Cyclic AMP-responsive element-binding protein 3

NameCyclic AMP-responsive element-binding protein 3
SynonymsCREB-3 Leucine zipper protein Luman LZIP Transcription factor LZIP-alpha
Gene NameCREB3
OrganismHuman
Amino acid sequence
>lcl|BSEQ0009196|Cyclic AMP-responsive element-binding protein 3
MELELDAGDQDLLAFLLEESGDLGTAPDEAVRAPLDWALPLSEVPSDWEVDDLLCSLLSP
PASLNILSSSNPCLVHHDHTYSLPRETVSMDLGECEISLTGRTGFMGLAIHTFPFAESES
CRKEGTQMTPQHMEELAEQEIARLVLTDEEKSLLEKEGLILPETLPLTKTEEQILKRVRR
KIRNKRSAQESRRKKKVYVGGLESRVLKYTAQNMELQNKVQLLEEQNLSLLDQLRKLQAM
VIEISNKTSSSSTCILVLLVSFCLLLVPAMYSSDTRGSLPAEHGVLSRQLRALPSEDPYQ
LELPALQSEVPKDSTHQWLDGSDCVLQAPGNTSCLLHYMPQAPSAEPPLEWPFPDLFSEP
LCRGPILPLQANLTRKGGWLPTGSPSVILQDRYSG
Number of residues395
Molecular Weight43916.65
Theoretical pINone
GO Classification
Functions
    cAMP response element binding
RNA polymerase II core promoter proximal region sequence-specific DNA binding
CCR1 chemokine receptor binding
transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding
DNA binding
protein homodimerization activity
transcription factor activity, sequence-specific DNA binding
cAMP response element binding protein binding
protein dimerization activity
chromatin binding
transcription factor activity, RNA polymerase II core promoter proximal region sequence-specific binding
RNA polymerase II regulatory region sequence-specific DNA binding
Processes
    regulation of cell growth
positive regulation of transcription from RNA polymerase II promoter
chemotaxis
transcription from RNA polymerase II promoter
establishment of viral latency
positive regulation of calcium ion transport
negative regulation of ligand-dependent nuclear receptor transcription coactivator activity
positive regulation of monocyte chemotaxis
induction of positive chemotaxis
positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response
transcription, DNA-templated
negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway
release from viral latency
response to endoplasmic reticulum stress
positive regulation of deacetylase activity
regulation of cell proliferation
positive regulation of defense response to virus by host
cytoplasmic sequestering of transcription factor
positive regulation of cell migration
viral process
positive regulation of transcription, DNA-templated
negative regulation of cell cycle
Components
    Golgi membrane
neuronal cell body
cytoplasm
Golgi apparatus
membrane
integral component of membrane
cytosol
nucleus
endoplasmic reticulum
endoplasmic reticulum membrane
nuclear body
integral component of endoplasmic reticulum membrane
General FunctionTranscriptional activator activity, rna polymerase ii core promoter proximal region sequence-specific binding
Specific FunctionEndoplasmic 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 also a role in the human immunodeficiency virus type 1 (HIV-1) virus protein expression and in the herpes simplex virus-1 (HSV-1) latent infection and reactivation from latency. Isoform 2 plays a role in the unfolded protein response (UPR). Isoform 2 acts as a positive regulator of LKN-1/CCL15-induced chemotaxis signaling of leukocyte cell migration. Isoform 2 may play a role as a cellular tumor suppressor that is targeted by the hepatitis C virus (HSV) core protein. Isoform 2 represses the VP16-mediated transactivation of immediate early genes of the HSV-1 virus by sequestring host cell factor-1 HCFC1 in the ER membrane of sensory neurons, thereby preventing the initiation of the replicative cascade leading to latent infection. Isoform 3 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). Isoform 3 decreases the acetylation level of histone H4. Isoform 3 does not promote the chemotactic activity of leukocyte cells.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. Activates transcription of genes required for reactivation of the latent HSV-1 virus. Down-regulates Tat-dependent transcription of the HIV-1 LTR by interacting with HIV-1 Tat. It's transcriptional activity is inhibited by CREBZF in a HCFC1-dependent manner, by the viral transactivator protein VP16 and by the HCV core protein. Binds DNA to the cAMP response element (CRE) (consensus: 5'-GTGACGT[AG][AG]-3') and C/EBP sequences present in many viral and 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.
