CR3L2_DANRE
ID CR3L2_DANRE Reviewed; 519 AA.
AC A1L224;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Cyclic AMP-responsive element-binding protein 3-like protein 2;
DE Short=cAMP-responsive element-binding protein 3-like protein 2;
DE Contains:
DE RecName: Full=Processed cyclic AMP-responsive element-binding protein 3-like protein 2;
GN Name=creb3l2; ORFNames=zgc:158603;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription factor involved in unfolded protein response
CC (UPR). In the absence of endoplasmic reticulum (ER) stress, inserted
CC into ER membranes, with N-terminal DNA-binding and transcription
CC activation domains oriented toward the cytosolic face of the membrane.
CC In response to ER stress, transported to the Golgi, where it is cleaved
CC in a site-specific manner by resident proteases S1P/mbtps1 and
CC S2P/mbtps2. The released N-terminal cytosolic domain is translocated to
CC the nucleus to effect transcription of specific target genes. Plays a
CC critical role in chondrogenesis. May protect neuroblastoma cells from
CC ER stress-induced death. In vitro activates transcription of target
CC genes via direct binding to the CRE site.
CC {ECO:0000250|UniProtKB:Q8BH52}.
CC -!- SUBUNIT: Binds DNA as a dimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8BH52}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q8BH52}. Note=ER membrane resident protein. Upon
CC ER stress, translocated to the Golgi apparatus where it is cleaved. The
CC cytosolic N-terminal fragment (processed cyclic AMP-responsive element-
CC binding protein 3-like protein 1) is transported into the nucleus.
CC {ECO:0000250|UniProtKB:Q8BH52}.
CC -!- SUBCELLULAR LOCATION: [Processed cyclic AMP-responsive element-binding
CC protein 3-like protein 2]: Nucleus {ECO:0000250|UniProtKB:Q8BH52}.
CC Note=Upon ER stress, translocated into the nucleus.
CC {ECO:0000250|UniProtKB:Q8BH52}.
CC -!- PTM: Upon ER stress, translocated to the Golgi apparatus, where it is
CC processed by regulated intramembrane proteolysis (RIP) to release the
CC cytosol-facing N-terminal transcription factor domain. The cleavage is
CC performed sequentially by site-1 and site-2 proteases (S1P/mbtps1 and
CC S2P/mbtps2). {ECO:0000250|UniProtKB:Q8BH52}.
CC -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC129318; AAI29319.1; -; mRNA.
DR RefSeq; NP_001074120.1; NM_001080651.2.
DR AlphaFoldDB; A1L224; -.
DR SMR; A1L224; -.
DR STRING; 7955.ENSDARP00000087416; -.
DR PaxDb; A1L224; -.
DR PRIDE; A1L224; -.
DR Ensembl; ENSDART00000092984; ENSDARP00000087416; ENSDARG00000063563.
DR Ensembl; ENSDART00000158466; ENSDARP00000130319; ENSDARG00000063563.
DR GeneID; 791169; -.
DR KEGG; dre:791169; -.
DR CTD; 64764; -.
DR ZFIN; ZDB-GENE-070112-1542; creb3l2.
DR eggNOG; KOG0709; Eukaryota.
DR GeneTree; ENSGT00940000157659; -.
DR HOGENOM; CLU_037638_0_0_1; -.
DR InParanoid; A1L224; -.
DR OMA; IQVEHSY; -.
DR OrthoDB; 644485at2759; -.
DR PhylomeDB; A1L224; -.
DR TreeFam; TF316079; -.
DR PRO; PR:A1L224; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 4.
DR Bgee; ENSDARG00000063563; Expressed in caudal fin and 31 other tissues.
DR ExpressionAtlas; A1L224; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0035497; F:cAMP response element binding; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0051216; P:cartilage development; ISS:UniProtKB.
DR GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; IMP:ZFIN.
DR GO; GO:0003330; P:regulation of extracellular matrix constituent secretion; IMP:ZFIN.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR InterPro; IPR029804; BBF2H7.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR46004:SF2; PTHR46004:SF2; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 2: Evidence at transcript level;
KW Activator; Developmental protein; DNA-binding; Endoplasmic reticulum;
KW Glycoprotein; Membrane; Nucleus; Reference proteome; Signal-anchor;
KW Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix; Unfolded protein response.
FT CHAIN 1..519
FT /note="Cyclic AMP-responsive element-binding protein 3-like
FT protein 2"
FT /id="PRO_0000288071"
FT CHAIN 1..?
FT /note="Processed cyclic AMP-responsive element-binding
FT protein 3-like protein 2"
FT /id="PRO_0000296213"
FT TOPO_DOM 1..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..519
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 291..354
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 58..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..322
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 333..354
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT MOTIF 423..426
FT /note="S1P recognition"
FT /evidence="ECO:0000250|UniProtKB:Q70SY1"
FT COMPBIAS 202..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 519 AA; 56901 MW; F1A6F0E891ADD496 CRC64;
MEIMDSGEPF LQWDKNLSEL SEAGENDILY STHFTDLLDD LSQEALLGQL LSDPFLSGRG
DAMDTEEELT RASPVPPHIQ AEHSYSLCGD SRPQSPLSHL PGEPGSDAAD SESDEWPMEQ
EDKGIKMEPL LCVPLPALTL TVTPAGSAPE PVIDSCDSAQ SLSLPQVKED SNSPQIKLEP
HEVDQFLNLS PKGLECLQMP PTPPSSVGSD SEGSQSPVHP CAPASPTQTP AVLKVAPRAP
SSLSSSPLLT APHKLQGSGP LLLTEEEKRT LIAEGYPVPT KLPLSKAEEK ALKKIRRKIK
NKISAQESRR KKKEYVDALE KKVETCSNEN HELRRKVENL ECTNKSLLQQ LHSLQAVVAG
KVPRSCRVTG TQTSTCLMVV VLCFSLFLGS FYPGLSPCSS ITKADLSREI SIHDSYTTTV
KSRSLLSIQE PGGLDEPHPI GLGGEYPEWD RQADVMAAWR FEQQHKEEEA ELHKAEHRPL
LLSTNETHAQ KAILIDLHTH RSNETAKVIQ LDRTVNETS
