ID KAD3_MOUSE Reviewed; 227 AA. AC Q9WTP7; Q3UDN7; Q8BGX5; Q9D7Z1; Q9DB57; Q9DBM5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 193. DE RecName: Full=GTP:AMP phosphotransferase AK3, mitochondrial {ECO:0000250|UniProtKB:Q9UIJ7}; DE EC=2.7.4.10 {ECO:0000250|UniProtKB:Q9UIJ7}; DE AltName: Full=Adenylate kinase 3 {ECO:0000312|MGI:MGI:1860835}; GN Name=Ak3 {ECO:0000312|MGI:MGI:1860835}; 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 MRNA]. RC STRAIN=C57BL/6J, and NOD; RC TISSUE=Amnion, Bone marrow, Cerebellum, Eye, Liver, Stomach, Testis, RC and Thymus; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon, and Mammary gland; 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 9-227. RA Noma T.; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, 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). RN [5] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-20; LYS-29; LYS-57; LYS-64; RP LYS-80; LYS-174 AND LYS-189, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-29; LYS-34; LYS-64; LYS-80; RP LYS-174; LYS-189 AND LYS-203, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria RT identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- FUNCTION: Mitochondrial adenylate kinase with a specific GTP:AMP CC phosphotransferase activity. Could also use ITP as phosphate donor. Its CC physiological function is to recycle GTP into GDP which is necessary CC for the TCA cycle in the mitochondrial matrix. CC {ECO:0000250|UniProtKB:Q9UIJ7}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + AMP = a ribonucleoside 5'- CC diphosphate + ADP; Xref=Rhea:RHEA:13749, ChEBI:CHEBI:57930, CC ChEBI:CHEBI:61557, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; CC EC=2.7.4.10; Evidence={ECO:0000250|UniProtKB:Q9UIJ7, CC ECO:0000255|HAMAP-Rule:MF_03169}; CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + AMP = GDP + ADP; Xref=Rhea:RHEA:29863, CC ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:456215, CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9UIJ7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ITP + AMP = IDP + ADP; Xref=Rhea:RHEA:29867, CC ChEBI:CHEBI:58280, ChEBI:CHEBI:61402, ChEBI:CHEBI:456215, CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9UIJ7}; CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9UIJ7, ECO:0000255|HAMAP- CC Rule:MF_03169}. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix CC {ECO:0000250|UniProtKB:Q9UIJ7, ECO:0000255|HAMAP-Rule:MF_03169}. CC -!- DOMAIN: Consists of three domains, a large central CORE domain and two CC small peripheral domains, NMPbind and LID, which undergo movements CC during catalysis. The LID domain closes over the site of phosphoryl CC transfer upon GTP binding. Assembling and disassembling the active CC center during each catalytic cycle provides an effective means to CC prevent GTP hydrolysis. {ECO:0000250|UniProtKB:Q9UIJ7, CC ECO:0000255|HAMAP-Rule:MF_03169}. CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK3 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_03169}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK004864; BAB23625.1; -; mRNA. DR EMBL; AK005194; BAB23876.1; -; mRNA. DR EMBL; AK008681; BAB25829.1; -; mRNA. DR EMBL; AK031631; BAC27488.1; -; mRNA. DR EMBL; AK053644; BAC35459.1; -; mRNA. DR EMBL; AK089027; BAC40707.1; -; mRNA. DR EMBL; AK147060; BAE27644.1; -; mRNA. DR EMBL; AK149996; BAE29224.1; -; mRNA. DR EMBL; BC016432; AAH16432.1; -; mRNA. DR EMBL; BC019174; AAH19174.1; -; mRNA. DR EMBL; BC024871; AAH24871.1; -; mRNA. DR EMBL; BC058191; AAH58191.1; -; mRNA. DR EMBL; AB020203; BAA77360.1; -; mRNA. DR CCDS; CCDS29730.1; -. DR RefSeq; NP_067274.1; NM_021299.2. DR AlphaFoldDB; Q9WTP7; -. DR SMR; Q9WTP7; -. DR BioGRID; 207863; 4. DR FunCoup; Q9WTP7; 1722. DR IntAct; Q9WTP7; 1. DR STRING; 10090.ENSMUSP00000025696; -. DR GlyGen; Q9WTP7; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9WTP7; -. DR PhosphoSitePlus; Q9WTP7; -. DR SwissPalm; Q9WTP7; -. DR jPOST; Q9WTP7; -. DR PaxDb; 10090-ENSMUSP00000025696; -. DR PeptideAtlas; Q9WTP7; -. DR ProteomicsDB; 268950; -. DR Pumba; Q9WTP7; -. DR Antibodypedia; 24061; 406 antibodies from 28 providers. DR DNASU; 56248; -. DR Ensembl; ENSMUST00000025696.5; ENSMUSP00000025696.5; ENSMUSG00000024782.8. DR GeneID; 56248; -. DR KEGG; mmu:56248; -. DR UCSC; uc008hcx.1; mouse. DR AGR; MGI:1860835; -. DR CTD; 50808; -. DR MGI; MGI:1860835; Ak3. DR VEuPathDB; HostDB:ENSMUSG00000024782; -. DR eggNOG; KOG3078; Eukaryota. DR GeneTree; ENSGT00940000155120; -. DR HOGENOM; CLU_032354_1_1_1; -. DR InParanoid; Q9WTP7; -. DR OMA; TIAHFST; -. DR OrthoDB; 439792at2759; -. DR PhylomeDB; Q9WTP7; -. DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production. DR BioGRID-ORCS; 56248; 1 hit in 77 CRISPR screens. DR PRO; PR:Q9WTP7; -. DR Proteomes; UP000000589; Chromosome 19. DR RNAct; Q9WTP7; protein. DR Bgee; ENSMUSG00000024782; Expressed in epithelium of stomach and 269 other cell types or tissues. DR ExpressionAtlas; Q9WTP7; baseline and differential. DR GO; GO:0005759; C:mitochondrial matrix; IDA:BHF-UCL. