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Acylglycerol kinase, mitochondrial (hAGK) (EC 2.7.1.107) (EC 2.7.1.94) (Multiple substrate lipid kinase) (HsMuLK) (MuLK) (Multi-substrate lipid kinase)

 AGK_HUMAN               Reviewed;         422 AA.
Q53H12; Q75KN1; Q96GC3; Q9NP48;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
22-NOV-2017, entry version 121.
RecName: Full=Acylglycerol kinase, mitochondrial {ECO:0000303|PubMed:15939762};
Short=hAGK {ECO:0000303|PubMed:15939762};
EC=2.7.1.107 {ECO:0000269|PubMed:15939762};
EC=2.7.1.94 {ECO:0000269|PubMed:15939762};
AltName: Full=Multiple substrate lipid kinase {ECO:0000303|PubMed:16269826};
Short=HsMuLK {ECO:0000303|PubMed:16269826};
Short=MuLK {ECO:0000303|PubMed:16269826};
Short=Multi-substrate lipid kinase {ECO:0000303|PubMed:16269826};
Name=AGK {ECO:0000303|PubMed:15939762, ECO:0000312|HGNC:HGNC:21869};
Synonyms=MULK {ECO:0000303|PubMed:16269826};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
PubMed=16269826; DOI=10.1194/jlr.M500321-JLR200;
Van Overloop H., Gijsbers S., Van Veldhoven P.P.;
"Further characterization of mammalian ceramide kinase: substrate
delivery and (stereo)specificity, tissue distribution, and subcellular
localization studies.";
J. Lipid Res. 47:268-283(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Liver;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Gall bladder, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, COFACTOR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
INDUCTION, AND MUTAGENESIS OF GLY-126.
PubMed=15939762; DOI=10.1083/jcb.200407123;
Bektas M., Payne S.G., Liu H., Goparaju S., Milstien S., Spiegel S.;
"A novel acylglycerol kinase that produces lysophosphatidic acid
modulates cross talk with EGFR in prostate cancer cells.";
J. Cell Biol. 169:801-811(2005).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
INVOLVEMENT IN MTDPS10.
PubMed=22284826; DOI=10.1016/j.ajhg.2011.12.005;
Mayr J.A., Haack T.B., Graf E., Zimmermann F.A., Wieland T.,
Haberberger B., Superti-Furga A., Kirschner J., Steinmann B.,
Baumgartner M.R., Moroni I., Lamantea E., Zeviani M., Rodenburg R.J.,
Smeitink J., Strom T.M., Meitinger T., Sperl W., Prokisch H.;
"Lack of the mitochondrial protein acylglycerol kinase causes Sengers
syndrome.";
Am. J. Hum. Genet. 90:314-320(2012).
[10]
INVOLVEMENT IN CTRCT38.
PubMed=22415731; DOI=10.1002/humu.22071;
Aldahmesh M.A., Khan A.O., Mohamed J.Y., Alghamdi M.H., Alkuraya F.S.;
"Identification of a truncation mutation of acylglycerol kinase (AGK)
gene in a novel autosomal recessive cataract locus.";
Hum. Mutat. 33:960-962(2012).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[12]
INVOLVEMENT IN MTDPS10.
PubMed=22277967; DOI=10.1126/scitranslmed.3003310;
Calvo S.E., Compton A.G., Hershman S.G., Lim S.C., Lieber D.S.,
Tucker E.J., Laskowski A., Garone C., Liu S., Jaffe D.B.,
Christodoulou J., Fletcher J.M., Bruno D.L., Goldblatt J., Dimauro S.,
Thorburn D.R., Mootha V.K.;
"Molecular diagnosis of infantile mitochondrial disease with targeted
next-generation sequencing.";
Sci. Transl. Med. 4:118RA10-118RA10(2012).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[15]
FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE TIM22 COMPLEX,
AND MUTAGENESIS OF GLY-126.
PubMed=28712724; DOI=10.1016/j.molcel.2017.06.013;
Vukotic M., Nolte H., Koenig T., Saita S., Ananjew M., Krueger M.,
Tatsuta T., Langer T.;
"Acylglycerol kinase mutated in Sengers Syndrome is a subunit of the
TIM22 protein translocase in mitochondria.";
Mol. Cell 0:0-0(2017).
[16]
FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE TIM22 COMPLEX,
INVOLVEMENT IN MTDPS10, AND MUTAGENESIS OF GLY-126.
