THAP5_MACFA
ID THAP5_MACFA Reviewed; 396 AA.
AC Q4R7M0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=THAP domain-containing protein 5;
GN Name=THAP5; ORFNames=QtsA-14855;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has sequence-specific DNA-binding activity and can function
CC as transcriptional repressor (in vitro). May be a regulator of cell
CC cycle: THAP5 overexpression in human cell lines causes cell cycle
CC arrest at G2/M phase. {ECO:0000250|UniProtKB:Q7Z6K1}.
CC -!- SUBUNIT: Interacts with HTRA2; under apoptotic conditions. Interacts
CC with ABRAXAS2. {ECO:0000250|UniProtKB:Q7Z6K1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7Z6K1}.
CC -!- PTM: Cleaved by HTRA2 during apoptosis. {ECO:0000250|UniProtKB:Q7Z6K1}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AB168795; BAE00902.1; -; mRNA.
DR RefSeq; NP_001271042.1; NM_001284113.1.
DR AlphaFoldDB; Q4R7M0; -.
DR SMR; Q4R7M0; -.
DR STRING; 9541.XP_005550595.1; -.
DR GeneID; 101926281; -.
DR CTD; 168451; -.
DR eggNOG; ENOG502RYVM; Eukaryota.
DR OrthoDB; 1382095at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0045786; P:negative regulation of cell cycle; ISS:UniProtKB.
DR InterPro; IPR006612; THAP_Znf.
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; Repressor; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..396
FT /note="THAP domain-containing protein 5"
FT /id="PRO_0000333818"
FT ZN_FING 2..85
FT /note="THAP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00309"
FT REGION 86..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 349..382
FT /evidence="ECO:0000255"
FT MOTIF 322..325
FT /note="HCFC1-binding motif (HBM)"
FT /evidence="ECO:0000250"
FT COMPBIAS 92..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 396 AA; 45663 MW; FA25385FB15D0CF1 CRC64;
MMPRYCAAIC CKNRRGRNNK DRKLSFYPFP LHDKERLEKW LKNMKRDSWV PSKYQFLCSD
HFTPDSLDIR WGIRYLKQTA VPTIFSLPED NQGKDPSKKK SQKKNLEDEK EVCPKAKSEE
SFVLNETKKN IVNTNVPPQH PELLHSSSLV KPPAPKTGSI QNNMLTVNLV KQHTGKPEST
LETSVYQDTG IGDFHTCFED LNSTTITLTT SNSESIHQSL ETQDVLEVTT NHLANPDFTS
NSMEIKSAQE NPFLFSTINQ TVEELNTSKE SVIAIFVPAE NSKPSVNSFI STQKETMEME
DIDIEDSLYK DVDYGTEVLQ IEHSYCRQDI NKEHLWQKVF KLHSKITLLE LKEQQTLGRL
KSLEALVRQL KQENWLSEEN VKIIENHFTT YEVTMI