ID   ABT1_BOVIN              Reviewed;         275 AA.
AC   Q148M8;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Activator of basal transcription 1;
GN   Name=ABT1;
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 MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Could be a novel TATA-binding protein (TBP) which can
CC       function as a basal transcription activator. Can act as a regulator of
CC       basal transcription for class II genes (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with ESF1/ABTAP. Interacts with IGHMBP2.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ESF2/ABP1 family. {ECO:0000305}.
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DR   EMBL; BC118119; AAI18120.1; -; mRNA.
DR   RefSeq; NP_001069620.1; NM_001076152.2.
DR   AlphaFoldDB; Q148M8; -.
DR   STRING; 9913.ENSBTAP00000014277; -.
DR   PaxDb; Q148M8; -.
DR   PRIDE; Q148M8; -.
DR   Ensembl; ENSBTAT00000014277; ENSBTAP00000014277; ENSBTAG00000010784.
DR   GeneID; 539270; -.
DR   KEGG; bta:539270; -.
DR   CTD; 29777; -.
DR   VEuPathDB; HostDB:ENSBTAG00000010784; -.
DR   VGNC; VGNC:25514; ABT1.
DR   eggNOG; KOG3152; Eukaryota.
DR   GeneTree; ENSGT00390000002062; -.
DR   HOGENOM; CLU_054086_3_1_1; -.
DR   InParanoid; Q148M8; -.
DR   OMA; TRPNSSW; -.
DR   OrthoDB; 1377351at2759; -.
DR   TreeFam; TF314506; -.
DR   Proteomes; UP000009136; Chromosome 23.
DR   Bgee; ENSBTAG00000010784; Expressed in conceptus and 106 other tissues.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0034462; P:small-subunit processome assembly; IBA:GO_Central.
DR   GO; GO:0021522; P:spinal cord motor neuron differentiation; IEA:Ensembl.
DR   CDD; cd12263; RRM_ABT1_like; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR039119; ABT1/Esf2.
DR   InterPro; IPR034353; ABT1/ESF2_RRM.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   PANTHER; PTHR12311; PTHR12311; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Coiled coil; DNA-binding; Nucleus; Reference proteome;
KW   RNA-binding; Transcription; Transcription regulation.
FT   CHAIN           1..275
FT                   /note="Activator of basal transcription 1"
FT                   /id="PRO_0000285382"
FT   DOMAIN          46..145
FT                   /note="RRM"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          164..194
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        220..234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULW3"
SQ   SEQUENCE   275 AA;  31160 MW;  5A3DF2E16174ECA6 CRC64;
     MEVEGLELDT AELGPLEGSH QKLEAEEEQE ESEDAAGGSK KRVVPGIVYL GHIPPRFRPL
     HVRNLLSAYG EVGRVFFQAE DGFVKRKKKA AAASAAGGKK RSKYSKDYTE GWVEFRDKRV
     AKRVAVSLHN TPMGSRRRSP FRYDLWNLKY LHRFTWSHLS EHLAFERQVR RQRLRAEVAQ
     AKRETDFYLR SVERGQRFLA ADGDSTRPNG SWAFAQRPTE QEMRARKAAR PGGRERARLA
     NAQDQARSNR GLLAKIFGAP TPSESRGNSS PARNS