Nme4
entrez
56520
canonical
uniprot
Q9WV84
canonical
ensembl
ENSMUSG00000024177
resolver
ensp
ENSMUSP00000025007
resolver
ensp
ENSMUSP00000157943
resolver
enst
ENSMUST00000025007
resolver
genesymbol
Nme4
resolver
uniprot_entry
NDKD_MOUSE
resolver
activity_regulation
ACTIVITY REGULATION: Binding to anionic phospholipids, predominantly to cardiolipin inhibits its phosphotransfer activity. {ECO:0000250|UniProtKB:O00746}.
uniprot
proteins
amino_acid_sequence
MGSLFGRVAALRALLCGPRFQCLLVRPSSGGPPWPQERTLVAVKPDGVQRRLVGTVIQRFERRGFKLVGMKMLQAPESILAEHYRDLQRKPFYPALISYMSSGPVVAMVWEGPNVVHISRAMIGHTDSTEAAPGTIRGDFSVHISRNVIHASDSVDGAQREIELWFQSSELLNWADGGHHSSCYPA
uniprot
proteins
ec_number
2.7.4.6
uniprot
proteins
function
FUNCTION: Mitochondria-specific nucleoside diphosphate kinase that catalyzes the transfer of a gamma-phosphoryl group from ATP to a nucleoside diphosphate via a ping-pong mechanism involving a phosphohistidine intermediate, participating in nucleoside triphosphate homeostasis (By similarity). In vitro, purine nucleoside triphosphates are much more effective as donors and acceptors than pyrimidine nucleoside triphosphates, and ribonucleosides derivatives are superior to their deoxyribonucleosides counterparts (By similarity). Associates with cardiolipin-containing mitochondrial inner membrane and locally produces ADP in the mitochondrial intermembrane space, which is directly taken up via the ADP/ATP translocase (ANT) into the matrix to stimulate respiratory ATP regeneration. Also directly provides GTP for mitochondrial GTPases, such as the dynamin-related GTPase OPA1. Additionally, catalyzes the anionic phospholipid transfer, namely cardiolipin, from the mitochondrial inner membrane (IM) to the outer membrane (OM) through the formation of contact sites between IM and OM, in a nucleoside diphosphate kinase-independent manner. The switch between the nucleoside diphosphate kinase and the phospholipid transfer activity may depend on the availability and accessibility of cardiolipin and other anionic phospholipids in the IM outer leaflet and OM inner leaflet (By similarity). {ECO:0000250|UniProtKB:O00746, ECO:0000250|UniProtKB:P87355}.
uniprot
proteins
mass_dalton
20549
uniprot
proteins
protein_family
NDK family
uniprot
proteins
pubmed
12383506
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16476741
uniprot
proteins
pubmed
21183079
uniprot
proteins
sequence_length
186
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000250|UniProtKB:O00746}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00746}. Mitochondrion matrix {ECO:0000250|UniProtKB:O00746}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:O00746}. Note=Predominantly localized in the mitochondrion intermembrane space. Colocalizes with OPA1 in mitochondria. Phospholipid binding mediates mitochondrial inner membrane binding. Fully membrane-bound, when attached simultaneously to inner membrane (IM) and outer membrane (OM) through the formation of contact sites between IM and OM. The additional binding to OM may depend on the availability or accessibility of cardiolipin and/or other anionic phospholipids in the IM outer leaflet and the OM inner leaflet. {ECO:0000250|UniProtKB:O00746}.
uniprot
proteins