBI-12142257;
CC       Q9UPQ8; P48165: GJA8; NbExp=3; IntAct=EBI-8645574, EBI-17458373;
CC       Q9UPQ8; Q8TED1: GPX8; NbExp=3; IntAct=EBI-8645574, EBI-11721746;
CC       Q9UPQ8; Q09470: KCNA1; NbExp=7; IntAct=EBI-8645574, EBI-8286599;
CC       Q9UPQ8; Q16322: KCNA10; NbExp=5; IntAct=EBI-8645574, EBI-12265328;
CC       Q9UPQ8; P22001: KCNA3; NbExp=6; IntAct=EBI-8645574, EBI-8627664;
CC       Q9UPQ8; P17658: KCNA6; NbExp=4; IntAct=EBI-8645574, EBI-6426142;
CC       Q9UPQ8; Q9HCJ2: LRRC4C; NbExp=4; IntAct=EBI-8645574, EBI-3925442;
CC       Q9UPQ8; Q92536: SLC7A6; NbExp=3; IntAct=EBI-8645574, EBI-2880595;
CC       Q9UPQ8; Q8TBG9: SYNPR; NbExp=3; IntAct=EBI-8645574, EBI-10273251;
CC       Q9UPQ8; Q96B21: TMEM45B; NbExp=3; IntAct=EBI-8645574, EBI-3923061;
CC       Q9UPQ8; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-8645574, EBI-11742770;
CC       Q9UPQ8; Q9H7M9: VSIR; NbExp=3; IntAct=EBI-8645574, EBI-744988;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:16923818}; Multi-pass membrane protein
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- DISEASE: Congenital disorder of glycosylation 1M (CDG1M) [MIM:610768]:
CC       A form of congenital disorder of glycosylation, a multisystem disorder
CC       caused by a defect in glycoprotein biosynthesis and characterized by
CC       under-glycosylated serum glycoproteins. Congenital disorders of
CC       glycosylation result in a wide variety of clinical features, such as
CC       defects in the nervous system development, psychomotor retardation,
CC       dysmorphic features, hypotonia, coagulation disorders, and
CC       immunodeficiency. The broad spectrum of features reflects the critical
CC       role of N-glycoproteins during embryonic development, differentiation,
CC       and maintenance of cell functions. CDG1M is a very severe disease with
CC       death occurring in early life. {ECO:0000269|PubMed:17273964}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- MISCELLANEOUS: Complements the defects in growth, dolichol kinase
CC       activity and protein N-glycosylation at the restrictive temperature in
CC       yeast sec59 mutant cells. {ECO:0000269|PubMed:12213788}.
CC   -!- SIMILARITY: Belongs to the polyprenol kinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA83046.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB029017; BAA83046.2; ALT_INIT; mRNA.
DR   EMBL; AY358759; AAQ89119.1; -; mRNA.
DR   EMBL; AL672142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC035556; AAH35556.1; -; mRNA.
DR   CCDS; CCDS6915.1; -.
DR   RefSeq; NP_055723.1; NM_014908.3.
DR   AlphaFoldDB; Q9UPQ8; -.
DR   BioGRID; 116517; 55.
DR   IntAct; Q9UPQ8; 31.
DR   MINT; Q9UPQ8; -.
DR   STRING; 9606.ENSP00000361667; -.
DR   iPTMnet; Q9UPQ8; -.
DR   PhosphoSitePlus; Q9UPQ8; -.
DR   SwissPalm; Q9UPQ8; -.
DR   BioMuta; DOLK; -.
DR   DMDM; 20140913; -.
DR   EPD; Q9UPQ8; -.
DR   jPOST; Q9UPQ8; -.
DR   MassIVE; Q9UPQ8; -.
DR   MaxQB; Q9UPQ8; -.
DR   PaxDb; 9606-ENSP00000361667; -.
DR   PeptideAtlas; Q9UPQ8; -.
DR   ProteomicsDB; 85419; -.
DR   Pumba; Q9UPQ8; -.
