CR3LB_DANRE
ID CR3LB_DANRE Reviewed; 428 AA.
AC Q1LYG4;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Cyclic AMP-responsive element-binding protein 3-like protein 3-B;
DE Short=cAMP-responsive element-binding protein 3-like protein 3-B;
DE Contains:
DE RecName: Full=Processed cyclic AMP-responsive element-binding protein 3-like protein 3-B;
GN Name=creb3l3b; Synonyms=creb3l3; ORFNames=si:dkey-110c1.2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Transcriptional activator. Binds the cAMP response element
CC (CRE). Activates transcription through box-B element and CRE. Seems to
CC function synergistically with atf6 (By similarity). Regulates FGF21
CC transcription (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q91XE9}.
CC -!- SUBUNIT: Binds DNA as a dimer. {ECO:0000250|UniProtKB:Q68CJ9}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q68CJ9}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q68CJ9}.
CC -!- SUBCELLULAR LOCATION: [Processed cyclic AMP-responsive element-binding
CC protein 3-like protein 3-B]: Nucleus {ECO:0000250|UniProtKB:Q68CJ9}.
CC -!- PTM: Controlled by regulated intramembrane proteolysis (RIP). A
CC fragment containing the cytoplasmic transcription factor domain is
CC released by proteolysis. The cleavage seems to be performed
CC sequentially by site-1 and site-2 proteases (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK05095.1; Type=Erroneous initiation; Evidence={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; BX005203; CAK05095.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q1LYG4; -.
DR SMR; Q1LYG4; -.
DR STRING; 7955.ENSDARP00000113661; -.
DR PaxDb; Q1LYG4; -.
DR ZFIN; ZDB-GENE-030131-4298; creb3l3a.
DR eggNOG; KOG0709; Eukaryota.
DR InParanoid; Q1LYG4; -.
DR PhylomeDB; Q1LYG4; -.
DR Reactome; R-DRE-8874211; CREB3 factors activate genes.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0035497; F:cAMP response element binding; IEA:InterPro.
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:0030968; P:endoplasmic reticulum unfolded protein response; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR029806; CREBH.
DR PANTHER; PTHR45996:SF1; PTHR45996:SF1; 1.
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 3: Inferred from homology;
KW Activator; DNA-binding; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Nucleus; Reference proteome; Signal-anchor; Transcription;
KW Transcription regulation; Transmembrane; Transmembrane helix.
FT CHAIN 1..428
FT /note="Cyclic AMP-responsive element-binding protein 3-like
FT protein 3-B"
FT /id="PRO_0000288078"
FT CHAIN 1..?
FT /note="Processed cyclic AMP-responsive element-binding
FT protein 3-like protein 3-B"
FT /id="PRO_0000302807"
FT TOPO_DOM 1..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..303
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..428
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 210..273
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 67..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..241
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 252..273
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 381..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 330..331
FT /note="Cleavage; by PS1"
FT /evidence="ECO:0000250"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 428 AA; 48332 MW; 6BE0FD8359655862 CRC64;
MDHYSDQGGD GIELLDLLFD KNDGILRYEN MGQQNNQLWP VQDPHMMMTP QGNEDFFNAL
IGGSDSVSGS PVWSPSPSDS GISEDPHSDH IDSPPPNASP PMEPHIVVSQ TQHSLNINFP
FDFNGWETGF LPDQSGGTQC ASETPQAQQT TGFPLTVKDL LLSGTPEPAA KVSQQSYQEL
ILTEDEKRLL AKEGMTLPNQ FPLTKYEERI LKKIRRKIRN KQSAQESRKK KKEYIDGLES
RMAACSAHNH ELQRKVFQLE KCNISLMEQL RRLQALVMNG SNKPVQAGTC VLVLLLSFTL
ILLPNLKPFT DTKVSQHGDF SPMRVQSRSL HNLQSSRVLR NLDHPYSMTE NAKILPRFPE
DKTMEEIASL LGRLHRRPQF TEYDPESHNH SFDQHDEHHH GDPITGHVAT VTLNPRRGSR
RSPHADDM
