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Protein

Cyclic AMP-responsive element-binding protein 3-like protein 2

Gene

Creb3l2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Transcription factor involved in unfolded protein response (UPR). In the absence of endoplasmic reticulum (ER) stress, inserted into ER membranes, with N-terminal DNA-binding and transcription activation domains oriented toward the cytosolic face of the membrane. In response to ER stress, transported to the Golgi, where it is cleaved in a site-specific manner by resident proteases S1P/MBTPS1 and S2P/MBTPS2. The released N-terminal cytosolic domain is translocated to the nucleus to effect transcription of specific target genes. Plays a critical role in chondrogenesis by activating the transcription of SEC23A, which promotes the transport and secretion of cartilage matrix proteins, and possibly that of ER biogenesis-related genes. In a neuroblastoma cell line, protects cells from ER stress-induced death. In vitro activates transcription of target genes via direct binding to the CRE site.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Transcription, Transcription regulation, Unfolded protein response

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclic AMP-responsive element-binding protein 3-like protein 2
Short name:
cAMP-responsive element-binding protein 3-like protein 2
Alternative name(s):
SCI-related protein Ra69
Cleaved into the following chain:
Gene namesi
Name:Creb3l2
Synonyms:Ra69
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi1306040. Creb3l2.

Subcellular locationi

  • Endoplasmic reticulum membrane By similarity; Single-pass type II membrane protein By similarity

  • Note: ER membrane resident protein. Upon ER stress, translocated to the Golgi apparatus where it is cleaved. The cytosolic N-terminal fragment (processed cyclic AMP-responsive element-binding protein 3-like protein 1) is transported into the nucleus.By similarity
Processed cyclic AMP-responsive element-binding protein 3-like protein 2 :
  • Nucleus By similarity

  • Note: Upon ER stress, translocated into the nucleus.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 378378CytoplasmicSequence analysisAdd
BLAST
Transmembranei379 – 39921Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini400 – 521122LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 521521Cyclic AMP-responsive element-binding protein 3-like protein 2PRO_0000288070Add
BLAST
Chaini1 – ?Processed cyclic AMP-responsive element-binding protein 3-like protein 2PRO_0000296212

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei93 – 931PhosphoserineBy similarity
Cross-linki178 – 178Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei191 – 1911PhosphoserineBy similarity
Glycosylationi505 – 5051N-linked (GlcNAc...)Sequence analysis
Glycosylationi518 – 5181N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Upon ER stress, translocated to the Golgi apparatus, where it is processed by regulated intramembrane proteolysis (RIP) to release the cytosol-facing N-terminal transcription factor domain. The cleavage is performed sequentially by site-1 and site-2 proteases (S1P/MBTPS1 and S2P/MBTPS2).By similarity
N-glycosylated.By similarity
Ubiquitinated by HRD1/SYVN1; undergoes 'Lys-48'-linked ubiquitination, followed by rapid proteasomal degradation under normal conditions. Upon ER stress, SYVN1 E3 ubiquitin-protein ligase dissociates from its substrate, ubiquitination does not occur and CREB3L2 is stabilized.By similarity

Keywords - PTMi

Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ6QDP7.

Expressioni

Gene expression databases

BgeeiENSRNOG00000012826.
GenevisibleiQ6QDP7. RN.

Interactioni

Subunit structurei

Binds DNA as a dimer.By similarity

Protein-protein interaction databases

BioGridi263374. 2 interactions.
STRINGi10116.ENSRNOP00000017338.

Structurei

3D structure databases

ProteinModelPortaliQ6QDP7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini294 – 35764bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni296 – 32530Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni336 – 35722Leucine-zipperPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi427 – 4304S1P recognitionBy similarity

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

eggNOGiKOG0709. Eukaryota.
ENOG410ZZQM. LUCA.
GeneTreeiENSGT00520000055538.
HOGENOMiHOG000060150.
HOVERGENiHBG057480.
InParanoidiQ6QDP7.
KOiK09048.
OMAiHFTEFLD.
OrthoDBiEOG091G081Z.
PhylomeDBiQ6QDP7.
TreeFamiTF316079.

