KAD3_MOUSE
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 03-AUG-2022, entry version 174.
DE RecName: Full=GTP:AMP phosphotransferase AK3, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03169};
DE EC=2.7.4.10 {ECO:0000255|HAMAP-Rule:MF_03169};
DE AltName: Full=Adenylate kinase 3 {ECO:0000255|HAMAP-Rule:MF_03169};
DE Short=AK 3 {ECO:0000255|HAMAP-Rule:MF_03169};
DE AltName: Full=Adenylate kinase 3 alpha-like 1 {ECO:0000255|HAMAP-Rule:MF_03169};
GN Name=Ak3; Synonyms=Ak3l, Ak3l1, Akl3l;
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, and
RC 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, 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).
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: Involved in maintaining the homeostasis of cellular
CC nucleotides by catalyzing the interconversion of nucleoside phosphates.
CC Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase
CC activities. {ECO:0000255|HAMAP-Rule:MF_03169}.
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:0000255|HAMAP-Rule:MF_03169};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03169}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC 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 dissambling the active center
CC during each catalytic cycle provides an effective means to prevent GTP
CC hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03169}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK3 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03169}.
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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_021299.1.
DR AlphaFoldDB; Q9WTP7; -.
DR SMR; Q9WTP7; -.
DR BioGRID; 207863; 2.
DR IntAct; Q9WTP7; 1.
DR STRING; 10090.ENSMUSP00000025696; -.
DR iPTMnet; Q9WTP7; -.
DR PhosphoSitePlus; Q9WTP7; -.
DR SwissPalm; Q9WTP7; -.
DR EPD; Q9WTP7; -.
DR jPOST; Q9WTP7; -.
DR MaxQB; Q9WTP7; -.
DR PaxDb; Q9WTP7; -.
DR PeptideAtlas; Q9WTP7; -.
DR PRIDE; Q9WTP7; -.
DR ProteomicsDB; 268950; -.
DR Antibodypedia; 24061; 400 antibodies from 28 providers.
DR DNASU; 56248; -.
DR Ensembl; ENSMUST00000025696; ENSMUSP00000025696; ENSMUSG00000024782.
DR GeneID; 56248; -.
DR KEGG; mmu:56248; -.
DR UCSC; uc008hcx.1; mouse.
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; MSPVIAW; -.
DR OrthoDB; 1004067at2759; -.
DR PhylomeDB; Q9WTP7; -.
DR TreeFam; TF312916; -.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 56248; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Ak3; mouse.
DR PRO; PR:Q9WTP7; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9WTP7; protein.
DR Bgee; ENSMUSG00000024782; Expressed in epithelium of stomach and 266 other tissues.
DR ExpressionAtlas; Q9WTP7; baseline and differential.
DR Genevisible; Q9WTP7; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0004017; F:adenylate kinase activity; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046899; F:nucleoside triphosphate adenylate kinase activity; ISO:MGI.
DR GO; GO:0006172; P:ADP biosynthetic process; ISO:MGI.
DR GO; GO:0046033; P:AMP metabolic process; ISO:MGI.
DR GO; GO:0006756; P:AMP phosphorylation; ISO:MGI.
DR GO; GO:0046034; P:ATP metabolic process; ISO:MGI.
DR GO; GO:0046060; P:dATP metabolic process; ISO:MGI.
DR GO; GO:0046039; P:GTP metabolic process; ISO:MGI.
DR GO; GO:0046041; P:ITP metabolic process; ISO:MGI.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046051; P:UTP metabolic process; ISO:MGI.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR23359; PTHR23359; 1.
DR Pfam; PF05191; ADK_lid; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF57774; SSF57774; 1.
DR TIGRFAMs; TIGR01351; adk; 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..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 38
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 43
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 64..66
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 91..94
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 98
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 128
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 137..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 161
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 172
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
FT BINDING 201
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03169"
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
