AGK_MOUSE
ID AGK_MOUSE Reviewed; 421 AA.
AC Q9ESW4; Q9D087;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Acylglycerol kinase, mitochondrial {ECO:0000250|UniProtKB:Q53H12};
DE EC=2.7.1.107 {ECO:0000269|PubMed:15252046};
DE EC=2.7.1.138 {ECO:0000269|PubMed:15252046};
DE EC=2.7.1.94 {ECO:0000269|PubMed:15252046, ECO:0000269|PubMed:18004883};
DE AltName: Full=Multiple substrate lipid kinase {ECO:0000303|PubMed:15252046};
DE Short=MuLK {ECO:0000303|PubMed:15252046};
DE Short=Multi-substrate lipid kinase {ECO:0000303|PubMed:15252046};
GN Name=Agk {ECO:0000312|MGI:MGI:1917173};
GN Synonyms=Mulk {ECO:0000303|PubMed:15252046};
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 [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, COFACTOR, AND ACTIVITY
RP REGULATION.
RC STRAIN=FVB/N; TISSUE=Carcinoma;
RX PubMed=15252046; DOI=10.1074/jbc.m405932200;
RA Waggoner D.W., Johnson L.B., Mann P.C., Morris V., Guastella J.,
RA Bajjalieh S.M.;
RT "MuLK, a eukaryotic multi-substrate lipid kinase.";
RL J. Biol. Chem. 279:38228-38235(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=16269826; DOI=10.1194/jlr.m500321-jlr200;
RA Van Overloop H., Gijsbers S., Van Veldhoven P.P.;
RT "Further characterization of mammalian ceramide kinase: substrate delivery
RT and (stereo)specificity, tissue distribution, and subcellular localization
RT studies.";
RL J. Lipid Res. 47:268-283(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver, and Mammary tumor;
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18004883; DOI=10.1021/bi701584v;
RA Epand R.M., Shulga Y.V., Timmons H.C., Perri A.L., Belani J.D.,
RA Perinpanathan K., Johnson-McIntire L.B., Bajjalieh S., Dicu A.O., Elias C.,
RA Rychnovsky S.D., Topham M.K.;
RT "Substrate chirality and specificity of diacylglycerol kinases and the
RT multisubstrate lipid kinase.";
RL Biochemistry 46:14225-14231(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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: Lipid kinase that can phosphorylate both monoacylglycerol and
CC diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic
CC acid (PA), respectively (PubMed:15252046). Phosphorylates ceramide but
CC not sphingosine (PubMed:15252046). Phosphorylates 1,2-dioleoylglycerol
CC more rapidly than 2,3-dioleoylglycerol (PubMed:18004883). Independently
CC of its lipid kinase activity, acts as a component of the TIM22 complex
CC (By similarity). The TIM22 complex mediates the import and insertion of
CC multi-pass transmembrane proteins into the mitochondrial inner membrane
CC by forming a twin-pore translocase that uses the membrane potential as
CC the external driving force (By similarity). In the TIM22 complex,
CC required for the import of a subset of metabolite carriers into
CC mitochondria, such as ANT1/SLC25A4 and SLC25A24, while it is not
CC required for the import of TIMM23 (By similarity). Overexpression
CC increases the formation and secretion of LPA, resulting in
CC transactivation of EGFR and activation of the downstream MAPK signaling
CC pathway, leading to increased cell growth (By similarity).
