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Q61817

- CREB3_MOUSE

UniProt

Q61817 - CREB3_MOUSE

Protein

Cyclic AMP-responsive element-binding protein 3

Gene

Creb3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (09 Nov 2004)
      Previous versions | rss
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    Functioni

    Endoplasmic reticulum (ER)-bound transcription factor that plays a role in the unfolded protein response (UPR). Involved in cell proliferation and migration, tumor suppression and inflammatory gene expression. Plays a role in the unfolded protein response (UPR). Acts as a positive regulator of LKN-1/CCL15-induced chemotaxis signaling of leukocyte cell migration. 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). Decreases the acetylation level of histone H4. Does not promote the chemotactic activity of leukocyte cells By similarity.By similarity
    Processed cyclic AMP-responsive element-binding protein 3: acts as a transcription factor that activates unfolded protein response (UPR) target genes during endoplasmic reticulum (ER) stress response. Promotes cell survival against ER stress-induced apoptotic cell death during UPR. Activates transcription from CRE and C/EBP-containing reporter genes. Induces transcriptional activation of chemokine receptors. It's transcriptional activity is inhibited by CREBZF in a HCFC1-dependent manner. Binds DNA to the cAMP response element (CRE) (consensus: 5'-GTGACGT[AG][AG]-3') and C/EBP sequences present in many cellular promoters. Binds to the unfolded protein respons element (UPRE) consensus sequences sites. Binds DNA to the 5'-CCAC[GA]-3'half of ERSE II (5'-ATTGG-N-CCACG-3'). Associates with chromatin to the HERPUD1 promoter By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei301 – 3022Cleavage; by PS1By similarity

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. protein homodimerization activity Source: UniProtKB
    3. RNA polymerase II regulatory region sequence-specific DNA binding Source: UniProtKB
    4. sequence-specific DNA binding Source: MGI
    5. sequence-specific DNA binding transcription factor activity Source: UniProtKB

    GO - Biological processi

    1. chemotaxis Source: UniProtKB-KW
    2. cytoplasmic sequestering of transcription factor Source: UniProtKB
    3. establishment of viral latency Source: UniProtKB
    4. induction of positive chemotaxis Source: UniProtKB
    5. negative regulation of ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
    6. positive regulation of deacetylase activity Source: UniProtKB
    7. positive regulation of defense response to virus by host Source: UniProtKB
    8. positive regulation of monocyte chemotaxis Source: UniProtKB
    9. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    10. positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response Source: UniProtKB
    11. regulation of cell growth Source: UniProtKB
    12. release from viral latency Source: UniProtKB
    13. response to endoplasmic reticulum stress Source: UniProtKB
    14. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Chemotaxis, Transcription, Transcription regulation, Unfolded protein response

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclic AMP-responsive element-binding protein 3
    Short name:
    CREB-3
    Short name:
    cAMP-responsive element-binding protein 3
    Alternative name(s):
    Transcription factor LZIP
    Cleaved into the following chain:
    Gene namesi
    Name:Creb3
    Synonyms:Lzip
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:99946. Creb3.

    Subcellular locationi

    Endoplasmic reticulum membrane By similarity; Single-pass type II membrane protein By similarity. Membrane By similarity. Nucleus PROSITE-ProRule annotation. Cytoplasm By similarity
    Note: Colocalizes with TM7SF4 in the ER membrane of immature dendritic cell (DC). Colocalizes with CANX, CCR1, HCFC1 in the ER membrane. Colocalizes with HCFC1 in neuronal cell bodies of the trigeminal ganglia By similarity.By similarity
    Chain Processed cyclic AMP-responsive element-binding protein 3 : Nucleus PROSITE-ProRule annotation
    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) By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. endoplasmic reticulum membrane Source: UniProtKB
    3. Golgi membrane Source: UniProtKB
    4. integral component of endoplasmic reticulum membrane Source: UniProtKB
    5. membrane Source: UniProtKB
    6. neuronal cell body Source: UniProtKB
    7. nuclear body Source: UniProtKB
    8. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 404404Cyclic AMP-responsive element-binding protein 3PRO_0000076603Add
    BLAST
    Chaini1 – ?Processed cyclic AMP-responsive element-binding protein 3PRO_0000296205

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi342 – 3421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi380 – 3801N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The ER membrane embedded cyclic AMP-responsive element-binding protein 3 form is 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 TM7SF4 By similarity.By similarity
    The processed cyclic AMP-responsive element-binding protein 3 is rapidly degraded.By similarity
    N-glycosylated.By similarity

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PRIDEiQ61817.

    PTM databases

    PhosphoSiteiQ61817.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    CleanExiMM_CREB3.
    GenevestigatoriQ61817.

