BAF1_CAEEL
ID BAF1_CAEEL Reviewed; 89 AA.
AC Q03565; Q9BMU1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Barrier-to-autointegration factor 1;
GN Name=baf-1; ORFNames=B0464.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Bristol N2;
RA Kohara Y., Shin-i T., Suzuki Y., Sugano S., Potdevin M., Thierry-Mieg Y.,
RA Thierry-Mieg D., Thierry-Mieg J.;
RT "The Caenorhabditis elegans transcriptome project, a complementary view of
RT the genome.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND INTERACTION WITH EMR-1 AND LEM-2.
RX PubMed=12684533; DOI=10.1073/pnas.0730821100;
RA Liu J., Lee K.K., Segura-Totten M., Neufeld E., Wilson K.L., Gruenbaum Y.;
RT "MAN1 and emerin have overlapping function(s) essential for chromosome
RT segregation and cell division in Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4598-4603(2003).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17170708; DOI=10.1038/sj.emboj.7601470;
RA Gorjanacz M., Klerkx E.P., Galy V., Santarella R., Lopez-Iglesias C.,
RA Askjaer P., Mattaj I.W.;
RT "Caenorhabditis elegans BAF-1 and its kinase VRK-1 participate directly in
RT post-mitotic nuclear envelope assembly.";
RL EMBO J. 26:132-143(2007).
RN [6]
RP PHOSPHORYLATION, DEPHOSPHORYLATION, AND INTERACTION WITH LEM-4L.
RX PubMed=22770216; DOI=10.1016/j.cell.2012.04.043;
RA Asencio C., Davidson I.F., Santarella-Mellwig R., Ly-Hartig T.B., Mall M.,
RA Wallenfang M.R., Mattaj I.W., Gorjanacz M.;
RT "Coordination of kinase and phosphatase activities by Lem4 enables nuclear
RT envelope reassembly during mitosis.";
RL Cell 150:122-135(2012).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF GLY-38.
RX PubMed=22383942; DOI=10.1371/journal.pone.0024555;
RA Dittrich C.M., Kratz K., Sendoel A., Gruenbaum Y., Jiricny J.,
RA Hengartner M.O.;
RT "LEM-3 - a LEM domain containing nuclease involved in the DNA damage
RT response in C. elegans.";
RL PLoS ONE 7:E24555-E24555(2012).
CC -!- FUNCTION: DNA-binding protein which plays an essential role in nuclear
CC envelope formation (PubMed:17170708). Required for normal chromosome
CC segregation during mitosis (PubMed:12684533). Associates with the
CC nuclear lamina via its interaction with LEM domain containing proteins
CC emr-1 and lem-2 (PubMed:12684533). In association with lem-3, plays a
CC role in radiation-induced DNA damage repair response (PubMed:22383942).
CC {ECO:0000269|PubMed:12684533, ECO:0000269|PubMed:17170708,
CC ECO:0000269|PubMed:22383942}.
CC -!- SUBUNIT: Interacts with emr-1 and lem-2. Interacts with lem-4l, leading
CC to decreased phosphorylation by VRK1 and promoting dephosphorylation by
CC protein phosphatase 2A (PP2A). {ECO:0000269|PubMed:12684533,
CC ECO:0000269|PubMed:22770216}.
CC -!- INTERACTION:
CC Q03565; Q9XTB5: lem-2; NbExp=2; IntAct=EBI-2535603, EBI-2535391;
CC Q03565; Q19848: vrk-1; NbExp=3; IntAct=EBI-2535603, EBI-2414048;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17170708}.
CC -!- PTM: Phosphorylated by vrk-1. Phosphorylation by vrk-1 in mitosis is
CC essential to achieve correct timing of recruitment of nuclear envelope
CC components during nuclear envelope assembly. Dephosphorylated by
CC protein phosphatase 2A (PP2A) following interaction with lem-4l during
CC mitotic exit, leading to mitotic nuclear envelope reassembly.
CC {ECO:0000269|PubMed:22770216}.
CC -!- DISRUPTION PHENOTYPE: Embryonically lethal. Embryos suffer loss of
CC nuclear structure and of a continuous nuclear membrane. baf-1 is
CC delocalized to the chromatin. At permissive temperature (15 degrees
CC Celsius) about 30% of the embryos die, and the survivors appear normal.
CC {ECO:0000269|PubMed:17170708}.
CC -!- SIMILARITY: Belongs to the BAF family. {ECO:0000305}.
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DR EMBL; Z19152; CAA79543.2; -; Genomic_DNA.
DR EMBL; AF303272; AAG50230.1; -; mRNA.
DR PIR; G88555; G88555.
DR PIR; S28284; S28284.
DR RefSeq; NP_499085.1; NM_066684.5.
DR AlphaFoldDB; Q03565; -.
DR SMR; Q03565; -.
DR BioGRID; 41527; 8.
DR IntAct; Q03565; 4.
DR STRING; 6239.B0464.7; -.
DR iPTMnet; Q03565; -.
DR EPD; Q03565; -.
DR PaxDb; Q03565; -.
DR PeptideAtlas; Q03565; -.
DR EnsemblMetazoa; B0464.7.1; B0464.7.1; WBGene00000235.
DR GeneID; 176330; -.
DR UCSC; B0464.7.1; c. elegans.
DR CTD; 176330; -.
DR WormBase; B0464.7; CE26704; WBGene00000235; baf-1.
DR eggNOG; KOG4233; Eukaryota.
DR GeneTree; ENSGT00390000018613; -.
DR HOGENOM; CLU_167806_0_0_1; -.
DR InParanoid; Q03565; -.
DR OMA; EMFTDWL; -.
DR OrthoDB; 1617480at2759; -.
DR PhylomeDB; Q03565; -.
DR SignaLink; Q03565; -.
DR PRO; PR:Q03565; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000235; Expressed in embryo and 4 other tissues.
DR GO; GO:0000793; C:condensed chromosome; IDA:WormBase.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:WormBase.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:WormBase.
DR GO; GO:0042802; F:identical protein binding; ISS:WormBase.
DR GO; GO:0030261; P:chromosome condensation; IBA:GO_Central.
DR GO; GO:0051276; P:chromosome organization; IMP:WormBase.
DR GO; GO:0007059; P:chromosome segregation; IMP:WormBase.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0010165; P:response to X-ray; IMP:WormBase.
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 DNA damage; DNA repair; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..89
FT /note="Barrier-to-autointegration factor 1"
FT /id="PRO_0000221031"
FT MUTAGEN 38
FT /note="G->D: In t1639; at the permissive temperature of 15
FT degrees Celsius, progeny of X-ray-irradiated adults die at
FT the embryonic stage in a unc-32 mutant background. In
FT addition, progeny of non-irradiated adults dies at the
FT embryonic stage in a lem-3 and unc-32 mutant background."
FT /evidence="ECO:0000269|PubMed:22383942"
SQ SEQUENCE 89 AA; 9954 MW; 9DE71FABDC53245F CRC64;
MSTSVKHREF VGEPMGDKEV TCIAGIGPTY GTKLTDAGFD KAYVLFGQYL LLKKDEDLFI
EWLKETAGVT ANHAKTAFNC LNEWADQFM
