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HSF3_CHICK
ID   HSF3_CHICK              Reviewed;         467 AA.
AC   P38531; I7GGG0;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Heat shock factor protein 3;
DE            Short=HSF 3;
DE   AltName: Full=HSF 3C;
DE   AltName: Full=HSTF 3C;
DE   AltName: Full=Heat shock transcription factor 3;
DE            Short=HSTF 3;
GN   Name=HSF3;
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. HSF3 binds DNA
CC       constitutively only when the C-terminal region is deleted.
CC   -!- SUBUNIT: Homotrimer.
CC   -!- INTERACTION:
CC       P38531; P06876: Myb; Xeno; NbExp=2; IntAct=EBI-16212976, EBI-366934;
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. High levels are found in
CC       erythrocytes and low levels in liver.
CC   -!- DEVELOPMENTAL STAGE: Expressed during development.
CC   -!- SIMILARITY: Belongs to the HSF family. {ECO:0000305}.
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DR   EMBL; L06126; AFP54345.1; -; mRNA.
DR   PIR; A48092; A48092.
DR   RefSeq; NP_001291970.1; NM_001305041.1.
DR   AlphaFoldDB; P38531; -.
DR   SMR; P38531; -.
DR   BioGRID; 682892; 3.
DR   DIP; DIP-235N; -.
DR   IntAct; P38531; 1.
DR   STRING; 9031.ENSGALP00000039922; -.
DR   PaxDb; P38531; -.
DR   GeneID; 422169; -.
DR   KEGG; gga:422169; -.
DR   CTD; 245525; -.
DR   VEuPathDB; HostDB:geneid_422169; -.
DR   eggNOG; KOG0627; Eukaryota.
DR   HOGENOM; CLU_038829_3_0_1; -.
DR   InParanoid; P38531; -.
DR   OrthoDB; 1154048at2759; -.
DR   PhylomeDB; P38531; -.
DR   TreeFam; TF330401; -.
DR   PRO; PR:P38531; -.
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:0003677; F:DNA binding; IDA:AgBase.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:ARUK-UCL.
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; IDA:ARUK-UCL.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:AgBase.
DR   GO; GO:0034605; P:cellular response to heat; IDA:AgBase.
DR   GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; IMP:AgBase.
DR   GO; GO:1902751; P:positive regulation of cell cycle G2/M phase transition; IMP:AgBase.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:AgBase.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:AgBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR   GO; GO:0070207; P:protein homotrimerization; IDA:AgBase.
DR   GO; GO:0031620; P:regulation of fever generation; IMP:AgBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0009408; P:response to heat; IDA:AgBase.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR027729; HSF3.
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:SF148; PTHR10015:SF148; 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   1: Evidence at protein level;
KW   Activator; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Stress response; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..467
FT                   /note="Heat shock factor protein 3"
FT                   /id="PRO_0000124576"
FT   DNA_BIND        16..121
FT                   /evidence="ECO:0000250"
FT   REGION          128..201
FT                   /note="Hydrophobic repeat HR-A/B"
FT   REGION          364..389
FT                   /note="Hydrophobic repeat HR-C"
FT   REGION          427..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   467 AA;  51869 MW;  2BCA7A072FAC1B56 CRC64;
     MREGSALPGA PGAAPVPGFL AKLWALVEDP QSDDVICWSR NGENFCILDE QRFAKELLPK
     YFKHNNISSF IRQLNMYGFR KVVALENGMI TAEKNSVIEF QHPFFKQGNA HLLENIKRKV
     SAVRTEDLKV CAEDLHKVLS EVQEMREQQN NMDIRLANMK RENKALWKEV AVLRQKHSQQ
     QKLLSKILQF ILSLMRGNYI VGVKRKRSLT DAAGASPSKY SRQYVRIPVE SGQAMAFSEH
     NSDDEDGNRT GLIIRDITDT LENATNGLLA VAHTSGRDRE TQTALDPGLP ICQVSQPNEL
     SCAEPIPPVH INDVSKPNEM GNVAVELHTA QANAPEDPVS VIDSILNENN SGNQNDPLLD
     REEIQDFLNC IDASLEELQA MLSGKQYSFG SEAFSDVFNP ELPALDMNLM ETSPGMENIA
     NMEDSTEDLG ASERETAGSK GGQEGTESCD SSVLFQNCVL KWNFSSL
 
 
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