KAD5_MOUSE
ID KAD5_MOUSE Reviewed; 562 AA.
AC Q920P5;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Adenylate kinase isoenzyme 5;
DE Short=AK 5;
DE EC=2.7.4.3;
DE EC=2.7.4.6;
DE AltName: Full=ATP-AMP transphosphorylase 5;
GN Name=Ak5;
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] (ISOFORM 2).
RC TISSUE=Brain;
RA Noma T.;
RT "Adenylate kinase isozyme 5.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
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 [4]
RP INTERACTION WITH YWHAZ.
RX PubMed=16959763; DOI=10.1074/mcp.m600147-mcp200;
RA Angrand P.O., Segura I., Voelkel P., Ghidelli S., Terry R., Brajenovic M.,
RA Vintersten K., Klein R., Superti-Furga G., Drewes G., Kuster B.,
RA Bouwmeester T., Acker-Palmer A.;
RT "Transgenic mouse proteomics identifies new 14-3-3-associated proteins
RT involved in cytoskeletal rearrangements and cell signaling.";
RL Mol. Cell. Proteomics 5:2211-2227(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: Nucleoside monophosphate (NMP) kinase that catalyzes the
CC reversible transfer of the terminal phosphate group between nucleoside
CC triphosphates and monophosphates. Active on AMP and dAMP with ATP as a
CC donor. When GTP is used as phosphate donor, the enzyme phosphorylates
CC AMP, CMP, and to a small extent dCMP. Also displays broad nucleoside
CC diphosphate kinase activity. {ECO:0000250|UniProtKB:Q9Y6K8}.
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:0000250|UniProtKB:Q9Y6K8};
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;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6K8};
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:0000250|UniProtKB:Q9Y6K8};
CC -!- SUBUNIT: Monomer. Interacts with YWHAZ (PubMed:16959763).
CC {ECO:0000250|UniProtKB:P00568, ECO:0000269|PubMed:16959763}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y6K8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q920P5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q920P5-2; Sequence=VSP_037880;
CC -!- TISSUE SPECIFICITY: Brain specific. {ECO:0000250|UniProtKB:Q9Y6K8}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000305}.
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DR EMBL; AB060081; BAB69859.1; -; mRNA.
DR EMBL; AK053807; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC111139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC116720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS38675.1; -. [Q920P5-1]
DR RefSeq; NP_001074746.1; NM_001081277.1. [Q920P5-1]
DR AlphaFoldDB; Q920P5; -.
DR SMR; Q920P5; -.
DR BioGRID; 230921; 6.
DR IntAct; Q920P5; 2.
DR STRING; 10090.ENSMUSP00000042785; -.
DR iPTMnet; Q920P5; -.
DR PhosphoSitePlus; Q920P5; -.
DR MaxQB; Q920P5; -.
DR PaxDb; Q920P5; -.
DR PeptideAtlas; Q920P5; -.
DR PRIDE; Q920P5; -.
DR ProteomicsDB; 269238; -. [Q920P5-1]
DR ProteomicsDB; 269239; -. [Q920P5-2]
DR Antibodypedia; 19726; 378 antibodies from 28 providers.
DR DNASU; 229949; -.
DR Ensembl; ENSMUST00000045262; ENSMUSP00000042785; ENSMUSG00000039058. [Q920P5-1]
DR GeneID; 229949; -.
DR KEGG; mmu:229949; -.
DR UCSC; uc008rtq.1; mouse. [Q920P5-1]
DR CTD; 26289; -.
DR MGI; MGI:2677491; Ak5.
DR VEuPathDB; HostDB:ENSMUSG00000039058; -.
DR eggNOG; KOG3079; Eukaryota.
DR GeneTree; ENSGT00940000155917; -.
DR HOGENOM; CLU_034712_1_0_1; -.
DR InParanoid; Q920P5; -.
DR OMA; TGEQGND; -.
DR OrthoDB; 1378291at2759; -.
DR PhylomeDB; Q920P5; -.
DR TreeFam; TF313747; -.
DR Reactome; R-MMU-499943; Interconversion of nucleotide di- and triphosphates.
DR BioGRID-ORCS; 229949; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Ak5; mouse.
DR PRO; PR:Q920P5; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q920P5; protein.
DR Bgee; ENSMUSG00000039058; Expressed in dentate gyrus of hippocampal formation granule cell and 149 other tissues.
DR ExpressionAtlas; Q920P5; baseline and differential.
DR Genevisible; Q920P5; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; ISS:UniProtKB.
DR GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; ISS:UniProtKB.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; ISS:UniProtKB.
DR CDD; cd01428; ADK; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 2.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR006267; AK1/5.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 3.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR01360; aden_kin_iso1; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..562
FT /note="Adenylate kinase isoenzyme 5"
FT /id="PRO_0000158931"
FT REGION 133..316
FT /note="Adenylate kinase 1"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6K8"
FT REGION 162..193
FT /note="NMP 1"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT REGION 256..266
FT /note="LID 1"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT REGION 377..559
FT /note="Adenylate kinase 2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6K8"
FT REGION 406..435
FT /note="NMP 2"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT REGION 499..509
FT /note="LID 2"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 142..147
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 168
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 191..193
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 219..222
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 226
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 263
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 274
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 386..391
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 407
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 412
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 433..435
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 462..465
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 469
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 500
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 506
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 517
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT BINDING 545
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00568"
FT VAR_SEQ 1..369
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_037880"
FT CONFLICT 249
FT /note="R -> K (in Ref. 2; AK053807)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 562 AA; 63323 MW; D94CEC3D3875D055 CRC64;
MNTNDAKEYL ARRDIPQLFE SLLNGLMCSK PEDPIEYLET CLQKVKELGG CDKVKWDTFV
SQEKKTLPPL NGGQSRRSFL RNVMPENSNF PYRRYDRLPP IHQFSIESDT DLSETAELIE
EYEVFDPTRP RPKIILVIGG PGSGKGTQSL KIAERYGFQY ISVGELLRKK IHSASSNRKW
SLIAKIITNG ELAPQETTIT EIKQKLMQIP DEEGIVIDGF PRDVAQALSF EDQICTPDLV
VFLACANQRL KERLQKRAEQ QGRPDDNLKA TQRRLVNFKQ NAAPLVKYFQ EKGLIVTFDA
DRDEDAVFHD ISVAVDSKLF PNKEAPMDSS DLDPSMMFDA GEIIDTGSDY DNQDDDQLNV
FGEDTEGGFM EDLRKCKIIF LMGGPGSGKG TQCEKLAEKY GFTHLSTGEL LRQELTSESE
RSKLIRDIME RGDLVPSGVV LELLKEAMVA SLGNTKGFLI DGYPREVKQG EEFGRRIGDP
HLVICMDCSA DTMTNRLLQR SQSSQRGEDG AKSIAKRLEA YHRASIPVVT YYERKTQLRK
VNAEGTPEQV FLQLCTAIDS VF
