KAD1_MOUSE
ID KAD1_MOUSE Reviewed; 194 AA.
AC Q9R0Y5; A2AK80; Q542C5; Q9R0Y4;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Adenylate kinase isoenzyme 1 {ECO:0000255|HAMAP-Rule:MF_03171};
DE Short=AK 1 {ECO:0000255|HAMAP-Rule:MF_03171};
DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_03171};
DE EC=2.7.4.6 {ECO:0000255|HAMAP-Rule:MF_03171};
DE AltName: Full=ATP-AMP transphosphorylase 1 {ECO:0000255|HAMAP-Rule:MF_03171};
DE AltName: Full=ATP:AMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_03171};
DE AltName: Full=Adenylate monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_03171};
DE AltName: Full=Myokinase {ECO:0000255|HAMAP-Rule:MF_03171};
GN Name=Ak1;
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 [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=10557075; DOI=10.1038/sj.onc.1202970;
RA Collavin L., Lazarevic D., Utrera R., Marzinotto S., Monte M.,
RA Schneider C.;
RT "wt p53 dependent expression of a membrane-associated isoform of adenylate
RT kinase.";
RL Oncogene 18:5879-5888(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=CD-1;
RX PubMed=16790685; DOI=10.1095/biolreprod.106.053512;
RA Cao W., Haig-Ladewig L., Gerton G.L., Moss S.B.;
RT "Adenylate kinases 1 and 2 are part of the accessory structures in the
RT mouse sperm flagellum.";
RL Biol. Reprod. 75:492-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Adipose tissue;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor, and Retina;
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 [6]
RP PROTEIN SEQUENCE OF 32-44; 64-77; 84-97 AND 150-166, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC 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).
CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC group between ATP and AMP. Also possesses broad nucleoside diphosphate
CC kinase activity. Plays an important role in cellular energy homeostasis
CC and in adenine nucleotide metabolism (By similarity). May provide a
CC mechanism to buffer the adenylate energy charge for sperm motility.
CC {ECO:0000250, ECO:0000269|PubMed:16790685}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03171};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-
CC deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316,
CC ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03171};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-
CC triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03171};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03171}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03171}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Ak1a;
CC IsoId=Q9R0Y5-1; Sequence=Displayed;
CC Name=2; Synonyms=Ak1b;
CC IsoId=Q9R0Y5-2; Sequence=VSP_024843;
CC -!- DEVELOPMENTAL STAGE: Up-regulated during late spermiogenesis, when the
CC flagellum is being assembled. {ECO:0000269|PubMed:16790685}.
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 ATP binding. Assembling and dissambling the active center
CC during each catalytic cycle provides an effective means to prevent ATP
CC hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03171}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03171}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM16612.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; AJ010108; CAB52407.1; -; mRNA.
DR EMBL; AJ010109; CAB52408.1; -; mRNA.
DR EMBL; DQ486026; ABF46940.1; -; mRNA.
DR EMBL; AK046613; BAC32808.1; -; mRNA.
DR EMBL; AK089270; BAC40822.1; -; mRNA.
DR EMBL; AL772271; CAM16612.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL772271; CAM16613.1; -; Genomic_DNA.
DR EMBL; AL772271; CAM16614.1; -; Genomic_DNA.
DR EMBL; BC014802; AAH14802.1; -; mRNA.
DR EMBL; BC054366; AAH54366.1; -; mRNA.
DR CCDS; CCDS15924.1; -. [Q9R0Y5-2]
DR CCDS; CCDS57167.1; -. [Q9R0Y5-1]
DR RefSeq; NP_001185719.1; NM_001198790.1. [Q9R0Y5-1]
DR RefSeq; NP_001185720.1; NM_001198791.1. [Q9R0Y5-1]
DR RefSeq; NP_001185721.1; NM_001198792.1. [Q9R0Y5-1]
DR RefSeq; NP_067490.1; NM_021515.3. [Q9R0Y5-2]
DR RefSeq; XP_006497687.1; XM_006497624.3.
DR AlphaFoldDB; Q9R0Y5; -.
DR BMRB; Q9R0Y5; -.
DR SMR; Q9R0Y5; -.
DR BioGRID; 198045; 7.
DR IntAct; Q9R0Y5; 8.
DR MINT; Q9R0Y5; -.
DR STRING; 10090.ENSMUSP00000068479; -.
DR iPTMnet; Q9R0Y5; -.
