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Cyclic AMP-responsive element-binding protein 3-like protein 3 (cAMP-responsive element-binding protein 3-like protein 3) (Transcription factor CREB-H) [Cleaved into: Processed cyclic AMP-responsive element-binding protein 3-like protein 3]

 CR3L3_RAT               Reviewed;         470 AA.
Q5FVM5;
29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2005, sequence version 1.
05-DEC-2018, entry version 105.
RecName: Full=Cyclic AMP-responsive element-binding protein 3-like protein 3;
Short=cAMP-responsive element-binding protein 3-like protein 3;
AltName: Full=Transcription factor CREB-H;
Contains:
RecName: Full=Processed cyclic AMP-responsive element-binding protein 3-like protein 3;
Name=Creb3l3;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2]
FUNCTION.
PubMed=15800215; DOI=10.1093/nar/gki332;
Chin K.-T., Zhou H.-J., Wong C.-M., Lee J.M.-F., Chan C.-P.,
Qiang B.-Q., Yuan J.-G., Ng I.-O., Jin D.-Y.;
"The liver-enriched transcription factor CREB-H is a growth suppressor
protein underexpressed in hepatocellular carcinoma.";
Nucleic Acids Res. 33:1859-1873(2005).
-!- FUNCTION: Transcription factor that may act during endoplasmic
reticulum stress by activating unfolded protein response target
genes. Activated in response to cAMP stimulation. Binds the cAMP
response element (CRE). Activates transcription through box-B
element and CRE. Seems to function synergistically with ATF6. In
acute inflammatory response, may activate expression of acute
phase response (APR) genes (By similarity). May be involved in
growth suppression. {ECO:0000250, ECO:0000269|PubMed:15800215}.
-!- SUBUNIT: Binds DNA as a dimer. Probably homodimerizes. Probably
forms a heterodimer with ATF6. Interacts with ATF6 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Processed cyclic AMP-responsive element-
binding protein 3-like protein 3: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00978}. Note=Under ER stress the cleaved N-terminal
cytoplasmic domain translocates into the nucleus.
-!- PTM: Controlled by regulated intramembrane proteolysis (RIP).
Following ER stress a fragment containing the cytoplasmic
transcription factor domain is released by proteolysis. The
cleavage seems to be performed sequentially by site-1 and site-2
proteases (PS1 and PS2) (By similarity). {ECO:0000250}.
-!- PTM: N-glycosylation is required for optimal proteolytic
activation. {ECO:0000250}.
-!- SIMILARITY: Belongs to the bZIP family. ATF subfamily.
{ECO:0000305}.
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EMBL; BC089877; AAH89877.1; -; mRNA.
RefSeq; NP_001012115.1; NM_001012115.1.
UniGene; Rn.20059; -.
ProteinModelPortal; Q5FVM5; -.
STRING; 10116.ENSRNOP00000044840; -.
PhosphoSitePlus; Q5FVM5; -.
PaxDb; Q5FVM5; -.
PRIDE; Q5FVM5; -.
Ensembl; ENSRNOT00000044484; ENSRNOP00000044840; ENSRNOG00000032202.
GeneID; 314638; -.
KEGG; rno:314638; -.
UCSC; RGD:1308152; rat.
CTD; 84699; -.
RGD; 1308152; Creb3l3.
eggNOG; KOG0709; Eukaryota.
eggNOG; ENOG410ZZQM; LUCA.
GeneTree; ENSGT00940000159261; -.
HOGENOM; HOG000059566; -.
HOVERGEN; HBG090496; -.
InParanoid; Q5FVM5; -.
KO; K09048; -.
OMA; DLEMWSP; -.
OrthoDB; EOG091G07QR; -.
PhylomeDB; Q5FVM5; -.
TreeFam; TF316079; -.
Reactome; R-RNO-8874211; CREB3 factors activate genes.
PRO; PR:Q5FVM5; -.
Proteomes; UP000002494; Chromosome 7.
Bgee; ENSRNOG00000032202; Expressed in 5 organ(s), highest expression level in liver.
Genevisible; Q5FVM5; RN.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0035497; F:cAMP response element binding; IEA:InterPro.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:InterPro.
GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IEA:Ensembl.
InterPro; IPR004827; bZIP.
InterPro; IPR029806; CREBH.
PANTHER; PTHR22952:SF98; PTHR22952:SF98; 1.
Pfam; PF00170; bZIP_1; 1.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
2: Evidence at transcript level;
Activator; Complete proteome; DNA-binding; Endoplasmic reticulum;
Glycoprotein; Membrane; Nucleus; Reference proteome; Signal-anchor;
Transcription; Transcription regulation; Transmembrane;
Transmembrane helix; Unfolded protein response.
CHAIN 1 470 Cyclic AMP-responsive element-binding
protein 3-like protein 3.
/FTId=PRO_0000288076.
CHAIN 1 ? Processed cyclic AMP-responsive element-
binding protein 3-like protein 3.
/FTId=PRO_0000296217.
TOPO_DOM 1 319 Cytoplasmic. {ECO:0000255}.
TRANSMEM 320 340 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 341 470 Lumenal. {ECO:0000255}.
DOMAIN 239 302 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 241 270 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 281 302 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
COMPBIAS 183 186 Poly-Gly.
SITE 359 360 Cleavage; by PS1. {ECO:0000250}.
CARBOHYD 410 410 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 417 417 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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


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