KAD8_MOUSE
ID KAD8_MOUSE Reviewed; 479 AA.
AC Q32M07; Q497L2;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Adenylate kinase 8;
DE Short=AK 8;
DE EC=2.7.4.3;
DE EC=2.7.4.6;
DE AltName: Full=ATP-AMP transphosphorylase 8;
GN Name=Ak8;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: Nucleoside monophosphate (NMP) kinase that catalyzes the
CC reversible transfer of the terminal phosphate group between nucleoside
CC triphosphates and monophosphates. Has highest activity toward AMP, and
CC weaker activity toward dAMP, CMP and dCMP. Also displays broad
CC nucleoside diphosphate kinase activity. {ECO:0000250|UniProtKB:Q96MA6}.
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:Q96MA6};
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:Q96MA6};
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:Q96MA6};
CC -!- SUBUNIT: Interacts with CFAP45 and CFAP52; CFAP45 and AK8 dimerization
CC may create a cavity at the interface of the dimer that can accommodate
CC AMP. {ECO:0000250|UniProtKB:Q96MA6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q96MA6}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:Q96MA6}. Note=Located in the proximal region of
CC respiratory cilia. {ECO:0000250|UniProtKB:Q96MA6}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000305}.
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DR EMBL; AL731851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL732526; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC100481; AAI00482.1; -; mRNA.
DR EMBL; BC109352; AAI09353.1; -; mRNA.
DR CCDS; CCDS15846.1; -.
DR RefSeq; NP_001029046.2; NM_001033874.2.
DR AlphaFoldDB; Q32M07; -.
DR SMR; Q32M07; -.
DR BioGRID; 213092; 1.
DR STRING; 10090.ENSMUSP00000073789; -.
DR PhosphoSitePlus; Q32M07; -.
DR MaxQB; Q32M07; -.
DR PaxDb; Q32M07; -.
DR PRIDE; Q32M07; -.
DR ProteomicsDB; 301712; -.
DR Antibodypedia; 18213; 114 antibodies from 27 providers.
DR DNASU; 68870; -.
DR Ensembl; ENSMUST00000074156; ENSMUSP00000073789; ENSMUSG00000026807.
DR GeneID; 68870; -.
DR KEGG; mmu:68870; -.
DR UCSC; uc008izd.1; mouse.
DR CTD; 158067; -.
DR MGI; MGI:1916120; Ak8.
DR VEuPathDB; HostDB:ENSMUSG00000026807; -.
DR eggNOG; KOG3078; Eukaryota.
DR eggNOG; KOG3079; Eukaryota.
DR GeneTree; ENSGT00940000161613; -.
DR HOGENOM; CLU_044905_0_0_1; -.
DR InParanoid; Q32M07; -.
DR OMA; DCIRRGW; -.
DR OrthoDB; 961384at2759; -.
DR PhylomeDB; Q32M07; -.
DR TreeFam; TF328560; -.
DR Reactome; R-MMU-499943; Interconversion of nucleotide di- and triphosphates.
DR BioGRID-ORCS; 68870; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Ak8; mouse.
DR PRO; PR:Q32M07; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q32M07; protein.
DR Bgee; ENSMUSG00000026807; Expressed in seminiferous tubule of testis and 78 other tissues.
DR Genevisible; Q32M07; MM.
DR GO; GO:0097729; C:9+2 motile cilium; ISO:MGI.
DR GO; GO:0005930; C:axoneme; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0036126; C:sperm flagellum; IDA:MGI.
DR GO; GO:0004017; F:adenylate kinase activity; ISS:UniProtKB.
DR GO; GO:0016208; F:AMP binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004127; F:cytidylate kinase activity; ISS:UniProtKB.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; ISS:UniProtKB.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; ISS:UniProtKB.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0021591; P:ventricular system development; IMP:MGI.
DR CDD; cd01428; ADK; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR036193; ADK_active_lid_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 2.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF57774; SSF57774; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell projection; Cytoplasm; Cytoskeleton; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..479
FT /note="Adenylate kinase 8"
FT /id="PRO_0000279385"
FT REGION 58..258
FT /note="Adenylate kinase 1"
FT /evidence="ECO:0000250|UniProtKB:Q96MA6"
FT REGION 87..113
FT /note="NMP 1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 177..206
FT /note="LID 1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 269..471
FT /note="Adenylate kinase 2"
FT /evidence="ECO:0000250|UniProtKB:Q96MA6"
FT REGION 298..327
FT /note="NMP 2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 391..424
FT /note="LID 2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 67..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 140..143
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 147
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 203
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 278..283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 325..327
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 354..357
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 361
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 392
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT CONFLICT 468
FT /note="S -> G (in Ref. 2; AAI00482)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 479 AA; 55073 MW; 4475836B92D069E1 CRC64;
MDATTAPHRI PPEMPQYGED YYIFEMMQNM LEQLLIHQPE DPISFMITHL RRNNDNVPKV
VILGPPASGK TTIAMWLCKH LNSNLITKES LLEREFSRLS VEAKSYYQVY KKIPNSILVS
LVQERLNEDD CLRKGWILDG IPERREQALM IQTLGLAPKH VIVLNAPDTV LIERNVGKRI
DPVTGEIYHT TFDWPPEPEI QNRLRQPEGI SEIETAKKLL EYHRHIIRIL PSYPKILKTI
SSDQPCVDVF YQALTYVQSG HRCNAPFTPK VLLCGPLGSG KRLQATLLAQ KYGLVNISCG
QLLKEAVAAK SSFGELIQPF FEKRMTVPDS IITKVLADRM EQQDCIQKGW VLHGFPRDLD
QARMLNSMGY NPNRVFFLSV PLDSILERLT LRRTDPVTGE RFHLMYKPPP TIEVQVRLLQ
NPKDSEEYIK LQTDLFYRNS GDLEQYYDRA IIVNGDQDPY TVFEYIESGI INPLPRKVT
