Q8K3Y6
uniprot
Q8K3Y6
canonical
amino_acid_sequence
MADPGVCCFITKILCAHGGRMTLEELLGEIRLPEAQLYELLETAGPDRFVLLETGGQAGITRSVVATTRARVCRRKYCQRPCDSLHLCKLNLLGRCHYAQSQRNLCKYSHDVLSEQNFQILKNHELSGLNQEELACLLVQSDPFFLPEICKSYKGEGRKQTCGQPQPCERLHICEHFTRGNCSYLNCLRSHNLMDRKVLTIMREHGLSPDVVQNIQDICNNKHARRNPPGTRAAHPHRRGGAHRDRSKSRDRFLHNSLEFLSPVVSPLGSGPPSPDVTSCKDSLEDVSVDVTQKFKYLGTHDRAQLSPVSSKAAGVQGPSQMRASQEFSEDGNLDDIFSRNRSDSSSSRASAAKVAQRNEAVAMKMGMEVKGKKEAPDIDRVPFLNSYIDGVTMEKASVSGIPGKKFTANDLENLLLLNDTWKNVAKPQDLQTTGRITDSGQDKAFLQNKYGGNPVWASASTHNAPNGSSQIMDETPNVSKSSTSGFAIKPAIAGGKEAVYSGVQSPRSQVLAVPGEATTPVQSNRLPQSPLSSSSHRAAASGSPGKNSTHTSVSPAIESSRMTSDPDEYLLRYILNPLFRMDNHGPKEICQDHLYKGCQQSHCDRSHFHLPYRWQMFVYTTWRDFQDMESIEQAYCDPHVELILIENHQINFQKMTCDSYPIRRLSTPSYEEKPLSAVFATKWIWYWKNEFNEYIQYGNESPGHTSSDINSAYLESFFQSCPRGVLPFQAGSQKYELSFQGMIQTNIASKTQRHVVRRPVFVSSNDVEQKRRGPE
uniprot
proteins
function
FUNCTION: Antiviral protein which inhibits the replication of viruses by recruiting the cellular RNA degradation machineries to degrade the viral mRNAs. Binds to a ZAP-responsive element (ZRE) present in the target viral mRNA, recruits cellular poly(A)-specific ribonuclease PARN to remove the poly(A) tail, and the 3'-5' exoribonuclease complex exosome to degrade the RNA body from the 3'-end. It also recruits the decapping complex DCP1-DCP2 through RNA helicase p72 (DDX17) to remove the cap structure of the viral mRNA to initiate its degradation from the 5'-end. Its target viruses belong to families which include retroviridae: human immunodeficiency virus type 1 (HIV-1) and moloney and murine leukemia virus (MoMLV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), togaviridae: sindbis virus (SINV) and Ross river virus (RRV). Specifically targets the multiply spliced but not unspliced or singly spliced HIV-1 mRNAs for degradation. {ECO:0000269|PubMed:12215647, ECO:0000269|PubMed:14557641, ECO:0000269|PubMed:17182693, ECO:0000269|PubMed:17185417, ECO:0000269|PubMed:17928353, ECO:0000269|PubMed:18225958, ECO:0000269|PubMed:21876179}.
uniprot
proteins
mass_dalton
86771
uniprot
proteins
mutagenesis
MUTAGEN 88; /note="C->R: Results in a non-functional protein with a dominant negative phenotype."; /evidence="ECO:0000269|PubMed:20181706
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-274 is essential for sequential phosphorylation of Ser-270, Ser-266, Ser-262 and Ser-257 by GSK3-beta. Phosphorylation by GSK3-beta enhances its antiviral activity. {ECO:0000269|PubMed:22514281}.
uniprot
proteins
protein_family
ARTD/PARP family
uniprot
proteins
pubmed
12215647
uniprot
proteins
pubmed
14557641
uniprot
proteins
pubmed
15358138
uniprot
proteins
pubmed
15542630
uniprot
proteins
pubmed
17182693
uniprot
proteins
pubmed
17185417
uniprot
proteins
pubmed
17928353
uniprot
proteins
pubmed
18225958
uniprot
proteins
pubmed
18334637
uniprot
proteins
pubmed
20181706
uniprot
proteins
pubmed
21204022
uniprot
proteins
pubmed
21876179
uniprot
proteins
pubmed
22407013
uniprot
proteins
pubmed
22514281
uniprot
proteins
pubmed
22673903
uniprot
proteins
sequence_length
776
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15358138, ECO:0000269|PubMed:17928353}. Nucleus {ECO:0000269|PubMed:15358138}. Note=Localizes in the cytoplasm at steady state, but shuttles between nucleus and cytoplasm in a XPO1-dependent manner. {ECO:0000269|PubMed:15358138}.
uniprot
proteins