MED1_XENLA
ID MED1_XENLA Reviewed; 1570 AA.
AC Q6INP8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 1;
DE AltName: Full=Mediator complex subunit 1;
GN Name=med1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) 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).
CC {ECO:0000250|UniProtKB:Q15648}.
CC -!- SUBUNIT: Component of the Mediator complex.
CC {ECO:0000250|UniProtKB:Q15648}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15648}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 1 family.
CC {ECO:0000305}.
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DR EMBL; BC072226; AAH72226.1; -; mRNA.
DR RefSeq; NP_001085198.1; NM_001091729.1.
DR AlphaFoldDB; Q6INP8; -.
DR SMR; Q6INP8; -.
DR MaxQB; Q6INP8; -.
DR PRIDE; Q6INP8; -.
DR DNASU; 432291; -.
DR GeneID; 432291; -.
DR KEGG; xla:432291; -.
DR CTD; 5469; -.
DR OMA; HAMKLTY; -.
DR OrthoDB; 57581at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 432291; Expressed in egg cell and 19 other tissues.
DR GO; GO:0016592; C:mediator complex; IEA:InterPro.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:UniProt.
DR InterPro; IPR019680; Mediator_Med1.
DR Pfam; PF10744; Med1; 1.
PE 2: Evidence at transcript level;
KW Activator; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1570
FT /note="Mediator of RNA polymerase II transcription subunit
FT 1"
FT /id="PRO_0000302020"
FT REGION 592..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..1561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 585..589
FT /note="LXXLL motif 1"
FT MOTIF 626..630
FT /note="LXXLL motif 2"
FT COMPBIAS 633..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1010
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1041
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1419..1488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1506..1521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1528..1549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1570 AA; 165682 MW; B93DDDEEC5E2040F CRC64;
MSSLLERLHS KYSQNRPWPE TIKLVRQIME KRTGMMSGSH QHLVTCLETL QKALKVSSLS
AMTDRLESIA RQNGLTSHLS PNGTECYITT DMFYLEVLLD TEGQLCDVKV AHHRENPVSC
PELVEQLREK NFEDFSQHLK GLVNLYKVPG DNKLETKMYL ALQSLELDLT KMAAIYWQAT
NATVLEKILH GTVGYLTPRS GGQVMSLKYY VSPYDLFDDG TGASISLSEG HAVPRSLGMN
VSVTIEATTS MYKLPIAPLI VGSHAMDNKG TPSFTSITNA NSVDLPACFF LKFPQPIPVS
RAFIQKIEHC TGIPLIDGSH TFLPHYELVT QFELAKEKDP GPLNHNMRFY ASLPGQQHCY
FLNKDAPLPD GRSLQGTLLS KIPFQHPSRV PVILSLIRHQ VAYNTLIGSC VKRTMLKEDC
PGLLQFEVAP LSDSCFSISF QHPVNDSLVC VVMDVQDSTH VSCKLYKGLS DALICTDDFI
TKVVQRCMSI PVTMRAIRRK AETIQADTPA LSLIAETVED MVKKNLPPAS SPGYGMTSAL
SGLTTPTSSY TSGQNSSLFN MGMKERHDST GHGDDFNKVT QNPILTSLLQ ITNNTGGTLG
SSPTQPQHTP PPVSSPASNT KNHPMLMNLL KDNPAQDFSN LYGGSPMERQ NSSGSPRTEL
GASATGKPKK KRPRTGAEKM KNQTEDDFQR ELFSMDVDSQ NTIFDVGMAG DALDTPHITP
APSQCGTPPT VYQQSIPHAQ SNMQRMVRIP STDAIIPDVT DILSDIAEEA SKLSGPGEDC
PNLGTPVRDS SSSGHSQSTL FDTDVFQVDG GGGSGGENPY PDPVDLIVDS HGSPNSDSPN
TFFNSVDFNP DLLNSQSQSG FTDDLNDDSS QSGDNDFKDF AGPGLASLNI VSGLPVDGGD
GKYKMGLGAD TLDFSIISTG GSKTLGGPDI QETQSRSQSP LLSNDLGKDR PQKQKVKESS
NGGGAGGGLS GMQSAGMEGK SMKRSRTPSS DGKSKDKPPK RKKTESDGKS PSHITNRPFT
PPTSTGGSKS PGTSGRSQTP PGMATPPIPK ITIQIPKGTV SVGKPSSHGQ YSSSGSSSSS
SSKSHHGHSS LSSSASGKIK SNKSDGSSGM KIGSSGGGMY SGQSGQSSSQ SKNSSQSMGK
AGSSPITKHG LSSNVSNSSG SKTKPQGKPS VLMNPSLSKP NISPSHSRPS GGSDKMSSPM
KPMPGTPPSS KAKSPIGSGG QHLSGGGSNS TTKSSSGLVS SGSLSQKPNS SSSSSSSSSS
SSSSSSSSSS SFCGGVSQNL HGNSKGKSPS RNKKPSLTAV IDKLKHGVGT GGPGSEDPMD
GGGGGGSTGA PSHGMSSKHG MVVGEFPTKR EKSEKDKSKG SGSGGSSDPS KKGGGDSKGS
VGTGVAKIII SKHDGGSPSI KAKVTLQKPE GGGDGLRSQM QKNYGSPLIS GSTPKHERCS
PSHNKSPAYT PQALDSESES GSSSIAEKSY QNSPSSDDGG GSGSRAQTEY SAEKHKKHKK
EKKRLKDKDR DREKKKSYGM KPESWSKSPI SADPTMAMSG GSMMSSDRGV RPTPSFLMDD
DDLMDVPLTL