ID A0A2U9CS79_SCOMX Unreviewed; 498 AA.
AC A0A2U9CS79;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Heat shock transcription factor 2 {ECO:0000313|Ensembl:ENSSMAP00000068260.1};
DE SubName: Full=Putative heat shock factor protein 2 {ECO:0000313|EMBL:AWP19534.1};
GN Name=LOC118290344 {ECO:0000313|Ensembl:ENSSMAP00000068260.1};
GN ORFNames=SMAX5B_022125 {ECO:0000313|EMBL:AWP19534.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP19534.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP19534.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSMAP00000068260.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the HSF family. {ECO:0000256|ARBA:ARBA00006403,
CC ECO:0000256|RuleBase:RU004020}.
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DR EMBL; CP026262; AWP19534.1; -; Genomic_DNA.
DR STRING; 52904.ENSSMAP00000027792; -.
DR Ensembl; ENSSMAT00000046935.1; ENSSMAP00000068260.1; ENSSMAG00000017011.2.
DR GeneTree; ENSGT00940000155906; -.
DR OMA; GKQCGID; -.
DR OrthoDB; 1117127at2759; -.
DR Proteomes; UP000246464; Chromosome 20.
DR Proteomes; UP000694558; Chromosome 20.
DR Bgee; ENSSMAG00000017011; Expressed in actinopterygian pyloric caecum and 6 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR000232; HSF_DNA-bd.
DR InterPro; IPR027725; HSF_fam.
DR InterPro; IPR010542; Vert_HSTF_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10015:SF185; HEAT SHOCK FACTOR PROTEIN 2; 1.
DR PANTHER; PTHR10015; HEAT SHOCK TRANSCRIPTION FACTOR; 1.
DR Pfam; PF00447; HSF_DNA-bind; 1.
DR Pfam; PF06546; Vert_HS_TF; 1.
DR PRINTS; PR00056; HSFDOMAIN.
DR SMART; SM00415; HSF; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS00434; HSF_DOMAIN; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Stress response {ECO:0000313|EMBL:AWP19534.1}.
FT DOMAIN 49..73
FT /note="HSF-type DNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS00434"
FT REGION 419..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 498 AA; 55643 MW; 63DC9D19BFAA2471 CRC64;
MKHNSNVPGF LTKLWTLVED ADTNEFICWS QEGNSFLVLD EQRFAKEILP KLFKHNNMAS
FIRQLNMYGF RKVLHMDTGI VKQERDGPVE FQHPDFRHGQ DDLLENIKRK VSNARPEDNK
IRQEDLTKIL ASVHSVHSKQ ENIDARLATL KRENEALWRE ISDLRQKHAH QQQLIKKLIQ
FIVTLVQNNR ILNLKRKRPL LMNSSGKKPK YIHPIYDDKV CVEQSSVNSV KGSEVSDDVI
ICDLTENDPE VTEGSPRAHE MGDAEVVEVE LASCAVLQAE TESSTSCTDG KLTEASVAAD
GSSLQLNKPS GLSLEDPMKM MDSILNENGV ISQNINLLGK VELMDYLDSI DCSLEDFQAM
LYGKQFGMDF DAIEESVSYK ENSAQLNRGR TGEDNTDKQL VQYASCPLLA FFDGCTPPSE
LDPGTSSSSS TSSSSQPSSS SSHLPSELLD TSLESRPPIR SSLIRLEPLT EAEASEETLF
YLCELSPAGL EADSAQHC
//
