AGK_DANRE
ID AGK_DANRE Reviewed; 422 AA.
AC Q7ZW00; Q1LX48;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 122.
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};
GN ORFNames=si:ch211-238n5.3, zgc:55462;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) 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).
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.
CC {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; BX470166; CAK04664.1; -; Genomic_DNA.
DR EMBL; BC045347; AAH45347.1; -; mRNA.
DR RefSeq; NP_956174.1; NM_199880.1.
DR AlphaFoldDB; Q7ZW00; -.
DR SMR; Q7ZW00; -.
DR STRING; 7955.ENSDARP00000011155; -.
DR PaxDb; Q7ZW00; -.
DR Ensembl; ENSDART00000006109; ENSDARP00000011155; ENSDARG00000009837.
DR GeneID; 334270; -.
DR KEGG; dre:334270; -.
DR CTD; 55750; -.
DR ZFIN; ZDB-GENE-030131-6202; agk.
DR eggNOG; KOG4435; Eukaryota.
DR GeneTree; ENSGT00940000154961; -.
DR HOGENOM; CLU_042458_0_0_1; -.
DR InParanoid; Q7ZW00; -.
DR OMA; FFCDPRR; -.
DR OrthoDB; 1312024at2759; -.
DR PhylomeDB; Q7ZW00; -.
DR TreeFam; TF320485; -.
DR Reactome; R-DRE-1483206; Glycerophospholipid biosynthesis.
DR UniPathway; UPA00230; -.
DR PRO; PR:Q7ZW00; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 18.
DR Bgee; ENSDARG00000009837; Expressed in swim bladder and 28 other tissues.
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; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0004143; F:diacylglycerol kinase activity; ISS:UniProtKB.
DR GO; GO:0102773; F:dihydroceramide kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0001727; F:lipid kinase activity; IBA:GO_Central.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Lipid metabolism; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..422
FT /note="Acylglycerol kinase, mitochondrial"
FT /id="PRO_0000252383"
FT DOMAIN 61..202
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT REGION 18..34
FT /note="Hydrophobic"
FT /evidence="ECO:0000250|UniProtKB:Q53H12"
FT CONFLICT 35
FT /note="N -> K (in Ref. 2; AAH45347)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 47545 MW; 856F387D221AC956 CRC64;
MARVVKVFRT LRNHWKKSTF AVCVLSYGGH WLYGNHCDSV LRREACIEAR AFGQQLIGPQ
EILKKATVIL NPAACKGKAN QLFEKNAAPI LHLAGVEVKI VKTDYEGQAK KLMELMEQTD
MLIIAGGDGT LQEVITGLLR RADEEIFSKT PIGFIPLGSS NSLSQSLHLV SDNKVQHITS
ATLSILKGET VPLDVLQIKG EKEQPVFALL GLRWGAFRDV ATSISKYWYL GPLKTRAAHW
FSSLKQWPQV HVASLSYLAP VPRPPDLPDE IPQRPNLLYR IYRRLQNYWN PPLEEPPKEP
EPEQWESKDV STLELTVLTH NKNPVKRRVD DSMLISLDPE SLTAGQFITE GTNKSVDPME
PIENAVQIEA SAARLELPEE GAGFYDIDNQ EYEAMSVEVR LLPRKLRFFC SAERREQLAE
AQ
