DOLK_MOUSE
ID DOLK_MOUSE Reviewed; 534 AA.
AC Q8R2Y3;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Dolichol kinase {ECO:0000312|MGI:MGI:2677836};
DE EC=2.7.1.108 {ECO:0000250|UniProtKB:Q9UPQ8};
DE AltName: Full=Transmembrane protein 15 {ECO:0000312|MGI:MGI:2677836};
GN Name=Dolk {ECO:0000312|MGI:MGI:2677836};
GN Synonyms=Tmem15 {ECO:0000312|MGI:MGI:2677836};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:BAF82000.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ddY {ECO:0000312|EMBL:BAF82000.1};
RC TISSUE=Spinal cord {ECO:0000312|EMBL:BAF82000.1};
RA Nishizawa M., Minami T., Ito S.;
RT "Mouse mRNAs expressed in the spinal cord.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:BAE26024.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung {ECO:0000312|EMBL:BAE26024.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0000312|EMBL:BAF82000.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000312|EMBL:AAH26973.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3 {ECO:0000312|EMBL:AAH26973.1};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH26973.1};
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes CTP-mediated phosphorylation of dolichol, the
CC terminal step in de novo dolichyl monophosphate (Dol-P) biosynthesis.
CC Dol-P is a lipid carrier essential for the synthesis of N-linked and O-
CC linked oligosaccharides and for GPI anchors.
CC {ECO:0000250|UniProtKB:Q9UPQ8}.
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:0000250|UniProtKB:Q9UPQ8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13134;
CC Evidence={ECO:0000250|UniProtKB:Q9UPQ8};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9UPQ8}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9UPQ8}.
CC -!- SIMILARITY: Belongs to the polyprenol kinase family.
CC {ECO:0000250|UniProtKB:Q9UPQ8}.
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DR EMBL; AB073968; BAF82000.1; -; mRNA.
DR EMBL; AK144705; BAE26024.1; -; mRNA.
DR EMBL; AL954388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466542; EDL08455.1; -; Genomic_DNA.
DR EMBL; BC026973; AAH26973.1; -; mRNA.
DR CCDS; CCDS15877.1; -.
DR RefSeq; NP_808316.1; NM_177648.3.
DR AlphaFoldDB; Q8R2Y3; -.
DR BioGRID; 230666; 2.
DR IntAct; Q8R2Y3; 1.
DR STRING; 10090.ENSMUSP00000097792; -.
DR PhosphoSitePlus; Q8R2Y3; -.
DR MaxQB; Q8R2Y3; -.
DR PaxDb; Q8R2Y3; -.
DR PeptideAtlas; Q8R2Y3; -.
DR PRIDE; Q8R2Y3; -.
DR ProteomicsDB; 277372; -.
DR Antibodypedia; 53680; 75 antibodies from 18 providers.
DR Ensembl; ENSMUST00000100219; ENSMUSP00000097792; ENSMUSG00000075419.
DR GeneID; 227697; -.
DR KEGG; mmu:227697; -.
DR UCSC; uc008jby.1; mouse.
DR CTD; 22845; -.
DR MGI; MGI:2677836; Dolk.
DR VEuPathDB; HostDB:ENSMUSG00000075419; -.
DR eggNOG; KOG2468; Eukaryota.
DR GeneTree; ENSGT00390000004067; -.
DR HOGENOM; CLU_027611_2_1_1; -.
DR InParanoid; Q8R2Y3; -.
DR OMA; GPGGWLC; -.
DR OrthoDB; 1533260at2759; -.
DR PhylomeDB; Q8R2Y3; -.
DR TreeFam; TF323379; -.
DR Reactome; R-MMU-446199; Synthesis of Dolichyl-phosphate.
DR BioGRID-ORCS; 227697; 29 hits in 76 CRISPR screens.
DR ChiTaRS; Dolk; mouse.
DR PRO; PR:Q8R2Y3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8R2Y3; protein.
DR Bgee; ENSMUSG00000075419; Expressed in humerus cartilage element and 243 other tissues.
DR Genevisible; Q8R2Y3; MM.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0004168; F:dolichol kinase activity; ISS:UniProtKB.
DR GO; GO:0043048; P:dolichyl monophosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; Lipid metabolism; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..534
FT /note="Dolichol kinase"
FT /id="PRO_0000355581"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 17..37
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..72
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 73..93
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 110..130
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..132
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 133..153
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 162..182
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..186
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 187..207
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 221..241
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..252
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 253..273
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 294..314
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..333
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 334..350
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 356..376
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..397
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 398..418
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 433..453
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..468
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 469..489
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255"
FT TOPO_DOM 490..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 492..512
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255"
FT TOPO_DOM 513..534
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 455..470
FT /note="CTP-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UPQ8"
SQ SEQUENCE 534 AA; 59145 MW; 3DCFD916081B3443 CRC64;
MTRQCPPQES GAALSGSVLA EAAVVFAVVL SIHAAVWDRY SWCAVALAVQ AFYVQYKWDR
LLQQGNAVFQ FRMSANSGLL PASMVMPLLG LVMKERCQTA GNPYFERFGI VVAATGMAVA
LFSSVLALGI TRPVPTNTCA ISGLAGGVII YIMRHSLSVG EVIEVLEVLL IFVYLNMILL
YLLPRCFTPG EALLVLGGIS FVLNQLIKRS LTESQGDPVD FFLLVVVVGM VLMGVFFSTL
FVFMDSGTWA SSIFFHLMTC VLGLGVVLPW LHWLIRRNPL LWLLQFLFYT ETRIYLLAYW
SLLASVACLV VLYQNAKRSS SESKKHRAPT ITRKYFHFIV VATYIPGIIF DRPLLYVAAT
VCLAVFIFLE YVRYFRIKPL GHTLRSLLSL FLDERDSGPL ILTHIYLLLG MSLPIWLIPR
PCTQKDSLEG ARALVPYAGV LAVGVGDTVA SIFGSTMGEI RWPGTKKTFE GTMTSIFAQI
ISVALILIFD SGVDLNYSYA WILGSISTVS LLEAYTTQID NLLLPLYLLI LLMA
