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BATF_BOVIN
ID   BATF_BOVIN              Reviewed;         125 AA.
AC   E1BD44;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Basic leucine zipper transcriptional factor ATF-like;
DE   AltName: Full=B-cell-activating transcription factor;
DE            Short=B-ATF;
GN   Name=BATF;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA   Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA   Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
CC   -!- FUNCTION: AP-1 family transcription factor that controls the
CC       differentiation of lineage-specific cells in the immune system:
CC       specifically mediates the differentiation of T-helper 17 cells (Th17),
CC       follicular T-helper cells (TfH), CD8(+) dendritic cells and class-
CC       switch recombination (CSR) in B-cells. Acts via the formation of a
CC       heterodimer with JUNB that recognizes and binds DNA sequence 5'-
CC       TGA[CG]TCA-3'. The BATF-JUNB heterodimer also forms a complex with IRF4
CC       (or IRF8) in immune cells, leading to recognition of AICE sequence (5'-
CC       TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by
CC       cooperative binding of BATF and IRF4 (or IRF8) and activation of genes.
CC       Controls differentiation of T-helper cells producing interleukin-17
CC       (Th17 cells) by binding to Th17-associated gene promoters: regulates
CC       expression of the transcription factor RORC itself and RORC target
CC       genes such as IL17 (IL17A or IL17B). Also involved in differentiation
CC       of follicular T-helper cells (TfH) by directing expression of BCL6 and
CC       MAF. In B-cells, involved in class-switch recombination (CSR) by
CC       controlling the expression of both AICDA and of germline transcripts of
CC       the intervening heavy-chain region and constant heavy-chain region
CC       (I(H)-C(H)). Following infection, can participate in CD8(+) dendritic
CC       cell differentiation via interaction with IRF4 and IRF8 to mediate
CC       cooperative gene activation. Regulates effector CD8(+) T-cell
CC       differentiation by regulating expression of SIRT1. Following DNA
CC       damage, part of a differentiation checkpoint that limits self-renewal
CC       of hematopoietic stem cells (HSCs): up-regulated by STAT3, leading to
CC       differentiation of HSCs, thereby restricting self-renewal of HSCs (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer; mainly heterodimerizes with JUNB. The BATF-JUNB
CC       heterodimer interacts with IRF4 and IRF8. Interacts (via bZIP domain)
CC       with IRF4 and IRF8; the interaction is direct. Also forms heterodimers
CC       with JUN and JUND. Interacts with IFI35 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC       Cytoplasm {ECO:0000250}. Note=Present in the nucleus and cytoplasm, but
CC       shows increased nuclear translocation after activation of T-cells.
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated on serine and threonine residues and at least one
CC       tyrosine residue. Phosphorylation at Ser-43 inhibit DNA binding
CC       activity and transforms it as a negative regulator of AP-1 mediated
CC       transcription (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR   EMBL; DAAA02029620; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001193207.1; NM_001206278.1.
DR   AlphaFoldDB; E1BD44; -.
DR   SMR; E1BD44; -.
DR   STRING; 9913.ENSBTAP00000035554; -.
DR   PaxDb; E1BD44; -.
DR   PRIDE; E1BD44; -.
DR   Ensembl; ENSBTAT00000035684; ENSBTAP00000035554; ENSBTAG00000025405.
DR   GeneID; 617628; -.
DR   KEGG; bta:617628; -.
DR   CTD; 10538; -.
DR   VEuPathDB; HostDB:ENSBTAG00000025405; -.
DR   VGNC; VGNC:26425; BATF.
DR   eggNOG; KOG1414; Eukaryota.
DR   GeneTree; ENSGT00940000159745; -.
DR   HOGENOM; CLU_088612_4_0_1; -.
DR   InParanoid; E1BD44; -.
DR   OMA; CTGLTPQ; -.
DR   OrthoDB; 1544557at2759; -.
DR   TreeFam; TF332340; -.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000025405; Expressed in pharyngeal tonsil and 81 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
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; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0042832; P:defense response to protozoan; ISS:UniProtKB.
DR   GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR   GO; GO:0060218; P:hematopoietic stem cell differentiation; ISS:UniProtKB.
DR   GO; GO:0045190; P:isotype switching; ISS:UniProtKB.
DR   GO; GO:0002320; P:lymphoid progenitor cell differentiation; ISS:UniProtKB.
DR   GO; GO:0043011; P:myeloid dendritic cell differentiation; ISS:UniProtKB.
DR   GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0072539; P:T-helper 17 cell differentiation; ISS:UniProtKB.
DR   GO; GO:0072540; P:T-helper 17 cell lineage commitment; ISS:UniProtKB.
DR   GO; GO:0045064; P:T-helper 2 cell differentiation; ISS:UniProtKB.
DR   InterPro; IPR000837; AP-1.
DR   InterPro; IPR029820; BATF.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   PANTHER; PTHR23351; PTHR23351; 1.
DR   PANTHER; PTHR23351:SF14; PTHR23351:SF14; 1.
DR   Pfam; PF00170; bZIP_1; 1.
DR   PRINTS; PR00042; LEUZIPPRFOS.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; SSF57959; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   3: Inferred from homology;
KW   Activator; Cytoplasm; Differentiation; DNA-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..125
FT                   /note="Basic leucine zipper transcriptional factor ATF-
FT                   like"
FT                   /id="PRO_0000420463"
FT   DOMAIN          26..89
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          28..50
FT                   /note="Basic motif"
FT   REGION          54..75
FT                   /note="Leucine-zipper"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..41
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         43
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O35284"
FT   MOD_RES         48
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O35284"
SQ   SEQUENCE   125 AA;  14079 MW;  0BF32190D0B1786B CRC64;
     MPHSSDSSDS SFSRSPPPGK QDSSDDVRKV QRREKNRIAA QKSRQRQTQK ADTLHLESED
     LEKQNAALRK EIKQLTEEMK YFTSVLSSHE PLCSVLAPGA PSPPEVVYST HAFHQPHVSS
     PRFQP
 
 
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