DVE1_CAEEL
ID DVE1_CAEEL Reviewed; 468 AA.
AC Q86MI0; A0A1X7RBT0; A0A1X7RBW4; Q86MH8;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Homeobox protein dve-1 {ECO:0000305};
DE AltName: Full=Defective proventriculus homolog protein {ECO:0000312|WormBase:ZK1193.5a};
GN Name=dve-1 {ECO:0000312|WormBase:ZK1193.5a};
GN ORFNames=ZK1193.5 {ECO:0000312|WormBase:ZK1193.5a};
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, INTERACTION WITH UBL-5, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=17925224; DOI=10.1016/j.devcel.2007.07.016;
RA Haynes C.M., Petrova K., Benedetti C., Yang Y., Ron D.;
RT "ClpP mediates activation of a mitochondrial unfolded protein response in
RT C. elegans.";
RL Dev. Cell 13:467-480(2007).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, SUMOYLATION AT 327, AND MUTAGENESIS OF
RP LYS-327.
RX PubMed=30642431; DOI=10.7554/elife.41792;
RA Gao K., Li Y., Hu S., Liu Y.;
RT "SUMO peptidase ULP-4 regulates mitochondrial UPR-mediated innate immunity
RT and lifespan extension.";
RL Elife 8:0-0(2019).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH HDA-1, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=32934238; DOI=10.1038/s41467-020-18501-w;
RA Shao L.W., Peng Q., Dong M., Gao K., Li Y., Li Y., Li C.Y., Liu Y.;
RT "Histone deacetylase HDA-1 modulates mitochondrial stress response and
RT longevity.";
RL Nat. Commun. 11:4639-4639(2020).
RN [5] {ECO:0000305}
RP INTERACTION WITH LIN-40, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=32789178; DOI=10.1126/sciadv.abb2529;
RA Zhu D., Wu X., Zhou J., Li X., Huang X., Li J., Wu J., Bian Q., Wang Y.,
RA Tian Y.;
RT "NuRD mediates mitochondrial stress-induced longevity via chromatin
RT remodeling in response to acetyl-CoA level.";
RL Sci. Adv. 6:eabb2529-eabb2529(2020).
CC -!- FUNCTION: Probable transcription factor that acts during mitochondrial
CC stress by activating the mitochondrial unfolded protein response
CC (mtUPR) (PubMed:17925224, PubMed:30642431). Required during
CC mitochondrial stress for the activation of genes involved in the mtUPR,
CC in concert with histone deacetylase hda-1 (PubMed:32934238). May play a
CC role in modulating the decline in protein homeostasis associated with
CC normal aging (PubMed:32934238). Required for embryonic development and
CC maintenance of mitochondrial morphology (PubMed:17925224).
CC {ECO:0000269|PubMed:17925224, ECO:0000269|PubMed:30642431,
CC ECO:0000269|PubMed:32934238}.
CC -!- SUBUNIT: Interacts with ubiquitin-like protein ubl-5; the interaction
CC occurs in a mitochondrial stress-dependent manner (PubMed:17925224).
CC Interacts with lin-40; probably associates with a NuRD (Nucleosome
CC Remodeling and Deacetylase) complex via lin-40 (PubMed:32789178).
CC Interacts with histone deacetylase hda-1 (PubMed:32934238).
CC {ECO:0000269|PubMed:17925224, ECO:0000269|PubMed:32789178,
CC ECO:0000269|PubMed:32934238}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC ECO:0000255|RuleBase:RU000682, ECO:0000269|PubMed:17925224,
CC ECO:0000269|PubMed:32789178, ECO:0000269|PubMed:32934238}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:30642431}. Note=Upon mitochondrial stress
CC translocates from cytosol into the nucleus.
CC {ECO:0000269|PubMed:30642431, ECO:0000269|PubMed:32789178}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=a {ECO:0000312|WormBase:ZK1193.5a};
CC IsoId=Q86MI0-1; Sequence=Displayed;
CC Name=e {ECO:0000312|WormBase:ZK1193.5e};
CC IsoId=Q86MI0-2; Sequence=VSP_060958;
CC Name=c {ECO:0000312|WormBase:ZK1193.5c};
CC IsoId=Q86MI0-3; Sequence=VSP_060957;
CC Name=d {ECO:0000312|WormBase:ZK1193.5d};
CC IsoId=Q86MI0-4; Sequence=VSP_060957, VSP_060958;
CC -!- DEVELOPMENTAL STAGE: Widely expressed in embryos, but particularly in
CC intestinal precursor cells (at protein level).
CC {ECO:0000269|PubMed:17925224}.
CC -!- PTM: Sumoylated at Lys-327; sumoylation is required for cytosolic
CC localization (PubMed:30642431). May be desumoylated by ulp-4
CC (PubMed:30642431). {ECO:0000269|PubMed:30642431}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown inhibits expression of
CC hsp-60 when adults are exposed to conditions causing mitochondrial
CC unfolded protein stress (PubMed:17925224). Causes abnormal
CC mitochondrial morphology (PubMed:17925224). Drastically reduces the
CC protein level of hda-1, possibly via ubiquitin-mediated degradation
CC (PubMed:32934238). Under conditions of mitochondrial stress, partially
CC suppresses nuclear accumulation of lin-40 and lin-53 (PubMed:32789178).
CC {ECO:0000269|PubMed:17925224, ECO:0000269|PubMed:32789178,
CC ECO:0000269|PubMed:32934238}.
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DR EMBL; BX284606; CCD71636.1; -; Genomic_DNA.
DR EMBL; BX284606; CCD71638.2; -; Genomic_DNA.
