HSF2_CHICK
ID HSF2_CHICK Reviewed; 564 AA.
AC P38530; I7FPS8;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Heat shock factor protein 2;
DE Short=HSF 2;
DE AltName: Full=HSF 3B;
DE AltName: Full=HSTF 3B;
DE AltName: Full=Heat shock transcription factor 2;
DE Short=HSTF 2;
GN Name=HSF2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8455593; DOI=10.1128/mcb.13.4.1983-1997.1993;
RA Nakai A., Morimoto R.I.;
RT "Characterization of a novel chicken heat shock transcription factor, heat
RT shock factor 3, suggests a new regulatory pathway.";
RL Mol. Cell. Biol. 13:1983-1997(1993).
CC -!- FUNCTION: DNA-binding protein that specifically binds heat shock
CC promoter elements (HSE) and activates transcription. HSF2 shows
CC constitutive DNA binding activity, even without heat shock.
CC -!- SUBUNIT: Homotrimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Cytoplasmic during normal growth and moves to the nucleus upon
CC activation. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in most tissues with the exceptions of
CC blood and liver.
CC -!- DEVELOPMENTAL STAGE: Expressed during development.
CC -!- SIMILARITY: Belongs to the HSF family. {ECO:0000305}.
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DR EMBL; L06125; AFP54344.1; -; mRNA.
DR AlphaFoldDB; P38530; -.
DR SMR; P38530; -.
DR STRING; 9031.ENSGALP00000031100; -.
DR PaxDb; P38530; -.
DR PRIDE; P38530; -.
DR VEuPathDB; HostDB:geneid_421724; -.
DR eggNOG; KOG0627; Eukaryota.
DR HOGENOM; CLU_038829_1_0_1; -.
DR InParanoid; P38530; -.
DR OrthoDB; 1154048at2759; -.
DR PhylomeDB; P38530; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0000785; C:chromatin; IDA:AgBase.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:AgBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:AgBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:AgBase.
DR GO; GO:0070207; P:protein homotrimerization; IDA:AgBase.
DR GO; GO:0050821; P:protein stabilization; IMP:AgBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009416; P:response to light stimulus; IDA:AgBase.
DR GO; GO:0014070; P:response to organic cyclic compound; IDA:AgBase.
DR GO; GO:0010243; P:response to organonitrogen compound; IDA:AgBase.
DR GO; GO:1903935; P:response to sodium arsenite; IMP:AgBase.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR027712; HSF2.
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; PTHR10015; 1.
DR PANTHER; PTHR10015:SF185; PTHR10015:SF185; 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; SSF46785; 1.
DR PROSITE; PS00434; HSF_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Activator; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..564
FT /note="Heat shock factor protein 2"
FT /id="PRO_0000124575"
FT DNA_BIND 21..126
FT /evidence="ECO:0000250"
FT REGION 133..206
FT /note="Hydrophobic repeat HR-A/B"
FT REGION 271..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..415
FT /note="Hydrophobic repeat HR-C"
FT REGION 448..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 564 AA; 62827 MW; 3875ED4966ECF5C6 CRC64;
MKQEPQQQQP AQQPPPAGAG VPAFLSKLWA LVGEAPSNQL ITWSQNGQSF LVLDEQRFAK
EILPKYFKHN NMASFVRQLN MYGFRKVVHV DSGIVKLERD GLVEFQHPYF KQGREDLLEH
IKRKVSSSRP EENKISQEDL SKIISSAQKV EIKQETIESR LSALKRENES LWREVAELRA
KHLKQQQVIR KIVQFIVTLV QNNQLVSLKR KRPLLLNTNG PTKSNVFQQI VKEPADNNNH
VPLNRTEGLK QREQISDDII IYDVTEDVAD EENTMVDEEN APITPETNED TTSDSSNCSR
SPDIVIVEDD NEEEYAPVIQ GDKSTESVAV SANDPLSPVS DSTSPLMSSA VQLNNQSTLT
AEDPVSMMDS ILNENGVISQ NINLLGKVEL LDYLDSIDCS LEDFQAMLSG RQFSIDPDLL
FDLFTSSVQM NPTDHIPNTK METKGIETTK SNAGPAASQE TQVSKPKSDK QLIQYTAFPL
LAFLDGNPGS TVESGSSATE TPSSVDKPLE VDELLESSLD PEPTQSKLVR LEPLTEAEAS
EATLFYLCEL APAPMDTDMP FLDN
