ID   BAF1_CAEBR              Reviewed;          89 AA.
AC   A8XAC6;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Barrier-to-autointegration factor 1 {ECO:0000250|UniProtKB:Q03565};
GN   Name=baf-1 {ECO:0000312|WormBase:CBG10084}; ORFNames=CBG10084;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: DNA-binding protein which plays an essential role in nuclear
CC       envelope formation. Required for normal chromosome segregation during
CC       mitosis. Associates with the nuclear lamina via its interaction with
CC       LEM domain containing proteins emr-1 and lem-2 (By similarity).
CC       {ECO:0000250}.
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) (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q03565}.
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the BAF family. {ECO:0000250|UniProtKB:Q03565}.
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DR   EMBL; HE601459; CAP29594.1; -; Genomic_DNA.
DR   RefSeq; XP_002641745.1; XM_002641699.1.
DR   AlphaFoldDB; A8XAC6; -.
DR   SMR; A8XAC6; -.
DR   STRING; 6238.CBG10084; -.
DR   EnsemblMetazoa; CBG10084.1; CBG10084.1; WBGene00031563.
DR   GeneID; 8583739; -.
DR   KEGG; cbr:CBG_10084; -.
DR   CTD; 8583739; -.
DR   WormBase; CBG10084; CBP16782; WBGene00031563; Cbr-baf-1.
DR   eggNOG; KOG4233; Eukaryota.
DR   HOGENOM; CLU_167806_0_0_1; -.
DR   InParanoid; A8XAC6; -.
DR   OMA; EMFTDWL; -.
DR   OrthoDB; 1617480at2759; -.
DR   Proteomes; UP000008549; Chromosome III.
DR   GO; GO:0000779; C:condensed chromosome, centromeric region; IEA:EnsemblMetazoa.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblMetazoa.
DR   GO; GO:0005635; C:nuclear envelope; IEA:EnsemblMetazoa.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0030261; P:chromosome condensation; IBA:GO_Central.
DR   GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; IEA:EnsemblMetazoa.
DR   GO; GO:0010165; P:response to X-ray; IEA:EnsemblMetazoa.
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   3: Inferred from homology;
KW   DNA-binding; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..89
FT                   /note="Barrier-to-autointegration factor 1"
FT                   /id="PRO_0000405116"
SQ   SEQUENCE   89 AA;  9922 MW;  9B271FAA6C4B0EB0 CRC64;
     MSTSVKHREF VGEPMGDKEV TCIAGIGPTY GTKLTDAGFD KAYVLFGQYL LLKKDEDLFV
     EWLKETAGVT ANHAKSAFNC LNEWAEQFI