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Database: UniProt
Entry: A0A3P8VV71_CYNSE
LinkDB: A0A3P8VV71_CYNSE
Original site: A0A3P8VV71_CYNSE 
ID   A0A3P8VV71_CYNSE        Unreviewed;      2163 AA.
AC   A0A3P8VV71;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 13 {ECO:0000256|RuleBase:RU364134};
OS   Cynoglossus semilaevis (Tongue sole).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC   Cynoglossinae; Cynoglossus.
OX   NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000018227.1, ECO:0000313|Proteomes:UP000265120};
RN   [1] {ECO:0000313|Ensembl:ENSCSEP00000018227.1, ECO:0000313|Proteomes:UP000265120}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24487278;
RA   Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA   Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA   Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA   Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA   Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA   Zhao Y., Schartl M., Tang Q., Wang J.;
RT   "Whole-genome sequence of a flatfish provides insights into ZW sex
RT   chromosome evolution and adaptation to a benthic lifestyle.";
RL   Nat. Genet. 46:253-260(2014).
RN   [2] {ECO:0000313|Ensembl:ENSCSEP00000018227.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC       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. {ECO:0000256|RuleBase:RU364134}.
CC   -!- SUBUNIT: Component of the Mediator complex.
CC       {ECO:0000256|RuleBase:RU364134}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU364134}.
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 13 family.
CC       {ECO:0000256|ARBA:ARBA00009354, ECO:0000256|RuleBase:RU364134}.
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DR   RefSeq; XP_008331054.1; XM_008332832.2.
DR   STRING; 244447.ENSCSEP00000018227; -.
DR   Ensembl; ENSCSET00000018452.1; ENSCSEP00000018227.1; ENSCSEG00000011668.1.
DR   GeneID; 103395204; -.
DR   KEGG; csem:103395204; -.
DR   CTD; 100004024; -.
DR   GeneTree; ENSGT00390000013680; -.
DR   InParanoid; A0A3P8VV71; -.
DR   OrthoDB; 9289at2759; -.
DR   Proteomes; UP000265120; Chromosome 19.
DR   GO; GO:0016592; C:mediator complex; IEA:InterPro.
DR   GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   InterPro; IPR009401; Med13_C.
DR   InterPro; IPR041285; MID_MedPIWI.
DR   PANTHER; PTHR48249; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 13; 1.
DR   PANTHER; PTHR48249:SF4; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 13; 1.
DR   Pfam; PF06333; Med13_C; 1.
DR   Pfam; PF18296; MID_MedPIWI; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|RuleBase:RU364134};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364134};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265120};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491, ECO:0000256|RuleBase:RU364134};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU364134};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|RuleBase:RU364134}.
FT   DOMAIN          1375..1720
FT                   /note="MID"
FT                   /evidence="ECO:0000259|Pfam:PF18296"
FT   DOMAIN          1756..2152
FT                   /note="Mediator complex subunit Med13 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06333"
FT   REGION          328..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          427..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          532..616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          739..776
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          802..830
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          982..1059
