SPIB_MOUSE
ID SPIB_MOUSE Reviewed; 267 AA.
AC O35906; O35907; O35909; O55199;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Transcription factor Spi-B;
GN Name=Spib;
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 [GENOMIC DNA] (ISOFORMS IA; IC AND IIA), AND
RP ALTERNATIVE PROMOTER USAGE.
RC STRAIN=129/Sv;
RX PubMed=9511763; DOI=10.1016/s0378-1119(97)00629-x;
RA Chen H.-M., Gonzalez D.A., Radomska H.S., Voso M.T., Sun Z., Zhang P.,
RA Zhang D.-E., Tenen D.G.;
RT "Two promoters direct expression of the murine Spi-B gene, an Ets family
RT transcription factor.";
RL Gene 207:209-218(1998).
RN [2]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8691135; DOI=10.1084/jem.184.1.203;
RA Su G.H., Ip H.S., Cobb B.S., Lu M.-M., Chen H.-M., Simon M.C.;
RT "The Ets protein Spi-B is expressed exclusively in B cells and T cells
RT during development.";
RL J. Exp. Med. 184:203-214(1996).
RN [3]
RP FUNCTION.
RX PubMed=9384589; DOI=10.1093/emboj/16.23.7118;
RA Su G.H., Chen H.-M., Muthusamy N., Garrett-Sinha L.A., Baunoch D.,
RA Tenen D.G., Simon M.C.;
RT "Defective B cell receptor-mediated responses in mice lacking the Ets
RT protein, Spi-B.";
RL EMBO J. 16:7118-7129(1997).
RN [4]
RP FUNCTION.
RX PubMed=10229183; DOI=10.1016/s1074-7613(00)80040-0;
RA Garrett-Sinha L.A., Su G.H., Rao S., Kabak S., Hao Z., Clark M.R.,
RA Simon M.C.;
RT "PU.1 and Spi-B are required for normal B cell receptor-mediated signal
RT transduction.";
RL Immunity 10:399-408(1999).
RN [5]
RP FUNCTION.
RX PubMed=11313289; DOI=10.1182/blood.v97.9.2908;
RA Garrett-Sinha L.A., Dahl R., Rao S., Barton K.P., Simon M.C.;
RT "PU.1 exhibits partial functional redundancy with Spi-B, but not with Ets-1
RT or Elf-1.";
RL Blood 97:2908-2912(2001).
RN [6]
RP FUNCTION.
RX PubMed=11672537; DOI=10.1016/s1074-7613(01)00219-9;
RA Hu C.-J., Rao S., Ramirez-Bergeron D.L., Garrett-Sinha L.A., Gerondakis S.,
RA Clark M.R., Simon M.C.;
RT "PU.1/Spi-B regulation of c-rel is essential for mature B cell survival.";
RL Immunity 15:545-555(2001).
RN [7]
RP FUNCTION.
RX PubMed=11980719; DOI=10.1093/emboj/21.9.2220;
RA Dahl R., Ramirez-Bergeron D.L., Rao S., Simon M.C.;
RT "Spi-B can functionally replace PU.1 in myeloid but not lymphoid
RT development.";
RL EMBO J. 21:2220-2230(2002).
RN [8]
RP FUNCTION.
RX PubMed=12431391; DOI=10.1016/s0161-5890(02)00201-8;
RA Kim N., Martin T.E., Simon M.C., Storb U.;
RT "The transcription factor Spi-B is not required for somatic
RT hypermutation.";
RL Mol. Immunol. 39:577-583(2003).
CC -!- FUNCTION: Sequence specific transcriptional activator which binds to
CC the PU-box, a purine-rich DNA sequence (5'-GAGGAA-3') that can act as a
CC lymphoid-specific enhancer. Promotes development of plasmacytoid
CC dendritic cells (pDCs), also known as type 2 DC precursors (pre-DC2) or
CC natural interferon (IFN)-producing cells. These cells have the capacity
CC to produce large amounts of interferon and block viral replication.
CC Required for B-cell receptor (BCR) signaling, which is necessary for
CC normal B-cell development and antigenic stimulation.
CC {ECO:0000269|PubMed:10229183, ECO:0000269|PubMed:11313289,
CC ECO:0000269|PubMed:11672537, ECO:0000269|PubMed:11980719,
CC ECO:0000269|PubMed:12431391, ECO:0000269|PubMed:8691135,
CC ECO:0000269|PubMed:9384589}.
CC -!- SUBUNIT: Can form homotypic interactions. Interacts with IRF4. May also
CC interact with CREBBP, EP300, SPI1/PU.1 related, JUN and TBP (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q01892}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
CC Name=IA;
CC IsoId=O35906-1; Sequence=Displayed;
CC Name=IC;
CC IsoId=O35906-2; Sequence=VSP_013908;
CC Name=IIA;
CC IsoId=O35906-3; Sequence=VSP_013907;
CC -!- TISSUE SPECIFICITY: Expressed in the medulla of the thymus, the spleen
CC and germinal centers of the lymph nodes. Expressed in B-cells and T-
CC cells, expression increases during B-cell maturation and decreases
CC during T-cell maturation. {ECO:0000269|PubMed:8691135}.
CC -!- DOMAIN: The protein contains a weakly acidic N-terminal transactivation
CC domain (TAD) followed by a second TAD rich in proline, serine and
CC threonine. Each of these domains may be required for transcriptional
CC activation of a subset of target genes (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform IA]: Produced by alternative promoter usage.
