ID M7AXA2_CHEMY Unreviewed; 1882 AA.
AC M7AXA2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 13 {ECO:0000256|RuleBase:RU364134};
GN ORFNames=UY3_18636 {ECO:0000313|EMBL:EMP24398.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP24398.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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 EMBL; KB601989; EMP24398.1; -; Genomic_DNA.
DR STRING; 8469.M7AXA2; -.
DR eggNOG; KOG3600; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
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:SF1; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 13-LIKE; 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:UP000031443};
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 1183..1433
FT /note="MID"
FT /evidence="ECO:0000259|Pfam:PF18296"
FT DOMAIN 1469..1871
FT /note="Mediator complex subunit Med13 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06333"
FT REGION 126..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1284..1343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1718..1752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1284..1323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1882 AA; 207023 MW; 04CF7A8F89203C1F CRC64;
MAQSSPAPFQ VLLSPYGLNG TLTGQAYKMS DPATRKLIEE WQYFYPMVLK KKEGLKEEEE
LGYDDDFPVA VEIIVGGVRM VYPSAFVLIS QNDIPLSQSA ASAGGHISVG QQGLGSMKDS
SNCGMPLTPP TSPEQAIIGE SGGTQSSVSH SASQEGAVTL HSPKKSGKIP PKFHNHMVHR
VWKECILNRS QSKHKLFKQR CAIGPSRPTT ISQPGFSVGS SSSSSLPPPA SSKHKTTERQ
EKGEKLQKRP MMPFHHRPSV TEELCMEQDT SGQKLGLVGM EPSLEVSNSR KYEKQLSIPS
RNPSKQINLN PMDSPHSPTS PLPPTLSPQP RGQEAEHLDP PSVAVNPALY GNGLELQPLP
SLDDRTVLVG QRLPLMAEVS ETALYCGIIQ NNESSDKWQS YVLPASDDPE FKPPELRYDR
YDAKMEVNSD STALKRLLAQ PNKRFKILED NKPVQTLNYL DALPLIQQPG EGLGDVSDPY
TFEDGDIKYS FTGNKKCKLG TEKDPLKKNK SEDGIGTKEI PTTGHSTPVP DGKDAMSIFS
SAPKADTRQD CAAGRVGSSS LTQVTDLAPS LHDLDNIFDN SDEDELGAVS PALRSSKMPP
AGAEERPLGK DGRTAVPYPP TVADLQRMFP TPPSLEQHPA FSPVMNYKDG ISSETVTALG
MMESPMVNMV PTQLTEFKME VEEGLGSPKP EEIKDFSYVH KVPSFQPFVG SSMFAPLKIL
PSQCLLPLKI PDACMFRPSW AIPPKIEQLP MPPAATFIRD GYNNVPSVGS LADQDYLQMN
TPQMNTPVTL NSAAPASNSG AGVLPSPATP RFSVPTPRTP RTPRTPRGGG TASGQGSVKY
DSTDQGSPAS TPSTTRPLNS VEPPTVQPIP EAHSLYVTLI LSDSVLNIFK DRNFDSCCIC
ACNMNIKGAD VGLYIPDSSN EDQYRCTCGF SAIMNRKLGY NSGLFIEDEL DIFGKTSDIG
QAAERRLMMC QTTLLPQLGE GARRGQEPPM SLLLLLQNQH TQPFTSLSCL DYMSSNNRQT
LPFMNWSYDR VQADSNDSWI ECFNALEQGR QYVDNPTGGK VDEALVRSAT VHSWPHSNVL
DISMLSSQDV VRMLLSLQPF LQDAIQKKRT GRTWENIQHV QGPLTWQQFH KMAGRGTYGS
EESPEPLPIP TLLVGYDKDF LTISPFSLPF WERLLLDPYG GHRDVAYIVL CPENEALLDG
AKTFFRDLSA VYEMCRLGQH KPICKVLRDG IMRVGKTMAQ KVTDELVSEW FNQSWGSEEC
DNHSRLKLYA QVCRHHLGFS GIVGPGQNNS TGGNSTDRPP GSTGSGGDTE PGQNSSQQQQ
EGQESVTERE RIGIPTDPES ADSHAYPPAV VIYMVDPFTY TADEESASAN YWLLSLMRCY
TEMLDNLPDN MKNSFILQIV PCQYMLQTMK DEQVFYIQHL KSLAFSVYCQ CRRPLPTQIH
IKSLTGFGPA ASIEMTLKNP ERPSPIQLYS PPFILAPIKD KQTELGETFG EASQKYNVLF
VGYCLSHDQR WLLASCTDLH GELLETCIVN IDLPNRSRRS KVSARKIGLQ KLWEWCVGIV
QMTSLPWRVV IGRLGRLGHG ELKDWSILLG ECSLQTISKQ LKEVCRMCGI STADSPSILS
ACLVAMEPQG SFVVMPDAVT MGSVFGRSTA LNLQSSQLNT PQDASCTHIL VFPTSATIQV
APANYPNEDG FSPNNDDMFD LPFPDDMDND IGILITGNLH SSPNSSPVPS PGSPSGIGVG
SHFQHSRSQG ERLLSREAPE ELKQQPLALG YFVSTAKAEN LPQWFWSSCP QAQNQCPLFL
KASLHHHISV AQTDELLSVR NSQRVPHPLD SKTTSDVLRF VLEQYNALSW LTCNPATQDR
SSCLPVHFVV LTQLYNAIMN IL
//