PubMed=28712726; DOI=10.1016/j.molcel.2017.06.014;
Kang Y., Stroud D.A., Baker M.J., De Souza D.P., Frazier A.E.,
Liem M., Tull D., Mathivanan S., McConville M.J., Thorburn D.R.,
Ryan M.T., Stojanovski D.;
"Sengers syndrome-associated mitochondrial acylglycerol kinase is a
subunit of the human TIM22 protein import complex.";
Mol. Cell 0:0-0(2017).
[17]
VARIANT MTDPS10 327-LYS--GLN-422 DEL.
PubMed=23266196; DOI=10.1016/j.ymgme.2012.11.282;
Siriwardena K., Mackay N., Levandovskiy V., Blaser S., Raiman J.,
Kantor P.F., Ackerley C., Robinson B.H., Schulze A., Cameron J.M.;
"Mitochondrial citrate synthase crystals: novel finding in Sengers
syndrome caused by acylglycerol kinase (AGK) mutations.";
Mol. Genet. Metab. 108:40-50(2013).
[18]
VARIANTS MTDPS10 137-ARG--GLN-422 DEL AND 291-GLN--GLN-422 DEL.
PubMed=25208612; DOI=10.1186/s13023-014-0119-3;
Haghighi A., Haack T.B., Atiq M., Mottaghi H., Haghighi-Kakhki H.,
Bashir R.A., Ahting U., Feichtinger R.G., Mayr J.A., Roetig A.,
Lebre A.S., Klopstock T., Dworschak A., Pulido N., Saeed M.A.,
Saleh-Gohari N., Holzerova E., Chinnery P.F., Taylor R.W.,
Prokisch H.;
"Sengers syndrome: six novel AGK mutations in seven new families and
review of the phenotypic and mutational spectrum of 29 patients.";
Orphanet J. Rare Dis. 9:119-119(2014).
-!- FUNCTION: Lipid kinase that can phosphorylate both
monoacylglycerol and diacylglycerol to form lysophosphatidic acid
(LPA) and phosphatidic acid (PA), respectively (PubMed:15939762).
Does not phosphorylate sphingosine (PubMed:15939762).
Independently of its lipid kinase activity, acts as a component of
the TIM22 complex (PubMed:28712724, PubMed:28712726). The TIM22
complex mediates the import and insertion of multi-pass
transmembrane proteins into the mitochondrial inner membrane by
forming a twin-pore translocase that uses the membrane potential
as the external driving force (PubMed:28712724, PubMed:28712726).
In the TIM22 complex, required for the import of a subset of
metabolite carriers into mitochtondria, such as ANT1/SLC25A4 and
SLC25A24, while it is not required for the import of TIMM23
(PubMed:28712724). Overexpression increases the formation and
secretion of LPA, resulting in transactivation of EGFR and
activation of the downstream MAPK signaling pathway, leading to
increased cell growth (PubMed:15939762).
{ECO:0000269|PubMed:15939762, ECO:0000269|PubMed:28712724,
ECO:0000269|PubMed:28712726}.
-!- CATALYTIC ACTIVITY: ATP + acylglycerol = ADP + acyl-sn-glycerol 3-
phosphate. {ECO:0000269|PubMed:15939762}.
-!- CATALYTIC ACTIVITY: ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-
diacyl-sn-glycerol 3-phosphate. {ECO:0000269|PubMed:15939762}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:15939762};
-!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
{ECO:0000269|PubMed:15939762}.
-!- SUBUNIT: Component of the TIM22 complex, which core is composed of
TIMM22, associated with TIMM10 (TIMM10A and/or TIMM10B), TIMM9,
AGK and TIMM29 (PubMed:28712724, PubMed:28712726).
{ECO:0000269|PubMed:28712724, ECO:0000269|PubMed:28712726}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000269|PubMed:15939762, ECO:0000269|PubMed:16269826,
ECO:0000269|PubMed:28712724, ECO:0000269|PubMed:28712726};
Peripheral membrane protein {ECO:0000269|PubMed:28712724}.
Mitochondrion intermembrane space {ECO:0000269|PubMed:28712724,
ECO:0000269|PubMed:28712726}. Note=Localizes in the mitochondrion
intermembrane space, where it associates with the inner membrane
(PubMed:28712724). It is unclear whether the N-terminal
hydrophobic region forms a transmembrane region or associates with
the membrane without crossing it (PubMed:28712724,
PubMed:28712726). {ECO:0000269|PubMed:28712724,
ECO:0000269|PubMed:28712726}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q53H12-1; Sequence=Displayed;
Name=2;
IsoId=Q53H12-2; Sequence=VSP_020925, VSP_020926;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in muscle, heart, kidney and
brain. {ECO:0000269|PubMed:15939762}.
