Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Zinc finger CCCH-type antiviral protein 1

Gene

Zc3hav1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Isoform 1 is a more potent viral inhibitor than isoform 2. Isoform 2 acts as a positive regulator of DDX58/RIG-I signaling resulting in activation of the downstream effector IRF3 leading to the expression of type I IFNs and IFN stimulated genes (ISGs).1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri73 – 8614C3H1-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri87 – 11327C3H1-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri150 – 17223C3H1-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri173 – 19422C3H1-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger CCCH-type antiviral protein 1
Alternative name(s):
ADP-ribosyltransferase diphtheria toxin-like 13
Short name:
ARTD13
Gene namesi
Name:Zc3hav1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1926031. Zc3hav1.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: Localizes in the cytoplasm at steady state, but shuttles between nucleus and cytoplasm in a XPO1-dependent manner.By similarity

GO - Cellular componenti

  • cytoplasm Source: MGI
  • Golgi apparatus Source: MGI
  • late endosome Source: MGI
  • lysosome Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 946945Zinc finger CCCH-type antiviral protein 1PRO_0000331461Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei257 – 2571PhosphoserineCombined sources
Modified residuei262 – 2621Phosphoserine; by GSK3-betaBy similarity
Modified residuei265 – 2651PhosphoserineCombined sources
Modified residuei269 – 2691PhosphoserineCombined sources
Modified residuei273 – 2731PhosphoserineCombined sources
Modified residuei277 – 2771PhosphothreonineCombined sources
Modified residuei324 – 3241PhosphoserineCombined sources
Modified residuei350 – 3501PhosphoserineCombined sources
Modified residuei425 – 4251PhosphoserineBy similarity
Modified residuei508 – 5081PhosphotyrosineCombined sources
Modified residuei553 – 5531PhosphoserineCombined sources
Modified residuei583 – 5831PhosphoserineBy similarity
Modified residuei680 – 6801PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation at Ser-273 is essential for sequential phosphorylation of Ser-269, Ser-265, Ser-262 and Ser-257 by GSK3-beta. Phosphorylation by GSK3-beta enhances its antiviral activity (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ3UPF5.
MaxQBiQ3UPF5.
PaxDbiQ3UPF5.
PeptideAtlasiQ3UPF5.
PRIDEiQ3UPF5.

PTM databases

iPTMnetiQ3UPF5.
PhosphoSiteiQ3UPF5.

Expressioni

Gene expression databases

BgeeiENSMUSG00000029826.
ExpressionAtlasiQ3UPF5. baseline and differential.
GenevisibleiQ3UPF5. MM.

Interactioni

Subunit structurei

Homodimer or homooligomer. Homooligomerization is essential for its antiviral activity (By similarity). Interacts with EXOSC5 (By similarity). Interacts (via N-terminal domain) with DDX17 in an RNA-independent manner (By similarity). 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 (By similarity). Isoform 2 interacts (via zinc-fingers) with DDX58/RIG-I in an RNA-dependent manner (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi219626. 1 interaction.
IntActiQ3UPF5. 1 interaction.
MINTiMINT-4125302.
STRINGi10090.ENSMUSP00000031850.

Structurei

3D structure databases

ProteinModelPortaliQ3UPF5.
SMRiQ3UPF5. Positions 3-225, 817-922.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini684 – 77188WWEPROSITE-ProRule annotationAdd
BLAST
Domaini805 – 946142PARP catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 254253N-terminal domainAdd
BLAST
Regioni224 – 25431Binding to EXOSC5By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi69 – 768Nuclear localization signalBy similarity
Motifi283 – 2908Nuclear export signalBy similarity
Motifi412 – 4132Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi572 – 5765Poly-Met

Domaini

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 (By similarity).By similarity

Sequence similaritiesi

Contains 2 C3H1-type zinc fingers.PROSITE-ProRule annotation
Contains 1 PARP catalytic domain.PROSITE-ProRule annotation
Contains 1 WWE domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri73 – 8614C3H1-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri87 – 11327C3H1-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri150 – 17223C3H1-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri173 – 19422C3H1-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410KE5N. Eukaryota.
ENOG410YD9T. LUCA.
GeneTreeiENSGT00760000119084.
HOGENOMiHOG000236279.
HOVERGENiHBG050384.
InParanoidiQ3UPF5.
KOiK15259.
PhylomeDBiQ3UPF5.
TreeFamiTF338389.

