IF16_PONAB
ID IF16_PONAB Reviewed; 785 AA.
AC Q5RD14;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Gamma-interferon-inducible protein 16;
DE Short=Ifi-16;
DE AltName: Full=Interferon-inducible myeloid differentiation transcriptional activator;
GN Name=IFI16;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds double-stranded DNA. Binds preferentially to
CC supercoiled DNA and cruciform DNA structures. Seems to be involved in
CC transcriptional regulation. May function as a transcriptional
CC repressor. Could have a role in the regulation of hematopoietic
CC differentiation through activation of unknown target genes. Controls
CC cellular proliferation by modulating the functions of cell cycle
CC regulatory factors including p53/TP53 and the retinoblastoma protein.
CC May be involved in TP53-mediated transcriptional activation by
CC enhancing TP53 sequence-specific DNA binding and modulating TP53
CC phosphorylation status. Seems to be involved in energy-level-dependent
CC activation of the ATM/ AMPK/TP53 pathway coupled to regulation of
CC autophagy. May be involved in regulation of TP53-mediated cell death
CC also involving BRCA1. May be involved in the senescence of prostate
CC epithelial cells. Involved in innate immune response by recognizing
CC viral dsDNA in the cytosol and probably in the nucleus. After binding
CC to viral DNA in the cytoplasm recruits TMEM173/STING and mediates the
CC induction of IFN-beta. Has anti-inflammatory activity and inhibits the
CC activation of the AIM2 inflammasome, probably via association with
CC AIM2. Proposed to bind viral DNA in the nucleus and to induce the
CC formation of nuclear caspase-1-activating inflammasome formation via
CC association with PYCARD. Inhibits replication of herpesviruses probably
CC by interfering with promoter recruitment of members of the Sp1 family
CC of transcription factors (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms homooligomers. Interacts with TMEM173, AIM2, PYCARD and
CC CASP1. Interacts with BRCA1, TP53, E2F1, RB1 and SP1. Interacts with
CC MTA1 (By similarity). Interacts with MTA1. Interacts with PYDC5 (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q16666}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The HIN-20 domains mediates dsDNA binding via electrostatic
CC interactions. {ECO:0000250}.
CC -!- PTM: Lysine acetylation in the multipartite nuclear localization signal
CC (NLS) regulates the subcellular location. {ECO:0000250}.
CC -!- PTM: Phosphorylated on Ser and Thr. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HIN-200 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH90343.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR858104; CAH90343.1; ALT_INIT; mRNA.
DR RefSeq; NP_001125164.1; NM_001131692.1.
DR AlphaFoldDB; Q5RD14; -.
DR SMR; Q5RD14; -.
DR STRING; 9601.ENSPPYP00000000774; -.
DR GeneID; 100172051; -.
DR KEGG; pon:100172051; -.
DR CTD; 3428; -.
DR eggNOG; ENOG502QTQS; Eukaryota.
DR HOGENOM; CLU_022874_0_0_1; -.
DR InParanoid; Q5RD14; -.
DR OrthoDB; 1304994at2759; -.
DR TreeFam; TF337385; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0002218; P:activation of innate immune response; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0035458; P:cellular response to interferon-beta; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 2.40.50.140; -; 4.
DR InterPro; IPR004020; DAPIN.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR040205; HIN-200.
DR InterPro; IPR004021; HIN200/IF120x.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR12200; PTHR12200; 2.
DR Pfam; PF02760; HIN; 2.
DR Pfam; PF02758; PYRIN; 1.
DR SMART; SM01289; PYRIN; 1.
DR PROSITE; PS50824; DAPIN; 1.
DR PROSITE; PS50834; HIN_200; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Apoptosis; Autophagy; Cytoplasm; DNA-binding;
KW Immunity; Inflammatory response; Innate immunity; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..785
FT /note="Gamma-interferon-inducible protein 16"
FT /id="PRO_0000334523"
FT DOMAIN 5..92
FT /note="Pyrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00061"
FT DOMAIN 193..393
FT /note="HIN-200 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00106"
FT DOMAIN 566..765
FT /note="HIN-200 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00106"
FT REGION 88..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..393
FT /note="Interaction with TP53 C-terminus"
FT /evidence="ECO:0000250"
FT REGION 388..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..766
FT /note="Interaction with TP53 core domain"
FT /evidence="ECO:0000250"
FT MOTIF 96..100
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 128..131
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 134..136
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 140..143
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 106..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16666"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16666"
FT MOD_RES 99
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16666"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16666"
FT MOD_RES 128
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q16666"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16666"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16666"
FT MOD_RES 214
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16666"
FT MOD_RES 444
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16666"
FT MOD_RES 451
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16666"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16666"
FT MOD_RES 598
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16666"
FT MOD_RES 614
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16666"
FT MOD_RES 780
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16666"
FT CROSSLNK 116
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16666"
FT CROSSLNK 128
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q16666"
FT CROSSLNK 683
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16666"
SQ SEQUENCE 785 AA; 88381 MW; C40FAF54C9A455C1 CRC64;
MEKKYKNIVL LKGLEVINDY HFRMVKSLLS NDLKLNLKMR EEYDKIQIAD LMEEKFRGDA
GLGKLIQIFK DIPTLEDLAE TLKKEKLKAK GLAPSRKRKK EVDAASPAPS TSSTVKTEGA
EATPGAQKRK KTTKEKSGPK GSKVSKEQTQ PPCPAGAGMS TAMGRSPSPK TSSSAPPNTS
STENPKTVAK CQATPRRSVL QKGPVIVKVL STTKPFEYET PEMEKKIMFH ATVATQTQFF
HVKVLNTSLK EKFNGKKIII ISDYLEYDSL LEVNEESTVS EAGPNQKFEV PNKIINRAKE
TLKIDILHKQ ASGNIVYGVF TLHKKTVNQK TTIYKIQDDR GKMDVVGTGQ CHNIPCEEGD
KLQLYCFRLR KKNQMSTLIS EMHSFIQIKK KTNPRNNDPK SMKLPQEQSQ LPNPSEAGTT
FPESHLWTPQ MPPTTPSSSF FTKKSEDTIS KMNDFMRMQI LKEESHFPGP FMTSIGPAES
YPHTPQMPPS TPSSSFLTTK SEDTISKMND FMRMQILKEE SHFPRPFMTS IGPAESYPHT
PQMPPSTPSS SFLTTWKPKL QTEPEEVSIE DSAQSDLKEV MVLNATESFV YEPKEQKKMF
HATVATEKEV FRVKVFNIDL KEKFTPKKII AISNYVCRNG FLEVYPFTLV ADVNADPKME
IPKGLIRSAN ITPKINQLCS QTKGSFVNGV FEVHKKNVRG EFTYYEIQDN TGKMEVVVHG
RLTTINCEEG DKLKLTCFEL APKSGNTGEL RSVIHSHIKV IKTRKNKKDI LNPDSSMETS
PDFFF