-!- INDUCTION: Overexpressed in prostate cancer, suggesting that it
may play a role in initiation and progression of prostate cancer,
processes in which lysophosphatidic acid (LPA) plays key roles.
{ECO:0000269|PubMed:15939762}.
-!- DISEASE: Mitochondrial DNA depletion syndrome 10 (MTDPS10)
[MIM:212350]: An autosomal recessive mitochondrial disorder
characterized by congenital cataracts, hypertrophic
cardiomyopathy, skeletal myopathy, exercise intolerance, and
lactic acidosis. Mental development is normal, but affected
individuals may die early from cardiomyopathy.
{ECO:0000269|PubMed:22277967, ECO:0000269|PubMed:22284826,
ECO:0000269|PubMed:23266196, ECO:0000269|PubMed:25208612,
ECO:0000269|PubMed:28712726}. Note=The disease is caused by
mutations affecting the gene represented in this entry. The TIM22
complex and import of proteins into mitochondrion are affected in
patients suffering of MTDPS10 (PubMed:28712726).
{ECO:0000269|PubMed:28712726}.
-!- DISEASE: Cataract 38 (CTRCT38) [MIM:614691]: An opacification of
the crystalline lens of the eye becoming evident at birth. It
frequently results in visual impairment or blindness. Opacities
vary in morphology, are often confined to a portion of the lens,
and may be static or progressive. In general, the more posteriorly
located and dense an opacity, the greater the impact on visual
function. {ECO:0000269|PubMed:22415731}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the AGK family. {ECO:0000305}.
-!- CAUTION: According to a report, the N-terminal hydrophobic region
forms a transmembrane region that crosses the mitochondrion inner
membrane (PubMed:28712726). According to another report, the N-
terminal hydrophobic region associates with the membrane without
crossing it (PubMed:28712724). {ECO:0000269|PubMed:28712724,
ECO:0000269|PubMed:28712726}.
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EMBL; AJ278150; CAB93536.1; -; mRNA.
EMBL; AK001704; BAA91848.1; -; mRNA.
EMBL; AK222769; BAD96489.1; -; mRNA.
EMBL; AC004918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC073878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC099547; AAS07537.1; -; Genomic_DNA.
EMBL; BC009775; AAH09775.1; -; mRNA.
EMBL; BC022777; AAH22777.1; -; mRNA.
CCDS; CCDS5865.1; -. [Q53H12-1]
RefSeq; NP_060708.1; NM_018238.3. [Q53H12-1]
RefSeq; XP_011514699.1; XM_011516397.2. [Q53H12-1]
UniGene; Hs.743318; -.
ProteinModelPortal; Q53H12; -.
BioGrid; 120868; 29.
IntAct; Q53H12; 21.
MINT; MINT-1378485; -.
STRING; 9606.ENSP00000347581; -.
ChEMBL; CHEMBL2417354; -.
SwissLipids; SLP:000000638; -.
iPTMnet; Q53H12; -.
PhosphoSitePlus; Q53H12; -.
SwissPalm; Q53H12; -.
BioMuta; AGK; -.
DMDM; 116248550; -.
EPD; Q53H12; -.
MaxQB; Q53H12; -.
PaxDb; Q53H12; -.
PeptideAtlas; Q53H12; -.
PRIDE; Q53H12; -.
DNASU; 55750; -.
Ensembl; ENST00000355413; ENSP00000347581; ENSG00000006530. [Q53H12-1]
Ensembl; ENST00000492693; ENSP00000418789; ENSG00000006530. [Q53H12-2]
Ensembl; ENST00000575872; ENSP00000458417; ENSG00000262327.
GeneID; 55750; -.
KEGG; hsa:55750; -.
UCSC; uc003vwi.3; human. [Q53H12-1]
CTD; 55750; -.
DisGeNET; 55750; -.
EuPathDB; HostDB:ENSG00000006530.15; -.
GeneCards; AGK; -.
HGNC; HGNC:21869; AGK.
HPA; HPA020959; -.
HPA; HPA053471; -.
MalaCards; AGK; -.
MIM; 212350; phenotype.
MIM; 610345; gene.
MIM; 614691; phenotype.
neXtProt; NX_Q53H12; -.
OpenTargets; ENSG00000006530; -.
Orphanet; 1369; Congenital cataract - hypertrophic cardiomyopathy - mitochondrial myopathy.
Orphanet; 91492; Non-syndromic congenital cataract.
PharmGKB; PA162375851; -.
eggNOG; KOG4435; Eukaryota.
eggNOG; COG1597; LUCA.
GeneTree; ENSGT00690000101761; -.
HOGENOM; HOG000252977; -.
