ID   HEXI1_DANRE             Reviewed;         319 AA.
AC   A5D8S8;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Protein HEXIM1;
GN   Name=hexim1; ORFNames=zgc:162976;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcriptional regulator which functions as a general RNA
CC       polymerase II transcription inhibitor. Core component of the 7SK RNP
CC       complex: in cooperation with 7SK snRNA sequesters P-TEFb in a large
CC       inactive 7SK snRNP complex preventing RNA polymerase II phosphorylation
CC       and subsequent transcriptional elongation. Plays a role in the
CC       regulation of DNA virus-mediated innate immune response by assembling
CC       into the HDP-RNP complex, a complex that serves as a platform for IRF3
CC       phosphorylation and subsequent innate immune response activation
CC       through the cGAS-STING pathway. {ECO:0000250|UniProtKB:O94992}.
CC   -!- SUBUNIT: Homooligomer and heterooligomer. Core component of the 7SK RNP
CC       complex. {ECO:0000250|UniProtKB:O94992}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O94992}. Cytoplasm
CC       {ECO:0000250|UniProtKB:O94992}. Note=Binds alpha-importin and is mostly
CC       nuclear. {ECO:0000250|UniProtKB:O94992}.
CC   -!- SIMILARITY: Belongs to the HEXIM family. {ECO:0000305}.
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DR   EMBL; BC141797; AAI41798.1; -; mRNA.
DR   RefSeq; NP_001091859.1; NM_001098389.1.
DR   AlphaFoldDB; A5D8S8; -.
DR   SMR; A5D8S8; -.
DR   STRING; 7955.ENSDARP00000053002; -.
DR   PaxDb; A5D8S8; -.
DR   PeptideAtlas; A5D8S8; -.
DR   GeneID; 562319; -.
DR   KEGG; dre:562319; -.
DR   CTD; 10614; -.
DR   ZFIN; ZDB-GENE-030131-4637; hexim1.
DR   eggNOG; ENOG502QQP8; Eukaryota.
DR   InParanoid; A5D8S8; -.
DR   OrthoDB; 1055089at2759; -.
DR   PhylomeDB; A5D8S8; -.
DR   PRO; PR:A5D8S8; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0097322; F:7SK snRNA binding; IBA:GO_Central.
DR   GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0065003; P:protein-containing complex assembly; IPI:ZFIN.
DR   InterPro; IPR024872; HEXIM.
DR   PANTHER; PTHR13469; PTHR13469; 1.
DR   Pfam; PF15313; HEXIM; 1.
DR   PRINTS; PR02094; HEXIMFAMILY.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..319
FT                   /note="Protein HEXIM1"
FT                   /id="PRO_0000305269"
FT   REGION          1..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          240..306
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..111
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..203
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   319 AA;  36219 MW;  762A2AE3A8B1FB09 CRC64;
     MELIKEETAP EDDSRGRQRD CRTSVVSSKQ VQRNQLEICP GLVSGDVHPM CRDRSDPEPR
     TGDAASDDGF PADKTSSKRD SECAAVNTDG VSDGRQGKKK HRRRPSKKKR RWKPYFKLTW
     EEKKELDERE TARASRVRAE MFAKGLPVAP YNTTQFLMEE HDREEPDLNT ELGGRKSGAI
     RSEDTASEDE NFEAEEDDEE EGGGGSDGMG RPGQAGGEFL QKDFSETYEK YHVEALQNMS
     KQELVREYLE LEKCMSRLEE ENNWLRHVRR NPESPADGTG SQRVRELEVE VEKLRAENNE
     LLLKTPASNE PGLNQSQPS