CR3L2_XENLA
ID CR3L2_XENLA Reviewed; 525 AA.
AC A2VD01;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
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;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) 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}.
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DR EMBL; BC129061; AAI29062.1; -; mRNA.
DR RefSeq; NP_001091333.1; NM_001097864.1.
DR AlphaFoldDB; A2VD01; -.
DR SMR; A2VD01; -.
DR DNASU; 100037168; -.
DR GeneID; 100037168; -.
DR KEGG; xla:100037168; -.
DR CTD; 100037168; -.
DR Xenbase; XB-GENE-996214; creb3l2.L.
DR OrthoDB; 644485at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 100037168; Expressed in internal ear and 19 other tissues.
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; IEA:InterPro.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
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: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..525
FT /note="Cyclic AMP-responsive element-binding protein 3-like
FT protein 2"
FT /id="PRO_0000288072"
FT CHAIN 1..?
FT /note="Processed cyclic AMP-responsive element-binding
FT protein 3-like protein 2"
FT /id="PRO_0000296214"
FT TOPO_DOM 1..382
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 404..525
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 299..362
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 85..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..330
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 309..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..362
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT MOTIF 433..436
FT /note="S1P recognition"
FT /evidence="ECO:0000250|UniProtKB:Q70SY1"
FT COMPBIAS 86..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 525 AA; 57625 MW; 44644A533FA13D9F CRC64;
MEIMESGDPV IQWDRKLSEL SEAAESDSLY NNTPFSELLD DSALLDVLGQ LMGDPFLTEK
YEMMEVEMNP SSPSPMIKAE HSYSLCGDSR PQSPFTHASS DDNFSDTDLT GDDWCLNGEL
TATTPTTKIK VEIPLEETPG LTPSVTLATS AVSASPEVGV SSQLPVPEQV KLLSPVALPQ
IKLEPHEVDQ FLNLCPKEVA PTEALQMPPT PPSSHGSDSE GGQSPTRSLP PSSPVQSQAG
GKMAARSPSA LSNSPLLTAP HKLQGSGPLM LTEEEKRTLV AEGYPIPTKL PLTKAEEKAL
KKIRRKIKNK ISAQESRRKK KEYMDSLEKR VENSSSENSE LRKKVEVLES TNRTLLQQLQ
RLQAMVTGKV TRSCKAAGTQ TGTCLMMVVL CFAVIFGSFT QNLDMYSSSS KTIHEPSQYS
APESYAASIV RSRKLLIFEE HQAVEELHSS AVMLETQDTW EVQADTISKQ QAALLEELHL
SQEKPFSLSN DSSSDMPVRH RFTSEFGHND TTKVIELDRT VNTTS