Family and domain databases

Gene3Di3.90.228.10. 1 hit.
InterProiIPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004170. WWE-dom.
IPR000571. Znf_CCCH.
[Graphical view]
PfamiPF00644. PARP. 1 hit.
PF02825. WWE. 1 hit.
[Graphical view]
PROSITEiPS51059. PARP_CATALYTIC. 1 hit.
PS50918. WWE. 1 hit.
PS50103. ZF_C3H1. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q3UPF5-1) [UniParc]FASTAAdd to basket
Also known as: ZAPL

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTDPEVFCFI TKILCAHGGR MTLEELLGEI SLPEAQLYEL LKAAGPDRFV
60 70 80 90 100
LLETGDQAGI TRSVVATTRA RVCRRKYCQR PCDSLHLCKL NLLGRCHYAQ
110 120 130 140 150
SQRNLCKYSH DVLSEQNFQV LKNHELSGLN QEELAVLLVQ SDPFFMPEIC
160 170 180 190 200
KSYKGEGRKQ ICGQPQPCER LHICEHFTRG NCSYLNCLRS HNLMDRKVLA
210 220 230 240 250
IMREHGLSSD VVQNIQDICN NKHTRRNPPS MRAPHPHRRG GAHRDRSKSR
260 270 280 290 300
DRFHHNSLEV LSTVSPLGSG PPSPDVTGCK DPLEDVSADV TQKFKYLGTQ
310 320 330 340 350
DRAQLSSVSS KAAGVRGPSQ MRASQEFLED GDPDGLFSRN RSDSSTSRTS
360 370 380 390 400
AAGFPLVAAQ RNEAGAMKMG MPSGHHVEVK GKNEDIDRVP FLNSYIDGVT
410 420 430 440 450
MEEATVSGIL GKRATDNGLE EMILSSNHQK SVAKTQDPQT AGRITDSGQD
460 470 480 490 500
TAFLHSKYEE NPAWPGTSTH NGPNGFSQIM DETPNVSKSS PTGFGIKSAV
510 520 530 540 550
TGGKEAVYSG VQSLRSHVLA MPGETTTPVQ GSNRLPPSPL SSSTSHRVAA
560 570 580 590 600
SGSPGKSSTH ASVSPASEPS RMMMMMSDPA EYSLCYIVNP VSPRMDDHGL
610 620 630 640 650
KEICLDHLYR GCQQVNCNKN HFHLPYRWQL FILPTWMDFQ DMEYIERAYC
660 670 680 690 700
DPQIEIIVIE KHRINFKKMT CDSYPIRRLS TPSFVEKTLN SVFTTKWLWY
710 720 730 740 750
WRNELNEYTQ YGHESPSHTS SEINSAYLES FFHSCPRGVL QFHAGSQNYE
760 770 780 790 800
LSFQGMIQTN IASKTQRHVV RRPVFVSSKD VEQKRRGPDH QPVMPQADAL
810 820 830 840 850
TLFSSPQRNA STVSSNEYEF IELNNQDEEY AKISEQFKAS MKQFKIVTIK
860 870 880 890 900
RIWNQKLWDT FERKKQKMKN KTEMFLFHAV GRIHMDYICK NNFEWILHGN
910 920 930 940
REIRYGKGLC WRRENCDSSH AHGFLEMPLA SLGRTASLDS SGLQRK
Length:946
Mass (Da):106,688
Last modified:October 11, 2005 - v1
Checksum:iBE2EFE5FBC6062EA
GO
Isoform 2 (identifier: Q3UPF5-2) [UniParc]FASTAAdd to basket
Also known as: ZAPS

The sequence of this isoform differs from the canonical sequence as follows:
     789-789: D → E
     790-946: Missing.

