KAD6_MOUSE
ID KAD6_MOUSE Reviewed; 172 AA.
AC Q8VCP8;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Adenylate kinase isoenzyme 6 {ECO:0000255|HAMAP-Rule:MF_03173};
DE Short=AK6 {ECO:0000255|HAMAP-Rule:MF_03173};
DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_03173};
DE AltName: Full=Coilin-interacting nuclear ATPase protein {ECO:0000255|HAMAP-Rule:MF_03173};
DE AltName: Full=Dual activity adenylate kinase/ATPase {ECO:0000255|HAMAP-Rule:MF_03173};
DE Short=AK/ATPase {ECO:0000255|HAMAP-Rule:MF_03173};
GN Name=Ak6; Synonyms=Cinap;
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=FVB/N; TISSUE=Mammary tumor;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Broad-specificity nucleoside monophosphate (NMP) kinase that
CC catalyzes the reversible transfer of the terminal phosphate group
CC between nucleoside triphosphates and monophosphates. May have a role in
CC nuclear energy homeostasis. Has also ATPase activity. May be involved
CC in regulation of Cajal body (CB) formation. {ECO:0000255|HAMAP-
CC Rule:MF_03173}.
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_03173};
CC -!- SUBUNIT: Monomer and homodimer. Interacts with COIL (via C-terminus).
CC {ECO:0000255|HAMAP-Rule:MF_03173}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000255|HAMAP-
CC Rule:MF_03173}. Nucleus, Cajal body {ECO:0000255|HAMAP-Rule:MF_03173}.
CC Note=Displays widespread diffuse nucleoplasmic distribution but not
CC detected in nucleoli. Detected in Cajal bodies but not in all cells.
CC {ECO:0000255|HAMAP-Rule:MF_03173}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03173}.
CC -!- CAUTION: AK6 and TAF9 were initially considered as products of the same
CC gene since they share two exons. However, they are translated from
CC different initiation codons and reading frames and encode unrelated
CC proteins. This arrangement is conserved in some mammalian species.
CC {ECO:0000305}.
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DR EMBL; BC019453; AAH19453.1; -; mRNA.
DR CCDS; CCDS26734.1; -.
DR RefSeq; NP_081868.1; NM_027592.3.
DR AlphaFoldDB; Q8VCP8; -.
DR SMR; Q8VCP8; -.
DR STRING; 10090.ENSMUSP00000022135; -.
DR iPTMnet; Q8VCP8; -.
DR PhosphoSitePlus; Q8VCP8; -.
DR EPD; Q8VCP8; -.
DR jPOST; Q8VCP8; -.
DR PaxDb; Q8VCP8; -.
DR PeptideAtlas; Q8VCP8; -.
DR PRIDE; Q8VCP8; -.
DR ProteomicsDB; 269172; -.
DR DNASU; 108143; -.
DR Ensembl; ENSMUST00000022135; ENSMUSP00000022135; ENSMUSG00000078941.
DR GeneID; 102216272; -.
DR KEGG; mmu:102216272; -.
DR UCSC; uc007rrg.3; mouse.
DR CTD; 102157402; -.
DR MGI; MGI:5510732; Ak6.
DR VEuPathDB; HostDB:ENSMUSG00000078941; -.
DR eggNOG; KOG3347; Eukaryota.
DR GeneTree; ENSGT00940000155097; -.
DR HOGENOM; CLU_079096_3_1_1; -.
DR OMA; QCEIFGT; -.
DR PhylomeDB; Q8VCP8; -.
DR TreeFam; TF313388; -.
DR Reactome; R-MMU-499943; Interconversion of nucleotide di- and triphosphates.
DR BioGRID-ORCS; 102216272; 24 hits in 56 CRISPR screens.
DR ChiTaRS; Ak6; mouse.
DR PRO; PR:Q8VCP8; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8VCP8; protein.
DR Bgee; ENSMUSG00000078941; Expressed in ventricular zone and 268 other tissues.
DR ExpressionAtlas; Q8VCP8; baseline and differential.
DR Genevisible; Q8VCP8; MM.
DR GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004017; F:adenylate kinase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00039; Adenylate_kinase_AK6; 1.
DR InterPro; IPR020618; Adenyl_kinase_AK6.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12595; PTHR12595; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW Transferase.
FT CHAIN 1..172
FT /note="Adenylate kinase isoenzyme 6"
FT /id="PRO_0000153897"
FT REGION 33..56
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT REGION 108..118
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 13..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 39
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 148..149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
SQ SEQUENCE 172 AA; 19947 MW; 55F56E3420103514 CRC64;
MKLPNILLTG TPGVGKTTLG KELASRSGLK YVNVGDLARE GQLYDGYDEE YGCPILDEDR
VVDELEHQMQ EGGVIVDYHG CDFFPERWFH IVFVLRTDNG VLYKRLETRG YNEKKLQDNI
QCEIFQVLYE EAIASYKEEI VHQLPSNEPE QLEDNINQIS KWIEQWVKDH NP
