BAF_RAT
ID BAF_RAT Reviewed; 89 AA.
AC Q9R1T1;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Barrier-to-autointegration factor;
DE AltName: Full=LAP2-binding protein 1;
DE Contains:
DE RecName: Full=Barrier-to-autointegration factor, N-terminally processed;
GN Name=Banf1; Synonyms=Baf, L2bp1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH TMPO.
RC TISSUE=Fetal keratinocyte;
RX PubMed=10393804; DOI=10.1242/jcs.112.15.2485;
RA Furukawa K.;
RT "LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-
RT chromatin interaction.";
RL J. Cell Sci. 112:2485-2492(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 42-53, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
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 (By similarity). Heterodimerizes with BANF2 (By
CC similarity). Interacts with ANKLE2/LEM4, leading to decreased
CC phosphorylation by VRK1 and promoting dephosphorylation by protein
CC phosphatase 2A (PP2A) (By similarity). Binds non-specifically to
CC double-stranded DNA, and is found as a hexamer or dodecamer upon DNA
CC binding (By similarity). Binds to LEM domain-containing nuclear
CC proteins such as LEMD3/MAN1, TMPO/LAP2 and EMD (emerin)
CC (PubMed:10393804). Interacts with ANKLE1 (via LEM domain); the
CC interaction may favor BANF1 dimerization (By similarity). Interacts
CC with CRX and LMNA (lamin-A) (By similarity). Binds linker histone H1.1
CC and core histones H3 (By similarity). Interacts with LEMD2 (via LEM
CC domain) (By similarity). {ECO:0000250|UniProtKB:O75531,
CC ECO:0000269|PubMed:10393804}.
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; AB024333; BAA83101.1; -; mRNA.
DR EMBL; BC084726; AAH84726.1; -; mRNA.
DR RefSeq; NP_446083.1; NM_053631.3.
DR RefSeq; XP_006230692.1; XM_006230630.3.
DR RefSeq; XP_006230693.1; XM_006230631.1.
DR AlphaFoldDB; Q9R1T1; -.
DR SMR; Q9R1T1; -.
DR STRING; 10116.ENSRNOP00000027734; -.
DR iPTMnet; Q9R1T1; -.
DR PhosphoSitePlus; Q9R1T1; -.
DR jPOST; Q9R1T1; -.
DR PaxDb; Q9R1T1; -.
DR PRIDE; Q9R1T1; -.
DR Ensembl; ENSRNOT00000027734; ENSRNOP00000027734; ENSRNOG00000020460.
DR GeneID; 114087; -.
DR KEGG; rno:114087; -.
DR UCSC; RGD:620662; rat.
DR CTD; 8815; -.
DR RGD; 620662; Banf1.
DR eggNOG; KOG4233; Eukaryota.
DR GeneTree; ENSGT00390000018613; -.
DR HOGENOM; CLU_167806_0_0_1; -.
DR InParanoid; Q9R1T1; -.
DR OMA; SKQQGDC; -.
DR OrthoDB; 1617480at2759; -.
DR PhylomeDB; Q9R1T1; -.
DR TreeFam; TF315060; -.
DR PRO; PR:Q9R1T1; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020460; Expressed in skeletal muscle tissue and 20 other tissues.
DR Genevisible; Q9R1T1; RN.
DR GO; GO:0000793; C:condensed chromosome; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0097726; F:LEM domain binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
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:0015074; P:DNA integration; ISO:RGD.
DR GO; GO:0007084; P:mitotic nuclear membrane reassembly; ISS:UniProtKB.
DR GO; GO:0045824; P:negative regulation of innate immune response; ISO:RGD.
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; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Chromosome; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..89
FT /note="Barrier-to-autointegration factor"
FT /id="PRO_0000423193"
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_0000221029"
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; 10045 MW; 9D9930BBDC92F4C7 CRC64;
MTTSQKHRDF VAEPMGEKPV GSLAGIGDAL GKRLEERGFD KAYVVLGQFL VLKKDEDLFR
EWLKDTCGAN AKQSRDCFGC LREWCDAFL
