CR3L3_RAT
ID CR3L3_RAT Reviewed; 470 AA.
AC Q5FVM5;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cyclic AMP-responsive element-binding protein 3-like protein 3;
DE Short=cAMP-responsive element-binding protein 3-like protein 3;
DE AltName: Full=Transcription factor CREB-H;
DE Contains:
DE RecName: Full=Processed cyclic AMP-responsive element-binding protein 3-like protein 3;
GN Name=Creb3l3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 FUNCTION.
RX PubMed=15800215; DOI=10.1093/nar/gki332;
RA Chin K.-T., Zhou H.-J., Wong C.-M., Lee J.M.-F., Chan C.-P., Qiang B.-Q.,
RA Yuan J.-G., Ng I.-O., Jin D.-Y.;
RT "The liver-enriched transcription factor CREB-H is a growth suppressor
RT protein underexpressed in hepatocellular carcinoma.";
RL Nucleic Acids Res. 33:1859-1873(2005).
CC -!- FUNCTION: Transcription factor that may act during endoplasmic
CC reticulum stress by activating unfolded protein response target genes.
CC Activated in response to cAMP stimulation. Binds the cAMP response
CC element (CRE). Activates transcription through box-B element and CRE.
CC Seems to function synergistically with ATF6. In acute inflammatory
CC response, may activate expression of acute phase response (APR) genes
CC (By similarity). May be involved in growth suppression. Regulates FGF21
CC transcription (By similarity). Plays a crucial role in the regulation
CC of triglyceride metabolism and is required for the maintenance of
CC normal plasma triglyceride concentrations (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q91XE9,
CC ECO:0000269|PubMed:15800215}.
CC -!- SUBUNIT: Binds DNA as a dimer. May form homodimers (By similarity).
CC Interacts with ATF6 (By similarity). Interacts with SYNV1/HRD1; this
CC interaction leads to CREB3L3 ubiquitination and proteasomal degradation
CC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q68CJ9,
CC ECO:0000250|UniProtKB:Q91XE9}.
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]: Nucleus {ECO:0000255|PROSITE-
CC ProRule:PRU00978}. Note=Under ER stress the cleaved N-terminal
CC cytoplasmic domain translocates into the nucleus.
CC -!- PTM: Controlled by regulated intramembrane proteolysis (RIP). Following
CC ER stress a fragment containing the cytoplasmic transcription factor
CC domain is released by proteolysis. The cleavage seems to be performed
CC sequentially by site-1 and site-2 proteases (PS1 and PS2) (By
CC similarity). {ECO:0000250}.
CC -!- PTM: N-glycosylation is required for optimal proteolytic activation.
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated at Lys-290 by SYNV1/HRD1 via 'Lys-27'-linked
CC ubiquitin. {ECO:0000250|UniProtKB:Q68CJ9}.
CC -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
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DR EMBL; BC089877; AAH89877.1; -; mRNA.
DR RefSeq; NP_001012115.1; NM_001012115.1.
DR AlphaFoldDB; Q5FVM5; -.
DR SMR; Q5FVM5; -.
DR STRING; 10116.ENSRNOP00000044840; -.
DR GlyGen; Q5FVM5; 2 sites.
DR PhosphoSitePlus; Q5FVM5; -.
DR PaxDb; Q5FVM5; -.
DR Ensembl; ENSRNOT00000044484; ENSRNOP00000044840; ENSRNOG00000032202.
DR GeneID; 314638; -.
DR KEGG; rno:314638; -.
DR UCSC; RGD:1308152; rat.
DR CTD; 84699; -.
DR RGD; 1308152; Creb3l3.
DR eggNOG; KOG0709; Eukaryota.
DR GeneTree; ENSGT00940000159261; -.
DR HOGENOM; CLU_047257_1_0_1; -.
DR InParanoid; Q5FVM5; -.
DR OMA; PGTWHED; -.
DR OrthoDB; 644485at2759; -.
DR PhylomeDB; Q5FVM5; -.
DR TreeFam; TF316079; -.
DR Reactome; R-RNO-8874211; CREB3 factors activate genes.
DR PRO; PR:Q5FVM5; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000032202; Expressed in liver and 10 other tissues.
DR Genevisible; Q5FVM5; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
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:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
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:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
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; ISO:RGD.
DR GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; ISO:RGD.
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 2: Evidence at transcript level;
KW Activator; DNA-binding; Endoplasmic reticulum; Glycoprotein;
KW Isopeptide bond; Membrane; Nucleus; Reference proteome; Signal-anchor;
KW Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix; Ubl conjugation; Unfolded protein response.
FT CHAIN 1..470
FT /note="Cyclic AMP-responsive element-binding protein 3-like
FT protein 3"
FT /id="PRO_0000288076"
FT CHAIN 1..?
FT /note="Processed cyclic AMP-responsive element-binding
FT protein 3-like protein 3"
FT /id="PRO_0000296217"
FT TOPO_DOM 1..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..470
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 239..302
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 59..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..270
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 281..302
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 79..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 359..360
FT /note="Cleavage; by PS1"
FT /evidence="ECO:0000250"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 290
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q68CJ9"
SQ SEQUENCE 470 AA; 50862 MW; 2A550CFEE14B9A73 CRC64;
MDGDISTGKM ASPACAMAPL DSMEVLDLLF DGQDGILRNV DLAESWILTR EEQKVLPNSD
SDEFLNSILG PGDSDPSSPI WSPADSDSGI SEDLPSDSQD TPPGSGPGSA NVAARCHPSK
QGEGPCPSYL PSTACPEPPR TQVHESSVAI DLDMWSTDTL YPEEQAGSPS RFNLTVKELL
LSGGGGDLQQ HPLAASQLLG PGSGHCQELV LTEDEKKLLA KEGVTLPTQL PLTKYEERVL
KKIRRKIRNK QSAQESRKKK KEYIDGLENR MSACTAQNQE LQRKVLHLEK QNLSLLEQLK
HLQALVVQST SKPAHAGTCI AVLLLSFVLI ILPSISPFTA NKVDSPGDFI PVRVFSRTLH
NHAASRVAPD VTPGPEVPGP HKGSSGGLSA DWGNFLEIPM LDDPTEELDN TTLVLANSTE
DLGRATLLDW VASEPLLGQM GLEIPGEEIW LSWVPRWLRV RVVQDALGVL
