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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_MOUSE             Reviewed;         479 AA.
Q91XE9; Q8BWS0;
29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
28-MAR-2018, entry version 133.
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; Synonyms=Crebh;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
STRAIN=C57BL/10; TISSUE=Liver;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; 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).
[4]
INDUCTION.
PubMed=16469704; DOI=10.1016/j.cell.2005.11.040;
Zhang K., Shen X., Wu J., Sakaki K., Saunders T., Rutkowski D.T.,
Back S.H., Kaufman R.J.;
"Endoplasmic reticulum stress activates cleavage of CREBH to induce a
systemic inflammatory response.";
Cell 124:587-599(2006).
-!- FUNCTION: Transcription factor that may act during endoplasmic
reticulum stress by activating unfolded protein response target
genes. Activated in response to cAMP stimulation. Binds to the
cAMP response element (CRE). Activates transcription through box-B
element (By similarity). Activates transcription through CRE.
Seems to function synergistically with ATF6. In acute inflammatory
response, may activate expression of acute phase response (APR)
genes. 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. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Exclusively expressed in adult liver.
Differentially expressed in cancer cell lines.
{ECO:0000269|PubMed:15800215}.
-!- INDUCTION: By IL6. Proinflammatory cytokines and
lipopolysaccharide activate the UPR and induce cleavage of CREBH
in the liver. {ECO:0000269|PubMed:16469704}.
-!- PTM: 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 (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; AF392874; AAM73673.1; -; mRNA.
EMBL; AK050186; BAC34115.1; -; mRNA.
EMBL; AK077258; BAC36714.1; -; mRNA.
EMBL; BC010786; AAH10786.1; -; mRNA.
EMBL; BC028820; AAH28820.1; -; mRNA.
CCDS; CCDS24043.1; -.
RefSeq; NP_663340.1; NM_145365.3.
UniGene; Mm.294693; -.
ProteinModelPortal; Q91XE9; -.
BioGrid; 229005; 1.
STRING; 10090.ENSMUSP00000112836; -.
iPTMnet; Q91XE9; -.
PhosphoSitePlus; Q91XE9; -.
MaxQB; Q91XE9; -.
PaxDb; Q91XE9; -.
PRIDE; Q91XE9; -.
Ensembl; ENSMUST00000117422; ENSMUSP00000112836; ENSMUSG00000035041.
GeneID; 208677; -.
KEGG; mmu:208677; -.
UCSC; uc007gfw.1; mouse.
CTD; 84699; -.
MGI; MGI:2384786; Creb3l3.
eggNOG; KOG0709; Eukaryota.
eggNOG; ENOG410ZZQM; LUCA.
GeneTree; ENSGT00520000055538; -.
HOGENOM; HOG000059566; -.
HOVERGEN; HBG090496; -.
InParanoid; Q91XE9; -.
KO; K09048; -.
OMA; DLEMWSP; -.
OrthoDB; EOG091G07QR; -.
PhylomeDB; Q91XE9; -.
TreeFam; TF316079; -.
Reactome; R-MMU-8874211; CREB3 factors activate genes.
PMAP-CutDB; Q91XE9; -.
PRO; PR:Q91XE9; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000035041; -.
CleanEx; MM_CREB3L3; -.
Genevisible; Q91XE9; MM.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
GO; GO:0035497; F:cAMP response element binding; IEA:InterPro.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:InterPro.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IMP:ParkinsonsUK-UCL.
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 1 479 Cyclic AMP-responsive element-binding
protein 3-like protein 3.
/FTId=PRO_0000288075.
CHAIN 1 ? Processed cyclic AMP-responsive element-
binding protein 3-like protein 3.
/FTId=PRO_0000307123.
TOPO_DOM 1 317 Cytoplasmic. {ECO:0000255}.
TRANSMEM 318 338 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 339 479 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}.
SITE 359 360 Cleavage; by PS1. {ECO:0000250}.
CARBOHYD 411 411 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 418 418 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 425 425 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 270 270 R -> L (in Ref. 2; BAC34115).
{ECO:0000305}.
SEQUENCE 479 AA; 52145 MW; 948A06FE79DB3779 CRC64;
MDGDIAAGKM ASPVCAMAPL DSMEVLDLLF DRQDGILRNV ELAEGWILAR EEQKVLLNSD
SDEFLNCILG PGDSDPSSPL WSPADSDSGI SEDLPSDPQD TPPRSGTEPA NTVARCHTRE
QGKGPCPSYL PSTPCPEPPR TQVQESSVAI DLDMWSTDTL YPEEPAGSPS RFNLTVKELL
LSGGSGDLQQ HSLAASQLLG PGSGHCQELV LTEDEKKLLA KEGVTLPTQL PLTKYEERVL
KKIRRKIRNK QSAQESRKKK KEYIDGLENR MSACTAQNQE LQRKVLHLEK QNLSLLEQLK
HLQALVVQST SKPAHAGTCI AVLLLSFALI ILPSISPFNS NKVDSPGDFV PVRVFSRTLH
NHAASRVAPD VTPGSEVPGP WPDVGTPHKG PSSGGLSADW GNFLEIPMLD NLTEELDNST
LVLANSTEDL GRATLLDWVA SEPLLSPGRV GLEIPGEMWL SWVPRWLRVR LVQDALGVL


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