Transmembrane Regions255-271
GenBank Protein ID
UniProtKB IDO43889
UniProtKB Entry NameCREB3_HUMAN
Cellular LocationEndoplasmic reticulum membrane
Gene sequence
>lcl|BSEQ0013664|Cyclic AMP-responsive element-binding protein 3 (CREB3)
ATGGAGCTGGAATTGGATGCTGGTGACCAAGACCTGCTGGCCTTCCTGCTAGAGGAAAGT
GGAGATTTGGGGACGGCACCCGATGAGGCCGTGAGGGCCCCACTGGACTGGGCGCTGCCG
CTTTCTGAGGTACCGAGCGACTGGGAAGTAGATGATTTGCTGTGCTCCCTGCTGAGTCCC
CCAGCGTCGTTGAACATTCTCAGCTCCTCCAACCCCTGCCTTGTCCACCATGACCACACC
TACTCCCTCCCACGGGAAACTGTCTCTATGGATCTAGAGAGTGAGAGCTGTAGAAAAGAG
GGGACCCAGATGACTCCACAGCATATGGAGGAGCTGGCAGAGCAGGAGATTGCTAGGCTA
GTACTGACAGATGAGGAGAAGAGTCTATTGGAGAAGGAGGGGCTTATTCTGCCTGAGACA
CTTCCTCTCACTAAGACAGAGGAACAAATTCTGAAACGTGTGCGGAGGAAGATTCGAAAT
AAAAGATCTGCTCAAGAGAGCCGCAGGAAAAAGAAGGTGTATGTTGGGGGTTTAGAGAGC
AGGGTCTTGAAATACACAGCCCAGAATATGGAGCTTCAGAACAAAGTACAGCTTCTGGAG
GAACAGAATTTGTCCCTTCTAGATCAACTGAGGAAACTCCAGGCCATGGTGATTGAGATA
TCAAACAAAACCAGCAGCAGCAGCACCTGCATCTTGGTCCTACTAGTCTCCTTCTGCCTC
CTCCTTGTACCTGCTATGTACTCCTCTGACACAAGGGGGAGCCTGCCAGCTGAGCATGGA
GTGTTGTCCCGCCAGCTTCGTGCCCTCCCCAGTGAGGACCCTTACCAGCTGGAGCTGCCT
GCCCTGCAGTCAGAAGTGCCGAAAGACAGCACACACCAGTGGTTGGACGGCTCAGACTGT
GTACTCCAGGCCCCTGGCAACACTTCCTGCCTGCTGCATTACATGCCTCAGGCTCCCAGT
GCAGAGCCTCCCCTGGAGTGGCCATTCCCTGACCTCTTCTCAGAGCCTCTCTGCCGAGGT
CCCATCCTCCCCCTGCAGGCAAATCTCACAAGGAAGGGAGGATGGCTTCCTACTGGTAGC
CCCTCTGTCATTTTGCAGGACAGATACTCAGGCTAG
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC IDHGNC:2347
Chromosome Location9
LocusNone
References
  1. Lu R, Yang P, O'Hare P, Misra V: Luman, a new member of the CREB/ATF family, binds to herpes simplex virus VP16-associated host cellular factor. Mol Cell Biol. 1997 Sep;17(9):5117-26.[9271389 ]
  2. Freiman RN, Herr W: Viral mimicry: common mode of association with HCF by VP16 and the cellular protein LZIP. Genes Dev. 1997 Dec 1;11(23):3122-7.[9389645 ]
  3. Jin DY, Wang HL, Zhou Y, Chun AC, Kibler KV, Hou YD, Kung H, Jeang KT: Hepatitis C virus core protein-induced loss of LZIP function correlates with cellular transformation. EMBO J. 2000 Feb 15;19(4):729-40.[10675342 ]
  4. Kang H, Kim YS, Ko J: A novel isoform of human LZIP negatively regulates the transactivation of the glucocorticoid receptor. Mol Endocrinol. 2009 Nov;23(11):1746-57. doi: 10.1210/me.2009-0009. Epub 2009 Sep 24.[19779205 ]
  5. Lu R, Misra V: Potential role for luman, the cellular homologue of herpes simplex virus VP16 (alpha gene trans-inducing factor), in herpesvirus latency. J Virol. 2000 Jan;74(2):934-43.[10623756 ]
  6. Mahajan SS, Wilson AC: Mutations in host cell factor 1 separate its role in cell proliferation from recruitment of VP16 and LZIP. Mol Cell Biol. 2000 Feb;20(3):919-28.[10629049 ]
