Q8K3Y6 · ZCCHV_RAT
- ProteinZinc finger CCCH-type antiviral protein 1
- GeneZc3hav1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids776 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | identical protein binding | |
Molecular Function | metal ion binding | |
Molecular Function | RNA binding | |
Biological Process | cellular response to exogenous dsRNA | |
Biological Process | cellular response to virus | |
Biological Process | defense response to virus | |
Biological Process | innate immune response | |
Biological Process | negative regulation of viral genome replication | |
Biological Process | positive regulation of mRNA catabolic process | |
Biological Process | positive regulation of type I interferon production | |
Biological Process | regulation of defense response to virus by host | |
Biological Process | response to virus |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameZinc finger CCCH-type antiviral protein 1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ8K3Y6
Proteomes
Organism-specific databases
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 88 | Results in a non-functional protein with a dominant negative phenotype. | ||||
Sequence: C → R |
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000211344 | 2-776 | Zinc finger CCCH-type antiviral protein 1 | |||
Sequence: ADPGVCCFITKILCAHGGRMTLEELLGEIRLPEAQLYELLETAGPDRFVLLETGGQAGITRSVVATTRARVCRRKYCQRPCDSLHLCKLNLLGRCHYAQSQRNLCKYSHDVLSEQNFQILKNHELSGLNQEELACLLVQSDPFFLPEICKSYKGEGRKQTCGQPQPCERLHICEHFTRGNCSYLNCLRSHNLMDRKVLTIMREHGLSPDVVQNIQDICNNKHARRNPPGTRAAHPHRRGGAHRDRSKSRDRFLHNSLEFLSPVVSPLGSGPPSPDVTSCKDSLEDVSVDVTQKFKYLGTHDRAQLSPVSSKAAGVQGPSQMRASQEFSEDGNLDDIFSRNRSDSSSSRASAAKVAQRNEAVAMKMGMEVKGKKEAPDIDRVPFLNSYIDGVTMEKASVSGIPGKKFTANDLENLLLLNDTWKNVAKPQDLQTTGRITDSGQDKAFLQNKYGGNPVWASASTHNAPNGSSQIMDETPNVSKSSTSGFAIKPAIAGGKEAVYSGVQSPRSQVLAVPGEATTPVQSNRLPQSPLSSSSHRAAASGSPGKNSTHTSVSPAIESSRMTSDPDEYLLRYILNPLFRMDNHGPKEICQDHLYKGCQQSHCDRSHFHLPYRWQMFVYTTWRDFQDMESIEQAYCDPHVELILIENHQINFQKMTCDSYPIRRLSTPSYEEKPLSAVFATKWIWYWKNEFNEYIQYGNESPGHTSSDINSAYLESFFQSCPRGVLPFQAGSQKYELSFQGMIQTNIASKTQRHVVRRPVFVSSNDVEQKRRGPE | ||||||
Modified residue | 257 | Phosphoserine; by GSK3-beta | ||||
Sequence: S | ||||||
Modified residue | 262 | Phosphoserine; by GSK3-beta | ||||
Sequence: S | ||||||
Modified residue | 266 | Phosphoserine; by GSK3-beta | ||||
Sequence: S | ||||||
Modified residue | 270 | Phosphoserine; by GSK3-beta | ||||
Sequence: S | ||||||
Modified residue | 274 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 278 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 283 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 325 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 351 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 398 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 501 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 544 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 667 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
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.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in the kidney and liver.
Induction
By type I interferon (IFN) and viruses.
Interaction
Subunit
Homodimer or homooligomer. Homooligomerization is essential for its antiviral activity. Interacts with EXOSC5. Interacts with EXOSC3, EXOSC7, DCP2 and DCP1A (By similarity).
Interacts with PARN in an RNA-independent manner (By similarity).
Interacts with XRN1 in an RNA-dependent manner (By similarity).
Interacts (via N-terminal domain) with DHX30 (via N-terminus) in an RNA-independent manner. Interacts (via N-terminal domain) with DDX17 in an RNA-independent manner
Interacts with PARN in an RNA-independent manner (By similarity).
Interacts with XRN1 in an RNA-dependent manner (By similarity).
