ID   NC2A_RAT                Reviewed;         205 AA.
AC   A0JPP1;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Dr1-associated corepressor;
DE   AltName: Full=Dr1-associated protein 1;
DE   AltName: Full=Negative cofactor 2-alpha;
DE            Short=NC2-alpha;
GN   Name=Drap1 {ECO:0000250|UniProtKB:Q14919};
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] {ECO:0000312|EMBL:AAI27525.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis {ECO:0000312|EMBL:AAI27525.1};
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: The association of the DR1/DRAP1 heterodimer with TBP results
CC       in a functional repression of both activated and basal transcription of
CC       class II genes. This interaction precludes the formation of a
CC       transcription-competent complex by inhibiting the association of TFIIA
CC       and/or TFIIB with TBP. Can bind to DNA on its own (By similarity).
CC       {ECO:0000250|UniProtKB:Q14919}.
CC   -!- SUBUNIT: Heterodimer with DR1. Binds BTAF1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q14919}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q14919}.
CC   -!- PTM: Phosphorylation reduces DNA binding, but has no effect on
CC       heterodimerization and TBP binding. {ECO:0000250|UniProtKB:Q14919}.
CC   -!- SIMILARITY: Belongs to the NC2 alpha/DRAP1 family. {ECO:0000305}.
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DR   EMBL; BC127524; AAI27525.1; -; mRNA.
DR   RefSeq; NP_001071136.1; NM_001077668.2.
DR   AlphaFoldDB; A0JPP1; -.
DR   SMR; A0JPP1; -.
DR   STRING; 10116.ENSRNOP00000032674; -.
DR   iPTMnet; A0JPP1; -.
DR   PhosphoSitePlus; A0JPP1; -.
DR   jPOST; A0JPP1; -.
DR   PaxDb; A0JPP1; -.
DR   PeptideAtlas; A0JPP1; -.
DR   PRIDE; A0JPP1; -.
DR   Ensembl; ENSRNOT00000038138; ENSRNOP00000032674; ENSRNOG00000020527.
DR   GeneID; 293674; -.
DR   KEGG; rno:293674; -.
DR   UCSC; RGD:1308477; rat.
DR   CTD; 10589; -.
DR   RGD; 1308477; Drap1.
DR   eggNOG; KOG1659; Eukaryota.
DR   GeneTree; ENSGT00390000012424; -.
DR   HOGENOM; CLU_045277_10_0_1; -.
DR   InParanoid; A0JPP1; -.
DR   OMA; QYMHMGN; -.
DR   OrthoDB; 1504101at2759; -.
DR   PhylomeDB; A0JPP1; -.
DR   TreeFam; TF313964; -.
DR   PRO; PR:A0JPP1; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000020527; Expressed in testis and 20 other tissues.
DR   Genevisible; A0JPP1; RN.
DR   GO; GO:0017054; C:negative cofactor 2 complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR   GO; GO:0001046; F:core promoter sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; ISO:RGD.
DR   GO; GO:0001091; F:RNA polymerase II general transcription initiation factor binding; ISO:RGD.
DR   GO; GO:0017025; F:TBP-class protein binding; ISO:RGD.
DR   GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR   GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR003958; CBFA_NFYB_domain.
DR   InterPro; IPR009072; Histone-fold.
DR   Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..205
FT                   /note="Dr1-associated corepressor"
FT                   /id="PRO_0000311698"
FT   DOMAIN          14..77
FT                   /note="Histone-fold"
FT                   /evidence="ECO:0000255"
FT   REGION          91..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..153
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..194
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   205 AA;  22326 MW;  F84F24F0D18D8C87 CRC64;
     MPSKKKKYNA RFPPARIKKI MQTDEEIGKV AAAVPVIISR ALELFLESLL KKACQVTQSR
     NAKTMTTSHL KQCIELEQQF DFLKDLVASV PDMQGDGEDN HTDGDKGPRR GRKPGSSGRK
     NGGTGSKSKD KKLSGTDSEQ EDESEDTDTD GEEETPQAPP QASHPPAHFQ SPPTPFMPFT
     SPLPLPPAPP GPSAPEAEDE EDYDS