CC -!- MISCELLANEOUS: [Isoform IC]: Produced by alternative splicing of
CC isoform IA. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform IIA]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
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DR EMBL; U87619; AAC53554.1; -; Genomic_DNA.
DR EMBL; U87614; AAC53554.1; JOINED; Genomic_DNA.
DR EMBL; U87616; AAC53554.1; JOINED; Genomic_DNA.
DR EMBL; U87617; AAC53554.1; JOINED; Genomic_DNA.
DR EMBL; U87618; AAC53554.1; JOINED; Genomic_DNA.
DR EMBL; U87619; AAC53556.1; -; Genomic_DNA.
DR EMBL; U87614; AAC53556.1; JOINED; Genomic_DNA.
DR EMBL; U87616; AAC53556.1; JOINED; Genomic_DNA.
DR EMBL; U87617; AAC53556.1; JOINED; Genomic_DNA.
DR EMBL; U87618; AAC53556.1; JOINED; Genomic_DNA.
DR EMBL; U87619; AAC53557.1; -; Genomic_DNA.
DR EMBL; U87616; AAC53557.1; JOINED; Genomic_DNA.
DR EMBL; U87617; AAC53557.1; JOINED; Genomic_DNA.
DR EMBL; U87618; AAC53557.1; JOINED; Genomic_DNA.
DR EMBL; U87620; AAC53559.1; -; Genomic_DNA.
DR CCDS; CCDS21209.1; -. [O35906-1]
DR RefSeq; NP_063919.1; NM_019866.1. [O35906-1]
DR RefSeq; XP_006540996.1; XM_006540933.3. [O35906-2]
DR RefSeq; XP_006540998.1; XM_006540935.3. [O35906-3]
DR AlphaFoldDB; O35906; -.
DR SMR; O35906; -.
DR STRING; 10090.ENSMUSP00000096084; -.
DR MaxQB; O35906; -.
DR PaxDb; O35906; -.
DR PRIDE; O35906; -.
DR ProteomicsDB; 258587; -. [O35906-3]
DR DNASU; 272382; -.
DR Ensembl; ENSMUST00000035323; ENSMUSP00000035539; ENSMUSG00000008193. [O35906-1]
DR GeneID; 272382; -.
DR KEGG; mmu:272382; -.
DR UCSC; uc009gpw.1; mouse. [O35906-1]
DR CTD; 6689; -.
DR MGI; MGI:892986; Spib.
DR VEuPathDB; HostDB:ENSMUSG00000008193; -.
DR eggNOG; KOG3805; Eukaryota.
DR GeneTree; ENSGT00940000162754; -.
DR HOGENOM; CLU_066451_2_0_1; -.
DR InParanoid; O35906; -.
DR OMA; CKHPSYP; -.
DR OrthoDB; 1272250at2759; -.
DR PhylomeDB; O35906; -.
DR TreeFam; TF352494; -.
DR BioGRID-ORCS; 272382; 2 hits in 73 CRISPR screens.
DR PRO; PR:O35906; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O35906; protein.
DR Bgee; ENSMUSG00000008193; Expressed in peripheral lymph node and 59 other tissues.
DR ExpressionAtlas; O35906; baseline and differential.
DR Genevisible; O35906; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IC:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0002327; P:immature B cell differentiation; IGI:ARUK-UCL.
DR GO; GO:0030225; P:macrophage differentiation; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000418; Ets_dom.
DR InterPro; IPR046328; ETS_fam.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11849; PTHR11849; 1.
DR Pfam; PF00178; Ets; 1.
DR PRINTS; PR00454; ETSDOMAIN.
DR SMART; SM00413; ETS; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR PROSITE; PS50061; ETS_DOMAIN_3; 1.
PE 2: Evidence at transcript level;
KW Activator; Alternative promoter usage; Alternative splicing; DNA-binding;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..267
FT /note="Transcription factor Spi-B"
FT /id="PRO_0000204137"
FT DNA_BIND 174..257
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 1..31
FT /note="TAD1 (Acidic)"
FT REGION 41..62
FT /note="TAD2"
FT VAR_SEQ 1..8
FT /note="MLALEAAQ -> MPLCLSPAR (in isoform IIA)"
FT /evidence="ECO:0000305"
FT /id="VSP_013907"
FT VAR_SEQ 17
FT /note="L -> LVGEGVSPRPEMTLSSLRQ (in isoform IC)"
FT /evidence="ECO:0000305"
FT /id="VSP_013908"
SQ SEQUENCE 267 AA; 29365 MW; D32485A93C44327F CRC64;
MLALEAAQLD GPHLSCLYPE GVFYDLDSCK PFSYPDSDGG LDSTWGWTEA PPAPAIAPYE
AFDPATAAFS HSQTVQLCYS HGPNPSTYSP MGTLDPAPSL EAPGPGLQVY PPEDFTSQTL
GSLAYAPYPS PVLSEEEDIM LDSPALEVSD SESDEALLAG SEGRGSEAGA RKKLRLYQFL
LGLLLRGDMR ECVWWVEPGA GVFQFSSKHK ELLARRWGQQ KGNRKRMTYQ KLARALRNYA
KTGEIRKVKR KLTYQFDSAL LPASRHV
