KAD6_BOVIN
ID KAD6_BOVIN Reviewed; 172 AA.
AC A5PJA1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 {ECO:0000255|HAMAP-Rule:MF_03173};
GN Synonyms=CINAP {ECO:0000255|HAMAP-Rule:MF_03173};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; BC142021; AAI42022.1; -; mRNA.
DR RefSeq; NP_001099078.1; NM_001105608.2.
DR AlphaFoldDB; A5PJA1; -.
DR SMR; A5PJA1; -.
DR STRING; 9913.ENSBTAP00000040135; -.
DR PaxDb; A5PJA1; -.
DR PRIDE; A5PJA1; -.
DR Ensembl; ENSBTAT00000040360; ENSBTAP00000040135; ENSBTAG00000046192.
DR GeneID; 102216273; -.
DR KEGG; bta:102216273; -.
DR CTD; 102157402; -.
DR VEuPathDB; HostDB:ENSBTAG00000046192; -.
DR VGNC; VGNC:25775; AK6.
DR eggNOG; KOG3347; Eukaryota.
DR GeneTree; ENSGT00390000015930; -.
DR HOGENOM; CLU_079096_3_3_1; -.
DR OMA; QCEIFGT; -.
DR OrthoDB; 1488235at2759; -.
DR TreeFam; TF313388; -.
DR Proteomes; UP000009136; Chromosome 20.
DR Bgee; ENSBTAG00000046192; Expressed in semen and 105 other tissues.
DR ExpressionAtlas; A5PJA1; baseline and differential.
DR GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 2: Evidence at transcript 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_0000314780"
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; 19927 MW; 25C41B5B759976D5 CRC64;
MLLPNILLTG TPGVGKTTLG KELASRSGLK YINVGDLARE GQLYDGYDEE YDCPILDEDR
VVDELENQMS EGGVIVDYHG CDFFPERWFH IVFVLKTDNS ILYKRLENRG YNEKKLKDNI
QCEIFQVLHE EALASYKEEI VHQLPSNKPE DLEDNINQIL KWIEHWVKDH SS
