ATF6B_MOUSE
ID ATF6B_MOUSE Reviewed; 699 AA.
AC O35451;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Cyclic AMP-dependent transcription factor ATF-6 beta;
DE Short=cAMP-dependent transcription factor ATF-6 beta;
DE AltName: Full=Activating transcription factor 6 beta;
DE Short=ATF6-beta;
DE AltName: Full=cAMP response element-binding protein-related protein;
DE Short=Creb-rp;
DE AltName: Full=cAMP-responsive element-binding protein-like 1;
DE Contains:
DE RecName: Full=Processed cyclic AMP-dependent transcription factor ATF-6 beta;
GN Name=Atf6b; Synonyms=Crebl1;
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 GENOMIC DNA].
RC STRAIN=129;
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Kidney;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 654-699.
RC STRAIN=C57BL/6 X CBA;
RX PubMed=9795100; DOI=10.1016/s0378-1119(98)00355-2;
RA Ikuta T., Sogawa N., Ariga H., Ikemura T., Matsumoto K.;
RT "Structural analysis of mouse tenascin-X: evolutionary aspects of
RT reduplication of FNIII repeats in the tenascin gene family.";
RL Gene 217:1-13(1998).
CC -!- FUNCTION: [Cyclic AMP-dependent transcription factor ATF-6 beta]:
CC Precursor of the transcription factor form (Processed cyclic AMP-
CC dependent transcription factor ATF-6 beta), which is embedded in the
CC endoplasmic reticulum membrane. Endoplasmic reticulum stress promotes
CC processing of this form, releasing the transcription factor form that
CC translocates into the nucleus, where it activates transcription of
CC genes involved in the unfolded protein response (UPR).
CC {ECO:0000250|UniProtKB:Q99941}.
CC -!- FUNCTION: [Processed cyclic AMP-dependent transcription factor ATF-6
CC beta]: Transcription factor that acts in the unfolded protein response
CC (UPR) pathway by activating UPR target genes induced during ER stress.
CC Binds DNA on the 5'-CCAC[GA]-3' half of the ER stress response element
CC (ERSE) (5'-CCAATN(9)CCAC[GA]-3') when NF-Y is bound to ERSE.
CC {ECO:0000250|UniProtKB:Q99941}.
CC -!- SUBUNIT: [Processed cyclic AMP-dependent transcription factor ATF-6
CC beta]: Homodimer and heterodimer with ATF6-alpha. The dimer interacts
CC with the nuclear transcription factor Y (NF-Y) trimer through direct
CC binding to NF-Y subunit C (NF-YC). {ECO:0000250|UniProtKB:Q99941}.
CC -!- INTERACTION:
CC O35451; P20029: Hspa5; NbExp=2; IntAct=EBI-8361741, EBI-772325;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q99941}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Processed cyclic AMP-dependent transcription
CC factor ATF-6 beta]: Nucleus {ECO:0000250|UniProtKB:Q99941}. Note=Under
CC ER stress the cleaved N-terminal cytoplasmic domain translocates into
CC the nucleus. {ECO:0000250|UniProtKB:Q99941}.
CC -!- DOMAIN: The basic domain functions as a nuclear localization signal.
CC {ECO:0000250|UniProtKB:Q99941}.
CC -!- DOMAIN: The basic leucine-zipper domain is sufficient for association
CC with the NF-Y trimer and binding to ERSE.
CC {ECO:0000250|UniProtKB:Q99941}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q99941}.
CC -!- PTM: During unfolded protein response, a fragment of approximately 60
CC kDa containing the cytoplasmic transcription factor domain is released
CC by proteolysis. The cleavage is probably performed sequentially by
CC site-1 (MBTPS1, S1P) and site-2 (MBTPS2, S2P) proteases.
CC {ECO:0000250|UniProtKB:Q99941}.
CC -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
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DR EMBL; AF030001; AAB82014.1; -; Genomic_DNA.
DR EMBL; BC013534; AAH13534.1; -; mRNA.
DR EMBL; BC052635; AAH52635.1; -; mRNA.
DR EMBL; AB010266; BAA24435.1; -; Genomic_DNA.
DR PIR; T09069; T09069.
DR AlphaFoldDB; O35451; -.
DR SMR; O35451; -.
DR DIP; DIP-61156N; -.
