ID A0A3P9P727_POERE Unreviewed; 2106 AA.
AC A0A3P9P727;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 13 {ECO:0000256|RuleBase:RU364134};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000017620.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000017620.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000017620.1};
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 Ensembl; ENSPRET00000017807.1; ENSPREP00000017620.1; ENSPREG00000011827.1.
DR GeneTree; ENSGT00390000013680; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000011827; Expressed in caudal fin and 1 other cell type or tissue.
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; IPR021643; Mediator_Med13_N.
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; PF11597; Med13_N; 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:UP000242638};
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 11..229
FT /note="Mediator complex subunit Med13 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11597"
FT DOMAIN 1334..1663
FT /note="MID"
FT /evidence="ECO:0000259|Pfam:PF18296"
FT DOMAIN 1699..2095
FT /note="Mediator complex subunit Med13 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06333"
FT REGION 298..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1441..1570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1951..1984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..540
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..999
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1034
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1441..1507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1518..1555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1964..1984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2106 AA; 231836 MW; 5DD925E22954C63A CRC64;
MSSCFVPNGA SLEDCHSNIF CLADLTGIKW RRFVWQGPTS SPILFPVTEE DPILCSFSRC
LAADVLSVWR RHHTPGRREL WLFWWGDDPS FAELIHNELS SEENGEWESG LSYECRTLLF
KAIHNLLERC LMNRGFVRIG KWFVKPYQKE EKIINKSEHL SCAFTFFVHG DSNVCTSVEI
AQHQPLQRLG EEHLSLAQQS SSPLQVILSP YGLNGTLTSQ AFKMSDHPTQ KLIEEWRQFY
PICPNLKEVP EDKMEDADWE DDSLAAVEVL VAGVRMVYPS CLVLLPLSDL PAVVPQGSAN
TPGMQSGAHQ GQAAHRDSAM SSVTLTPPTS PEEAHTDYQP AQRWLKMSSG SDCYSSNNTL
HGGKIPRRLS SQMVETVWQE YNINRAGNKR KFTTLTNGAC EEEPDRSRLW DFVEPTHRPS
CNCSRPKNQK QRSSSTSGHP PSSGQPPQPA AKHKLGEKLE KGEKQQRRPQ TPFHHRNSVS
EEQSMEPQTQ RLCPRPQEEG SYPSLHHADT APPKAPSLHA HGPPADLVGS PPPPPLSPRP
CDHVDGELMP SGAKNSSTPI HQAFYPPSVE PCLMPQKGST EEPQPDSAAY PSNYNETLEP
TLFTGSAIKP GEDSTHNPWK YFNLPRKKAS SFLTPQLPMD KIRDDSSGGL ETVVSVTELM
CNSSRPLKVS QELVRTYTQR RNSHLGSSAG DGEDGDESDP YAFVDGDDEF SITEKRDKNG
PEKDCNKKQK VGPSIRSGLS EDCPCLTSPC NLFHFADGQG QSSCKPSAST SLIHEKDLVV
SLSDLEKMFN SDEDEQEVSW RKCSSAPECH FKSLDASDLM MMYPTPPSLD QNGYSPGNSG
TKDGLEMGAA LALLDSSQLS SHFKIEVEEG FCSPKPSEIK DFSFVYKPET CQSIIGCSMY
APLKTLPSQC LLPVKLPEDC VYTPSWTMGK MELMPPVSTV SLLTKDSVEP DYNQPFTPQT
NTPFLPGSAP PSNSGPGILP SPATPRFSVP TPRTPRTPRT PRGPSSVQGS LKYENSDLYS
PASTPSTCRP LSSVEPATVP SIPEAHSLYV TLILSESVMN LFKDCNFDSC CVCVCNMNIR
GADVGVYLKD NGEDQYPCTC GFSAVANRRF GQSAGLFLED ELDVVGRSSD AGRDTERRFE
ELRGSLKEKP PDELILLLQD QCTNPLAPMA GVEWPKPSAA AVAAPSSFLR VEERDCYNDC
YMALEHGRQF MDNMSGGKVD ETLVKSTSLH QWPKSADMSK LYSQDVLRVL LSLQPALQDT
IQKKGVRSWG VQGPLTWQQF HKMAGRGSYG TDESPEPLPI PTFLVGYEYD FVVLSPFGLP
YWEKLLLDPF GSQRDVGYVV ICPENQTLLR GAKTFFKDLS VMYEACQLGQ HKPICKSHPE
GVLTVGSPEG RSMTEQPLSD WFLKMAARES NNEAFHKLKL FAQVCRYDLA PNLSELPLDS
SLLSQRNPTK PAPQTSTSSS ASSGLQSTNT TSTNSSQPAQ VNSTPPPSSS SSSSSSSGSQ
TNGAMASGKP GSYMPFGSGG LQGSTTQNGP QQTNSQSAGG LGDGASSQPQ VSAETTMERD
KVGKPTDGES HAISYPPAIV VYIVDPFSYE NADKEVHSST YTLGLLRCFM EMLPFLPAHI
RNAVSVQIVP CQYLLQPVHS GDRHIYSQHL KSLAFSVYTQ CRRPLPNSTN FKALTGFGPG
LALDMALKNP ERPECLRLYT PSFILAPVKD KQTELGETFG EASQKYNVLF VGYCLSHDQR
WLLASCTDQH GELLESCIIS IDVPNRARRK KSSARRVGLQ KLWEWCVGLV QVTSLPWRVV
IGRLGRMGHG ELRDWSILLS RTNLQSLSKR LKETCRMCGI SAADTPSILS ACLVAMEPQG
SFVIMPDSVS TGSVFGRSTT LNMQTSQLST PQDTSCTHIL VFPTSAMVQV NTNTSEPIDI
SFNHINPDGS EGMGLFDLFG SDMDAELINI LPNSPTTSPV HSPGHHYHHG EAGKGQGADR
MESHEEALSI LQQPMALGYF ISTAKAGPLP DWFWSACPEA QNQCPLFLKA SLHLHVSSVQ
SDELLHSKHS HPLDSNHTSD VLRFVLEQYN ALSWLTCNPA TQDRRSCLPV HFVVLTQIYN
FIMNML
//
