NDK7_RAT
ID NDK7_RAT Reviewed; 395 AA.
AC Q9QXL7;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
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-R7;
GN Name=Nme7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
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, TISSUE SPECIFICITY, AND MASS
RP SPECTROMETRY.
RC STRAIN=Holtzman; TISSUE=Sperm;
RX PubMed=20966424; DOI=10.2164/jandrol.110.010967;
RA Suryawanshi A.R., Khan S.A., Gajbhiye R.K., Gurav M.Y., Khole V.V.;
RT "Differential proteomics leads to identification of domain specific
RT epididymal sperm proteins.";
RL J. Androl. 32:240-259(2011).
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 -!- TISSUE SPECIFICITY: Expressed in the flagellum of epididymal sperm but
CC not in testicular sperm (at protein level).
CC {ECO:0000269|PubMed:20966424}.
CC -!- MASS SPECTROMETRY: Mass=44511.35; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20966424};
CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
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DR EMBL; AF202049; AAF20907.1; -; mRNA.
DR RefSeq; NP_612541.1; NM_138532.1.
DR AlphaFoldDB; Q9QXL7; -.
DR SMR; Q9QXL7; -.
DR STRING; 10116.ENSRNOP00000055684; -.
DR PaxDb; Q9QXL7; -.
DR PRIDE; Q9QXL7; -.
DR GeneID; 171566; -.
DR KEGG; rno:171566; -.
DR UCSC; RGD:619880; rat.
DR CTD; 29922; -.
DR RGD; 619880; Nme7.
DR eggNOG; KOG0888; Eukaryota.
DR InParanoid; Q9QXL7; -.
DR OrthoDB; 1230088at2759; -.
DR PhylomeDB; Q9QXL7; -.
DR Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
DR PRO; PR:Q9QXL7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005879; C:axonemal microtubule; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0036064; C:ciliary basal body; ISO:RGD.
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; ISO:RGD.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:0060830; P:ciliary receptor clustering involved in smoothened signaling pathway; ISO:RGD.
DR GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR GO; GO:0007368; P:determination of left/right symmetry; ISO:RGD.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; ISO:RGD.
DR GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
DR GO; GO:0042073; P:intraciliary transport; ISO:RGD.
DR GO; GO:0060972; P:left/right pattern formation; ISO:RGD.
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; PF06565; DUF1126; 1.
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_0000137132"
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; 44540 MW; 09EC4A204D92B38A CRC64;
MKAGQQGRSC GLISPYLAPK NQSERFAFIA EWYDPNASLL RRYELLYYPV DGSVEMHDVK
NRRTFLKRTK YEDLRVEDLF IGNKVNVFSR QLVLIDYGDQ YTARQLGSRK EKTLALIKPD
AVSKAGEIIE MINKSGFTIT KLRMMTLSRK EAADFHVDHH SRPFYNELIQ FITSGPVIAM
EILRDDAICE WKRLLGPANS GIARSEAPGS VRALFGTDGI RNAAHGSDTF ESAAREMELF
FPSSGGCGPT NTAKFTNCTC CIIKPHAISE GMLGKILIAI RDACFEISAI QMFNMDRANV
EEFYEVYKGV LSDYNDMVTE LYSGPCVAIE IQQSNPTKTF REFCGPSDPE IARHLRPETL
RANFGKTKVQ NAVHCTDLPE DGLLEVQYFF KILDN