DR   Antibodypedia; 53680; 90 antibodies from 19 providers.
DR   DNASU; 22845; -.
DR   Ensembl; ENST00000372586.4; ENSP00000361667.3; ENSG00000175283.8.
DR   GeneID; 22845; -.
DR   KEGG; hsa:22845; -.
DR   MANE-Select; ENST00000372586.4; ENSP00000361667.3; NM_014908.4; NP_055723.1.
DR   UCSC; uc004bwr.4; human.
DR   AGR; HGNC:23406; -.
DR   CTD; 22845; -.
DR   DisGeNET; 22845; -.
DR   GeneCards; DOLK; -.
DR   GeneReviews; DOLK; -.
DR   HGNC; HGNC:23406; DOLK.
DR   HPA; ENSG00000175283; Low tissue specificity.
DR   MalaCards; DOLK; -.
DR   MIM; 610746; gene.
DR   MIM; 610768; phenotype.
DR   neXtProt; NX_Q9UPQ8; -.
DR   OpenTargets; ENSG00000175283; -.
DR   Orphanet; 91131; DK1-CDG.
DR   Orphanet; 154; Familial isolated dilated cardiomyopathy.
DR   PharmGKB; PA162384054; -.
DR   VEuPathDB; HostDB:ENSG00000175283; -.
DR   eggNOG; KOG2468; Eukaryota.
DR   GeneTree; ENSGT00390000004067; -.
DR   HOGENOM; CLU_027611_2_1_1; -.
DR   InParanoid; Q9UPQ8; -.
DR   OMA; QAFYIQF; -.
DR   OrthoDB; 2880128at2759; -.
DR   PhylomeDB; Q9UPQ8; -.
DR   TreeFam; TF323379; -.
DR   BRENDA; 2.7.1.108; 2681.
DR   PathwayCommons; Q9UPQ8; -.
DR   Reactome; R-HSA-446199; Synthesis of Dolichyl-phosphate.
DR   Reactome; R-HSA-4755583; Defective DOLK causes DOLK-CDG.
DR   SignaLink; Q9UPQ8; -.
DR   SIGNOR; Q9UPQ8; -.
DR   BioGRID-ORCS; 22845; 409 hits in 1157 CRISPR screens.
DR   GeneWiki; Dolichol_kinase; -.
DR   GenomeRNAi; 22845; -.
DR   Pharos; Q9UPQ8; Tbio.
DR   PRO; PR:Q9UPQ8; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q9UPQ8; Protein.
DR   Bgee; ENSG00000175283; Expressed in primordial germ cell in gonad and 180 other cell types or tissues.
DR   ExpressionAtlas; Q9UPQ8; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0004168; F:dolichol kinase activity; IDA:UniProtKB.
DR   GO; GO:0006489; P:dolichyl diphosphate biosynthetic process; TAS:Reactome.
DR   GO; GO:0043048; P:dolichyl monophosphate biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   InterPro; IPR032974; Polypren_kinase.
DR   PANTHER; PTHR13205:SF15; DOLICHOL KINASE; 1.
DR   PANTHER; PTHR13205; TRANSMEMBRANE PROTEIN 15-RELATED; 1.
DR   Genevisible; Q9UPQ8; HS.