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1479..1546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1564..1612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2009..2044
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..460
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..481
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..501
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..548
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..583
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..613
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        739..763
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        982..1009
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1013..1027
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1028..1059
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1564..1604
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2029..2043
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2163 AA;  237404 MW;  6B5DA088D9D230EC CRC64;
     MSSCFVPNGA SLEDCHSNLF CLADLTGIKW KRFVWQGPTS APILFPVTEE DPILCSFSRC
     LKADVLSVWR RSQRQGRREL WLFWWGDDPN FADLIHHELA VEDDGLWENG LSYECRTLLF
     KAIHNLLERC LMNRSFVRIG KWFVKPYEKD EKPINKSEHL SCAFTFFLHG DSNVCTSVEI
     NQHQPVYHLT EEHLTLAQQA SNPFQVILSP FGLNGTLTGQ SFKMSDPPTQ KLIEEWNQFY
     PIGPSAKQGL SEDKTEDMHW EDDSLASVEV LVGGVRMVYP ACLVLVPQSD IPVVAPVGSS
     HCTAIYSGGH QVPASQREPA ISLVTLTPPT SPEEVQTGSD NTKVDSNSSK KWVNMPPSSD
     GFSMDRTSHH GGKIPRRLST QVVERVWQEC NINRAQNKRK YSAATNGTCE EELTEKVGTW
     NFVEPSQRSH CNCSRHKSVK QRTGSTPGQA QLSGQASQPP TKHKAGGEKL EKGEKQQKRP
     QTPFHHRSLT NDEASLDSET NVGQRLAMRN QDGGRLPSIC SADVSAIQKT PQLHSGAVNS
     GPSDQANSPQ PPSLSPHPCE RSEESGEGMK NPSTPNSQHF YQQPPDPCLV GVKGGSEELS
     STESISQHFN SHHPHPGVSA YSDSPEPVVY IGAAVNQEED NSHTPWRLFN LPRRKEAEVP
     TPLLPGDKLK DEASLSQENL VSVTEIMSTS KWPLKVSEEL IQMYRARRNQ YLSAAITDGD
     HEPEADPYAF EEGDVKFTFS KKDKAGGERD PGKKHKGEDG GSCPSDDAQR AAAHNHTVST
     SLIHEIDLAV SINDLDNLFN SDEDELAPGS RRPVNGTDEK FGNKDPKPST LDPVSCISSA
     DLHQMFPTPP SLEQHIMGYS PMNMCSKDYG SMESNAGMTT LDGTSSLGNH FKIEVEESFC
     SPKPSEIKDY SFVYKPELCQ AFVGCSMFAP LKTLPSQCLP PIKMPEEGIY RPSWTMGRDM
     TFLSKDSTIT SVANVMDQDY NQTYTPQTHT PFMSNSAPPS NSGTGILPSP ATPRFSAPTP
     RTPRTPRTPR GPSSVQGSLK YENSDLYSPA STPSTCRPLN SVEPATVPSI PEAHSLYVTL
     ILSESVMNLF KDCNFDSCCI CVCNMNIKGA DVGVYLSDPV SEAQEPCSCG FSAVVNRRYG
     NGSGLFLEDE LDIIGRGSDV SREAEKRFEE LRLSSLEKSG VGRGDRVPDE LIVLVQDQCT
     NPFSPISILE HDLVTRGTGG VSVPPCVRVE EKDYCSDCYM ALEHGRQFMD NMSGGKVDEA
     LVKSSCLHHW GKQNAVDVSA LCSQDVLRAL MSLQPVLQDA IQKKRTVRSW GVQGPLTWQQ
     FHKMAGRGSY GTDESPEPLP IPTFLVGYEY DFVVLSPFCL PYWEKLLLDP FGSQRDIGYL
     VICPDNEALL SGAKSFFRDL TAVYESCRLG QHRPISKGYP DGIVLVGGSG AKSLMDQPVS
     DWFLKAASGN SDAFAKLKLY AQVCRHNLAP YLASQPLDSS LLTQPNPSPS SSQSSSTQLS
     SSTSSSVGQQ SSTTAAGPTV PNSSSNAGSG NSSASTNNLV TTSGQSGPAL LSAKANCFPS
     FGSMSSQGQG VGPQSGQLGQ QAGTQNAGSS GDNSSSQAQG PSEPPESTLE REKVGLPTDG
     ESHAITYPPA IVVYIIDPFS YEETENGTGP VPAHSSVWTL GLLRCYLEML QFLPAHIRNS
     VYVQIVPCQY LLQPVRREER HIYAQHLKSL AFSVFAQCRR PLPISTNVKS LTGFGPGLAI
     DTALKSPERP ECLRLYTPPF ILAPVKDKQT ELGETFGEAS QKYNVLFVGY CLSHDQRWLL
     ATCTDLYGEL LETCIINVDV PNRARRKKGS VRRFGLQKLW DWCLGLVQMT SVPWRVVIGR
     LGRIGHGELK DWSILLSRRN LQSLSRRLKD MCRMCGISAS DTPSILSVCL VAMEPQGSFI
     IMPDSVSTGS VFGRSTTLTM QTSQLSTPQD TSCTHILVFP TSAFVQVASS SYTNIDTNID
     ILNATTDGSD IFDLLDQENE LVDPDIINIS PNTSPVHSPG SHYHHGGDGS KGQSTDRMES
     HEEVPNLLQQ PLALGYFVST ARAGPLPDWF WSACPQAQNQ CPLFLKASLH LHVSSVQSDE
     LLHSKHSHPL DSNQTSDVLR YVLEQYNALS WLTCDPATQD RRSCLPIHFV VLNQMYNFIM
     NML
//
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