ATF6H_CAEEL
ID ATF6H_CAEEL Reviewed; 589 AA.
AC Q20435;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Transcription factor atf-6 homolog {ECO:0000303|PubMed:16184190};
DE AltName: Full=Cyclic AMP-dependent transcription factor ATF-6 homolog {ECO:0000305};
GN Name=atf-6 {ECO:0000312|WormBase:F45E6.2};
GN ORFNames=F45E6.2 {ECO:0000312|WormBase:F45E6.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16184190; DOI=10.1371/journal.pgen.0010037;
RA Shen X., Ellis R.E., Sakaki K., Kaufman R.J.;
RT "Genetic interactions due to constitutive and inducible gene regulation
RT mediated by the unfolded protein response in C. elegans.";
RL PLoS Genet. 1:e37-e37(2005).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=20733002; DOI=10.1128/mcb.00922-10;
RA Mao X.R., Crowder C.M.;
RT "Protein misfolding induces hypoxic preconditioning via a subset of the
RT unfolded protein response machinery.";
RL Mol. Cell. Biol. 30:5033-5042(2010).
RN [4] {ECO:0000305}
RP FUNCTION, REPRESSION BY MIR-124, AND DISRUPTION PHENOTYPE.
RX PubMed=25186652; DOI=10.1002/jcb.24961;
RA Wang N., Liu J., Xie F., Gao X., Ye J.H., Sun L.Y., Wei R., Ai J.;
RT "miR-124/ATF-6, a novel lifespan extension pathway of Astragalus
RT polysaccharide in Caenorhabditis elegans.";
RL J. Cell. Biochem. 116:242-251(2015).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=31570707; DOI=10.1038/s41467-019-12070-3;
RA Waldherr S.M., Strovas T.J., Vadset T.A., Liachko N.F., Kraemer B.C.;
RT "Constitutive XBP-1s-mediated activation of the endoplasmic reticulum
RT unfolded protein response protects against pathological tau.";
RL Nat. Commun. 10:4443-4443(2019).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=32905769; DOI=10.1016/j.celrep.2020.108125;
RA Burkewitz K., Feng G., Dutta S., Kelley C.A., Steinbaugh M., Cram E.J.,
RA Mair W.B.;
RT "Atf-6 Regulates Lifespan through ER-Mitochondrial Calcium Homeostasis.";
RL Cell Rep. 32:108125-108125(2020).
CC -!- FUNCTION: Transcription factor (By similarity). Plays a role in the
CC unfolded protein response (UPR), perhaps mainly during constitutive
CC endoplasmic reticulum (ER) stress, by activating transcription of genes
CC involved in the UPR (PubMed:16184190). Plays a role in modulating
CC lifespan, acting by positively regulating expression of calcium-binding
CC chaperone crt-1, thereby influencing ER calcium homeostasis
CC (PubMed:25186652, PubMed:32905769). By activating the UPR pathway,
CC confers adaptive protection to subsequent exposure to hypoxia
CC (PubMed:20733002). Involved in protection against proteotoxicity,
CC probably acting via the UPR (PubMed:31570707). Probably acts in the UPR
CC in parallel with the ire-1-xbp-1 and pek-1 pathways (PubMed:16184190).
CC May be regulated by endopeptidase S2P-mediated proteolytic cleavage
CC (PubMed:16184190). {ECO:0000250|UniProtKB:P18850,
CC ECO:0000269|PubMed:16184190, ECO:0000269|PubMed:20733002,
CC ECO:0000269|PubMed:25186652, ECO:0000269|PubMed:31570707,
CC ECO:0000269|PubMed:32905769, ECO:0000303|PubMed:16184190}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is repressed by micro-RNA mir-124 (at protein
CC level). {ECO:0000269|PubMed:25186652}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes lifespan extension
CC (PubMed:25186652). Knockdown causes no obvious other phenotypes, but in
CC an ire-1 mutant background causes sluggish movement, arrested
CC development at the L2 larval stage, and lethality soon thereafter;
CC larvae have intestinal degeneration and develop many vacuoles in the
CC intestinal cells (PubMed:16184190). In combination with RNAi-mediated
CC knockdown of xbp-1, causes lethality early in larval development
CC (PubMed:16184190). {ECO:0000269|PubMed:16184190,
CC ECO:0000269|PubMed:25186652}.
