EKI1_MOUSE
ID EKI1_MOUSE Reviewed; 363 AA.
AC Q9D4V0; F6Y9V2; Q8BXQ0;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Ethanolamine kinase 1;
DE Short=EKI 1;
DE EC=2.7.1.82;
GN Name=Etnk1; Synonyms=Eki1;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina, and Testis;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and 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: Highly specific for ethanolamine phosphorylation. May be a
CC rate-controlling step in phosphatidylethanolamine biosynthesis.
CC {ECO:0000250|UniProtKB:Q9HBU6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + ethanolamine = ADP + H(+) + phosphoethanolamine;
CC Xref=Rhea:RHEA:13069, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:58190, ChEBI:CHEBI:456216;
CC EC=2.7.1.82; Evidence={ECO:0000250|UniProtKB:Q9HBU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13070;
CC Evidence={ECO:0000250|UniProtKB:Q9HBU6};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3.
CC {ECO:0000250|UniProtKB:Q9HBU6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9HBU6}.
CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC {ECO:0000305}.
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DR EMBL; AK016135; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK044502; BAC31953.1; -; mRNA.
DR EMBL; AC127354; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132955; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466572; EDL10659.1; -; Genomic_DNA.
DR CCDS; CCDS57468.1; -.
DR RefSeq; NP_083526.2; NM_029250.2.
DR AlphaFoldDB; Q9D4V0; -.
DR SMR; Q9D4V0; -.
DR BioGRID; 217392; 1.
DR STRING; 10090.ENSMUSP00000032413; -.
DR iPTMnet; Q9D4V0; -.
DR PhosphoSitePlus; Q9D4V0; -.
DR EPD; Q9D4V0; -.
DR MaxQB; Q9D4V0; -.
DR PaxDb; Q9D4V0; -.
DR PRIDE; Q9D4V0; -.
DR ProteomicsDB; 277816; -.
DR Antibodypedia; 24166; 213 antibodies from 22 providers.
DR DNASU; 75320; -.
DR Ensembl; ENSMUST00000032413; ENSMUSP00000032413; ENSMUSG00000030275.
DR GeneID; 75320; -.
DR KEGG; mmu:75320; -.
DR UCSC; uc009eqe.1; mouse.
DR CTD; 55500; -.
DR MGI; MGI:1922570; Etnk1.
DR VEuPathDB; HostDB:ENSMUSG00000030275; -.
DR eggNOG; KOG4720; Eukaryota.
DR GeneTree; ENSGT00950000182939; -.
DR HOGENOM; CLU_012712_1_0_1; -.
DR InParanoid; Q9D4V0; -.
DR OMA; FKMKPEA; -.
DR OrthoDB; 349250at2759; -.
DR PhylomeDB; Q9D4V0; -.
DR TreeFam; TF313549; -.
DR Reactome; R-MMU-1483213; Synthesis of PE.
DR UniPathway; UPA00558; UER00741.
DR BioGRID-ORCS; 75320; 11 hits in 77 CRISPR screens.
DR ChiTaRS; Etnk1; mouse.
DR PRO; PR:Q9D4V0; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9D4V0; protein.
DR Bgee; ENSMUSG00000030275; Expressed in caudate-putamen and 257 other tissues.
DR ExpressionAtlas; Q9D4V0; baseline and differential.
DR Genevisible; Q9D4V0; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004305; F:ethanolamine kinase activity; ISO:MGI.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; ISO:MGI.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Lipid biosynthesis; Lipid metabolism;
KW Nucleotide-binding; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase.
FT CHAIN 1..363
FT /note="Ethanolamine kinase 1"
FT /id="PRO_0000206228"
FT CONFLICT 126
FT /note="A -> L (in Ref. 1; AK016135)"
FT /evidence="ECO:0000305"
FT CONFLICT 280..281
FT /note="WL -> CV (in Ref. 1; AK016135)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 41984 MW; EB74674AA31F6C70 CRC64;
MANYIHVPPG SPEVPKLDVT VQDQEEQRCR DGALSLLRHL RPHWDPREVT LQLFTDGITN
KLIACYVGDT MEDVVLVRIY GNKTELLVDR DEEVKSFRVL QAHGCAPQLY CTFNNGLCYE
FIQGEALDPQ HVCNPAIFRL IARQLAKIHA IHAHNGWIPK SNLWLKMGKY FSLIPTGFAD
ENINKRFLSE IPSPQLLQEE MTWMKELLSS LGSPVVLCHN DLLCKNIIYN EKQGDVQFID
YEYSGYNYLA YDIGNHFNEF AGVSDVDYSL YPDRELQGQW LRSYLEAYKE YKGFGSDVTE
KEVETLFIQV NQFALASHFF WGLWALIQAK YSTIEFDFLG YAVVRFNQYF KMKPEVTALK
MPE