DR IntAct; O35451; 2.
DR STRING; 10090.ENSMUSP00000015605; -.
DR GlyGen; O35451; 5 sites.
DR iPTMnet; O35451; -.
DR PhosphoSitePlus; O35451; -.
DR CPTAC; non-CPTAC-3964; -.
DR MaxQB; O35451; -.
DR PaxDb; O35451; -.
DR PeptideAtlas; O35451; -.
DR PRIDE; O35451; -.
DR ProteomicsDB; 265145; -.
DR MGI; MGI:105121; Atf6b.
DR eggNOG; KOG4343; Eukaryota.
DR InParanoid; O35451; -.
DR PhylomeDB; O35451; -.
DR TreeFam; TF316079; -.
DR ChiTaRS; Atf6b; mouse.
DR PRO; PR:O35451; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O35451; protein.
DR GO; GO:0000794; C:condensed nuclear chromosome; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; NAS:ParkinsonsUK-UCL.
DR GO; GO:0005815; C:microtubule organizing center; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0035497; F:cAMP response element binding; IEA:InterPro.
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; ISO: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:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central.
DR GO; GO:0007076; P:mitotic chromosome condensation; ISS:UniProtKB.
DR GO; GO:1903892; P:negative regulation of ATF6-mediated unfolded protein response; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR029809; ATF6B.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR46164:SF2; PTHR46164:SF2; 2.
DR Pfam; PF00170; bZIP_1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; DNA-binding; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Nucleus; Reference proteome; Signal-anchor; Transcription;
KW Transcription regulation; Transmembrane; Transmembrane helix;
KW Unfolded protein response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q99941"
FT CHAIN 2..699
FT /note="Cyclic AMP-dependent transcription factor ATF-6
FT beta"
FT /id="PRO_0000076591"
FT CHAIN 2..?
FT /note="Processed cyclic AMP-dependent transcription factor
FT ATF-6 beta"
FT /id="PRO_0000296202"
FT TOPO_DOM 2..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..699
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 322..385
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 59..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..344
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 347..354
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 417..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..313
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..560
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 407
FT /note="Important for cleavage by MBTPS2"
FT /evidence="ECO:0000250|UniProtKB:P18850"
FT SITE 410
FT /note="Important for cleavage by MBTPS2"
FT /evidence="ECO:0000250|UniProtKB:P18850"
FT SITE 437..438
FT /note="Cleavage; by MBTPS1"
FT /evidence="ECO:0000250|UniProtKB:P18850"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q99941"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 624
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 673
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 699 AA; 76007 MW; 6EBE22386D63868B CRC64;
MAELMLLSEI ADPTRFFTDN LLSPEDWDST LYSGLDEVAE EQAQLFRCVE QDVPFDSSSL
DVGMDVSPPE PPWDPLPIFP DLQVKSEPSS PCSSSSLSSE SSHLSTEPPS QVPGVGEVLH
VKMESLAPPL CLLGDDPASP FETVQITVGS ASDDLSDIQT KLEPASPSSS VHSEASLLSA
DSPSQPFIGE EVLEVKTESP SPPGCLLWDV PASSLGAVQI SMGPSPDSSS GKAPATRKPP
LQPKPVVLTT VPVPPRAGPT SAAVLLQPLV QQPAVSPVVL IQGAIRVQPE GPAPAAPRPE
RKSIVPAPMP GNSCPPEVDA KLLKRQQRMI KNRESACQSR RKKKEYLQGL EARLQAVLAD
NQQLRRENAA LRRRLEALLA ENSGLKLGSG NRKVVCIMVF LLFIAFNFGP VSISEPPPAP
MSPRMSREEP RPQRHLLGFS EPGPAHGMEP LREAAQSPGE QQPSSAGRPS FRNLTAFPGG
AKELLLRDLD QLFLSSDCRH FNRTESLRLA DELSGWVQRH QRGRRKIPHR AQERQKSQLR
KKSPPVKPVP TQPPGPPERD PVGQLQLYRH PGRSQPEFLD AIDRREDTFY VVSFRRDHLL
LPAISHNKTS RPKMSLVMPA MAPNETVSGR GPPGDYEEMM QIECEVMDTR VIHIKTSTVP
PSLRKQPSPS PGNTTGGPLP GSAASPAHQA SQPLYLNHP
