CR3L4_RAT
ID CR3L4_RAT Reviewed; 367 AA.
AC Q5UEM7; Q5UEM6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
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 AltName: Full=Androgen-induced basic leucine zipper protein;
DE Short=AIbZIP;
DE Contains:
DE RecName: Full=Processed cyclic AMP-responsive element-binding protein 3-like protein 4;
GN Name=Creb3l4; Synonyms=Aibzip;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Sprague-Dawley; TISSUE=Prostate;
RA Savard M.-P., Pelletier M., Leveille N., Grenier J., Qi H., Labrie C.;
RT "Characterization of the transcriptional properties of mammalian AIbZIP
RT proteins.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional activator that may play a role in the
CC unfolded protein response. Binds to the UPR element (UPRE) but not to
CC CRE element. Preferentially binds DNA with to the consensus sequence
CC 5'-T[GT]ACGT[GA][GT]-3' and has transcriptional activation activity
CC from UPRE. Binds to NF-kappa-B site and has transcriptional activation
CC activity from NF-kappa-B-containing regulatory elements. Increases the
CC binding of CREM isoform Delta with CRE. The CREM isoform Delta-CREB3L4
CC heterodimer functions through CRE but not through UPRE and may recruit
CC HIRA to CRE to regulate histone exchange (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Binds DNA as a dimer. Forms a heterodimer with CREM isoform
CC Delta (By similarity). {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=Under ER stress the cleaved N-terminal
CC cytoplasmic domain translocates into the nucleus. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5UEM7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5UEM7-2; Sequence=VSP_025640;
CC -!- PTM: Controlled by regulated intramembrane proteolysis (RIP). Following
CC ER stress a fragment containing the cytoplasmic transcription factor
CC domain is released by proteolysis. The cleavage seems to be performed
CC sequentially by site-1 and site-2 proteases (PS1 and PS2). PS1 cleavage
CC may be suppressed by a determinant in the C-terminal region (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
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DR EMBL; AY750875; AAV29942.1; -; mRNA.
DR EMBL; AY750876; AAV29943.1; -; mRNA.
DR RefSeq; NP_001007094.1; NM_001007093.1. [Q5UEM7-1]
DR RefSeq; XP_006232689.1; XM_006232627.2. [Q5UEM7-1]
DR RefSeq; XP_008759369.1; XM_008761147.1. [Q5UEM7-2]
DR RefSeq; XP_017446367.1; XM_017590878.1. [Q5UEM7-1]
DR AlphaFoldDB; Q5UEM7; -.
DR SMR; Q5UEM7; -.
DR STRING; 10116.ENSRNOP00000033353; -.
DR GlyGen; Q5UEM7; 1 site.
DR iPTMnet; Q5UEM7; -.
DR PhosphoSitePlus; Q5UEM7; -.
DR PaxDb; Q5UEM7; -.
DR PRIDE; Q5UEM7; -.
DR Ensembl; ENSRNOT00000032062; ENSRNOP00000033353; ENSRNOG00000023493. [Q5UEM7-2]
DR GeneID; 310616; -.
DR KEGG; rno:310616; -.
DR UCSC; RGD:1359278; rat. [Q5UEM7-1]
DR CTD; 148327; -.
DR RGD; 1359278; Creb3l4.
DR VEuPathDB; HostDB:ENSRNOG00000023493; -.
DR eggNOG; KOG0709; Eukaryota.
DR GeneTree; ENSGT00940000160806; -.
DR HOGENOM; CLU_047257_3_0_1; -.
DR InParanoid; Q5UEM7; -.
DR OMA; DSCIFSD; -.
DR OrthoDB; 644485at2759; -.
DR PhylomeDB; Q5UEM7; -.
DR PRO; PR:Q5UEM7; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000023493; Expressed in colon and 17 other tissues.
DR Genevisible; Q5UEM7; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0035497; F:cAMP response element binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
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:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
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; Alternative splicing; 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..367
FT /note="Cyclic AMP-responsive element-binding protein 3-like
FT protein 4"
FT /id="PRO_0000288082"
FT CHAIN 1..?
FT /note="Processed cyclic AMP-responsive element-binding
FT protein 3-like protein 4"
FT /id="PRO_0000296222"
FT TOPO_DOM 1..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..367
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 189..252
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..52
FT /note="Required for transcriptional activation"
FT /evidence="ECO:0000250"
FT REGION 58..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..230
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 231..252
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT SITE 310..311
FT /note="Cleavage; by PS1"
FT /evidence="ECO:0000250"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 33..34
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_025640"
SQ SEQUENCE 367 AA; 40281 MW; 5670035EC3F9C37E CRC64;
MELGCPELLE PPEDIFSTGS FLELGFNGPP SKVPGLQKSE SDDFLNLFID PNMIRCSETS
PGSDSGVSED PGSPAPQAPS SPALYEVVYE AGALQGTQRE AGPTFGLISI QIDQWSPAFM
VPGACTVSDL PSEAHRHILP RVSTIAPPPP AALLSCQRLF LTDEEKHLLG QEGVTLPSHL
PLTKAEERIL KKIRRKIRNK QSAQDSRRRK KEYIDGLESR VAACSEQNQK LQRKVQELER
QNISLVAQVH QLQKFTAQTS SRAAQTSTCV LILLFSLALI ILPSFSPFQS QPEARSEGYQ
LHGVISRNIL THEDMTESPE SPVLKANLEE LPQVPATNGS TKMAHLKMRV KARPTGPIRG
MVHADEM