CR3L2_PONAB
ID CR3L2_PONAB Reviewed; 520 AA.
AC Q5RCM9;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Cyclic AMP-responsive element-binding protein 3-like protein 2;
DE Short=cAMP-responsive element-binding protein 3-like protein 2;
DE Contains:
DE RecName: Full=Processed cyclic AMP-responsive element-binding protein 3-like protein 2;
GN Name=CREB3L2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription factor involved in unfolded protein response
CC (UPR). In the absence of endoplasmic reticulum (ER) stress, inserted
CC into ER membranes, with N-terminal DNA-binding and transcription
CC activation domains oriented toward the cytosolic face of the membrane.
CC In response to ER stress, transported to the Golgi, where it is cleaved
CC in a site-specific manner by resident proteases S1P/MBTPS1 and
CC S2P/MBTPS2. The released N-terminal cytosolic domain is translocated to
CC the nucleus to effect transcription of specific target genes. Plays a
CC critical role in chondrogenesis by activating the transcription of
CC SEC23A, which promotes the transport and secretion of cartilage matrix
CC proteins, and possibly that of ER biogenesis-related genes (By
CC similarity). In a neuroblastoma cell line, protects cells from ER
CC stress-induced death. In vitro activates transcription of target genes
CC via direct binding to the CRE site (By similarity).
CC {ECO:0000250|UniProtKB:Q8BH52}.
CC -!- SUBUNIT: Binds DNA as a dimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8BH52}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q70SY1}. Note=ER membrane resident protein. Upon
CC ER stress, translocated to the Golgi apparatus where it is cleaved. The
CC cytosolic N-terminal fragment (processed cyclic AMP-responsive element-
CC binding protein 3-like protein 1) is transported into the nucleus.
CC {ECO:0000250|UniProtKB:Q8BH52}.
CC -!- SUBCELLULAR LOCATION: [Processed cyclic AMP-responsive element-binding
CC protein 3-like protein 2]: Nucleus {ECO:0000250|UniProtKB:Q70SY1}.
CC Note=Upon ER stress, translocated into the nucleus.
CC {ECO:0000250|UniProtKB:Q8BH52}.
CC -!- PTM: Upon ER stress, translocated to the Golgi apparatus, where it is
CC processed by regulated intramembrane proteolysis (RIP) to release the
CC cytosol-facing N-terminal transcription factor domain. The cleavage is
CC performed sequentially by site-1 and site-2 proteases (S1P/MBTPS1 and
CC S2P/MBTPS2). {ECO:0000250|UniProtKB:Q8BH52}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8BH52}.
CC -!- PTM: Ubiquitinated by HRD1/SYVN1; undergoes 'Lys-48'-linked
CC ubiquitination, followed by rapid proteasomal degradation under normal
CC conditions. Upon ER stress, SYVN1 E3 ubiquitin-protein ligase
CC dissociates from its substrate, ubiquitination does not occur and
CC CREB3L2 is stabilized. {ECO:0000250|UniProtKB:Q8BH52}.
CC -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
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DR EMBL; CR858241; CAH90478.1; -; mRNA.
DR RefSeq; NP_001124550.1; NM_001131078.1.
DR AlphaFoldDB; Q5RCM9; -.
DR SMR; Q5RCM9; -.
DR STRING; 9601.ENSPPYP00000020238; -.
DR GeneID; 100127093; -.
DR KEGG; pon:100127093; -.
DR CTD; 64764; -.
DR eggNOG; KOG0709; Eukaryota.
DR InParanoid; Q5RCM9; -.
DR OrthoDB; 644485at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
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; ISS:UniProtKB.
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:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0051216; P:cartilage development; ISS:UniProtKB.
DR GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
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:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR InterPro; IPR029804; BBF2H7.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR46004:SF2; PTHR46004:SF2; 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; Developmental protein; DNA-binding; Endoplasmic reticulum;
KW Glycoprotein; Isopeptide bond; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Signal-anchor; Transcription; Transcription regulation;
KW Transmembrane; Transmembrane helix; Ubl conjugation;
KW Unfolded protein response.
FT CHAIN 1..520
FT /note="Cyclic AMP-responsive element-binding protein 3-like
FT protein 2"
FT /id="PRO_0000288069"
FT CHAIN 1..?
FT /note="Processed cyclic AMP-responsive element-binding
FT protein 3-like protein 2"
FT /id="PRO_0000296211"
FT TOPO_DOM 1..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..520
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 294..357
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 195..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..325
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 336..357
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT MOTIF 427..430
FT /note="S1P recognition"
FT /evidence="ECO:0000250|UniProtKB:Q70SY1"
FT COMPBIAS 207..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q70SY1"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q70SY1"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q70SY1"
SQ SEQUENCE 520 AA; 57501 MW; 5F180D4E7EA38DB9 CRC64;
MEVLESGEQG VLQWDRKLSE LSEPGDGEAL MYHTHFSELL DEFSQNVLGQ LLNDPFLSEK
SVSTEVEPSP MSPAPLIQAE HSYSLCEEPR AQSPFTHITT SDSFNDDEVE SEKWYLSTDF
PSTTIKTEPI TDEPPPGLVP SVTLTITAIS TPFEKEEPPL EMNTGVDSSC QTIIPKIKLE
PHEVDQFLNF SPKEAPVDHL HLPPTPPSSH GSDSEGSLSP NPRLHPFSLP QTHSPSRAAP
RAPSALSSSP LLTAPHKLQG SGPLVLTEEE KRTLIAEGYP IPTKLPLTKS EEKALKKIRR
KIKNKISAQE SRRKKKEYMD SLEKKVESCS TENLELRKKV EVLENTNRTL LQQLQKLQTL
VMGKVSRTCK LAGTQTGTCL MVVVLCFAVA FGSFFQGYGP YPSATKMALP SQHSLQEPYT
ASVVRSRNLL IYEEHSPPEE PSSPGSAGEL GGWDRGSSLL RVSGLESRPD VDLPHFIISN
ETSLEKSVLL ELQQHLVSAK LEGNETLKVV ELDRRVNTTF
