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Protein

Zinc finger CCCH-type antiviral protein 1

Gene

Zc3hav1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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.7 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri73 – 86C3H1-type 1PROSITE-ProRule annotationAdd BLAST14
Zinc fingeri88 – 110C3H1-type 2PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri150 – 172C3H1-type 3PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri169 – 193C3H1-type 4PROSITE-ProRule annotationAdd BLAST25

GO - Molecular functioni

  • cadherin binding Source: RGD
  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW
  • RNA binding Source: RGD

GO - Biological processi

Keywordsi

Molecular functionRNA-binding
Biological processAntiviral defense, Immunity, Innate immunity
LigandMetal-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
Zinc finger antiviral protein
Short name:
ZAP
Short name:
rZAP
Gene namesi
Name:Zc3hav1
Synonyms:Zap
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi628694 Zc3hav1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi88C → R: Results in a non-functional protein with a dominant negative phenotype. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002113442 – 776Zinc finger CCCH-type antiviral protein 1Add BLAST775

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei257Phosphoserine; by GSK3-beta1 Publication1
Modified residuei262Phosphoserine; by GSK3-beta1 Publication1
Modified residuei266Phosphoserine; by GSK3-betaCombined sources1 Publication1
Modified residuei270Phosphoserine; by GSK3-betaCombined sources1 Publication1
Modified residuei274PhosphoserineCombined sources1 Publication1
Modified residuei278PhosphothreonineBy similarity1
Modified residuei283PhosphoserineBy similarity1
Modified residuei325PhosphoserineCombined sources1
Modified residuei351PhosphoserineBy similarity1
Modified residuei398PhosphoserineBy similarity1
Modified residuei501PhosphotyrosineBy similarity1
Modified residuei544PhosphoserineBy similarity1
Modified residuei667PhosphoserineBy similarity1

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ8K3Y6
PRIDEiQ8K3Y6

PTM databases

iPTMnetiQ8K3Y6
PhosphoSitePlusiQ8K3Y6

Expressioni

Tissue specificityi

Expressed in the kidney and liver.1 Publication

Inductioni

By type I interferon (IFN) and viruses.1 Publication

Interactioni

Subunit structurei

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.By similarity6 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • cadherin binding Source: RGD
  • identical protein binding Source: IntAct

Protein-protein interaction databases

DIPiDIP-29842N
IntActiQ8K3Y6, 7 interactors
STRINGi10116.ENSRNOP00000018782

Structurei

Secondary structure

1776
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 16Combined sources8
Turni17 – 19Combined sources3
Beta strandi20 – 22Combined sources3
Helixi23 – 30Combined sources8
Helixi34 – 44Combined sources11
Turni46 – 48Combined sources3
Beta strandi49 – 53Combined sources5
Beta strandi62 – 66Combined sources5
Helixi89 – 92Combined sources4
Helixi97 – 99Combined sources3
Helixi115 – 123Combined sources9
Helixi131 – 139Combined sources9
Helixi143 – 145Combined sources3
Beta strandi156 – 158Combined sources3
Beta strandi163 – 166Combined sources4
Helixi175 – 178Combined sources4
Helixi196 – 205Combined sources10
Helixi209 – 223Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3U9GX-ray1.80A1-225[»]
ProteinModelPortaliQ8K3Y6
SMRiQ8K3Y6
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini671 – 758WWEPROSITE-ProRule annotationAdd BLAST88

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 254N-terminal domainAdd BLAST253
Regioni224 – 254Binding to EXOSC5Add BLAST31

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi69 – 76Nuclear localization signal1 Publication8
Motifi284 – 291Nuclear export signal8
Motifi405 – 406Nuclear localization signalSequence analysis2

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi343 – 348Poly-Ser6
Compositional biasi415 – 418Poly-Leu4
Compositional biasi533 – 536Poly-Ser4

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri73 – 86C3H1-type 1PROSITE-ProRule annotationAdd BLAST14
Zinc fingeri88 – 110C3H1-type 2PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri150 – 172C3H1-type 3PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri169 – 193C3H1-type 4PROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IEI4 Eukaryota
ENOG410ZFB8 LUCA
HOGENOMiHOG000236279
HOVERGENiHBG050384
InParanoidiQ8K3Y6
PhylomeDBiQ8K3Y6

Family and domain databases

Gene3Di1.10.10.10, 1 hit
3.30.720.50, 1 hit
InterProiView protein in InterPro
IPR036388 WH-like_DNA-bd_sf
IPR004170 WWE-dom
IPR037197 WWE_dom_sf
IPR000571 Znf_CCCH
PfamiView protein in Pfam
PF02825 WWE, 1 hit
SUPFAMiSSF117839 SSF117839, 1 hit
PROSITEiView protein in PROSITE
PS50918 WWE, 1 hit
PS50103 ZF_C3H1, 2 hits

Sequencei

Sequence statusi: Complete.

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

Q8K3Y6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADPGVCCFI TKILCAHGGR MTLEELLGEI RLPEAQLYEL LETAGPDRFV
60 70 80 90 100
LLETGGQAGI TRSVVATTRA RVCRRKYCQR PCDSLHLCKL NLLGRCHYAQ
110 120 130 140 150
SQRNLCKYSH DVLSEQNFQI LKNHELSGLN QEELACLLVQ SDPFFLPEIC
160 170 180 190 200
KSYKGEGRKQ TCGQPQPCER LHICEHFTRG NCSYLNCLRS HNLMDRKVLT
210 220 230 240 250
IMREHGLSPD VVQNIQDICN NKHARRNPPG TRAAHPHRRG GAHRDRSKSR
260 270 280 290 300
DRFLHNSLEF LSPVVSPLGS GPPSPDVTSC KDSLEDVSVD VTQKFKYLGT
310 320 330 340 350
HDRAQLSPVS SKAAGVQGPS QMRASQEFSE DGNLDDIFSR NRSDSSSSRA
360 370 380 390 400
SAAKVAQRNE AVAMKMGMEV KGKKEAPDID RVPFLNSYID GVTMEKASVS
410 420 430 440 450
GIPGKKFTAN DLENLLLLND TWKNVAKPQD LQTTGRITDS GQDKAFLQNK
460 470 480 490 500
YGGNPVWASA STHNAPNGSS QIMDETPNVS KSSTSGFAIK PAIAGGKEAV
510 520 530 540 550
YSGVQSPRSQ VLAVPGEATT PVQSNRLPQS PLSSSSHRAA ASGSPGKNST
560 570 580 590 600
HTSVSPAIES SRMTSDPDEY LLRYILNPLF RMDNHGPKEI CQDHLYKGCQ
610 620 630 640 650
QSHCDRSHFH LPYRWQMFVY TTWRDFQDME SIEQAYCDPH VELILIENHQ
660 670 680 690 700
INFQKMTCDS YPIRRLSTPS YEEKPLSAVF ATKWIWYWKN EFNEYIQYGN
710 720 730 740 750
ESPGHTSSDI NSAYLESFFQ SCPRGVLPFQ AGSQKYELSF QGMIQTNIAS
760 770
KTQRHVVRRP VFVSSNDVEQ KRRGPE
Length:776
Mass (Da):86,771
Last modified:October 1, 2002 - v1
Checksum:iD13F61A9F8E5B552
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF521008 mRNA Translation: AAM75358.1
UniGeneiRn.199480
Rn.42053

Genome annotation databases

UCSCiRGD:628694 rat

Similar proteinsi

Entry informationi

Entry nameiZCCHV_RAT
AccessioniPrimary (citable) accession number: Q8K3Y6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: October 1, 2002
Last modified: March 28, 2018
This is version 96 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health