MED13_CAEEL
ID MED13_CAEEL Reviewed; 2862 AA.
AC Q93442; Q93863;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 13;
DE AltName: Full=CeTRAP240;
DE AltName: Full=Lethal protein 19;
DE AltName: Full=Mediator complex subunit 13;
GN Name=let-19; Synonyms=mdt-13, psa-7; ORFNames=K08F8.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH SUR-2 AND LET-425,
RP AND SUBCELLULAR LOCATION.
RX PubMed=15790964; DOI=10.1242/dev.01776;
RA Yoda A., Kouike H., Okano H., Sawa H.;
RT "Components of the transcriptional Mediator complex are required for
RT asymmetric cell division in C. elegans.";
RL Development 132:1885-1893(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15073178; DOI=10.1074/jbc.m401242200;
RA Wang J.-C., Walker A., Blackwell T.K., Yamamoto K.R.;
RT "The Caenorhabditis elegans ortholog of TRAP240, CeTRAP240/let-19,
RT selectively modulates gene expression and is essential for embryogenesis.";
RL J. Biol. Chem. 279:29270-29277(2004).
CC -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC regulated gene 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). Required for
CC asymmetric division of T-cells and for hypodermal development.
CC {ECO:0000250, ECO:0000269|PubMed:15073178,
CC ECO:0000269|PubMed:15790964}.
CC -!- SUBUNIT: Component of the Mediator complex (By similarity). Interacts
CC with sur-2/mdt-23 and let-425/mdt-6. {ECO:0000250,
CC ECO:0000269|PubMed:15790964}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15073178,
CC ECO:0000269|PubMed:15790964}.
CC -!- TISSUE SPECIFICITY: Widely expressed in most adult tissues including
CC the vulva, tail neurons, skeletal muscle, hypodermal cells, the
CC excretory canal and pharynx. {ECO:0000269|PubMed:15073178}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed in larvae and embryos.
CC {ECO:0000269|PubMed:15073178}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 13 family.
CC {ECO:0000305}.
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DR EMBL; AB223006; BAE16563.1; -; mRNA.
DR EMBL; Z66497; CAA91289.2; -; Genomic_DNA.
DR EMBL; Z68314; CAA91289.2; JOINED; Genomic_DNA.
DR PIR; T20566; T20566.
DR RefSeq; NP_495866.2; NM_063465.4.
DR SMR; Q93442; -.
DR BioGRID; 39729; 7.
DR IntAct; Q93442; 4.
DR STRING; 6239.K08F8.6; -.
DR EPD; Q93442; -.
DR PaxDb; Q93442; -.
DR PeptideAtlas; Q93442; -.
DR PRIDE; Q93442; -.
DR EnsemblMetazoa; K08F8.6.1; K08F8.6.1; WBGene00002295.
DR GeneID; 174402; -.
DR KEGG; cel:CELE_K08F8.6; -.
DR UCSC; K08F8.6; c. elegans.
DR CTD; 174402; -.
DR WormBase; K08F8.6; CE37536; WBGene00002295; let-19.
DR eggNOG; KOG3600; Eukaryota.
DR GeneTree; ENSGT00390000013680; -.
DR HOGENOM; CLU_226203_0_0_1; -.
DR InParanoid; Q93442; -.
DR OMA; WRFFDRK; -.
DR OrthoDB; 30695at2759; -.
DR SignaLink; Q93442; -.
DR PRO; PR:Q93442; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00002295; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR009401; Med13_C.
DR InterPro; IPR021643; Mediator_Med13_N.
DR InterPro; IPR041285; MID_MedPIWI.
DR Pfam; PF06333; Med13_C; 1.
DR Pfam; PF11597; Med13_N; 1.
DR Pfam; PF18296; MID_MedPIWI; 2.
PE 1: Evidence at protein level;
KW Activator; Coiled coil; Developmental protein; Nucleus; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..2862
FT /note="Mediator of RNA polymerase II transcription subunit
FT 13"
FT /id="PRO_0000314244"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1218..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1976..2009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2125..2151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2165..2192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2230..2862