CC {ECO:0000250|UniProtKB:Q53H12, ECO:0000269|PubMed:15252046,
CC ECO:0000269|PubMed:18004883}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a monoacylglycerol + ATP = ADP + H(+) + monoacyl-sn-glycero-3-
CC phosphate; Xref=Rhea:RHEA:19293, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17408, ChEBI:CHEBI:30616, ChEBI:CHEBI:77589,
CC ChEBI:CHEBI:456216; EC=2.7.1.94;
CC Evidence={ECO:0000269|PubMed:15252046};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19294;
CC Evidence={ECO:0000305|PubMed:15252046};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-
CC phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608,
CC ChEBI:CHEBI:456216; EC=2.7.1.107;
CC Evidence={ECO:0000269|PubMed:15252046, ECO:0000269|PubMed:18004883};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000305|PubMed:15252046, ECO:0000305|PubMed:18004883};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphing-4-enine + ATP = ADP + an N-acylsphing-4-enine
CC 1-phosphate + H(+); Xref=Rhea:RHEA:17929, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:52639, ChEBI:CHEBI:57674,
CC ChEBI:CHEBI:456216; EC=2.7.1.138;
CC Evidence={ECO:0000269|PubMed:15252046};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17930;
CC Evidence={ECO:0000305|PubMed:15252046};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:40327, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:52333, ChEBI:CHEBI:74546, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:15252046, ECO:0000269|PubMed:18004883};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000305|PubMed:15252046, ECO:0000305|PubMed:18004883};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-(9Z-octadecenoyl)-
CC sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:41079,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:74544,
CC ChEBI:CHEBI:75757, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:15252046};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41080;
CC Evidence={ECO:0000305|PubMed:15252046};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-
CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:43328, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:34071, ChEBI:CHEBI:74938, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:15252046};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43329;
CC Evidence={ECO:0000305|PubMed:15252046};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycerol + ATP = a 1-acyl-sn-glycero-3-phosphate +
CC ADP + H(+); Xref=Rhea:RHEA:33747, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57970, ChEBI:CHEBI:64683,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q53H12};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33748;
CC Evidence={ECO:0000250|UniProtKB:Q53H12};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycerol + ATP = 1-hexadecanoyl-sn-glycero-
CC 3-phosphate + ADP + H(+); Xref=Rhea:RHEA:43308, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57518, ChEBI:CHEBI:75542,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q53H12};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43309;
CC Evidence={ECO:0000250|UniProtKB:Q53H12};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + ATP = 2-
CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:43316, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:52392, ChEBI:CHEBI:78209, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q53H12};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43317;
CC Evidence={ECO:0000250|UniProtKB:Q53H12};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N-(hexanoyl)sphing-4-enine = ADP + H(+) + N-
CC hexanoylsphing-4-enine 1-phosphate; Xref=Rhea:RHEA:43312,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:63867,
CC ChEBI:CHEBI:82959, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q53H12};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43313;
CC Evidence={ECO:0000250|UniProtKB:Q53H12};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15252046};
CC -!- ACTIVITY REGULATION: Both the ceramide and diacylglycerol kinase
CC activities are inhibited by sphingosine and stimulated by cardiolipin
CC (PubMed:15252046). Both activities are stimulated by calcium when
CC magnesium concentrations are low but inhibited by calcium when
CC magnesium concentrations are high (PubMed:15252046).
CC {ECO:0000269|PubMed:15252046}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=45 uM for diacylglycerol {ECO:0000269|PubMed:15252046};
CC KM=34 uM for ceramide {ECO:0000269|PubMed:15252046};
CC Vmax=159 nmol/min/mg enzyme with dioeoylglycerol as substrate
CC {ECO:0000269|PubMed:15252046};
CC Vmax=37 nmol/min/mg enzyme with ceramide as substrate
CC {ECO:0000269|PubMed:15252046};
CC Vmax=23.6 nmol/min/mg enzyme with 1,2-dioleoylglycerol as substrate
CC {ECO:0000269|PubMed:18004883};
CC Vmax=10.21 nmol/min/mg enzyme with 2,3-dioleoylglycerol as substrate
CC {ECO:0000269|PubMed:18004883};
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000269|PubMed:15252046}.
CC -!- SUBUNIT: Component of the TIM22 complex, which core is composed of
CC TIMM22, associated with TIMM10 (TIMM10A and/or TIMM10B), TIMM9, AGK and
CC TIMM29. {ECO:0000250|UniProtKB:Q53H12}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q53H12}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q53H12}. Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:Q53H12}. Note=Localizes in the mitochondrion
CC intermembrane space, where it associates with the inner membrane. It is
CC unclear whether the N-terminal hydrophobic region forms a transmembrane
CC region or associates with the membrane without crossing it.
CC {ECO:0000250|UniProtKB:Q53H12}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ESW4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ESW4-2; Sequence=VSP_020927;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:15252046}.
CC -!- SIMILARITY: Belongs to the AGK family. {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:15252046) thought to have ceramide
CC kinase activity. Such activity is however unlikely in vivo.
CC {ECO:0000305|PubMed:15252046}.
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DR EMBL; AY772469; AAV38106.1; -; mRNA.
DR EMBL; AJ401619; CAC06108.1; -; mRNA.
DR EMBL; AK011715; BAB27796.1; -; mRNA.
DR EMBL; AK076224; BAC36260.1; -; mRNA.
DR EMBL; BC019145; AAH19145.1; -; mRNA.
DR EMBL; BC093525; AAH93525.1; -; mRNA.
DR CCDS; CCDS20027.1; -. [Q9ESW4-1]
DR RefSeq; NP_076027.1; NM_023538.2. [Q9ESW4-1]
DR AlphaFoldDB; Q9ESW4; -.
DR SMR; Q9ESW4; -.
