BTF3_MOUSE
ID BTF3_MOUSE Reviewed; 204 AA.
AC Q64152; Q64153; Q6GU63; Q6P3F3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Transcription factor BTF3;
DE AltName: Full=Nascent polypeptide-associated complex subunit beta;
DE Short=NAC-beta;
DE AltName: Full=RNA polymerase B transcription factor 3;
GN Name=Btf3;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N, and FVB/N-3; TISSUE=Jaw, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-65 AND 104-158.
RC TISSUE=Testis;
RX PubMed=7655515; DOI=10.1007/bf01969120;
RA Deng J.M., Behringer R.R.;
RT "An insertional mutation in the BTF3 transcription factor gene leads to an
RT early postimplantation lethality in mice.";
RL Transgenic Res. 4:264-269(1995).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-19, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: When associated with NACA, prevents inappropriate targeting
CC of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds
CC to nascent polypeptide chains as they emerge from the ribosome and
CC blocks their interaction with the signal recognition particle (SRP),
CC which normally targets nascent secretory peptides to the ER. BTF3 is
CC also a general transcription factor that can form a stable complex with
CC RNA polymerase II. Required for the initiation of transcription (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of the nascent polypeptide-associated complex (NAC),
CC which is a heterodimer of NACA and BTF3 (via NAC-A/B domains). NAC
CC associates with ribosomes through the BTF3/NACB subunit. Both subunits
CC can contact nascent polypeptide chains (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus. Note=The
CC heterodimer with NACA is cytoplasmic. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=BTF3a;
CC IsoId=Q64152-1; Sequence=Displayed;
CC Name=2; Synonyms=BTF3b;
CC IsoId=Q64152-2; Sequence=VSP_013588;
CC -!- SIMILARITY: Belongs to the NAC-beta family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC008233; AAH08233.1; -; mRNA.
DR EMBL; BC064010; AAH64010.1; -; mRNA.
DR EMBL; BC080837; AAH80837.1; -; mRNA.
DR EMBL; S79538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S79537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS26714.1; -. [Q64152-1]
DR CCDS; CCDS49340.1; -. [Q64152-2]
DR RefSeq; NP_001164011.1; NM_001170540.1. [Q64152-2]
DR RefSeq; NP_663430.2; NM_145455.3. [Q64152-1]
DR AlphaFoldDB; Q64152; -.
DR BioGRID; 230038; 32.
DR DIP; DIP-59968N; -.
DR IntAct; Q64152; 2.
DR MINT; Q64152; -.
DR STRING; 10090.ENSMUSP00000022163; -.
DR iPTMnet; Q64152; -.
DR PhosphoSitePlus; Q64152; -.
DR EPD; Q64152; -.
DR jPOST; Q64152; -.
DR MaxQB; Q64152; -.
DR PaxDb; Q64152; -.
DR PeptideAtlas; Q64152; -.
DR PRIDE; Q64152; -.
DR ProteomicsDB; 265383; -. [Q64152-1]
DR ProteomicsDB; 265384; -. [Q64152-2]
DR TopDownProteomics; Q64152-2; -. [Q64152-2]
DR Antibodypedia; 4573; 211 antibodies from 29 providers.
DR DNASU; 218490; -.
DR Ensembl; ENSMUST00000022163; ENSMUSP00000022163; ENSMUSG00000021660. [Q64152-1]
DR Ensembl; ENSMUST00000134542; ENSMUSP00000115500; ENSMUSG00000021660. [Q64152-2]
DR Ensembl; ENSMUST00000152704; ENSMUSP00000118093; ENSMUSG00000021660. [Q64152-2]
DR GeneID; 218490; -.
DR KEGG; mmu:218490; -.
DR UCSC; uc007rou.1; mouse. [Q64152-1]
DR CTD; 689; -.
DR MGI; MGI:1202875; Btf3.
DR VEuPathDB; HostDB:ENSMUSG00000021660; -.
DR eggNOG; KOG2240; Eukaryota.
DR GeneTree; ENSGT00940000153288; -.
DR HOGENOM; CLU_098726_3_0_1; -.
DR InParanoid; Q64152; -.
DR OrthoDB; 1435264at2759; -.
DR PhylomeDB; Q64152; -.
DR TreeFam; TF317546; -.
DR BioGRID-ORCS; 218490; 21 hits in 52 CRISPR screens.
DR ChiTaRS; Btf3; mouse.
DR PRO; PR:Q64152; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q64152; protein.
DR Bgee; ENSMUSG00000021660; Expressed in epiblast (generic) and 133 other tissues.
DR ExpressionAtlas; Q64152; baseline and differential.
DR Genevisible; Q64152; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005854; C:nascent polypeptide-associated complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042788; C:polysomal ribosome; IBA:GO_Central.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:1905551; P:negative regulation of protein localization to endoplasmic reticulum; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.20.70.30; -; 1.
DR InterPro; IPR039370; BTF3.
DR InterPro; IPR038187; NAC_A/B_dom_sf.
DR InterPro; IPR002715; Nas_poly-pep-assoc_cplx_dom.
DR PANTHER; PTHR10351; PTHR10351; 1.
DR Pfam; PF01849; NAC; 1.
DR SMART; SM01407; NAC; 1.
DR PROSITE; PS51151; NAC_AB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Cytoplasm; Methylation; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Transcription;
KW Transcription regulation; Transport.
FT CHAIN 1..204
FT /note="Transcription factor BTF3"
FT /id="PRO_0000213549"
FT DOMAIN 80..145
FT /note="NAC-A/B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00507"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20290"
FT MOD_RES 44
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20290"
FT MOD_RES 52
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20290"
FT MOD_RES 158
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20290"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20290"
FT VAR_SEQ 1..42
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013588"
FT CONFLICT 47
FT /note="I -> V (in Ref. 2; S79538)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="K -> R (in Ref. 2; S79538)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="N -> S (in Ref. 2; S79537)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 204 AA; 22031 MW; 35D92D331272F961 CRC64;
MRRTGAPTQA DSRGRGRARG GWPGAEATPS LPLGGSRGRE SQMKETIMNQ EKLAKLQAQV
RIGGKGTARR KKKVVHRTAT ADDKKLQFSL KKLGVNNISG IEEVNMFTNQ GTVIHFNNPK
VQASLAANTF TITGHAETKQ LTEMLPSILN QLGADSLTSL RRLAEALPKQ SVDGKAPLAT
GEDDDDEVPD LVENFDEASK NEAN
