BAF_PONAB
ID BAF_PONAB Reviewed; 89 AA.
AC Q5RBU9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Barrier-to-autointegration factor;
DE Contains:
DE RecName: Full=Barrier-to-autointegration factor, N-terminally processed;
GN Name=BANF1;
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: Non-specific DNA-binding protein that plays key roles in
CC mitotic nuclear reassembly, chromatin organization, DNA damage
CC response, gene expression and intrinsic immunity against foreign DNA.
CC Contains two non-specific double-stranded DNA (dsDNA)-binding sites
CC which promote DNA cross-bridging. Plays a key role in nuclear membrane
CC reformation at the end of mitosis by driving formation of a single
CC nucleus in a spindle-independent manner. Transiently cross-bridges
CC anaphase chromosomes via its ability to bridge distant DNA sites,
CC leading to the formation of a dense chromatin network at the chromosome
CC ensemble surface that limits membranes to the surface. Also acts as a
CC negative regulator of innate immune activation by restricting CGAS
CC activity toward self-DNA upon acute loss of nuclear membrane integrity.
CC Outcompetes CGAS for DNA-binding, thereby preventing CGAS activation
CC and subsequent damaging autoinflammatory responses. Involved in the
CC recognition of exogenous dsDNA in the cytosol: associates with
CC exogenous dsDNA immediately after its appearance in the cytosol at
CC endosome breakdown and is required to avoid autophagy.
CC {ECO:0000250|UniProtKB:O75531}.
CC -!- SUBUNIT: Homodimer. Heterodimerizes with BANF2. Interacts with
CC ANKLE2/LEM4, leading to decreased phosphorylation by VRK1 and promoting
CC dephosphorylation by protein phosphatase 2A (PP2A). Binds non-
CC specifically to double-stranded DNA, and is found as a hexamer or
CC dodecamer upon DNA binding. Binds to LEM domain-containing nuclear
CC proteins such as LEMD3/MAN1, TMPO/LAP2 and EMD (emerin). Interacts with
CC ANKLE1 (via LEM domain); the interaction may favor BANF1 dimerization.
CC Interacts with CRX and LMNA (lamin-A). Binds linker histone H1.1 and
CC core histones H3 (By similarity). Interacts with LEMD2 (via LEM domain)
CC (By similarity). {ECO:0000250|UniProtKB:O75531}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75531}.
CC Chromosome {ECO:0000250|UniProtKB:O75531}. Nucleus envelope
CC {ECO:0000250|UniProtKB:O75531}. Cytoplasm
CC {ECO:0000250|UniProtKB:O75531}. Note=Significantly enriched at the
CC nuclear inner membrane, diffusely throughout the nucleus during
CC interphase and concentrated at the chromosomes during the M-phase. The
CC phosphorylated form (by VRK1) shows a cytoplasmic localization whereas
CC the unphosphorylated form locates almost exclusively in the nucleus.
CC May be included in HIV-1 virions via its interaction with viral GAG
CC polyprotein. {ECO:0000250|UniProtKB:O75531}.
CC -!- DOMAIN: Has a helix-hairpin-helix (HhH) structural motif conserved
CC among proteins that bind non-specifically to DNA.
CC {ECO:0000250|UniProtKB:O75531}.
CC -!- DOMAIN: LEM domain proteins bind centrally on the BAF dimer.
CC {ECO:0000250|UniProtKB:O75531}.
CC -!- PTM: Ser-4 is the major site of phosphorylation as compared to Thr-2
CC and Thr-3. Phosphorylation on Thr-2; Thr-3 and Ser-4 disrupts its
CC ability to bind DNA and reduces its ability to bind LEM domain-
CC containing proteins. Non phosphorylated BAF seems to enhance binding
CC between EMD and LMNA. Dephosphorylated by protein phosphatase 2A (PP2A)
CC following interaction with ANKLE2/LEM4 during mitotic exit, leading to
CC mitotic nuclear envelope reassembly. {ECO:0000250|UniProtKB:O75531}.
CC -!- SIMILARITY: Belongs to the BAF family. {ECO:0000305}.
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DR EMBL; CR858534; CAH90761.1; -; mRNA.
DR RefSeq; NP_001125427.1; NM_001131955.1.
DR RefSeq; XP_009244397.1; XM_009246122.1.
DR RefSeq; XP_009244398.1; XM_009246123.1.
DR RefSeq; XP_009244399.1; XM_009246124.1.
DR AlphaFoldDB; Q5RBU9; -.
DR SMR; Q5RBU9; -.
DR STRING; 9601.ENSPPYP00000003516; -.
DR Ensembl; ENSPPYT00000039646; ENSPPYP00000029343; ENSPPYG00000030918.
DR GeneID; 100172334; -.
DR KEGG; pon:100172334; -.
DR CTD; 8815; -.
DR eggNOG; KOG4233; Eukaryota.
DR GeneTree; ENSGT00390000018613; -.
DR HOGENOM; CLU_167806_0_0_1; -.
DR InParanoid; Q5RBU9; -.
DR OMA; SKQQGDC; -.
DR OrthoDB; 1617480at2759; -.
DR TreeFam; TF315060; -.
DR Proteomes; UP000001595; Chromosome 11.
DR GO; GO:0000793; C:condensed chromosome; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0097726; F:LEM domain binding; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR GO; GO:0006325; P:chromatin organization; ISS:UniProtKB.
DR GO; GO:0007084; P:mitotic nuclear membrane reassembly; ISS:UniProtKB.
DR GO; GO:0045824; P:negative regulation of innate immune response; IEA:Ensembl.
DR GO; GO:0032480; P:negative regulation of type I interferon production; ISS:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IEA:Ensembl.
DR Gene3D; 1.10.150.40; -; 1.
DR InterPro; IPR004122; BAF_prot.
DR InterPro; IPR036617; BAF_sf.
DR PANTHER; PTHR12912; PTHR12912; 1.
DR Pfam; PF02961; BAF; 1.
DR SMART; SM01023; BAF; 1.
DR SUPFAM; SSF47798; SSF47798; 1.
PE 3: Inferred from homology;
KW Acetylation; Chromosome; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..89
FT /note="Barrier-to-autointegration factor"
FT /id="PRO_0000423192"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75531"
FT CHAIN 2..89
FT /note="Barrier-to-autointegration factor, N-terminally
FT processed"
FT /id="PRO_0000221028"
FT DOMAIN 20..35
FT /note="HhH"
FT /evidence="ECO:0000250|UniProtKB:O75531"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O75531"
FT MOD_RES 2
FT /note="N-acetylthreonine; in Barrier-to-autointegration
FT factor, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:O75531"
FT MOD_RES 2
FT /note="Phosphothreonine; by VRK1 and VRK2"
FT /evidence="ECO:0000250|UniProtKB:O75531"
FT MOD_RES 3
FT /note="Phosphothreonine; by VRK1 and VRK2"
FT /evidence="ECO:0000250|UniProtKB:O75531"
FT MOD_RES 4
FT /note="Phosphoserine; by VRK1 and VRK2"
FT /evidence="ECO:0000250|UniProtKB:O75531"
SQ SEQUENCE 89 AA; 10059 MW; 9A2180A2D284F5D0 CRC64;
MTTSQKHRDF VAEPMGEKPV GSLAGIGEVL GKKLEERGFD KAYVVLGQFL VLKKDEDLFR
EWLKDTCGAN AKQSRDCFGC LREWCDAFL
