CR3L4_MACFA
ID CR3L4_MACFA Reviewed; 395 AA.
AC Q5UEM8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 25-MAY-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 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 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC 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 (By
CC similarity). {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=Under ER stress the cleaved N-terminal
CC cytoplasmic domain translocates into the nucleus. {ECO:0000250}.
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; AY750874; AAV29941.1; -; mRNA.
DR RefSeq; XP_005541781.1; XM_005541724.2.
DR AlphaFoldDB; Q5UEM8; -.
DR SMR; Q5UEM8; -.
DR GeneID; 102134095; -.
DR KEGG; mcf:102134095; -.
DR CTD; 148327; -.
DR VEuPathDB; HostDB:ENSMFAG00000030893; -.
DR Proteomes; UP000233100; Chromosome 1.
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: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 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;
KW Unfolded protein response.
FT CHAIN 1..395
FT /note="Cyclic AMP-responsive element-binding protein 3-like
FT protein 4"
FT /id="PRO_0000288080"
FT CHAIN 1..?
FT /note="Processed cyclic AMP-responsive element-binding
FT protein 3-like protein 4"
FT /id="PRO_0000296220"
FT TOPO_DOM 1..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..395
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 217..280
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 79..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..248
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 259..280
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 354..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 338..339
FT /note="Cleavage; by PS1"
FT /evidence="ECO:0000250"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 395 AA; 43510 MW; 5586B84CBF7DC6C1 CRC64;
MDLGIPDLLD AWLEPPEDIF STGSVLELGL HCPPPEVPVT RLQEQGLQGW KSGGDHGCGL
QESEPEDFLK LFIDPNEVYR SEASPGNDSG TSEDPCRPDS PPAPRATSSP TLYEVVYEAG
ALERMQGETG PTVGLISIQL DQWSPAFMVP DSCMVSELPF DAHAHILPRA GTLAPVPCTT
LLPCQTLFLT DEEKRLLGQE GVSLPSHLPL TKAEERVLKK VRRKIRNKQS AQDSRRRKKE
YIDGLESRVA ACSAQNQELQ KKVQELERHN ISLVAQLRQL QTLIAQTSNK AAQTSTCVLI
LLFSLALIIL PSFSPFQGRP EAGPEDYQPH GVTSRNILTH KDITENLETQ VVESRLREPP
EAKDANDSTR TLLEKMGGKP RPSGRIGTVL HADEM