Show »
Length:789
Mass (Da):88,231
Checksum:i98C5633AE78BD4A5
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei789 – 7891D → E in isoform 2. 1 PublicationVSP_033213
Alternative sequencei790 – 946157Missing in isoform 2. 1 PublicationVSP_033214Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004770 mRNA. Translation: BAB23549.1.
AK080334 mRNA. Translation: BAC37881.1.
AK143568 mRNA. Translation: BAE25440.1.
AK169402 mRNA. Translation: BAE41148.1.
AK172379 mRNA. Translation: BAE42974.1.
AK020263 mRNA. Translation: BAB32047.2.
CCDSiCCDS20012.1. [Q3UPF5-2]
CCDS80522.1. [Q3UPF5-1]
RefSeqiNP_082697.1. NM_028421.1. [Q3UPF5-1]
NP_083140.1. NM_028864.2. [Q3UPF5-2]
UniGeneiMm.25243.
Mm.486484.

Genome annotation databases

EnsembliENSMUST00000031850; ENSMUSP00000031850; ENSMUSG00000029826. [Q3UPF5-2]
ENSMUST00000143702; ENSMUSP00000144312; ENSMUSG00000029826. [Q3UPF5-1]
GeneIDi78781.
KEGGimmu:78781.
UCSCiuc009bjz.2. mouse. [Q3UPF5-1]
uc009bka.1. mouse. [Q3UPF5-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004770 mRNA. Translation: BAB23549.1.
AK080334 mRNA. Translation: BAC37881.1.
AK143568 mRNA. Translation: BAE25440.1.
AK169402 mRNA. Translation: BAE41148.1.
AK172379 mRNA. Translation: BAE42974.1.
AK020263 mRNA. Translation: BAB32047.2.
CCDSiCCDS20012.1. [Q3UPF5-2]
CCDS80522.1. [Q3UPF5-1]
RefSeqiNP_082697.1. NM_028421.1. [Q3UPF5-1]
NP_083140.1. NM_028864.2. [Q3UPF5-2]
UniGeneiMm.25243.
Mm.486484.

3D structure databases

ProteinModelPortaliQ3UPF5.
SMRiQ3UPF5. Positions 3-225, 817-922.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi219626. 1 interaction.
IntActiQ3UPF5. 1 interaction.
MINTiMINT-4125302.
STRINGi10090.ENSMUSP00000031850.

PTM databases

iPTMnetiQ3UPF5.
PhosphoSiteiQ3UPF5.

Proteomic databases

EPDiQ3UPF5.
MaxQBiQ3UPF5.
PaxDbiQ3UPF5.
PeptideAtlasiQ3UPF5.
PRIDEiQ3UPF5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031850; ENSMUSP00000031850; ENSMUSG00000029826. [Q3UPF5-2]
ENSMUST00000143702; ENSMUSP00000144312; ENSMUSG00000029826. [Q3UPF5-1]
GeneIDi78781.
KEGGimmu:78781.
UCSCiuc009bjz.2. mouse. [Q3UPF5-1]
uc009bka.1. mouse. [Q3UPF5-2]

Organism-specific databases

CTDi56829.
MGIiMGI:1926031. Zc3hav1.

Phylogenomic databases

eggNOGiENOG410KE5N. Eukaryota.
ENOG410YD9T. LUCA.
GeneTreeiENSGT00760000119084.
HOGENOMiHOG000236279.
HOVERGENiHBG050384.
InParanoidiQ3UPF5.
KOiK15259.
PhylomeDBiQ3UPF5.
TreeFamiTF338389.

Miscellaneous databases

PROiQ3UPF5.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000029826.
ExpressionAtlasiQ3UPF5. baseline and differential.
GenevisibleiQ3UPF5. MM.

Family and domain databases

Gene3Di3.90.228.10. 1 hit.
InterProiIPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004170. WWE-dom.
IPR000571. Znf_CCCH.
[Graphical view]
PfamiPF00644. PARP. 1 hit.
PF02825. WWE. 1 hit.
[Graphical view]
PROSITEiPS51059. PARP_CATALYTIC. 1 hit.
PS50918. WWE. 1 hit.
PS50103. ZF_C3H1. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiZCCHV_MOUSE
AccessioniPrimary (citable) accession number: Q3UPF5
Secondary accession number(s): Q9CTU4, Q9DBS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: October 11, 2005
Last modified: September 7, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.