ID CR3L4_XENTR Reviewed; 428 AA.
AC Q08CW8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Cyclic AMP-responsive element-binding protein 3-like protein 4;
DE Short=cAMP-responsive element-binding protein 3-like protein 4;
DE Contains:
DE RecName: Full=Processed cyclic AMP-responsive element-binding protein 3-like protein 4;
GN Name=creb3l4;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=N6; TISSUE=Oviduct;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional activator. {ECO:0000250}.
CC -!- SUBUNIT: Binds DNA as a dimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Processed cyclic AMP-responsive element-binding
CC protein 3-like protein 4]: Nucleus {ECO:0000255|PROSITE-
CC ProRule:PRU00978}. Note=The cleaved N-terminal cytoplasmic domain
CC translocates into the nucleus. {ECO:0000250}.
CC -!- PTM: Controlled by regulated intramembrane proteolysis (RIP). A
CC fragment containing the cytoplasmic transcription factor domain is
CC released by proteolysis. The cleavage seems to be performed
CC sequentially by site-1 and site-2 proteases (PS1 and PS2) (By
CC similarity). {ECO:0000250}.
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; BC124053; AAI24054.1; -; mRNA.
DR RefSeq; NP_001072707.2; NM_001079239.1.
DR AlphaFoldDB; Q08CW8; -.
DR SMR; Q08CW8; -.
DR STRING; 8364.ENSXETP00000021974; -.
DR GlyCosmos; Q08CW8; 1 site, No reported glycans.
DR PaxDb; 8364-ENSXETP00000063665; -.
DR DNASU; 780164; -.
DR GeneID; 780164; -.
DR KEGG; xtr:780164; -.
DR AGR; Xenbase:XB-GENE-5761389; -.
DR CTD; 148327; -.
DR eggNOG; KOG0709; Eukaryota.
DR HOGENOM; CLU_047257_2_0_1; -.
DR InParanoid; Q08CW8; -.
DR OrthoDB; 5362396at2759; -.
DR Proteomes; UP000008143; Chromosome 8.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR CDD; cd14689; bZIP_CREB3; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR45996; AGAP001464-PB; 1.
DR PANTHER; PTHR45996:SF2; CYCLIC AMP-RESPONSIVE ELEMENT-BINDING PROTEIN 3-LIKE PROTEIN 4; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 2: Evidence at transcript level;
KW Activator; DNA-binding; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Nucleus; Reference proteome; Signal-anchor; Transcription;
KW Transcription regulation; Transmembrane; Transmembrane helix.
FT CHAIN 1..428
FT /note="Cyclic AMP-responsive element-binding protein 3-like
FT protein 4"
FT /id="PRO_0000288083"
FT CHAIN 1..?
FT /note="Processed cyclic AMP-responsive element-binding
FT protein 3-like protein 4"
FT /id="PRO_0000296223"
FT TOPO_DOM 1..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..428
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 216..279
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..68
FT /note="Required for transcriptional activation"
FT /evidence="ECO:0000250"
FT REGION 71..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..247
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 258..279
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 339..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..110
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 338..339
FT /note="Cleavage; by PS1"
FT /evidence="ECO:0000250"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 428 AA; 47511 MW; 063677BE20BE5CAB CRC64;
MLLGSLFEQT EELFHSEGFP GPDHSNFPLS ELQFPAEKLY EDWPVRGPMG LSEREDTDEF
LQMMINPNEV YSTGPAAAES PESDSGFSDD PRPDTPPQSE TSPPLPQPTP VYELVYDIGS
LEERKSQSDM SSVISIQLAE DWNSAPLLIP ESCIVNDLPP VCKSTPLPIR LTPADLIAVD
ALYPELHLTE EEKRLLSQEG VALPNNLPLT KAEERILKKV RRKIRNKQSA QDSRRRKKEY
IDGLESRVAA CSSQNQELHK KVVELEKHNI SLITQLRKLQ TLIKQTSNKA AQTSTCVLIL
LFSLALLVFP SYSPFRSRPS ASQEDSYRPT GVISRNILNK GGFSEVADPQ ASDTLHRAQQ
REEGDPGRHV VPPANPNPEE TEPVSNRART TPEPDEQVLA EPEAAILGQK GEPPGSDNLS
KTARADEM
//
