NDK7_MOUSE
ID NDK7_MOUSE Reviewed; 395 AA.
AC Q9QXL8;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Nucleoside diphosphate kinase 7;
DE Short=NDK 7;
DE Short=NDP kinase 7;
DE EC=2.7.4.6;
DE AltName: Full=nm23-M7;
GN Name=Nme7;
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].
RA Mehus J.G., Johnson J.D., Lambeth D.O.;
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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: 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. Microtubule inner protein (MIP) part of the dynein-
CC decorated doublet microtubules (DMTs) in cilia axoneme, which is
CC required for motile cilia beating (By similarity).
CC {ECO:0000250|UniProtKB:Q5E9Y9}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:Q5E9Y9}.
CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
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DR EMBL; AF202048; AAF20906.1; -; mRNA.
DR CCDS; CCDS15436.2; -.
DR AlphaFoldDB; Q9QXL8; -.
DR SMR; Q9QXL8; -.
DR IntAct; Q9QXL8; 1.
DR MINT; Q9QXL8; -.
DR STRING; 10090.ENSMUSP00000083192; -.
DR iPTMnet; Q9QXL8; -.
DR PhosphoSitePlus; Q9QXL8; -.
DR REPRODUCTION-2DPAGE; Q9QXL8; -.
DR EPD; Q9QXL8; -.
DR MaxQB; Q9QXL8; -.
DR PaxDb; Q9QXL8; -.
DR PRIDE; Q9QXL8; -.
DR ProteomicsDB; 293638; -.
DR MGI; MGI:2449121; Nme7.
DR eggNOG; KOG0888; Eukaryota.
DR InParanoid; Q9QXL8; -.
DR PhylomeDB; Q9QXL8; -.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR ChiTaRS; Nme7; mouse.
DR PRO; PR:Q9QXL8; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9QXL8; protein.
DR GO; GO:0005879; C:axonemal microtubule; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
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; IEA:UniProtKB-EC.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0060830; P:ciliary receptor clustering involved in smoothened signaling pathway; IMP:MGI.
DR GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; IMP:MGI.
DR GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
DR GO; GO:0042073; P:intraciliary transport; IMP:MGI.
DR GO; GO:0060972; P:left/right pattern formation; IMP:MGI.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IEA:InterPro.
DR GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
DR CDD; cd04415; NDPk7A; 1.
DR CDD; cd04412; NDPk7B; 1.
DR Gene3D; 3.30.70.141; -; 2.
DR InterPro; IPR006602; DM10_dom.
DR InterPro; IPR034907; NDK-like_dom.
DR InterPro; IPR036850; NDK-like_dom_sf.
DR InterPro; IPR011410; NDPK7.
DR InterPro; IPR035525; NDPk7A.
DR InterPro; IPR037993; NDPk7B.
DR InterPro; IPR001564; Nucleoside_diP_kinase.
DR Pfam; PF00334; NDK; 2.
DR PIRSF; PIRSF036503; NDK7; 1.
DR PRINTS; PR01243; NUCDPKINASE.
DR SMART; SM00676; DM10; 1.
DR SMART; SM00562; NDK; 2.
DR SUPFAM; SSF54919; SSF54919; 2.
DR PROSITE; PS51336; DM10; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell projection; Cytoplasm; Cytoskeleton; Kinase; Magnesium;
KW Metal-binding; Nucleotide metabolism; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..395
FT /note="Nucleoside diphosphate kinase 7"
FT /id="PRO_0000137131"
FT DOMAIN 22..110
FT /note="DM10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00665"
FT ACT_SITE 225
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 395 AA; 44434 MW; 57FF65826B80DC0A CRC64;
MRACQQGRSS SLVSPYMAPK NQSERFAFIA EWYDPNASLL RRYELLFYPV DGSVEMHDVK
NRRTFLKRTK YEDLRLEDLF IGNKVNVFSR QLVLIDYGDQ YTARQLGSRK EKTLALIKPD
AVSKAGEIIE MINKSGFTIT KLRMMTLTRK EAADFHVDHH SRPFYNELIQ FITSGPVIAM
EILRDDAICE WKRLLGPANS GLSRTDAPGS IRALFGTDGV RNAAHGPDTF ASAAREMELF
FPSSGGCGPA NTAKFTNCTC CIIKPHAISE GMLGKNLIAI RDACFGMSAI QMFNLDRANV
EEFYEVYKGV VSEYNDMVTE LCSGPCVAIE IQQSNPTKTF REFCGPADPE IARHLRPETL
RAIFGKTKVQ NAVHCTDLPE DGLLEVQYFF KILDN
