AGK_PONAB
ID AGK_PONAB Reviewed; 422 AA.
AC Q5RED7;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Acylglycerol kinase, mitochondrial {ECO:0000250|UniProtKB:Q53H12};
DE EC=2.7.1.107 {ECO:0000250|UniProtKB:Q53H12};
DE EC=2.7.1.138 {ECO:0000250|UniProtKB:Q9ESW4};
DE EC=2.7.1.94 {ECO:0000250|UniProtKB:Q53H12};
DE AltName: Full=Multiple substrate lipid kinase {ECO:0000250|UniProtKB:Q53H12};
DE Short=MuLK {ECO:0000250|UniProtKB:Q53H12};
DE Short=Multi-substrate lipid kinase {ECO:0000250|UniProtKB:Q53H12};
GN Name=AGK {ECO:0000250|UniProtKB:Q53H12};
GN Synonyms=MULK {ECO:0000250|UniProtKB:Q53H12};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lipid kinase that can phosphorylate both monoacylglycerol and
CC diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic
CC acid (PA), respectively (By similarity). Phosphorylates ceramide but
CC not sphingosine (By similarity). Phosphorylates 1,2-dioleoylglycerol
CC more rapidly than 2,3-dioleoylglycerol (By similarity). 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:0000250|UniProtKB:Q9ESW4}.
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:0000250|UniProtKB:Q53H12};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19294;
CC Evidence={ECO:0000250|UniProtKB:Q53H12};
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:0000250|UniProtKB:Q53H12};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000250|UniProtKB:Q53H12};
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:0000250|UniProtKB:Q9ESW4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17930;
CC Evidence={ECO:0000250|UniProtKB:Q9ESW4};
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:0000250|UniProtKB:Q53H12};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41080;
CC Evidence={ECO:0000250|UniProtKB:Q53H12};
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:0000250|UniProtKB:Q53H12};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000250|UniProtKB:Q53H12};
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=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:0000250|UniProtKB:Q9ESW4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43329;
CC Evidence={ECO:0000250|UniProtKB:Q9ESW4};
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:0000250|UniProtKB:Q53H12};
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000250|UniProtKB:Q53H12}.
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 -!- SIMILARITY: Belongs to the AGK family. {ECO:0000305}.
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DR EMBL; CR857592; CAH89870.1; -; mRNA.
DR RefSeq; NP_001124872.1; NM_001131400.1.
DR RefSeq; XP_009241570.1; XM_009243295.1.
DR AlphaFoldDB; Q5RED7; -.
DR SMR; Q5RED7; -.
DR STRING; 9601.ENSPPYP00000020268; -.
DR Ensembl; ENSPPYT00000021064; ENSPPYP00000020268; ENSPPYG00000018064.
DR GeneID; 100171735; -.
DR KEGG; pon:100171735; -.
DR CTD; 55750; -.
DR eggNOG; KOG4435; Eukaryota.
DR GeneTree; ENSGT00940000154961; -.
DR HOGENOM; CLU_042458_0_0_1; -.
DR InParanoid; Q5RED7; -.
DR OMA; FFCDPRR; -.
DR OrthoDB; 1312024at2759; -.
DR TreeFam; TF320485; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000001595; Chromosome 7.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISS:UniProtKB.
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:0042721; C:TIM22 mitochondrial import inner membrane insertion complex; ISS:UniProtKB.
DR GO; GO:0047620; F:acylglycerol kinase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0001729; F:ceramide kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004143; F:diacylglycerol kinase activity; ISS:UniProtKB.
DR GO; GO:0102773; F:dihydroceramide kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0046513; P:ceramide biosynthetic process; IEA:Ensembl.
DR GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Kinase; Lipid metabolism; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..422
FT /note="Acylglycerol kinase, mitochondrial"
FT /id="PRO_0000252382"
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 249..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"
SQ SEQUENCE 422 AA; 47068 MW; A3E092F9632A6538 CRC64;
MTVFFKTLRN HWKKTTAGLC LLTWGGHWLY GKHCDNLLRR AACQEAQVFG NQLIPPNAQV
KKATVFLNPA ACKGKARTLF EKNAAPILHL CGMDVTIVKT DYEGQAKKLL ELMENTDVII
VAGGDGTLQE VVTGVLRRTD EATFSKIPIG FIPLGETSSL SHTLFAESGN KVQHITDATL
AIVKGETVPL DVLQIKGEKE QPVFAMTGLR WGSFRDAGVK VSKYWYLGPL KIKAAHFFST
LKEWPQTHQA SISYTGPTER PPSEPEETPV QRPSLYRRIL RRLASYWAQP QDALSQEVSP
EVWKDVQLST IELSITTRNN QLDPTSKEDF LNICIEPDTI SKGDFITIGS RKVRNPKLHA
EGTECLQASQ CTLLIPEGAG GSFSIDSEEY EAMPVEVKLL PRKLQFFCDP RKREQMLTSP
AQ
