HSF4_CANLF
ID HSF4_CANLF Reviewed; 492 AA.
AC Q1HGE8; Q1HGE6; Q1HGE7;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Heat shock factor protein 4;
DE Short=HSF 4;
DE AltName: Full=Heat shock transcription factor 4;
DE Short=HSTF 4;
GN Name=HSF4;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), AND INVOLVEMENT IN
RP CATARACT.
RX PubMed=16939467; DOI=10.1111/j.1463-5224.2006.00496.x;
RA Mellersh C.S., Pettitt L., Forman O.P., Vaudin M., Barnett K.C.;
RT "Identification of mutations in HSF4 in dogs of three different breeds with
RT hereditary cataracts.";
RL Vet. Ophthalmol. 9:369-378(2006).
CC -!- FUNCTION: Heat-shock transcription factor that specifically binds heat
CC shock promoter elements (HSE) (By similarity). Required for
CC denucleation and organelle rupture and degradation that occur during
CC eye lens terminal differentiation, when fiber cells that compose the
CC lens degrade all membrane-bound organelles in order to provide lens
CC with transparency to allow the passage of light (By similarity). In
CC this process, may regulate denucleation of lens fiber cells in part by
CC activating DNASE2B transcription (By similarity). May be involved in
CC DNA repair through the transcriptional regulation of RAD51 (By
CC similarity). May up-regulate p53/TP53 protein in eye lens fiber cells,
CC possibly through protein stabilization (By similarity). In the eye
CC lens, controls the expression of alpha-crystallin B chain/CRYAB and
CC consequently may be involved in the regulation of lysosomal
CC acidification (By similarity). {ECO:0000250|UniProtKB:Q5CZP2,
CC ECO:0000250|UniProtKB:Q9R0L1, ECO:0000250|UniProtKB:Q9ULV5}.
CC -!- SUBUNIT: Homotrimer. Exhibits constitutive DNA binding and forms
CC trimers even in the absence of stress. Interacts with ALKBH4, DUSP26,
CC MAPK1, MAPK2, MAPK8 and MAP kinase p38. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9ULV5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ULV5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a;
CC IsoId=Q1HGE8-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q1HGE8-2; Sequence=VSP_021592;
CC Name=c;
CC IsoId=Q1HGE8-3; Sequence=VSP_021591;
CC -!- PTM: Phosphorylated mainly on serine residues. Phosphorylation on Ser-
CC 299 promotes sumoylation on Lys-294 (By similarity). {ECO:0000250}.
CC -!- PTM: Constitutively sumoylated. Sumoylation represses the
CC transcriptional activity and is promoted by phosphorylation on Ser-299
CC (By similarity). {ECO:0000250}.
CC -!- DISEASE: Note=Defects in HSF4 are a cause of forms of hereditary
CC cataract (HC) in dogs. Mutations in HSF4 seem to be causing a recessive
CC form of cataract in Staffordshire Bull terriers and Boston terriers and
CC a dominant cataract in Australian shepherds.
CC -!- SIMILARITY: Belongs to the HSF family. {ECO:0000305}.
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DR EMBL; DQ487185; ABF48488.1; -; mRNA.
DR EMBL; DQ487186; ABF48489.1; -; mRNA.
DR EMBL; DQ487187; ABF48490.1; -; mRNA.
DR RefSeq; NP_001041586.1; NM_001048121.1. [Q1HGE8-1]
DR AlphaFoldDB; Q1HGE8; -.
DR SMR; Q1HGE8; -.
DR STRING; 9612.ENSCAFP00000030227; -.
DR PaxDb; Q1HGE8; -.
DR Ensembl; ENSCAFT00030018436; ENSCAFP00030016096; ENSCAFG00030009600. [Q1HGE8-1]
DR Ensembl; ENSCAFT00030018468; ENSCAFP00030016124; ENSCAFG00030009600. [Q1HGE8-3]
DR Ensembl; ENSCAFT00040034244; ENSCAFP00040029812; ENSCAFG00040018221. [Q1HGE8-1]
DR Ensembl; ENSCAFT00040034273; ENSCAFP00040029836; ENSCAFG00040018221. [Q1HGE8-3]
DR Ensembl; ENSCAFT00845017857; ENSCAFP00845013908; ENSCAFG00845010066. [Q1HGE8-1]
DR Ensembl; ENSCAFT00845017932; ENSCAFP00845013968; ENSCAFG00845010066. [Q1HGE8-3]
DR GeneID; 489766; -.
DR KEGG; cfa:489766; -.
DR CTD; 3299; -.
DR VEuPathDB; HostDB:ENSCAFG00845010066; -.
DR eggNOG; KOG0627; Eukaryota.
DR GeneTree; ENSGT00940000158063; -.
DR InParanoid; Q1HGE8; -.
DR OrthoDB; 1154048at2759; -.
DR Proteomes; UP000002254; Chromosome 5.
DR Bgee; ENSCAFG00000020379; Expressed in temporal lobe and 46 other tissues.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0048468; P:cell development; IEA:Ensembl.
DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0033169; P:histone H3-K9 demethylation; IEA:Ensembl.
DR GO; GO:0070306; P:lens fiber cell differentiation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IEA:Ensembl.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000232; HSF_DNA-bd.
DR InterPro; IPR027725; HSF_fam.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10015; PTHR10015; 1.
DR Pfam; PF00447; HSF_DNA-bind; 1.
DR PRINTS; PR00056; HSFDOMAIN.
DR SMART; SM00415; HSF; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00434; HSF_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Stress response; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..492
FT /note="Heat shock factor protein 4"
FT /id="PRO_0000260264"
FT DNA_BIND 17..121
FT /evidence="ECO:0000250"
FT REGION 129..203
FT /note="Hydrophobic repeat HR-A/B"
FT REGION 245..323
FT /note="Interactions with DUSP26, MAPK1 and MAPK2"
FT /evidence="ECO:0000250"
FT REGION 250..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..390
FT /note="Hydrophobic repeat HR-C"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULV5"
FT CROSSLNK 294
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 287..362
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000303|PubMed:16939467"
FT /id="VSP_021591"
FT VAR_SEQ 287..320
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:16939467"
FT /id="VSP_021592"
SQ SEQUENCE 492 AA; 53064 MW; 1A6572DDA526FEDF CRC64;
MQEAPAALPT EPGPSPVPAF LGKLWALVGD PGTDHLIRWS PSGTSFLVSD QSRFAKEVLP
QYFKHSNMAS FVRQLNMYGF RKVVSIEQGG LLRPERDHVE FQHPSFVRGR EQLLERVRRK
VPALRSDDGR WRPEDLGRLL GEVQALRGVQ EITEARLREL RQQNEILWRE VVTLRQSHGQ
QHRVIGKLIQ CLFGPLQTGS SGAGAKRKLS LMLDEGSSCP TPAKFNTCPL PGALLQDPYF
IQSPLPETTL GLSSSHRTRG PIISDIHEDS PSPDGTRLSP SSGGRREKGL ALLKEEPASP
GGEGEAGLAL APNECDFCVT APPPLSVAVV QAILEGKGNF SPEGPRNAQQ PEPRGPREVP
DRGTLGLDRG ARSPENLLPP MLLRAPPESV EPAGPLDVLG PSHQGREWTL MDLDMELSLM
QPLGPERSET ELAVKGLNSP GPGKDSTLGA PLLLDVQAAL GGPALSLPGA LTIYSTPESR
ANYLGPGANP SP
