BAF_MOUSE
ID BAF_MOUSE Reviewed; 89 AA.
AC O54962; Q542E6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Barrier-to-autointegration factor {ECO:0000303|PubMed:9465049};
DE AltName: Full=LAP2-binding protein 1 {ECO:0000303|PubMed:10393804};
DE Contains:
DE RecName: Full=Barrier-to-autointegration factor, N-terminally processed;
GN Name=Banf1 {ECO:0000312|MGI:MGI:1346330};
GN Synonyms=Baf {ECO:0000303|PubMed:9465049},
GN L2bp1 {ECO:0000303|PubMed:10393804};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9465049; DOI=10.1073/pnas.95.4.1528;
RA Lee M.S., Craigie R.;
RT "A previously unidentified host protein protects retroviral DNA from
RT autointegration.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:1528-1533(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH TMPO.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Liver, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION.
RX PubMed=32156810; DOI=10.1128/mbio.00136-20;
RA Ma H., Qian W., Bambouskova M., Collins P.L., Porter S.I., Byrum A.K.,
RA Zhang R., Artyomov M., Oltz E.M., Mosammaparast N., Miner J.J.,
RA Diamond M.S.;
RT "Barrier-to-autointegration factor 1 protects against a basal cGAS-STING
RT response.";
RL MBio 11:0-0(2020).
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 (By similarity). Contains two non-specific double-stranded DNA (dsDNA)-
CC binding sites which promote DNA cross-bridging (By similarity). Plays a
CC key role in nuclear membrane reformation at the end of mitosis by
CC driving formation of a single nucleus in a spindle-independent manner
CC (By similarity). Transiently cross-bridges anaphase chromosomes via its
CC ability to bridge distant DNA sites, leading to the formation of a
CC dense chromatin network at the chromosome ensemble surface that limits
CC membranes to the surface (By similarity). Also acts as a negative
CC regulator of innate immune activation by restricting CGAS activity
CC toward self-DNA upon acute loss of nuclear membrane integrity
CC (PubMed:32156810). Outcompetes CGAS for DNA-binding, thereby preventing
CC CGAS activation and subsequent damaging autoinflammatory responses (By
CC similarity). Involved in the recognition of exogenous dsDNA in the
CC cytosol: associates with exogenous dsDNA immediately after its
CC appearance in the cytosol at endosome breakdown and is required to
CC avoid autophagy (By similarity). {ECO:0000250|UniProtKB:O75531,
CC ECO:0000269|PubMed:32156810}.
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; AF037080; AAC40032.1; -; mRNA.
DR EMBL; AB025349; BAA83102.1; -; mRNA.
DR EMBL; AK003025; BAB22518.1; -; mRNA.
DR EMBL; AK004212; BAB23223.1; -; mRNA.
DR EMBL; AK010257; BAB26800.1; -; mRNA.
DR EMBL; AK011079; BAB27383.1; -; mRNA.
DR EMBL; AK011100; BAB27397.1; -; mRNA.
DR EMBL; AK012588; BAB28337.1; -; mRNA.
DR EMBL; AK088896; BAC40639.1; -; mRNA.
DR EMBL; BC003709; AAH03709.1; -; mRNA.
DR CCDS; CCDS29458.1; -.
DR RefSeq; NP_001033320.1; NM_001038231.2.
DR RefSeq; NP_001273537.1; NM_001286608.1.
DR RefSeq; NP_035923.1; NM_011793.3.
DR AlphaFoldDB; O54962; -.
DR SMR; O54962; -.
DR BioGRID; 204742; 17.
DR IntAct; O54962; 3.
DR MINT; O54962; -.
DR STRING; 10090.ENSMUSP00000126202; -.
DR iPTMnet; O54962; -.
DR PhosphoSitePlus; O54962; -.
DR EPD; O54962; -.
DR jPOST; O54962; -.
DR MaxQB; O54962; -.
DR PaxDb; O54962; -.
DR PeptideAtlas; O54962; -.
DR PRIDE; O54962; -.
DR ProteomicsDB; 273534; -.
DR TopDownProteomics; O54962; -.
DR Antibodypedia; 30040; 275 antibodies from 29 providers.
DR DNASU; 23825; -.
DR Ensembl; ENSMUST00000025762; ENSMUSP00000025762; ENSMUSG00000024844.
DR Ensembl; ENSMUST00000170010; ENSMUSP00000126202; ENSMUSG00000024844.
DR Ensembl; ENSMUST00000237167; ENSMUSP00000158117; ENSMUSG00000024844.
DR GeneID; 23825; -.
DR KEGG; mmu:23825; -.
DR UCSC; uc008gcr.2; mouse.
DR CTD; 8815; -.
DR MGI; MGI:1346330; Banf1.
DR VEuPathDB; HostDB:ENSMUSG00000024844; -.
DR eggNOG; KOG4233; Eukaryota.
DR GeneTree; ENSGT00390000018613; -.
DR HOGENOM; CLU_167806_0_0_1; -.
DR InParanoid; O54962; -.
DR OMA; SKQQGDC; -.
DR OrthoDB; 1617480at2759; -.
DR PhylomeDB; O54962; -.
DR TreeFam; TF315060; -.
DR BioGRID-ORCS; 23825; 28 hits in 72 CRISPR screens.
DR ChiTaRS; Banf1; mouse.
DR PRO; PR:O54962; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; O54962; protein.
DR Bgee; ENSMUSG00000024844; Expressed in somite and 260 other tissues.
DR Genevisible; O54962; MM.
DR GO; GO:0000793; C:condensed chromosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0097726; F:LEM domain binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0075713; P:establishment of integrated proviral latency; TAS:MGI.
DR GO; GO:0007084; P:mitotic nuclear membrane reassembly; ISS:UniProtKB.
DR GO; GO:0045824; P:negative regulation of innate immune response; ISO:MGI.
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:MGI.
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; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..89
FT /note="Barrier-to-autointegration factor"
FT /id="PRO_0000423191"
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_0000221027"
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; 10103 MW; 828924AFCB91E0D0 CRC64;
MTTSQKHRDF VAEPMGEKPV GSLAGIGDVL SKRLEERGFD KAYVVLGQFL VLKKDEDLFR
EWLKDTCGAN AKQSRDCFGC LREWCDAFL