DR BioGRID; 213759; 4.
DR STRING; 10090.ENSMUSP00000031977; -.
DR SwissLipids; SLP:000000885; -.
DR iPTMnet; Q9ESW4; -.
DR PhosphoSitePlus; Q9ESW4; -.
DR SwissPalm; Q9ESW4; -.
DR EPD; Q9ESW4; -.
DR jPOST; Q9ESW4; -.
DR MaxQB; Q9ESW4; -.
DR PaxDb; Q9ESW4; -.
DR PeptideAtlas; Q9ESW4; -.
DR PRIDE; Q9ESW4; -.
DR ProteomicsDB; 296083; -. [Q9ESW4-1]
DR ProteomicsDB; 296084; -. [Q9ESW4-2]
DR Antibodypedia; 18305; 202 antibodies from 32 providers.
DR DNASU; 69923; -.
DR Ensembl; ENSMUST00000031977; ENSMUSP00000031977; ENSMUSG00000029916. [Q9ESW4-1]
DR GeneID; 69923; -.
DR KEGG; mmu:69923; -.
DR UCSC; uc009bmm.2; mouse. [Q9ESW4-2]
DR UCSC; uc009bmn.2; mouse. [Q9ESW4-1]
DR CTD; 55750; -.
DR MGI; MGI:1917173; Agk.
DR VEuPathDB; HostDB:ENSMUSG00000029916; -.
DR eggNOG; KOG4435; Eukaryota.
DR GeneTree; ENSGT00940000154961; -.
DR HOGENOM; CLU_042458_0_0_1; -.
DR InParanoid; Q9ESW4; -.
DR OMA; FFCDPRR; -.
DR OrthoDB; 1312024at2759; -.
DR PhylomeDB; Q9ESW4; -.
DR TreeFam; TF320485; -.
DR BRENDA; 2.7.1.94; 3474.
DR Reactome; R-MMU-1483206; Glycerophospholipid biosynthesis.
DR SABIO-RK; Q9ESW4; -.
DR UniPathway; UPA00230; -.
DR BioGRID-ORCS; 69923; 6 hits in 72 CRISPR screens.
DR ChiTaRS; Agk; mouse.
DR PRO; PR:Q9ESW4; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9ESW4; protein.
DR Bgee; ENSMUSG00000029916; Expressed in animal zygote and 93 other tissues.
DR ExpressionAtlas; Q9ESW4; baseline and differential.
DR Genevisible; Q9ESW4; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0042721; C:TIM22 mitochondrial import inner membrane insertion complex; ISS:UniProtKB.
DR GO; GO:0047620; F:acylglycerol kinase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0001729; F:ceramide kinase activity; IDA:MGI.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IDA:UniProtKB.
DR GO; GO:0102773; F:dihydroceramide kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0001727; F:lipid kinase activity; IDA:MGI.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0046513; P:ceramide biosynthetic process; IDA:MGI.
DR GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046834; P:lipid phosphorylation; IDA:MGI.
DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0006665; P:sphingolipid metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR045579; AGK_C.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR Pfam; PF19712; AGK_C; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Kinase; Lipid metabolism;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..421
FT /note="Acylglycerol kinase, mitochondrial"
FT /id="PRO_0000252381"
FT DOMAIN 58..199
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT REGION 15..31
FT /note="Hydrophobic"
FT /evidence="ECO:0000250|UniProtKB:Q53H12"
FT REGION 252..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q53H12"
FT VAR_SEQ 174..421
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020927"
SQ SEQUENCE 421 AA; 46976 MW; DBBC48C9EB3206FD CRC64;
MTAFFKTLRN HWKKTTAGLC LLTWGGHWLY GKHCDNLLRR AACQEAQVFG NQLIPPNAQV
KKATVFLNPA ACKGKARTLF EKNAAPILHL SGMDVTVVKT DYEGQAKKLL ELMESTDVII
VAGGDGTLQE VVTGVLRRTD EATFSKIPIG FIPLGQTSSL SHTLFAESGN KVQHITDATL
AIVKGETVPL DVLQIKGEKE QPVYAMTGLR WGSFRDAGVK VSKYWYLGPL KTKAAHFFST
LQEWPQTHQA SISYTGPRER PPIEPEETPP RPSLYRRILR RLASFWAQPQ DASSREVSPE
VWKDVQLSTI ELSITTRNTQ LDLMSKEDFM NICIEPDTVS KGDFIIIGSK KVRDPGLRAA
GTECLQASHC TLVLPEGTEG SFSIDSEEYE AMPVEVKLLP RKLRFFCDPR KREQMLPSTS
Q