HOVERGEN; HBG080751; -.
InParanoid; Q53H12; -.
KO; K09881; -.
OMA; TKAAHFF; -.
OrthoDB; EOG091G06YD; -.
PhylomeDB; Q53H12; -.
TreeFam; TF320485; -.
BRENDA; 2.7.1.94; 2681.
Reactome; R-HSA-1483206; Glycerophospholipid biosynthesis.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
SABIO-RK; Q53H12; -.
UniPathway; UPA00230; -.
ChiTaRS; AGK; human.
GeneWiki; AGK_(gene); -.
GenomeRNAi; 55750; -.
PRO; PR:Q53H12; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000006530; -.
CleanEx; HS_AGK; -.
ExpressionAtlas; Q53H12; baseline and differential.
Genevisible; Q53H12; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
GO; GO:0042721; C:mitochondrial inner membrane protein insertion complex; IDA:UniProtKB.
GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0047620; F:acylglycerol kinase activity; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0001729; F:ceramide kinase activity; IEA:Ensembl.
GO; GO:0004143; F:diacylglycerol kinase activity; IEA:UniProtKB-EC.
GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
GO; GO:0046513; P:ceramide biosynthetic process; IEA:Ensembl.
GO; GO:0046474; P:glycerophospholipid biosynthetic process; TAS:Reactome.
GO; GO:0045039; P:protein import into mitochondrial inner membrane; IDA:UniProtKB.
Gene3D; 3.40.50.10330; -; 1.
InterPro; IPR017438; ATP-NAD_kinase_N.
InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
Pfam; PF00781; DAGK_cat; 1.
SMART; SM00046; DAGKc; 1.
SUPFAM; SSF111331; SSF111331; 2.
PROSITE; PS50146; DAGK; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cardiomyopathy; Cataract;
Complete proteome; Disease mutation; Kinase; Membrane; Mitochondrion;
Mitochondrion inner membrane; Nucleotide-binding; Polymorphism;
Primary mitochondrial disease; Reference proteome; Transferase.
CHAIN 1 422 Acylglycerol kinase, mitochondrial.
/FTId=PRO_0000252380.
DOMAIN 58 199 DAGKc. {ECO:0000255|PROSITE-
ProRule:PRU00783}.
REGION 15 31 Hydrophobic. {ECO:0000305}.
VAR_SEQ 48 65 VFGNQLIPPNAQVKKATV -> HYQDESRWEPTLSRTPGS
(in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_020925.
VAR_SEQ 66 422 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_020926.
VARIANT 3 3 V -> M (in dbSNP:rs10262855).
/FTId=VAR_027848.
VARIANT 137 422 Missing (in MTDPS10).
{ECO:0000269|PubMed:25208612}.
/FTId=VAR_079050.
VARIANT 291 422 Missing (in MTDPS10).
{ECO:0000269|PubMed:25208612}.
/FTId=VAR_079051.
VARIANT 327 422 Missing (in MTDPS10).
{ECO:0000269|PubMed:23266196}.
/FTId=VAR_079052.
MUTAGEN 126 126 G->E: Abolishes lipid kinase activity.
Does not affect ability to associate with
the TIM22 complex and mediate import of
transmembrane proteins into the
mitochondrial inner membrane.
{ECO:0000269|PubMed:15939762,
ECO:0000269|PubMed:28712724,
ECO:0000269|PubMed:28712726}.
CONFLICT 94 94 D -> V (in Ref. 3; BAD96489).
{ECO:0000305}.
SEQUENCE 422 AA; 47137 MW; F9D85658616B8970 CRC64;
MTVFFKTLRN HWKKTTAGLC LLTWGGHWLY GKHCDNLLRR AACQEAQVFG NQLIPPNAQV
KKATVFLNPA ACKGKARTLF EKNAAPILHL SGMDVTIVKT DYEGQAKKLL ELMENTDVII
VAGGDGTLQE VVTGVLRRTD EATFSKIPIG FIPLGETSSL SHTLFAESGN KVQHITDATL
AIVKGETVPL DVLQIKGEKE QPVFAMTGLR WGSFRDAGVK VSKYWYLGPL KIKAAHFFST
LKEWPQTHQA SISYTGPTER PPNEPEETPV QRPSLYRRIL RRLASYWAQP QDALSQEVSP
EVWKDVQLST IELSITTRNN QLDPTSKEDF LNICIEPDTI SKGDFITIGS RKVRNPKLHV
EGTECLQASQ CTLLIPEGAG GSFSIDSEEY EAMPVEVKLL PRKLQFFCDP RKREQMLTSP
TQ


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