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Protein

IkB-like protein

Gene

A238L

Organism
African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

IkB-like protein that inhibits the binding of NF-kappa-B to DNA, thereby downregulating proinflammatory cytokine production (PubMed:8970976). Forms a heterodimer with the NF-kappa-B subunit RELA/p65 and prevents the activation of the NF-kappa-B transcription factor (By similarity). Inhibits calcineurin function, which is required for the induction of nuclear factor of activated T cells (NFAT)-dependent immune response genes (PubMed:23468591, PubMed:9677199). Prevents the binding of substrates to calcineurin without affecting the phosphatase activity (PubMed:23468591). Does not contain the serine residues that are phosphorylated by host IkB kinase and thus is not degraded following stimulation of the NFkB pathway (By similarity).By similarity3 Publications

GO - Biological processi

Keywordsi

Biological processHost-virus interaction, Inhibition of host NF-kappa-B by virus

Names & Taxonomyi

Protein namesi
Recommended name:
IkB-like protein
Alternative name(s):
Ankyrin repeat domain-containing protein A238L
p28
Gene namesi
Name:A238L
Ordered Locus Names:Mal-047
ORF Names:5EL
OrganismiAfrican swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV)
Taxonomic identifieri10500 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageAsfarviridaeAsfivirus
Virus hostiOrnithodoros (relapsing fever ticks) [TaxID: 6937]
Phacochoerus aethiopicus (Warthog) [TaxID: 85517]
Phacochoerus africanus (Warthog) [TaxID: 41426]
Potamochoerus larvatus (Bushpig) [TaxID: 273792]
Sus scrofa (Pig) [TaxID: 9823]
Proteomesi
  • UP000000860 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Host cytoplasm, Host nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1 – 199Missing : No defect in the competitive inhibition of PPP3CA-mediated dephosphorylation of a peptide substrate. Reduced interaction with PPP3CA while maintaining the competitive inhibition of PPP3CA-mediated dephosphorylation of a peptide substrate; when associated with 206-A--A-211. Reduced interaction with PPP3CA and severe loss of competitive inhibition of PPP3CA-mediated dephosphorylation of a peptide substrate; when associated with 228-A--A-232. 1 PublicationAdd BLAST199
Mutagenesisi206 – 211PKIIIT → AKAIAA: Partial loss of NFAT-mediated transcription inhibition. Reduced interaction with PPP3CA while maintaining the competitive inhibition of PPP3CA-mediated dephosphorylation of a peptide substrate; when associated with 1-M--H-199 DEL. 1 Publication6
Mutagenesisi228 – 232FLCVK → AACAA: Partial loss of NFAT-mediated transcription inhibition. Reduced interaction with PPP3CA and severe loss of competitive inhibition of PPP3CA-mediated dephosphorylation of a peptide substrate; when associated with 1-M--H-199 DEL. 1 Publication5

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003728381 – 239IkB-like proteinAdd BLAST239

Post-translational modificationi

The protein exists in a 28 kDa and a 32 kDa form, probably due to post-translational modifications which are neither phosphorylation, nor sumoylation.By similarity

Keywords - PTMi

Ubl conjugation

Interactioni

Subunit structurei

Interacts with host PPIA (PubMed:9677199). Interacts with host PPP3CA/Calcineurin (PubMed:9677199, PubMed:11000210, PubMed:23468591). Interacts with host RELA/p65; interaction of the 32 kDa form with host RELA results in the formation of a stable complex with NF-kappa-B (By similarity). Interacts with host PPP3R1 (PubMed:23468591). Interacts with host EP300; this interaction inhibits the association of host EP300 with host RELA, JUN and NFATC2 (By similarity).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PPP3CAQ08209-12EBI-16039701,EBI-15637215From a different organism.

Protein-protein interaction databases

DIPiDIP-60108N
ELMiO36972
IntActiO36972, 2 interactors

Structurei

Secondary structure

1239
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliO36972
SMRiO36972
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati48 – 77ANK 1Add BLAST30
Repeati87 – 116ANK 2Add BLAST30
Repeati124 – 153ANK 3Add BLAST30
Repeati158 – 187ANK 4Add BLAST30

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi81 – 87Nuclear localization signalBy similarity7
Motifi203 – 214Nuclear localization signalBy similarityAdd BLAST12
Motifi206 – 213PxIxITxC motif; Interaction with host PPP3CA2 Publications8
Motifi228 – 231FLCV motif1 Publication4

Domaini

The C-terminal region contains the docking motifs PxIxITxC and FLCV, which are required and sufficient for binding to host calcineurin.1 Publication

Sequence similaritiesi

Belongs to the asfivirus A238L family.Curated

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

OrthoDBiVOG090000K6

Family and domain databases

CDDicd00204 ANK, 1 hit
Gene3Di1.25.40.20, 1 hit
InterProiView protein in InterPro
IPR002110 Ankyrin_rpt
IPR020683 Ankyrin_rpt-contain_dom
IPR036770 Ankyrin_rpt-contain_sf
PfamiView protein in Pfam
PF00023 Ank, 1 hit
SMARTiView protein in SMART
SM00248 ANK, 4 hits
SUPFAMiSSF48403 SSF48403, 1 hit
PROSITEiView protein in PROSITE
PS50297 ANK_REP_REGION, 1 hit
PS50088 ANK_REPEAT, 1 hit

Sequencei

Sequence statusi: Complete.

O36972-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDTIGLFSVE AEHLFVEWVK KCIKKGDLTL FETLFNADPW IVNRCNKNKI
60 70 80 90 100
TVFMLICIYG RLDFLRFLFK QESYPGEIVN HYRRDKDGNS AWHYLAEKNN
110 120 130 140 150
HLLLEEVLDY FGKNGIRVCF PNFNGVTPIM KAAMRGRTLS VLSLLKYGAN
160 170 180 190 200
PNRKDYLKGF TTWDWAVFTG HADLVKTLNK GYQKPLFMHF PLYKLDVFHR
210 220 230
RFKKKPKIII TGCEDNVYEK LPEQNSNFLC VKKLNKYGK
Length:239
Mass (Da):28,080
Last modified:January 1, 1998 - v1
Checksum:iC6FA085308BF2CBD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF014479 Genomic DNA Translation: AAB71361.1
AY261361 Genomic DNA No translation available.

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF014479 Genomic DNA Translation: AAB71361.1
AY261361 Genomic DNA No translation available.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4F0ZX-ray1.70C200-239[»]
ProteinModelPortaliO36972
SMRiO36972
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60108N
ELMiO36972
IntActiO36972, 2 interactors

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

OrthoDBiVOG090000K6

Family and domain databases

CDDicd00204 ANK, 1 hit
Gene3Di1.25.40.20, 1 hit
InterProiView protein in InterPro
IPR002110 Ankyrin_rpt
IPR020683 Ankyrin_rpt-contain_dom
IPR036770 Ankyrin_rpt-contain_sf
PfamiView protein in Pfam
PF00023 Ank, 1 hit
SMARTiView protein in SMART
SM00248 ANK, 4 hits
SUPFAMiSSF48403 SSF48403, 1 hit
PROSITEiView protein in PROSITE
PS50297 ANK_REP_REGION, 1 hit
PS50088 ANK_REPEAT, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiIKBL_ASFM2
AccessioniPrimary (citable) accession number: O36972
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: January 1, 1998
Last modified: September 12, 2018
This is version 72 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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