NDKA_CANLF
ID NDKA_CANLF Reviewed; 152 AA.
AC Q50KA9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Nucleoside diphosphate kinase A;
DE Short=NDK A;
DE Short=NDP kinase A;
DE EC=2.7.4.6;
DE AltName: Full=nm23-C1;
GN Name=NME1; Synonyms=NM23A;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16141675; DOI=10.1292/jvms.67.837;
RA Takahashi M., Une R., Fukushima K., Fujiki M., Misumi K., Miyoshi N.,
RA Endo Y., Ohishi A., Akuzawa M.;
RT "Molecular cloning of canine nm23 cDNAs and their expression in normal and
RT tumor tissues.";
RL J. Vet. Med. Sci. 67:837-841(2005).
CC -!- FUNCTION: Major role in the synthesis of nucleoside triphosphates other
CC than ATP. The ATP gamma phosphate is transferred to the NDP beta
CC phosphate via a ping-pong mechanism, using a phosphorylated active-site
CC intermediate. Possesses nucleoside-diphosphate kinase,
CC serine/threonine-specific protein kinase, geranyl and farnesyl
CC pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease
CC activities. Involved in cell proliferation, differentiation and
CC development, signal transduction, G protein-coupled receptor
CC endocytosis, and gene expression. Required for neural development
CC including neural patterning and cell fate determination. During GZMA-
CC mediated cell death, works in concert with TREX1. NME1 nicks one strand
CC of DNA and TREX1 removes bases from the free 3' end to enhance DNA
CC damage and prevent DNA end reannealing and rapid repair (By
CC similarity). {ECO:0000250}.
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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Autophosphorylation at His-118 increases
CC serine/threonine protein kinase activity of the enzyme. Interaction
CC with the SET complex inhibits exonuclease activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Hexamer of two different chains: A and B (A6, A5B, A4B2, A3B3,
CC A2B4, AB5, B6). Interacts with PRUNE1. Component of the SET complex,
CC composed of at least ANP32A, APEX1, HMGB2, NME1, SET and TREX1. Within
CC this complex, interacts directly with SET. Also interacts with TREX1,
CC but only following translocation to the nucleus.
CC {ECO:0000250|UniProtKB:P15531}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
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DR EMBL; AB207044; BAD97837.1; -; mRNA.
DR RefSeq; NP_001019808.1; NM_001024637.1.
DR RefSeq; XP_005624397.1; XM_005624340.2.
DR RefSeq; XP_005624398.1; XM_005624341.2.
DR AlphaFoldDB; Q50KA9; -.
DR SMR; Q50KA9; -.
DR STRING; 9612.ENSCAFP00000025500; -.
DR PaxDb; Q50KA9; -.
DR PRIDE; Q50KA9; -.
DR Ensembl; ENSCAFT00030025724; ENSCAFP00030022464; ENSCAFG00030013879.
DR Ensembl; ENSCAFT00040048639; ENSCAFP00040042484; ENSCAFG00040025991.
DR Ensembl; ENSCAFT00845027047; ENSCAFP00845021284; ENSCAFG00845015140.
DR GeneID; 480558; -.
DR KEGG; cfa:480558; -.
DR CTD; 4830; -.
DR VEuPathDB; HostDB:ENSCAFG00845015140; -.
DR eggNOG; KOG0888; Eukaryota.
DR GeneTree; ENSGT00940000162213; -.
DR HOGENOM; CLU_060216_6_3_1; -.
DR InParanoid; Q50KA9; -.
DR OMA; KIVAMKM; -.
DR OrthoDB; 1334716at2759; -.
DR TreeFam; TF106373; -.
DR Reactome; R-CFA-499943; Interconversion of nucleotide di- and triphosphates.
DR Proteomes; UP000002254; Chromosome 9.
DR Bgee; ENSCAFG00000023628; Expressed in keratinocyte and 48 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IEA:InterPro.
DR GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.70.141; -; 1.
DR HAMAP; MF_00451; NDP_kinase; 1.
DR InterPro; IPR034907; NDK-like_dom.
DR InterPro; IPR036850; NDK-like_dom_sf.
DR InterPro; IPR001564; Nucleoside_diP_kinase.
DR InterPro; IPR023005; Nucleoside_diP_kinase_AS.
DR Pfam; PF00334; NDK; 1.
DR PRINTS; PR01243; NUCDPKINASE.
DR SMART; SM00562; NDK; 1.
DR SUPFAM; SSF54919; SSF54919; 1.
DR PROSITE; PS00469; NDP_KINASES; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Differentiation; Endocytosis; Isopeptide bond;
KW Kinase; Magnesium; Metal-binding; Neurogenesis; Nucleotide metabolism;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase; Ubl conjugation.
FT CHAIN 1..152
FT /note="Nucleoside diphosphate kinase A"
FT /id="PRO_0000137113"
FT ACT_SITE 118
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15531"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15531"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15531"
FT CROSSLNK 100
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P15531"
SQ SEQUENCE 152 AA; 17180 MW; 669D444D69380FE6 CRC64;
MANSERTFIA IKPDGVQRSL VGEIIKRFEQ KGFRLIAMKL IQASEDLLKE HYIDLKDRPF
FAGLVKYMQS GPVVAMVWEG LNVVKTGRVM LGETNPADSK PGTIRGDFCI QVGRNIIHGS
DSVESAEKEI GLWFQPEELV DYKSCAQNWI YE
