BAF_DANRE
ID BAF_DANRE Reviewed; 90 AA.
AC Q6P026;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Barrier-to-autointegration factor;
GN Name=banf1; Synonyms=baf; ORFNames=zgc:77767;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-3; THR-4 AND SER-5,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
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. {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.
CC {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 -!- SIMILARITY: Belongs to the BAF family. {ECO:0000305}.
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DR EMBL; BC065864; AAH65864.1; -; mRNA.
DR RefSeq; NP_991125.1; NM_205562.1.
DR RefSeq; XP_017208240.1; XM_017352751.1.
DR RefSeq; XP_017208241.1; XM_017352752.1.
DR AlphaFoldDB; Q6P026; -.
DR SMR; Q6P026; -.
DR STRING; 7955.ENSDARP00000053793; -.
DR iPTMnet; Q6P026; -.
DR PaxDb; Q6P026; -.
DR Ensembl; ENSDART00000053794; ENSDARP00000053793; ENSDARG00000037009.
DR GeneID; 334717; -.
DR KEGG; dre:334717; -.
DR CTD; 8815; -.
DR ZFIN; ZDB-GENE-030131-6657; banf1.
DR eggNOG; KOG4233; Eukaryota.
DR GeneTree; ENSGT00390000018613; -.
DR HOGENOM; CLU_167806_0_0_1; -.
DR InParanoid; Q6P026; -.
DR OMA; SKQQGDC; -.
DR OrthoDB; 1617480at2759; -.
DR PhylomeDB; Q6P026; -.
DR TreeFam; TF315060; -.
DR PRO; PR:Q6P026; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 21.
DR Bgee; ENSDARG00000037009; Expressed in blastula and 20 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; ISS:UniProtKB.
DR GO; GO:0030261; P:chromosome condensation; IBA:GO_Central.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0007084; P:mitotic nuclear membrane reassembly; ISS:UniProtKB.
DR GO; GO:0032480; P:negative regulation of type I interferon production; ISS:UniProtKB.
DR Gene3D; 1.10.150.40; -; 1.
DR InterPro; IPR004122; BAF_prot.
DR InterPro; IPR036617; BAF_sf.
DR Pfam; PF02961; BAF; 1.
DR SMART; SM01023; BAF; 1.
DR SUPFAM; SSF47798; SSF47798; 1.
PE 1: Evidence at protein level;
KW Chromosome; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..90
FT /note="Barrier-to-autointegration factor"
FT /id="PRO_0000223613"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
SQ SEQUENCE 90 AA; 10228 MW; AA70137964853DE7 CRC64;
MSSTSQKHKD FVAEPMGEKS VMALAGIGEV LGKRLEEKGF DKAYVVLGQF LVLRKDEELF
REWLKDTCGA NTKQQGDCYS CLREWCDSFL
