CR3L3_BOVIN
ID CR3L3_BOVIN Reviewed; 456 AA.
AC Q3SYZ3;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Cyclic AMP-responsive element-binding protein 3-like protein 3;
DE Short=cAMP-responsive element-binding protein 3-like protein 3;
DE Contains:
DE RecName: Full=Processed cyclic AMP-responsive element-binding protein 3-like protein 3;
GN Name=CREB3L3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription factor that may act during endoplasmic
CC reticulum stress by activating unfolded protein response target genes.
CC Activated in response to cAMP stimulation. In vitro, binds the cAMP
CC response element (CRE). Activates transcription through box-B element
CC and CRE. Seems to function synergistically with ATF6. In acute
CC inflammatory response, may activate expression of acute phase response
CC (APR) genes. May be involved in growth suppression (By similarity).
CC Regulates FGF21 transcription (By similarity). Plays a crucial role in
CC the regulation of triglyceride metabolism and is required for the
CC maintenance of normal plasma triglyceride concentrations (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q91XE9}.
CC -!- SUBUNIT: Binds DNA as a dimer. May form homodimers (By similarity).
CC Interacts with ATF6 (By similarity). Interacts with SYNV1/HRD1; this
CC interaction leads to CREB3L3 ubiquitination and proteasomal degradation
CC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q68CJ9,
CC ECO:0000250|UniProtKB:Q91XE9}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q68CJ9}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q68CJ9}.
CC -!- SUBCELLULAR LOCATION: [Processed cyclic AMP-responsive element-binding
CC protein 3-like protein 3]: Nucleus {ECO:0000250|UniProtKB:Q68CJ9}.
CC Note=Under ER stress the cleaved N-terminal cytoplasmic domain
CC 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) (By
CC similarity). {ECO:0000250}.
CC -!- PTM: N-glycosylation is required for optimal proteolytic activation.
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated at Lys-289 by SYNV1/HRD1 via 'Lys-27'-linked
CC ubiquitin. {ECO:0000250|UniProtKB:Q68CJ9}.
CC -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
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DR EMBL; BC103320; AAI03321.1; -; mRNA.
DR RefSeq; NP_001029604.1; NM_001034432.2.
DR AlphaFoldDB; Q3SYZ3; -.
DR SMR; Q3SYZ3; -.
DR STRING; 9913.ENSBTAP00000013478; -.
DR PaxDb; Q3SYZ3; -.
DR Ensembl; ENSBTAT00000013478; ENSBTAP00000013478; ENSBTAG00000010215.
DR GeneID; 513010; -.
DR KEGG; bta:513010; -.
DR CTD; 84699; -.
DR VEuPathDB; HostDB:ENSBTAG00000010215; -.
DR VGNC; VGNC:27696; CREB3L3.
DR eggNOG; KOG0709; Eukaryota.
DR GeneTree; ENSGT00940000159261; -.
DR HOGENOM; CLU_047257_1_0_1; -.
DR InParanoid; Q3SYZ3; -.
DR OMA; PGTWHED; -.
DR OrthoDB; 644485at2759; -.
DR TreeFam; TF316079; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000010215; Expressed in liver and 27 other tissues.
DR ExpressionAtlas; Q3SYZ3; baseline and differential.
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:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
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:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IEA:Ensembl.
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; IPR029806; CREBH.
DR PANTHER; PTHR45996:SF1; PTHR45996:SF1; 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; DNA-binding; Endoplasmic reticulum; Glycoprotein;
KW Isopeptide bond; Membrane; Nucleus; Reference proteome; Signal-anchor;
KW Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix; Ubl conjugation; Unfolded protein response.
FT CHAIN 1..456
FT /note="Cyclic AMP-responsive element-binding protein 3-like
FT protein 3"
FT /id="PRO_0000288073"
FT CHAIN 1..?
FT /note="Processed cyclic AMP-responsive element-binding
FT protein 3-like protein 3"
FT /id="PRO_0000296215"
FT TOPO_DOM 1..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..456
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 238..301
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..269
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 280..301
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 365..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 358..359
FT /note="Cleavage; by PS1"
FT /evidence="ECO:0000250"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 289
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q68CJ9"
SQ SEQUENCE 456 AA; 48689 MW; 7EB1705FA08DEBF3 CRC64;
MDGDLAIGKM ASSTSPMGPI DSLELLDLLF DRQDGVLRHV ELGEDWGHGE DQVLPGADSD
DFLNSILGSG DSDSPTWSPA ASDSGISEDL PSDTQDTPPH GGVPATPAGC HSVESGKGPC
PSYHPGPTCP ARHLGPVAPR LETSVAIDLE MWSPGVYAEE QTDLADSPSR YNLTVKDLLL
SSSSGDLQQH HLAAPHLLRP GTGHCQELVL TEDEKKLLAK EGITLPTQLP LTKYEERMLK
KIRRKIRNKQ SAQESRKKKK EYIDGLETRM SACTAQNQEL QRKVLHLEKQ NLSLLEQLKK
LQAIVVQSTS KSAQTGTCIA VLLFSFALIV LPSISPFASN RAESPGDFAP VRVFSRTLHN
DAASRVAPDT APGSEAPGPG PNTGALQERS PGSPPGEWES QDTRALDNST EDLDNSTLVQ
GNSVKELDQA TLLDCAPPEP AVSPGHVGLE AAGGEL