CC -!- SIMILARITY: Belongs to the bZIP family. ATF subfamily. {ECO:0000305}.
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DR EMBL; BX284606; CAA92180.1; -; Genomic_DNA.
DR PIR; T22229; T22229.
DR RefSeq; NP_510094.1; NM_077693.3.
DR SMR; Q20435; -.
DR DIP; DIP-26021N; -.
DR IntAct; Q20435; 4.
DR STRING; 6239.F45E6.2; -.
DR EPD; Q20435; -.
DR PaxDb; Q20435; -.
DR EnsemblMetazoa; F45E6.2.1; F45E6.2.1; WBGene00000222.
DR GeneID; 181405; -.
DR KEGG; cel:CELE_F45E6.2; -.
DR UCSC; F45E6.2; c. elegans.
DR CTD; 181405; -.
DR WormBase; F45E6.2; CE17828; WBGene00000222; atf-6.
DR eggNOG; KOG4343; Eukaryota.
DR GeneTree; ENSGT00940000175065; -.
DR HOGENOM; CLU_451479_0_0_1; -.
DR InParanoid; Q20435; -.
DR OMA; IERWVQV; -.
DR OrthoDB; 1083011at2759; -.
DR PhylomeDB; Q20435; -.
DR Reactome; R-CEL-381033; ATF6 (ATF6-alpha) activates chaperones.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00000222; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IDA:WormBase.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:UniProtKB.
DR GO; GO:0006990; P:positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response; IMP:WormBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0035966; P:response to topologically incorrect protein; IMP:WormBase.
DR GO; GO:1904576; P:response to tunicamycin; IMP:UniProtKB.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF07716; bZIP_2; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 1: Evidence at protein level;
KW Coiled coil; DNA-binding; Membrane; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..589
FT /note="Transcription factor atf-6 homolog"
FT /id="PRO_0000456083"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 250..299
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 252..275
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 281..295
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COILED 271..305
FT /evidence="ECO:0000255"
SQ SEQUENCE 589 AA; 67377 MW; 80ED5B67EA6FC8D0 CRC64;
MNFDNTVHES NFDDLLHNPN FPPQFDQLEL DSLLYGTDES QESTSSSSFG FSDQNAGFRS
RDGGSLGDSS SDSSPPLSCA NFTENDQEMW DFGFQSRSPF ENFEQQFGSP YQDDEVIAEP
TNEFMNARYL REEPAKHLPM QQKRIITILP KQSQPVKRIV SRPIQKVYRV KESPGSQQQT
YRVVQPLMPS PSQATQRQIK QMYYNEPVQE IHMQPKSGPL VRQVSEEPRY VPIAPTVDIK
AEPQVFTSEQ NRKIRNRMYA QASRMRKKEA DEHMKMNLQE LLQENEILRT ENAALKQRLA
FFEHEEPVVE VPQPFGRNQK KKRIIAAGSV LMMFGLFAVI SPFNVDNNLN INNQIMAISN
ETSMVARHGR VITYEDSAPV AKIPTQQPIH NYPNSTQNDC DMYKLNATET IRVNNDIERW
VQVHSFDNVP MKFSGGLLNK EAMRKFNYAQ KVKPASVYGP QTLAVQKKSE QAALRSRERT
WKQLDLLKTG NNIQLDNEKI QRKRQDIDKI ASIVRQKGDT LYIMTLQDYV LLPSLIKGAN
SVPKLSLLLP SVPMNGTLQD QYTLLRVDCE VTGTGQLTLS NKQLSYLMP
