THAP1_RAT
ID THAP1_RAT Reviewed; 210 AA.
AC Q5U208;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=THAP domain-containing protein 1;
GN Name=Thap1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: DNA-binding transcription regulator that regulates
CC endothelial cell proliferation and G1/S cell-cycle progression.
CC Specifically binds the 5'-[AT]NTNN[GT]GGCA[AGT]-3' core DNA sequence
CC and acts by modulating expression of pRB-E2F cell-cycle target genes,
CC including RRM1. May also have pro-apoptotic activity by potentiating
CC both serum-withdrawal and TNF-induced apoptosis (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PAWR. Component of a THAP1/THAP3-HCFC1-OGT
CC complex that contains, either THAP1 or THAP3, HCFC1 and OGT. Interacts
CC with OGT. Interacts (via the HBM) with HCFC1 (via the Kelch-repeat
CC domain); the interaction recruits HCFC1 to the RRM1 promoter (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Nucleus, PML
CC body {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the THAP1 family. {ECO:0000305}.
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DR EMBL; BC086347; AAH86347.1; -; mRNA.
DR RefSeq; NP_001008341.1; NM_001008340.1.
DR AlphaFoldDB; Q5U208; -.
DR SMR; Q5U208; -.
DR STRING; 10116.ENSRNOP00000019026; -.
DR PaxDb; Q5U208; -.
DR PRIDE; Q5U208; -.
DR GeneID; 306547; -.
DR KEGG; rno:306547; -.
DR CTD; 55145; -.
DR RGD; 1307589; Thap1.
DR VEuPathDB; HostDB:ENSRNOG00000056956; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_076186_2_1_1; -.
DR InParanoid; Q5U208; -.
DR OMA; LMPPLHT; -.
DR OrthoDB; 1382095at2759; -.
DR PhylomeDB; Q5U208; -.
DR TreeFam; TF330127; -.
DR PRO; PR:Q5U208; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000056956; Expressed in testis and 19 other tissues.
DR ExpressionAtlas; Q5U208; baseline and differential.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISO:RGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0001935; P:endothelial cell proliferation; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0006351; P:transcription, DNA-templated; ISO:RGD.
DR Gene3D; 6.20.210.20; -; 1.
DR InterPro; IPR026516; THAP1.
DR InterPro; IPR006612; THAP_Znf.
DR InterPro; IPR038441; THAP_Znf_sf.
DR PANTHER; PTHR46600; PTHR46600; 1.
DR Pfam; PF05485; THAP; 1.
DR SMART; SM00692; DM3; 1.
DR SMART; SM00980; THAP; 1.
DR PROSITE; PS50950; ZF_THAP; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Coiled coil; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..210
FT /note="THAP domain-containing protein 1"
FT /id="PRO_0000068641"
FT ZN_FING 5..57
FT /note="THAP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00309"
FT COILED 140..187
FT /evidence="ECO:0000255"
FT MOTIF 131..134
FT /note="HCFC1-binding motif (HBM)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 210 AA; 24688 MW; A123F6338571A62B CRC64;
MVQSCSAYGC KNRYDKDKPV SFHKFPLTRP SLCKQWEAAV RRKNFKPTKY SSICSEHFTP
DCFKRECNNK LLKENAVPTI FLYIEPHEKK EELEPQEQLP SPSPPTSQVD AAVGLLMPPL
QTPDNLSVFC DHNYTVEDTM HQRKRILHLE QQVEKLRKKL KTAQQRCRRQ ERQLEKLKEV
VHFQREKDDA SERGYVILPN DYFEIVEVPA
