EKI2_MOUSE
ID EKI2_MOUSE Reviewed; 385 AA.
AC A7MCT6; B7ZNN6; D3Z771; Q6XRG2;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Ethanolamine kinase 2;
DE Short=EKI 2;
DE EC=2.7.1.82;
DE AltName: Full=Ethanolamine kinase-like protein;
GN Name=Etnk2; Synonyms=Tuc1;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 11-385 (ISOFORM 2).
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 74-385 (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=C3H X 101;
RX PubMed=15161093; DOI=10.1016/j.modgep.2003.09.010;
RA Hurley T.M., McClive P.J., Sarraj M.A., Sinclair A.H.;
RT "Eki2 is upregulated specifically in the testis during mouse sex
RT determination.";
RL Gene Expr. Patterns 4:135-140(2004).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16861741; DOI=10.1074/jbc.m605861200;
RA Tian Y., Jackson P., Gunter C., Wang J., Rock C.O., Jackowski S.;
RT "Placental thrombosis and spontaneous fetal death in mice deficient in
RT ethanolamine kinase 2.";
RL J. Biol. Chem. 281:28438-28449(2006).
RN [5]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18755794; DOI=10.1210/en.2008-0584;
RA Gustin S.E., Western P.S., McClive P.J., Harley V.R., Koopman P.A.,
RA Sinclair A.H.;
RT "Testis development, fertility, and survival in ethanolamine kinase 2-
RT deficient mice.";
RL Endocrinology 149:6176-6186(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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. Does not
CC have choline kinase activity. {ECO:0000269|PubMed:16861741}.
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:0000269|PubMed:16861741};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A7MCT6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A7MCT6-2; Sequence=VSP_039099;
CC -!- TISSUE SPECIFICITY: Expressed in testis and liver. Low expression in
CC ovary and kidney. {ECO:0000269|PubMed:15161093,
CC ECO:0000269|PubMed:16861741, ECO:0000269|PubMed:18755794}.
CC -!- DEVELOPMENTAL STAGE: The expression is restricted to the gonads during
CC the sex determination period and throughout embryogenesis. In
CC developing testis, the expression is found only in the Sertoli cells.
CC The expression is strongest at day 11.5, more intense in the testis
CC than the ovary. From 12.5 dpc the expression in the ovary is reduced
CC and disappears. The expression at day 13.5 dpc is restricted to the
CC testis cords. {ECO:0000269|PubMed:15161093}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype in adults. No significant
CC effect is seen on liver phospholipid metabolism, neural development, or
CC testicular function. No abnormalities are detected in embryonic and
CC adult testis morphology, differentiation, function, or fertility.
CC PubMed:16861741 shows maternal-specific failure to support late
CC embryonic development, resulting in reduced perinatal size and survival
CC and suggesting compromised placental function.
CC {ECO:0000269|PubMed:16861741, ECO:0000269|PubMed:18755794}.
CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC {ECO:0000305}.
CC -!- CAUTION: According to PubMed:16861741, disruption of the gene causes
CC increased prevalence of placental thrombosis, reduced litter size and
CC increased pup mortality. No such effect was observed by
CC PubMed:18755794. One possible explanation lies in the fact that
CC PubMed:16861741 observed a remarkable 100% survival of control pups and
CC 16% mortality for mutant pups, while PubMed:18755794 observed 16%
CC mortality for both wild-type and mutant pups. According to
CC PubMed:18755794, the construct used in PubMed:16861741 may lead to
CC expression of a truncated transcript that might have deleterious
CC effects. {ECO:0000305}.
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DR EMBL; AC068906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC145351; AAI45352.1; -; mRNA.
DR EMBL; BC152310; AAI52311.1; -; mRNA.
DR EMBL; AY212244; AAP47267.1; -; mRNA.
DR CCDS; CCDS15296.2; -. [A7MCT6-1]
DR RefSeq; NP_780652.2; NM_175443.5. [A7MCT6-1]
DR AlphaFoldDB; A7MCT6; -.
