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

 CREB3_MOUSE             Reviewed;         404 AA.
Q61817; Q99M21; Q9CVK9;
09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
09-NOV-2004, sequence version 2.
12-SEP-2018, entry version 146.
RecName: Full=Cyclic AMP-responsive element-binding protein 3;
Short=CREB-3;
Short=cAMP-responsive element-binding protein 3;
AltName: Full=Transcription factor LZIP;
Contains:
RecName: Full=Processed cyclic AMP-responsive element-binding protein 3;
Name=Creb3; Synonyms=Lzip;
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 (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ;
PubMed=8112612; DOI=10.1016/0378-1119(94)90763-3;
Burbelo P.D., Gabriel G.C., Kibbey M.C., Yamada Y., Kleinman H.K.,
Weeks B.S.;
"LZIP-1 and LZIP-2: two novel members of the bZIP family.";
Gene 139:241-245(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-404.
STRAIN=C57BL/6J; TISSUE=Pancreas;
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).
-!- FUNCTION: Endoplasmic reticulum (ER)-bound sequence-specific
transcription factor that directly binds DNA and activates
transcription. Plays a role in the unfolded protein response
(UPR), promoting cell survival versus ER stress-induced apoptotic
cell death. Also involved in cell proliferation, migration and
differentiation, tumor suppression and inflammatory gene
expression. Acts as a positive regulator of LKN-1/CCL15-induced
chemotaxis signaling of leukocyte cell migration. Associates with
chromatin to the HERPUD1 promoter. Also induces transcriptional
activation of chemokine receptors. Functions as a negative
transcriptional regulator in ligand-induced transcriptional
activation of the glucocorticoid receptor NR3C1 by recruiting and
activating histone deacetylases (HDAC1, HDAC2 and HDAC6). Also
decreases the acetylation level of histone H4. Does not promote
the chemotactic activity of leukocyte cells.
{ECO:0000250|UniProtKB:O43889}.
-!- FUNCTION: Processed cyclic AMP-responsive element-binding protein
3: This is the transcriptionally active form that translocates to
the nucleus and activates unfolded protein response (UPR) target
genes during endoplasmic reticulum (ER) stress response. Binds the
cAMP response element (CRE) (consensus: 5'-GTGACGT[AG][AG]-3') and
C/EBP sequences present in many promoters to activate
transcription of the genes. Binds to the unfolded protein response
element (UPRE) consensus sequences sites. Binds DNA to the 5'-
CCAC[GA]-3'half of ERSE II (5'-ATTGG-N-CCACG-3').
{ECO:0000250|UniProtKB:O43889}.
-!- SUBUNIT: Homodimer. Interacts with HCFC1; the interaction is
required to stimulate CREB3 transcriptional activity. Interacts
with CREBZF; the interaction occurs only in combination with
HCFC1. Interacts (via central part and transmembrane region) with
DCSTAMP (via C-terminus cytoplasmic domain). Interacts with OS9.
Interacts (via leucine-zipper domain) with CREBRF (via leucine-
zipper domain); the interaction occurs only after CREB3 activation
and promotes CREB3 degradation. Interacts (via C-terminal domain)
with CCR1. {ECO:0000250|UniProtKB:O43889}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:O43889}; Single-pass type II membrane
protein {ECO:0000250|UniProtKB:O43889, ECO:0000255}. Golgi
apparatus {ECO:0000250|UniProtKB:O43889}. Nucleus
{ECO:0000250|UniProtKB:O43889}. Cytoplasm
{ECO:0000250|UniProtKB:O43889}. Note=Colocalizes with HCFC1 in
neuronal cell bodies of the trigeminal ganglia. Colocalizes with
DCSTAMP in the ER membrane of immature dendritic cell (DC).
Colocalizes with CANX, CCR1, HCFC1 in the ER membrane.
{ECO:0000250|UniProtKB:O43889}.
-!- SUBCELLULAR LOCATION: Processed cyclic AMP-responsive element-
binding protein 3: Nucleus {ECO:0000250|UniProtKB:O43889}.
Note=Upon RIP activation the transcriptional active processed
cyclic AMP-responsive element-binding protein 3 form translocates
into the nucleus. Detected in the nucleus upon dendritic cell
maturation and RIP activation. Colocalizes with CREBRF in nuclear
foci. Colocalizes with CREBZF in promyelocytic leukemia protein
nuclear bodies (PML-NB). {ECO:0000250|UniProtKB:O43889}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=LZIP-1;
IsoId=Q61817-1; Sequence=Displayed;
Name=2; Synonyms=LZIP-2;
IsoId=Q61817-2; Sequence=VSP_011839;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:8112612}.