FT /note="Mediates transcriptional repression"
FT REGION 2785..2811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 357..392
FT /evidence="ECO:0000255"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..640
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1270
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1988..2009
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2125..2141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2862 AA; 325137 MW; C035FBFE9121D1FA CRC64;
MSSAKDSDKD ASRKMKLQKR PEWNNGGSLE DCISNVYALL ELPGIKWKCY RTKPNAPRGV
ALTADFVLKA YSKCLLDGIL CTWRRKPLPP TDNKETPKLT NFSNDAPKEL WVFWYDDEPA
LLQKNCEGLD NDDELSSANQ MNIVSYEVRT IIFKALHVVL ERDLTKDGFV RFGRWFTVPY
DARENYLHFT YPSHSPAIRF NFFVHGSSTI CASVQAQRQP TLITLARRHL ECKTKRVVVV
VGPWSMRGQL VQDQIALLAD PKIQESAEKE WNQWKDYLQM EEKEPENVSE ERQKSPDSDP
PAPPQTTRVL LADSSDEEQS QSFEAIDESK KDDIPQRLRW MYEPDYRQEK SKEETPEEKE
KREQSREVRK QRRKLREERR KEVERQRTEV KNPDDYDSDV VTDEDVGEKE ECVNNDVPKM
VLLDIDGVRL LYPSKFLCVT IDEDRQMLES IGLKTNQQPP ELQAQNRRPR NKLVVNVANP
ILSTMAVYQY CENERLISKE NVPQKSATSG QLLPPLKEKF LNWKFTAKKY GCRGDVSCRH
CAEAEYQGES DGQVILDVDR HNRFLKYGPY TENSIRWHKI RSRIQKKFDF HAYHKKHPIG
PITPRKAGDS VKQTKQLSAV KRRRRARRER AQKKRRDKKR PTGSTRADSE DDSFRMDKLS
QDDWANFEGE HPKGIPEIEV DKDFELHNDI KIPKVPNDDN YKPKSFLPIT YLTNNVDNND
FESMPGDDDM SEERFNQIFK DKYNRWKPGM SRAEKIEHAH YQFDPSNQMT GSPREYHLKD
LPKKIQKYES ILPTPKGNKF FKGSICRKGL RGYDEICADQ DEKEMMRKAK WLKKARRKVS
KQQIKKAGQY HIDMQKQIVK RSLKRAIRKL KLTTKKDSQS KGTKQQKLVL LSYKKKKVDE
KKFQQYLKEV ENVLDKLDVN SFCKKNEKAG FSEKAIPSGY IIPDYESSIH CGMEEESDSE
IDEPRHGLGE GTCGQYLEGE SVDLADMEHH HNELPMEVTS IGHIRTVGEH IGPDGMLSPP
ASNEMPKGGP LSVGPPSIES QGLNQIYPTP PSVQMLLGDA AQAHSPVMHT KSRYAMNTLE
DDVERIAVPG GVGSLVEIEA DDIETKNMQK WSKLSNQSKL SKFIALSCKD PFLKSKKKKY
DTPVTSKFKI ENEPPSMSAE LVYAPMVTRN FYSAPHRTFG TLAQKVVDKR PSQFAIPSTS
TAAHPGLTTP MASIFQSPTM PPPHTPSPFS AGPMSHHPMG PPAYPGTPGS FPPTTPTYPG
MTPRPGPNFG PPGPVYPNSQ QMMGPGGYPP QMGMINSQRH FQNQQMYQQQ MVRMQQMRQM
GGPPGYGAPG VSPYQQVNAI TSPAGFGMPP NGPSSVQRLN NFVNQSQFGP NNGHPTPPYG
YMQQMIPQSP NFNQQYNGMG NQLMSPIHQH QFHQQQMVQQ QQQQQMQMHR QQMQMQNQNM
SQPFQPPTAQ MLQMQQNEQM RIAFSTLSER DKAKFQKRQG QLRSGIMPKS LQPAVLKNLK
NPPDANIPYM KQDALFRPPE SNSLQGESLT IAIVLSDTLL DLHFDSVFDA CPICSCSVSI
RSRDIGMYIT PHTVLYSTER GHTNMREHTT GPWSGFNVNS ATNCTCGFSA IRHRYLSCCS
GLFEEDADEA TASEHAVAPV IPPLDYPKKS TARDMSWFDS KSVHDLALLD QIRQMAFSNS
LGKAVSHMAT IKEHNRNLAI AVDLGNDVTV PSEYILSHVD ALELLMLGNS VLGPMKNTSI
ANQVASHNKF LGFFHPWGIQ IANGMTELEA SEWVDLLGVV TPTLEGSMKQ ARHIPAETPF
ELDGPMTWKQ IVTKSNRGKP PADDEEDFSL PEPVPAIMRA LTKEAIRAAP NIEQYYEQAG
LGPVDQPKDV MYITVIPDDD DIYSRTVEFM DTLTRTYEKM RLGRHIPFPV STGTATRFRE
AFKSCQSQFP FQEQQHLAYT NQTLRNMPQT LADTPDPVNS DPKVWSRRAK RKLDFEEELK
LPEAGSETID ESDDDEENEE VSKEENNELI DSEDVMDEVP KGFYEREGIL RVGAPMEPSR
SPHTVTNTPE FDNMTKYLSD ENGFVSRLRL YLQQMEDLVH FALSENPEAF DRRGYRYQLA
VEGRLKRQKH KMDIIEERLR FEASKDFDEQ SDRKEPLEEN DPEITPGIVI SNNPVESWID
DELEEKRQQR QKENEQYPPE AQQAPSPVPA GMIHIPETLS KEERAVQPTL EMILADPATV
APINAQNIVW KQRDTRVPNP FPSSNQPPVA FEAAGSPDTD AYSTLPHVIV VYVVNPFSYG
PEGHSALHMR IAILAFIRAF NSIMCKIPYE KRPQLQLEIV GMEGMDNVAK PIPDYFNDAK
IPFDLLNDRP IRVERPGESV QGELARSLSI AVYTHPRVFF PDVYKSASAR CMTAFGPGSQ
LMNTINKIEA LNKDSFARMA KRSKTTLDTM DMYRHPGMIQ AQQSTEKKNY IAYRVPSNIA
VLAPPPMVYQ MDEKGKAIMN QLDEQTLFIS YCLVGTDFLV ATATDAQGKL IDNCISNIKP
RRQSNQVYRY RNKTQILDGM GKLWSFILGI MASETKNWRL VVGRLGRIGH GEFRAWTHLL
NKTSLLRYSG SLKDICGACR SMPSVIGTPA ILSACLITLE PEPSIRIMPE FHDQELSTKK
SFLFQTPGDL SCTHILTFPV GTEINLEVQD QTADTKADEN WEFGDLDIME GLDDGDTEIM
KDLGLETPSS AAIRQTGGPS MFFSEDSSSI EIQNQPLASG YYISTAPAPE LPAWFWATCP
SAKRHSPVHL KSSLHIHISE VKNDDIAMES TKEKEKDKEK DEKDAHPLES RQTEEVLRHV
LESYNALSWL NLNRQTGDRY SCLPIHIQHL LRLYHSVARL LA