DR SMR; A7MCT6; -.
DR STRING; 10090.ENSMUSP00000114272; -.
DR iPTMnet; A7MCT6; -.
DR PhosphoSitePlus; A7MCT6; -.
DR jPOST; A7MCT6; -.
DR MaxQB; A7MCT6; -.
DR PaxDb; A7MCT6; -.
DR PRIDE; A7MCT6; -.
DR ProteomicsDB; 277850; -. [A7MCT6-1]
DR ProteomicsDB; 277851; -. [A7MCT6-2]
DR Antibodypedia; 34553; 171 antibodies from 25 providers.
DR DNASU; 214253; -.
DR Ensembl; ENSMUST00000135222; ENSMUSP00000114272; ENSMUSG00000070644. [A7MCT6-1]
DR GeneID; 214253; -.
DR KEGG; mmu:214253; -.
DR UCSC; uc007cqg.2; mouse. [A7MCT6-1]
DR UCSC; uc011wsa.2; mouse. [A7MCT6-2]
DR CTD; 55224; -.
DR MGI; MGI:2443760; Etnk2.
DR VEuPathDB; HostDB:ENSMUSG00000070644; -.
DR eggNOG; KOG4720; Eukaryota.
DR GeneTree; ENSGT00950000182939; -.
DR InParanoid; A7MCT6; -.
DR OMA; MDWLKEY; -.
DR OrthoDB; 349250at2759; -.
DR PhylomeDB; A7MCT6; -.
DR TreeFam; TF313549; -.
DR BRENDA; 2.7.1.82; 3474.
DR Reactome; R-MMU-1483213; Synthesis of PE.
DR UniPathway; UPA00558; UER00741.
DR BioGRID-ORCS; 214253; 10 hits in 71 CRISPR screens.
DR PRO; PR:A7MCT6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; A7MCT6; protein.
DR Bgee; ENSMUSG00000070644; Expressed in left lobe of liver and 66 other tissues.
DR ExpressionAtlas; A7MCT6; baseline and differential.
DR Genevisible; A7MCT6; 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; IDA:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IMP:MGI.
DR GO; GO:0016310; P:phosphorylation; IDA:UniProtKB.
DR GO; GO:0001890; P:placenta development; IMP:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Kinase; Lipid biosynthesis;
KW Lipid metabolism; Nucleotide-binding; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..385
FT /note="Ethanolamine kinase 2"
FT /id="PRO_0000393962"
FT VAR_SEQ 290..385
FT /note="VNVVDYSRYPARETQVQWLRYYLEAQKGTAASPREVERLYAQVNKFALASHF
FT FWALWALIQNQYSTISFDFLRYAVIRFNQYFKVKPQVSALEMPK -> RGGLL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039099"
FT CONFLICT 166
FT /note="R -> Q (in Ref. 3; AAP47267)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="V -> E (in Ref. 3; AAP47267)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="A -> S (in Ref. 3; AAP47267)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 44567 MW; 46C062858F7FFD29 CRC64;
MAVPPSAPVP CSPFYLRRQE PCPQCSWSME EKAVASAGCW EPPGPPRAAV PCFSVTVEQD
DILPGALRLI RELRPHWKPE QVRTKRFKDG ITNKLLACYV EEDMRDCVLV RVYGERTELL
VDRENEVRNF QLLRAHGCAP KLYCTFQNGL CYEYVQGVAL GPEHIREPQL FRLIALEMAK
IHTIHANGSL PKPTLWHKMH RYFTLVKDEI SPSLSADVPK VEVLEQELAW LKEHLSQLDS
PVVFCHNDLL CKNIIYDSDK GRVCFIDYEY AGYNYQAFDI GNHFNEFAGV NVVDYSRYPA
RETQVQWLRY YLEAQKGTAA SPREVERLYA QVNKFALASH FFWALWALIQ NQYSTISFDF
LRYAVIRFNQ YFKVKPQVSA LEMPK
