MED26_DANRE
ID MED26_DANRE Reviewed; 589 AA.
AC Q90YL3; Q7ZVI4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 26;
DE AltName: Full=Cofactor required for Sp1 transcriptional activation subunit 7;
DE Short=CRSP complex subunit 7;
DE AltName: Full=Mediator complex subunit 26;
GN Name=med26; Synonyms=crsp7;
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 [MRNA].
RA Hartmann E.;
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC the regulated transcription of nearly all RNA polymerase II-dependent
CC genes. Mediator functions as a bridge to convey information from gene-
CC specific regulatory proteins to the basal RNA polymerase II
CC transcription machinery. Mediator is recruited to promoters by direct
CC interactions with regulatory proteins and serves as a scaffold for the
CC assembly of a functional preinitiation complex with RNA polymerase II
CC and the general transcription factors (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the Mediator complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 26 family.
CC {ECO:0000305}.
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DR EMBL; AY034615; AAK61395.1; -; mRNA.
DR EMBL; BC045849; AAH45849.1; -; mRNA.
DR RefSeq; NP_998224.1; NM_213059.1.
DR AlphaFoldDB; Q90YL3; -.
DR SMR; Q90YL3; -.
DR PaxDb; Q90YL3; -.
DR GeneID; 406332; -.
DR KEGG; dre:406332; -.
DR CTD; 406332; -.
DR ZFIN; ZDB-GENE-040426-2005; crsp7.
DR InParanoid; Q90YL3; -.
DR OrthoDB; 459216at2759; -.
DR PhylomeDB; Q90YL3; -.
DR Reactome; R-DRE-212436; Generic Transcription Pathway.
DR PRO; PR:Q90YL3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0070847; C:core mediator complex; IBA:GO_Central.
DR GO; GO:0016592; C:mediator complex; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR Gene3D; 1.20.930.10; -; 1.
DR InterPro; IPR042376; MED26.
DR InterPro; IPR031416; Med26_C.
DR InterPro; IPR031417; Med26_Mid.
DR InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR017923; TFIIS_N.
DR PANTHER; PTHR15201; PTHR15201; 1.
DR Pfam; PF08711; Med26; 1.
DR Pfam; PF15693; Med26_C; 1.
DR Pfam; PF15694; Med26_M; 1.
DR SMART; SM00509; TFS2N; 1.
DR SUPFAM; SSF47676; SSF47676; 1.
DR PROSITE; PS51319; TFIIS_N; 1.
PE 2: Evidence at transcript level;
KW Activator; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..589
FT /note="Mediator of RNA polymerase II transcription subunit
FT 26"
FT /id="PRO_0000304960"
FT DOMAIN 10..87
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT REGION 83..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 21
FT /note="S -> G (in Ref. 2; AAH45849)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="K -> R (in Ref. 1; AAK61395)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="N -> S (in Ref. 2; AAH45849)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 589 AA; 65030 MW; 56FA22A35935B246 CRC64;
MTTASATPQQ MRDRLLQAID SHSNICNMVA VLDVITNLEK YPITKEALEE TRLGKLINDV
RKKTKDEDLA KRAKKLLRNW QKLIEPGQGD TPVRGPPNVP GSANGGAHPC RTDTPPAVPP
PSKVAPELKT RNDIHNTYSP KAEKSSSRKR RAEQRDSPHL PAKMSKTSLY EPVYSSSPPS
NGIRGTPEPL LEKDDEVPSD RIRLEHLDND RHNKIPVNAV KPHPSSPGLT KLPSTSSLLK
ASVLQQARVD SGGQHQPKSP RYSSSPRSAT HETMAKRSTT YAPKGTLSSP SLNSAQVPSP
LPTLQPLTSP AQVCISDGPS SVGLEGSLHL HRSSDRVSQP PHSTATLEPL SGALLATHGL
EGLETKAERE GASSNSDGKK RKKYRPRDYT VNLQGQSSED RTKPRLKERR LTFDPVTGQI
KPLTPKESHQ EEECHGQPIP EPSVRTDIPQ QKPPTSVPNP FQQTNWKELS RNEIIQSYLN
LQSNVLTSSG AQTHGAHFFM TEYLKREEHD VKEPRKMHVL APGSSTTELP GVSRDVTNED
LLRIHNEHWP GVNGCYDTKG AWFDWTDCIS LDPHGDESKL NILPYVCLD