Family and domain databases

InterProiIPR029804. BBF2H7.
IPR004827. bZIP.
[Graphical view]
PANTHERiPTHR22952:SF96. PTHR22952:SF96. 1 hit.
PfamiPF00170. bZIP_1. 1 hit.
[Graphical view]
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q6QDP7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVLESGEQS VLQWDRKLSE LSEPGETEAL MYHTHFSELL DEFSQNVLGQ
60 70 80 90 100
LLNDPFLSEK SVSMEVEPSP TSPAPLIQAE HSYSLSEEPR AQSPFTHVAA
110 120 130 140 150
SDGFNDEEVE SEKWYLSTEF PSATIKTEPI TEEQPPGLVP SVTLTITAIS
160 170 180 190 200
TPFEKEESPL DMSAGGDSSC QTLIPKIKLE PHEVDQFLNF SPKEASVDQL
210 220 230 240 250
HLPPTPPSSH SSDSEGSLSP NPRLHPFSLS QAHSPGRAMP RGPSALSTSP
260 270 280 290 300
LLTAPHKLQG SGPLVLTEEE KRTLIAEGYP IPTKLPLTKS EEKALKKIRR
310 320 330 340 350
KIKNKISAQE SRRKKKEYMD SLEKKVESCS TENLELRKKV EVLENTNRTL
360 370 380 390 400
LQQLQKLQTL VMGKVSRTCK LAGTQTGTCL MVVVLCFAVA FGSLFQGYGL
410 420 430 440 450
YPSATKMALP SQHPLSEPYT ASVVRSRNLL IYEEHSSLEE SSSPASAGEL
460 470 480 490 500
GGWDRGSSLL RASSGLEALP EVDLPHFIIS KETSLEKSVL LELQQHLVSS
510 520
KLEGNETLKV VELERRVNAT F
Length:521
Mass (Da):57,379
Last modified:July 5, 2004 - v1
Checksum:iE3949549518855E9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY546001 mRNA. Translation: AAS49162.1.
RefSeqiNP_001012188.1. NM_001012188.1.
UniGeneiRn.23031.

Genome annotation databases

EnsembliENSRNOT00000017338; ENSRNOP00000017338; ENSRNOG00000012826.
GeneIDi362339.
KEGGirno:362339.
UCSCiRGD:1306040. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY546001 mRNA. Translation: AAS49162.1.
RefSeqiNP_001012188.1. NM_001012188.1.
UniGeneiRn.23031.

3D structure databases

ProteinModelPortaliQ6QDP7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi263374. 2 interactions.
STRINGi10116.ENSRNOP00000017338.

Proteomic databases

PaxDbiQ6QDP7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000017338; ENSRNOP00000017338; ENSRNOG00000012826.
GeneIDi362339.
KEGGirno:362339.
UCSCiRGD:1306040. rat.

Organism-specific databases

CTDi64764.
RGDi1306040. Creb3l2.

Phylogenomic databases

eggNOGiKOG0709. Eukaryota.
ENOG410ZZQM. LUCA.
GeneTreeiENSGT00520000055538.
HOGENOMiHOG000060150.
HOVERGENiHBG057480.
InParanoidiQ6QDP7.
KOiK09048.
OMAiHFTEFLD.
OrthoDBiEOG091G081Z.
PhylomeDBiQ6QDP7.
TreeFamiTF316079.

Miscellaneous databases

PROiQ6QDP7.

Gene expression databases

BgeeiENSRNOG00000012826.
GenevisibleiQ6QDP7. RN.

Family and domain databases

InterProiIPR029804. BBF2H7.
IPR004827. bZIP.
[Graphical view]
PANTHERiPTHR22952:SF96. PTHR22952:SF96. 1 hit.
PfamiPF00170. bZIP_1. 1 hit.
[Graphical view]
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCR3L2_RAT
AccessioniPrimary (citable) accession number: Q6QDP7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: July 5, 2004
Last modified: September 7, 2016
This is version 92 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.