DR PhosphoSitePlus; Q9R0Y5; -.
DR SwissPalm; Q9R0Y5; -.
DR REPRODUCTION-2DPAGE; IPI00128209; -.
DR REPRODUCTION-2DPAGE; Q9R0Y5; -.
DR CPTAC; non-CPTAC-4043; -.
DR EPD; Q9R0Y5; -.
DR jPOST; Q9R0Y5; -.
DR MaxQB; Q9R0Y5; -.
DR PaxDb; Q9R0Y5; -.
DR PeptideAtlas; Q9R0Y5; -.
DR PRIDE; Q9R0Y5; -.
DR ProteomicsDB; 269148; -. [Q9R0Y5-1]
DR ProteomicsDB; 269149; -. [Q9R0Y5-2]
DR TopDownProteomics; Q9R0Y5-1; -. [Q9R0Y5-1]
DR Antibodypedia; 1017; 643 antibodies from 36 providers.
DR DNASU; 11636; -.
DR Ensembl; ENSMUST00000068271; ENSMUSP00000068479; ENSMUSG00000026817. [Q9R0Y5-2]
DR Ensembl; ENSMUST00000113277; ENSMUSP00000108902; ENSMUSG00000026817. [Q9R0Y5-1]
DR Ensembl; ENSMUST00000113278; ENSMUSP00000108903; ENSMUSG00000026817. [Q9R0Y5-1]
DR GeneID; 11636; -.
DR KEGG; mmu:11636; -.
DR UCSC; uc008jgh.2; mouse. [Q9R0Y5-1]
DR UCSC; uc008jgj.2; mouse. [Q9R0Y5-2]
DR CTD; 203; -.
DR MGI; MGI:87977; Ak1.
DR VEuPathDB; HostDB:ENSMUSG00000026817; -.
DR eggNOG; KOG3079; Eukaryota.
DR GeneTree; ENSGT00940000158325; -.
DR HOGENOM; CLU_032354_0_3_1; -.
DR InParanoid; Q9R0Y5; -.
DR OMA; TQCDRMI; -.
DR OrthoDB; 1378291at2759; -.
DR PhylomeDB; Q9R0Y5; -.
DR TreeFam; TF354283; -.
DR BRENDA; 2.7.4.3; 3474.
DR Reactome; R-MMU-499943; Interconversion of nucleotide di- and triphosphates.
DR BioGRID-ORCS; 11636; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Ak1; mouse.
DR PRO; PR:Q9R0Y5; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9R0Y5; protein.
DR Bgee; ENSMUSG00000026817; Expressed in extensor digitorum longus and 234 other tissues.
DR ExpressionAtlas; Q9R0Y5; baseline and differential.
DR Genevisible; Q9R0Y5; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0001520; C:outer dense fiber; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0030017; C:sarcomere; ISO:MGI.
DR GO; GO:0036126; C:sperm flagellum; IDA:MGI.
DR GO; GO:0004017; F:adenylate kinase activity; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; ISS:UniProtKB.
DR GO; GO:0016776; F:phosphotransferase activity, phosphate group as acceptor; 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:0046034; P:ATP metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046103; P:inosine biosynthetic process; ISO:MGI.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; ISS:UniProtKB.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0010828; P:positive regulation of glucose transmembrane transport; 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_03171; Adenylate_kinase_AK1; 1.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR028582; AK1.
DR InterPro; IPR006267; AK1/5.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01360; aden_kin_iso1; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..194
FT /note="Adenylate kinase isoenzyme 1"
FT /id="PRO_0000158911"
FT REGION 38..67
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT REGION 131..141
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 18..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 39
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 44
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 65..67
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 94..97
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 101
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 138
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 149
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P00568, ECO:0000255|HAMAP-
FT Rule:MF_03171"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..2
FT /note="ME -> MGCCVSSEPQEEGGRKTG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10557075,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_024843"
SQ SEQUENCE 194 AA; 21540 MW; 88E7862522967D14 CRC64;
MEEKLKKAKI IFVVGGPGSG KGTQCEKIVQ KYGYTHLSTG DLLRAEVSSG SERGKKLSAI
MEKGELVPLD TVLDMLRDAM LAKVDSSNGF LIDGYPREVK QGEEFEQKIG QPTLLLYVDA
GAETMTQRLL KRGETSGRVD DNEETIKKRL ETYYNATEPV ISFYDKRGIV RKVNAEGTVD
TVFSEVCTYL DSLK