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0004017; F:AMP kinase activity; ISO:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0042802; F:identical protein binding; ISO:GO_Central. DR GO; GO:0046899; F:nucleoside triphosphate adenylate kinase activity; ISS:UniProtKB. DR GO; GO:0006172; P:ADP biosynthetic process; ISO:GO_Central. DR GO; GO:0046033; P:AMP metabolic process; ISO:GO_Central. DR GO; GO:0006756; P:AMP phosphorylation; ISO:GO_Central. DR GO; GO:0046060; P:dATP metabolic process; ISO:GO_Central. DR GO; GO:0046039; P:GTP metabolic process; ISO:GO_Central. DR GO; GO:0046041; P:ITP metabolic process; ISO:GO_Central. DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0046051; P:UTP metabolic process; ISO:GO_Central. DR CDD; cd01428; ADK; 1. DR FunFam; 3.40.50.300:FF:000106; Adenylate kinase mitochondrial; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1. DR HAMAP; MF_03169; Adenylate_kinase_AK3; 1. DR InterPro; IPR006259; Adenyl_kin_sub. DR InterPro; IPR000850; Adenylat/UMP-CMP_kin. DR InterPro; IPR033690; Adenylat_kinase_CS. DR InterPro; IPR007862; Adenylate_kinase_lid-dom. DR InterPro; IPR036193; ADK_active_lid_dom_sf. DR InterPro; IPR028586; AK3/Ak4_mitochondrial. DR InterPro; IPR027417; P-loop_NTPase. DR NCBIfam; TIGR01351; adk; 1. DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1. DR Pfam; PF00406; ADK; 1. DR Pfam; PF05191; ADK_lid; 1. DR PRINTS; PR00094; ADENYLTKNASE. DR SUPFAM; SSF57774; Microbial and mitochondrial ADK, insert 'zinc finger' domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00113; ADENYLATE_KINASE; 1. PE 1: Evidence at protein level; KW Acetylation; GTP-binding; Kinase; Mitochondrion; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Transferase. FT CHAIN 1..227 FT /note="GTP:AMP phosphotransferase AK3, mitochondrial" FT /id="PRO_0000158923" FT REGION 37..66 FT /note="NMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169" FT REGION 127..164 FT /note="LID" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169" FT BINDING 17 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9UIJ7" FT BINDING 19 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9UIJ7" FT BINDING 20 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9UIJ7" FT BINDING 21 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9UIJ7" FT BINDING 22 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9UIJ7" FT BINDING 38 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000250|UniProtKB:Q9UIJ7" FT BINDING 43 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000250|UniProtKB:Q9UIJ7" FT BINDING 64 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000250|UniProtKB:Q9UIJ7" FT BINDING 91 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000250|UniProtKB:Q9UIJ7" FT BINDING 94 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000250|UniProtKB:P08760" FT BINDING 98 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000250|UniProtKB:Q9UIJ7" FT BINDING 128 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9UIJ7" FT BINDING 138 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9UIJ7" FT BINDING 139 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9UIJ7" FT BINDING 161 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9UIJ7" FT BINDING 172 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9UIJ7" FT BINDING 201 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q9UIJ7" FT MOD_RES 20 FT /note="N6-succinyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 29 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 29 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 34 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 37 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 57 FT /note="N6-succinyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 64 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 64 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 80 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 80 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 174 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 174 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 189 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 189 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 203 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT CONFLICT 171 FT /note="K -> E (in Ref. 1; BAB23625)" FT /evidence="ECO:0000305" FT CONFLICT 202 FT /note="N -> D (in Ref. 1; BAB23876)" FT /evidence="ECO:0000305" SQ SEQUENCE 227 AA; 25426 MW; 6601DF10971DE5AC CRC64; MGASGRLLRA VIMGAPGSGK GTVSSRITKH FELKHLSSGD LLRQNMLQGT EIGVLAKTFI DQGKLIPDDV MTRLALHELK TLTQCSWLLD GFPRTLPQAE ALDKVYQIDT VINLNVPFEV IKQRLTARWI HPASGRVYNI EFNPPKTVGI DDLTGEPLIQ REDDKPETVI KRLKAYEAQT EPVLQYYQKK GVLETFSGTE TNKIWPHVYS FLQTKVPETT QKASVTP //