PE   1: Evidence at protein level;
KW   Congenital disorder of glycosylation; Disease variant;
KW   Endoplasmic reticulum; Kinase; Lipid metabolism; Membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..538
FT                   /note="Dolichol kinase"
FT                   /id="PRO_0000072595"
FT   TOPO_DOM        1..13
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:16923818"
FT   TRANSMEM        14..34
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..74
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        75..95
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        96..111
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        112..132
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        133..134
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        135..155
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        156..163
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        164..184
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        185..188
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        189..209
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..224
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        225..245
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        246..254
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        255..275
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        276..297
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        298..318
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        319..337
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        338..354
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        355..359
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        360..380
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        381..401
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        402..422
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        423..436
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        437..457
FT                   /note="Helical; Name=13"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        458..472
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:16923818"
FT   TRANSMEM        473..493
FT                   /note="Helical; Name=14"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        494..495
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        496..516
FT                   /note="Helical; Name=15"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        517..538
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:16923818"
FT   REGION          459..474
FT                   /note="CTP-binding"
FT                   /evidence="ECO:0000269|PubMed:16923818"
FT   VARIANT         99
FT                   /note="C -> S (in CDG1M; 2% residual dolichol kinase
FT                   activity; fails to complement the temperature-sensitive
FT                   phenotype of DK1-deficient yeast cells; dbSNP:rs137853109)"
FT                   /evidence="ECO:0000269|PubMed:17273964"
FT                   /id="VAR_032851"
FT   VARIANT         224
FT                   /note="D -> V (in dbSNP:rs17485436)"
FT                   /id="VAR_049709"
FT   VARIANT         441
FT                   /note="Y -> S (in CDG1M; 4% residual dolichol kinase
FT                   activity; fails to complement the temperature-sensitive
FT                   phenotype of DK1-deficient yeast cells; dbSNP:rs137853110)"
FT                   /evidence="ECO:0000269|PubMed:17273964"
FT                   /id="VAR_032852"
FT   MUTAGEN         443
FT                   /note="G->D: Abolishes dolichol kinase activity."
FT                   /evidence="ECO:0000269|PubMed:16923818"
FT   MUTAGEN         451
FT                   /note="D->A: Reduces dolichol kinase activity."
FT                   /evidence="ECO:0000269|PubMed:16923818"
FT   MUTAGEN         470
FT                   /note="K->A: Reduces dolichol kinase activity. Significant
FT                   reduction in binding affinity for CTP; when associated with
FT                   A-471."
FT                   /evidence="ECO:0000269|PubMed:16923818"
FT   MUTAGEN         471
FT                   /note="K->A: Reduces dolichol kinase activity. Significant
FT                   reduction in binding affinity for CTP."
FT                   /evidence="ECO:0000269|PubMed:16923818"
FT   MUTAGEN         472
FT                   /note="T->A: Reduces dolichol kinase activity. Significant
FT                   reduction in binding affinity for CTP."
FT                   /evidence="ECO:0000269|PubMed:16923818"
FT   MUTAGEN         474
FT                   /note="E->A: No effect on dolichol kinase activity."
FT                   /evidence="ECO:0000269|PubMed:16923818"
FT   MUTAGEN         475
FT                   /note="G->A: No effect on dolichol kinase activity."
FT                   /evidence="ECO:0000269|PubMed:16923818"
SQ   SEQUENCE   538 AA;  59268 MW;  EB7D1BABD45362AD CRC64;
     MTRECPSPAP GPGAPLSGSV LAEAAVVFAV VLSIHATVWD RYSWCAVALA VQAFYVQYKW
     DRLLQQGSAV FQFRMSANSG LLPASMVMPL LGLVMKERCQ TAGNPFFERF GIVVAATGMA
     VALFSSVLAL GITRPVPTNT CVILGLAGGV IIYIMKHSLS VGEVIEVLEV LLIFVYLNMI
     LLYLLPRCFT PGEALLVLGG ISFVLNQLIK RSLTLVESQG DPVDFFLLVV VVGMVLMGIF
     FSTLFVFMDS GTWASSIFFH LMTCVLSLGV VLPWLHRLIR RNPLLWLLQF LFQTDTRIYL
     LAYWSLLATL ACLVVLYQNA KRSSSESKKH QAPTIARKYF HLIVVATYIP GIIFDRPLLY
     VAATVCLAVF IFLEYVRYFR IKPLGHTLRS FLSLFLDERD SGPLILTHIY LLLGMSLPIW
     LIPRPCTQKG SLGGARALVP YAGVLAVGVG DTVASIFGST MGEIRWPGTK KTFEGTMTSI
     FAQIISVALI LIFDSGVDLN YSYAWILGSI STVSLLEAYT TQIDNLLLPL YLLILLMA
//