    Interactioni

    Subunit structurei

    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 TM7SF4 (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 By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ61817. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ61817.
    SMRiQ61817. Positions 157-242.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 261261CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini283 – 404122LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei262 – 28221Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini185 – 24864bZIPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni187 – 22539Basic motifPROSITE-ProRule annotationAdd
    BLAST
    Regioni227 – 24822Leucine-zipperPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi19 – 235LXXLL motif 1
    Motifi64 – 685LXXLL motif 2
    Motifi87 – 904HCFC1-binding-motif (HBM)

    Sequence similaritiesi

    Belongs to the bZIP family. ATF subfamily.Curated
    Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG254445.
    HOGENOMiHOG000133026.
    HOVERGENiHBG051114.
    PhylomeDBiQ61817.

    Family and domain databases

    InterProiIPR004827. bZIP.
    [Graphical view]
    PfamiPF00170. bZIP_1. 1 hit.
    [Graphical view]
    SMARTiSM00338. BRLZ. 1 hit.
    [Graphical view]
    PROSITEiPS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q61817-1) [UniParc]FASTAAdd to Basket

    Also known as: LZIP-1

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDPGGQDLLA LDPGDQDLLG FLLEESGDLW AATEPDVKAS LDLELSPSEN    50
    SVQELSDWEV EDLLSSLLSP SVSRDVLGSS SSSILHDHNY SLPQEHVSID 100
    LGECEMISCR GRRELTGLAG STFPFADTES FEKEGFHVTP LPGEERAAEQ 150
    EMSRLILTEE EKKLLEKEGL TLPSTLPLTK VEEQVLKRVR RKIRNKRAAQ 200
    ESRKKKKVYV VGLESRVLKY TAQNRELQNK VQRLEEQNLS LLDQLRKLQA 250
    MVIEIANKTS SGSTCVLVLV FSFCLLLVPA MYSSDARGSV PAEYVVLHRK 300
    LRALPSEDDH QPKPSALSSE LPMDSTHQSL DSSEHMFLVS SNFSCVLYHA 350
    PQAEQPLHWP LWDLSSEMLF SDSNLLLQAN LSESEGWQPN HSPSLVIFQG 400
    RYSG 404
    Length:404
    Mass (Da):45,112
    Last modified:November 9, 2004 - v2
    Checksum:i96E4124256D4BD44
    GO
    Isoform 2 (identifier: Q61817-2) [UniParc]FASTAAdd to Basket

    Also known as: LZIP-2

    The sequence of this isoform differs from the canonical sequence as follows:
         102-126: Missing.

    Show »
    Length:379
    Mass (Da):42,441
    Checksum:i442BC9840B919997
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti263 – 2631S → T in AAC37645. (PubMed:8112612)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei102 – 12625Missing in isoform 2. 1 PublicationVSP_011839Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L22167 Unassigned DNA. Translation: AAC37645.1.
    BC002094 mRNA. Translation: AAH02094.1.
    AK007665 mRNA. Translation: BAB25173.1.
    CCDSiCCDS18102.1. [Q61817-2]
    UniGeneiMm.12407.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L22167 Unassigned DNA. Translation: AAC37645.1 .
    BC002094 mRNA. Translation: AAH02094.1 .
    AK007665 mRNA. Translation: BAB25173.1 .
    CCDSi CCDS18102.1. [Q61817-2 ]
    UniGenei Mm.12407.

    3D structure databases

    ProteinModelPortali Q61817.
    SMRi Q61817. Positions 157-242.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q61817. 1 interaction.

    PTM databases

    PhosphoSitei Q61817.

    Proteomic databases

    PRIDEi Q61817.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    MGIi MGI:99946. Creb3.

    Phylogenomic databases

    eggNOGi NOG254445.
    HOGENOMi HOG000133026.
    HOVERGENi HBG051114.
    PhylomeDBi Q61817.

    Miscellaneous databases

    PROi Q61817.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_CREB3.
    Genevestigatori Q61817.

    Family and domain databases

    InterProi IPR004827. bZIP.
    [Graphical view ]
    Pfami PF00170. bZIP_1. 1 hit.
    [Graphical view ]
    SMARTi SM00338. BRLZ. 1 hit.
    [Graphical view ]
    PROSITEi PS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "LZIP-1 and LZIP-2: two novel members of the bZIP family."
      Burbelo P.D., Gabriel G.C., Kibbey M.C., Yamada Y., Kleinman H.K., Weeks B.S.
      Gene 139:241-245(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
      Strain: BALB/c.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: FVB/N.
      Tissue: Mammary tumor.
    3. "The transcriptional landscape of the mammalian genome."
      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.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-404.
      Strain: C57BL/6J.
      Tissue: Pancreas.

    Entry informationi

    Entry nameiCREB3_MOUSE
    AccessioniPrimary (citable) accession number: Q61817
    Secondary accession number(s): Q99M21, Q9CVK9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 9, 2004
    Last sequence update: November 9, 2004
    Last modified: October 1, 2014
    This is version 123 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3