-!- PTM: First proteolytically cleaved by site-1 protease (S1P) that
generates membrane-associated N-terminus and a luminal C-terminus
forms. The membrane-associated N-terminus form is further
proteolytically processed probably by the site-2 protease (S2P)
through a regulated intramembrane proteolysis (RIP), releasing the
transcriptional active processed cyclic AMP-responsive element-
binding protein 3 form, which is transported to the nucleus. The
proteolytic cleavage is strongly induced during dendritic cell
(DC) maturation and inhibited by DCSTAMP. That form is rapidly
degraded. {ECO:0000250|UniProtKB:O43889}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:O43889}.
-!- SIMILARITY: Belongs to the bZIP family. ATF subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L22167; AAC37645.1; -; Unassigned_DNA.
EMBL; BC002094; AAH02094.1; -; mRNA.
EMBL; AK007665; BAB25173.1; -; mRNA.
CCDS; CCDS18102.1; -. [Q61817-2]
UniGene; Mm.12407; -.
ProteinModelPortal; Q61817; -.
SMR; Q61817; -.
IntAct; Q61817; 1.
PhosphoSitePlus; Q61817; -.
PRIDE; Q61817; -.
MGI; MGI:99946; Creb3.
HOGENOM; HOG000133026; -.
HOVERGEN; HBG051114; -.
InParanoid; Q61817; -.
PhylomeDB; Q61817; -.
PRO; PR:Q61817; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_CREB3; -.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; ISO:MGI.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
GO; GO:0016604; C:nuclear body; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0035497; F:cAMP response element binding; IEA:InterPro.
GO; GO:0008140; F:cAMP response element binding protein binding; ISO:MGI.
GO; GO:0031726; F:CCR1 chemokine receptor binding; ISO:MGI.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; ISO:MGI.
GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0000982; F:transcription factor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
GO; GO:0042994; P:cytoplasmic sequestering of transcription factor; ISS:UniProtKB.
GO; GO:0019043; P:establishment of viral latency; ISS:UniProtKB.
GO; GO:0050930; P:induction of positive chemotaxis; ISS:UniProtKB.
GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:2000326; P:negative regulation of nuclear receptor transcription coactivator activity; ISS:UniProtKB.
GO; GO:0051928; P:positive regulation of calcium ion transport; ISO:MGI.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:0090045; P:positive regulation of deacetylase activity; ISS:UniProtKB.
GO; GO:0002230; P:positive regulation of defense response to virus by host; ISS:UniProtKB.
GO; GO:0090026; P:positive regulation of monocyte chemotaxis; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0006990; P:positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; ISS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; ISO:MGI.
GO; GO:0019046; P:release from viral latency; ISS:UniProtKB.
GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; ISO:MGI.
InterPro; IPR004827; bZIP.
InterPro; IPR029808; Luman.
PANTHER; PTHR22952:SF100; PTHR22952:SF100; 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; Alternative splicing; Chemotaxis; Complete proteome;
Cytoplasm; DNA-binding; Endoplasmic reticulum; Glycoprotein;
Golgi apparatus; Membrane; Nucleus; Reference proteome; Repressor;
Signal-anchor; Transcription; Transcription regulation; Transmembrane;
Transmembrane helix; Unfolded protein response.
CHAIN 1 404 Cyclic AMP-responsive element-binding
protein 3.
/FTId=PRO_0000076603.
CHAIN 1 ? Processed cyclic AMP-responsive element-
binding protein 3.
/FTId=PRO_0000296205.
TOPO_DOM 1 261 Cytoplasmic. {ECO:0000255}.
TRANSMEM 262 282 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 283 404 Lumenal. {ECO:0000255}.
DOMAIN 185 248 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 187 225 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 227 248 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOTIF 19 23 LXXLL motif 1.
MOTIF 64 68 LXXLL motif 2.
MOTIF 87 90 HCFC1-binding-motif (HBM).
SITE 301 302 Cleavage; by PS1. {ECO:0000250}.
CARBOHYD 342 342 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 380 380 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 102 126 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_011839.
CONFLICT 263 263 S -> T (in Ref. 1; AAC37645).
{ECO:0000305}.
SEQUENCE 404 AA; 45112 MW; 96E4124256D4BD44 CRC64;
MDPGGQDLLA LDPGDQDLLG FLLEESGDLW AATEPDVKAS LDLELSPSEN SVQELSDWEV
EDLLSSLLSP SVSRDVLGSS SSSILHDHNY SLPQEHVSID LGECEMISCR GRRELTGLAG
STFPFADTES FEKEGFHVTP LPGEERAAEQ EMSRLILTEE EKKLLEKEGL TLPSTLPLTK
VEEQVLKRVR RKIRNKRAAQ ESRKKKKVYV VGLESRVLKY TAQNRELQNK VQRLEEQNLS
LLDQLRKLQA MVIEIANKTS SGSTCVLVLV FSFCLLLVPA MYSSDARGSV PAEYVVLHRK
LRALPSEDDH QPKPSALSSE LPMDSTHQSL DSSEHMFLVS SNFSCVLYHA PQAEQPLHWP
LWDLSSEMLF SDSNLLLQAN LSESEGWQPN HSPSLVIFQG RYSG


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