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CR3L4_XENTR
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   03-AUG-2022, entry version 88.
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}.
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DR   EMBL; BC124053; AAI24054.1; -; mRNA.
DR   RefSeq; NP_001072707.2; NM_001079239.1.
DR   AlphaFoldDB; Q08CW8; -.
DR   SMR; Q08CW8; -.
DR   STRING; 8364.ENSXETP00000063665; -.
DR   PaxDb; Q08CW8; -.
DR   DNASU; 780164; -.
DR   GeneID; 780164; -.
DR   KEGG; xtr:780164; -.
DR   CTD; 148327; -.
DR   Xenbase; XB-GENE-5761389; creb3l4.
DR   eggNOG; KOG0709; Eukaryota.
DR   HOGENOM; CLU_047257_2_0_1; -.
DR   InParanoid; Q08CW8; -.
DR   OrthoDB; 644485at2759; -.
DR   Proteomes; UP000008143; Chromosome 8.
DR   Proteomes; UP000790000; Unplaced.
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; IBA:GO_Central.
DR   GO; GO:0035497; F:cAMP response element binding; IEA:InterPro.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR029807; CREB4.
DR   PANTHER; PTHR45996:SF2; PTHR45996:SF2; 1.
DR   Pfam; PF00170; bZIP_1; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; SSF57959; 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
 
 
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