DR EMBL; BX284606; SMQ44713.1; -; Genomic_DNA.
DR EMBL; BX284606; SMQ44714.1; -; Genomic_DNA.
DR RefSeq; NP_001024984.1; NM_001029813.3. [Q86MI0-1]
DR AlphaFoldDB; Q86MI0; -.
DR SMR; Q86MI0; -.
DR IntAct; Q86MI0; 1.
DR STRING; 6239.ZK1193.5a; -.
DR EPD; Q86MI0; -.
DR PaxDb; Q86MI0; -.
DR PeptideAtlas; Q86MI0; -.
DR EnsemblMetazoa; ZK1193.5a.1; ZK1193.5a.1; WBGene00022861. [Q86MI0-1]
DR EnsemblMetazoa; ZK1193.5c.1; ZK1193.5c.1; WBGene00022861. [Q86MI0-3]
DR EnsemblMetazoa; ZK1193.5c.2; ZK1193.5c.2; WBGene00022861. [Q86MI0-3]
DR EnsemblMetazoa; ZK1193.5d.1; ZK1193.5d.1; WBGene00022861. [Q86MI0-4]
DR EnsemblMetazoa; ZK1193.5d.2; ZK1193.5d.2; WBGene00022861. [Q86MI0-4]
DR EnsemblMetazoa; ZK1193.5d.3; ZK1193.5d.3; WBGene00022861. [Q86MI0-4]
DR EnsemblMetazoa; ZK1193.5d.4; ZK1193.5d.4; WBGene00022861. [Q86MI0-4]
DR EnsemblMetazoa; ZK1193.5d.5; ZK1193.5d.5; WBGene00022861. [Q86MI0-4]
DR EnsemblMetazoa; ZK1193.5e.1; ZK1193.5e.1; WBGene00022861. [Q86MI0-2]
DR GeneID; 180398; -.
DR UCSC; ZK1193.5c; c. elegans.
DR CTD; 180398; -.
DR WormBase; ZK1193.5a; CE33746; WBGene00022861; dve-1.
DR WormBase; ZK1193.5c; CE52008; WBGene00022861; dve-1.
DR WormBase; ZK1193.5d; CE51993; WBGene00022861; dve-1.
DR WormBase; ZK1193.5e; CE51969; WBGene00022861; dve-1.
DR eggNOG; KOG3755; Eukaryota.
DR GeneTree; ENSGT00390000008096; -.
DR HOGENOM; CLU_072174_0_0_1; -.
DR InParanoid; Q86MI0; -.
DR OMA; LNQSPFR; -.
DR OrthoDB; 855819at2759; -.
DR PhylomeDB; Q86MI0; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00022861; Expressed in embryo and 3 other tissues.
DR ExpressionAtlas; Q86MI0; baseline and differential.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IPI:WormBase.
DR GO; GO:0051087; F:chaperone binding; IPI:WormBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0034514; P:mitochondrial unfolded protein response; IMP:UniProtKB.
DR GO; GO:0045088; P:regulation of innate immune response; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00086; homeodomain; 2.
DR CDD; cd11585; SATB1_N; 1.
DR Gene3D; 3.10.20.710; -; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR039673; SATB1/SATB2.
DR InterPro; IPR038224; SATB_ULD_sf.
DR InterPro; IPR032392; ULD.
DR PANTHER; PTHR15116; PTHR15116; 2.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF16534; ULD; 1.
DR SMART; SM00389; HOX; 2.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS50071; HOMEOBOX_2; 2.
DR PROSITE; PS51982; ULD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; DNA-binding; Homeobox; Nucleus;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..468
FT /note="Homeobox protein dve-1"
FT /id="PRO_0000452332"
FT DOMAIN 1..103
FT /note="ULD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01326"
FT DNA_BIND 179..248
FT /note="Homeobox 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT DNA_BIND 385..458
FT /note="Homeobox 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 295..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..208
FT /note="Missing (in isoform c and isoform d)"
FT /id="VSP_060957"
FT VAR_SEQ 381..383
FT /note="Missing (in isoform e and isoform d)"
FT /id="VSP_060958"
FT MUTAGEN 327
FT /note="K->R: Abolishes sumoylation. When associated with
FT RNAi-mediated knockdown of ulp-4, constitutively localized
FT in the nucleus and able to activate the mitochondrial
FT unfolded protein response (mtUPR)."
FT /evidence="ECO:0000269|PubMed:30642431"
SQ SEQUENCE 468 AA; 52834 MW; 70C6B33F43C04CFA CRC64;
MFPMRVIVET VRSQHCLTCS NEGHMITDTY AIVAGTTTLN QLVETVLAAL GHSSMSTSAR
GLIQVNNWKP LPFDQITENL DDTVENLFKD ISSHVVLKIL SKPSTDSNSV QCISEVKNKL
LKAAVNKNPN VLTNVDNQQV KDVINTIIAG DETLLNSEQI GAVNEWLDTL ETNEDRRSPT
QVQRFNTLYE IPRLDKWFKS DANPSKQKMN NYLSQLNQSP FRKNNSKISY QQICNWFTQK
RSSSRTLAPV DLVQVSSAQT AAQLLPGFQL NLLQSLFGEQ RQKFDFYDKL DETKIVGGSD
SPSPADDEIH SNSDETIQDT LFSINIKPEP EIDSIASSPD MANSMRESLS STSPKLLSGL
DLGAFSTHSS STNSMQNANS SVFSAARSRL MFDPLTELPV LEKWFEENPH PTWMQIDQYT
QCLNNCAYRE NYPHISQHNV KIWFKNRRAK CKRLLNGMQE KLEQKVFV