Interacts (via N-terminal domain) with DHX30 (via N-terminus) in an RNA-independent manner. Interacts (via N-terminal domain) with DDX17 in an RNA-independent manner
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q8K3Y6 | DDX17 Q92841 | 6 | EBI-8860250, EBI-746012 | |
XENO | Q8K3Y6 | EXOSC3 Q9NQT5 | 3 | EBI-8860250, EBI-371866 | |
XENO | Q8K3Y6 | EXOSC5 Q9NQT4 | 6 | EBI-8860250, EBI-371876 | |
BINARY | Q8K3Y6 | Zc3hav1 Q8K3Y6 | 3 | EBI-8860250, EBI-8860250 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, motif, zinc finger, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 2-254 | N-terminal domain | ||||
Sequence: ADPGVCCFITKILCAHGGRMTLEELLGEIRLPEAQLYELLETAGPDRFVLLETGGQAGITRSVVATTRARVCRRKYCQRPCDSLHLCKLNLLGRCHYAQSQRNLCKYSHDVLSEQNFQILKNHELSGLNQEELACLLVQSDPFFLPEICKSYKGEGRKQTCGQPQPCERLHICEHFTRGNCSYLNCLRSHNLMDRKVLTIMREHGLSPDVVQNIQDICNNKHARRNPPGTRAAHPHRRGGAHRDRSKSRDRFL | ||||||
Motif | 69-76 | Nuclear localization signal | ||||
Sequence: RARVCRRK | ||||||
Zinc finger | 73-86 | C3H1-type 1 | ||||
Sequence: CRRKYCQRPCDSLH | ||||||
Zinc finger | 88-110 | C3H1-type 2 | ||||
Sequence: CKLNLLGRCHYAQSQRNLCKYSH | ||||||
Zinc finger | 150-172 | C3H1-type 3 | ||||
Sequence: CKSYKGEGRKQTCGQPQPCERLH | ||||||
Zinc finger | 169-193 | C3H1-type 4 | ||||
Sequence: ERLHICEHFTRGNCSYLNCLRSHNL | ||||||
Region | 221-249 | Disordered | ||||
Sequence: NKHARRNPPGTRAAHPHRRGGAHRDRSKS | ||||||
Region | 224-254 | Binding to EXOSC5 | ||||
Sequence: ARRNPPGTRAAHPHRRGGAHRDRSKSRDRFL | ||||||
Compositional bias | 228-245 | Basic residues | ||||
Sequence: PPGTRAAHPHRRGGAHRD | ||||||
Motif | 284-291 | Nuclear export signal | ||||
Sequence: LEDVSVDV | ||||||
Compositional bias | 308-328 | Polar residues | ||||
Sequence: PVSSKAAGVQGPSQMRASQEF | ||||||
Region | 308-355 | Disordered | ||||
Sequence: PVSSKAAGVQGPSQMRASQEFSEDGNLDDIFSRNRSDSSSSRASAAKV | ||||||
Compositional bias | 339-354 | Polar residues | ||||
Sequence: SRNRSDSSSSRASAAK | ||||||
Motif | 405-406 | Nuclear localization signal | ||||
Sequence: KK | ||||||
Region | 457-483 | Disordered | ||||
Sequence: WASASTHNAPNGSSQIMDETPNVSKSS | ||||||
Region | 512-562 | Disordered | ||||
Sequence: LAVPGEATTPVQSNRLPQSPLSSSSHRAAASGSPGKNSTHTSVSPAIESSR | ||||||
Domain | 671-758 | WWE | ||||
Sequence: YEEKPLSAVFATKWIWYWKNEFNEYIQYGNESPGHTSSDINSAYLESFFQSCPRGVLPFQAGSQKYELSFQGMIQTNIASKTQRHVVR |
Domain
The N-terminal domain is sufficient to bind to viral RNAs and promote their degradation. The second and fourth zinc fingers are involved in binding to specific viral RNAs. Contains a divergent PARP homology ADP-ribosyltransferase domain which lacks the structural requirements for NAD[+] binding. It is therefore inactive.
Sequence similarities
Belongs to the ARTD/PARP family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length776
- Mass (Da)86,771
- Last updated2002-10-01 v1
- ChecksumD13F61A9F8E5B552
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F7F0B1 | F7F0B1_RAT | Zc3hav1 | 981 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 228-245 | Basic residues | ||||
Sequence: PPGTRAAHPHRRGGAHRD | ||||||
Compositional bias | 308-328 | Polar residues | ||||
Sequence: PVSSKAAGVQGPSQMRASQEF | ||||||
Compositional bias | 339-354 | Polar residues | ||||
Sequence: SRNRSDSSSSRASAAK |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF521008 EMBL· GenBank· DDBJ | AAM75358.1 EMBL· GenBank· DDBJ | mRNA |