DOLK_BOVIN
ID DOLK_BOVIN Reviewed; 538 AA.
AC Q58CR4; A0JN90; Q58DT7;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Dolichol kinase;
DE EC=2.7.1.108 {ECO:0000250|UniProtKB:Q9UPQ8};
DE AltName: Full=Transmembrane protein 15;
GN Name=DOLK; Synonyms=TMEM15;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal brain;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX46357.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BT021510; AAX46357.1; ALT_FRAME; mRNA.
DR EMBL; BT021883; AAX46730.1; -; mRNA.
DR EMBL; BC126569; AAI26570.1; -; mRNA.
DR RefSeq; NP_001030442.2; NM_001035365.3.
DR AlphaFoldDB; Q58CR4; -.
DR STRING; 9913.ENSBTAP00000054607; -.
DR PaxDb; Q58CR4; -.
DR PRIDE; Q58CR4; -.
DR Ensembl; ENSBTAT00000014016; ENSBTAP00000054607; ENSBTAG00000010601.
DR GeneID; 526844; -.
DR KEGG; bta:526844; -.
DR CTD; 22845; -.
DR VEuPathDB; HostDB:ENSBTAG00000010601; -.
DR VGNC; VGNC:28170; DOLK.
DR eggNOG; KOG2468; Eukaryota.
DR GeneTree; ENSGT00390000004067; -.
DR HOGENOM; CLU_027611_2_1_1; -.
DR InParanoid; Q58CR4; -.
DR OMA; GPGGWLC; -.
DR OrthoDB; 1533260at2759; -.
DR TreeFam; TF323379; -.
DR Reactome; R-BTA-446199; Synthesis of Dolichyl-phosphate.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000010601; Expressed in cortex of kidney and 103 other tissues.
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 2: Evidence at transcript level;
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_0000238931"
FT TOPO_DOM 1..18
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 19..39
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..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:0000250|UniProtKB:Q9UPQ8"
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:0000250|UniProtKB:Q9UPQ8"
FT REGION 459..474
FT /note="CTP-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UPQ8"
SQ SEQUENCE 538 AA; 59190 MW; 2E8619DC63E57929 CRC64;
MTRECAPPTP GSGAPLSGSV LAEAAVVFVV VLSIHAAVWD RYSWCAVALA VQAFYVQYKW
DRLLQQGSAV FQFRMSANSG LLPASVVMPL LGLVMKERCQ AAGNPYFERF GIVVAATGMA
VALFSSVLAL GITRPVPTNT CVISGLAGGV IIYIMKHSLS VGEVIEVLEA LLIFVYLNMI
LLYLLPRCFT PGEALLVLGG ISFMLNQLIK RSLTVVESQG DPLDFFLLVV VVGMVLMGIF
FSTLFVFMDS GTWASSIFFH LMTCVLGLGV VLPWLHRLIR RNPLLWLFQF LFQTETRVYL
LAYWCLLATV ACLVVLYQNA KRSSSESKKH QAPTITRKYF HFIVVATYIP GIILDRPLLY
VAATVCLAVF IFLEYVRYFR IKPLGHTLRS LLSLFLDERD SGPLILTHIY LLLGMSLPIW
LVPRPCTQKG SLGGARALVP YAGVLAVGVG DTVASIFGST MGEIRWPGTK KTFEGTMTSI
FAQIISVALI LIFDSGVDLN YSYAWILGSI STVSLLEAYT TQIDNLLLPL YLLILLMA