  7. Luciano RL, Wilson AC: N-terminal transcriptional activation domain of LZIP comprises two LxxLL motifs and the host cell factor-1 binding motif. Proc Natl Acad Sci U S A. 2000 Sep 26;97(20):10757-62.[10984507 ]
  8. Raggo C, Rapin N, Stirling J, Gobeil P, Smith-Windsor E, O'Hare P, Misra V: Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis. Mol Cell Biol. 2002 Aug;22(16):5639-49.[12138176 ]
  9. Ko J, Jang SW, Kim YS, Kim IS, Sung HJ, Kim HH, Park JY, Lee YH, Kim J, Na DS: Human LZIP binds to CCR1 and differentially affects the chemotactic activities of CCR1-dependent chemokines. FASEB J. 2004 May;18(7):890-2. Epub 2004 Mar 4.[15001559 ]
  10. DenBoer LM, Hardy-Smith PW, Hogan MR, Cockram GP, Audas TE, Lu R: Luman is capable of binding and activating transcription from the unfolded protein response element. Biochem Biophys Res Commun. 2005 May 27;331(1):113-9.[15845366 ]
  11. Misra V, Rapin N, Akhova O, Bainbridge M, Korchinski P: Zhangfei is a potent and specific inhibitor of the host cell factor-binding transcription factor Luman. J Biol Chem. 2005 Apr 15;280(15):15257-66. Epub 2005 Feb 9.[15705566 ]
  12. Blot G, Lopez-Verges S, Treand C, Kubat NJ, Delcroix-Genete D, Emiliani S, Benarous R, Berlioz-Torrent C: Luman, a new partner of HIV-1 TMgp41, interferes with Tat-mediated transcription of the HIV-1 LTR. J Mol Biol. 2006 Dec 15;364(5):1034-47. Epub 2006 Oct 3.[17054986 ]
  13. Liang G, Audas TE, Li Y, Cockram GP, Dean JD, Martyn AC, Kokame K, Lu R: Luman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress response protein Herp through an ER stress response element. Mol Cell Biol. 2006 Nov;26(21):7999-8010. Epub 2006 Aug 28.[16940180 ]
  14. Jang SW, Kim YS, Kim YR, Sung HJ, Ko J: Regulation of human LZIP expression by NF-kappaB and its involvement in monocyte cell migration induced by Lkn-1. J Biol Chem. 2007 Apr 13;282(15):11092-100. Epub 2007 Feb 12.[17296613 ]
  15. Sung HJ, Kim YS, Kang H, Ko J: Human LZIP induces monocyte CC chemokine receptor 2 expression leading to enhancement of monocyte chemoattractant protein 1/CCL2-induced cell migration. Exp Mol Med. 2008 Jun 30;40(3):332-8.[18587271 ]
  16. Audas TE, Li Y, Liang G, Lu R: A novel protein, Luman/CREB3 recruitment factor, inhibits Luman activation of the unfolded protein response. Mol Cell Biol. 2008 Jun;28(12):3952-66. doi: 10.1128/MCB.01439-07. Epub 2008 Apr 7.[18391022 ]
  17. Eleveld-Trancikova D, Sanecka A, van Hout-Kuijer MA, Looman MW, Hendriks IA, Jansen BJ, Adema GJ: DC-STAMP interacts with ER-resident transcription factor LUMAN which becomes activated during DC maturation. Mol Immunol. 2010 Jul;47(11-12):1963-73. doi: 10.1016/j.molimm.2010.04.019. Epub 2010 May 23.[20546900 ]
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