ID A0A1W4W489_AGRPL Unreviewed; 2244 AA.
AC A0A1W4W489;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 13 {ECO:0000256|ARBA:ARBA00019618, ECO:0000256|RuleBase:RU364134};
GN Name=LOC108732592 {ECO:0000313|RefSeq:XP_018318971.1};
OS Agrilus planipennis (Emerald ash borer) (Agrilus marcopoli).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia;
OC Buprestoidea; Buprestidae; Agrilinae; Agrilus.
OX NCBI_TaxID=224129 {ECO:0000313|Proteomes:UP000192223, ECO:0000313|RefSeq:XP_018318971.1};
RN [1] {ECO:0000313|RefSeq:XP_018318971.1}
RP IDENTIFICATION.
RC TISSUE=Entire body {ECO:0000313|RefSeq:XP_018318971.1};
RG RefSeq;
RL Submitted (NOV-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_018318971.1; XM_018463469.2.
DR EnsemblMetazoa; XM_018463469.2; XP_018318971.1; LOC108732592.
DR GeneID; 108732592; -.
DR OrthoDB; 9289at2759; -.
DR Proteomes; UP000192223; Unplaced.
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:SF3; 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:UP000192223};
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 1471..1775
FT /note="MID"
FT /evidence="ECO:0000259|Pfam:PF18296"
FT DOMAIN 1813..2233
FT /note="Mediator complex subunit Med13 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06333"
FT REGION 311..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1569..1635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2063..2119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..577
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1041
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1058
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1181
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1581..1597
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1598..1635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2071..2093
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2103..2119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2244 AA; 243192 MW; FC2241E50823A56C CRC64;
MLGDFRMTVI VEIKISSDRP HSISKTQNTQ GDQGSWESGL SYECRSLLFK ALHNLIERCL
LSRDFVRIGK WFVQPHEGGS KSTEASSSSS THLSFSFAFF VHGESTVCAS VDVRQHPAVR
KLTRWHLQQA QASSQGLQVM LAPFGLAGTL TGHIFKPNES TTRLLEDWGQ FYPLDRTSMS
TGDLNIVEVV VGSSKMRYPS CYVLVTDMDD SANLPVLNSG IVGGTAATAP TGAGQPSITP
VPQTTPNVIQ QNGIKNGSST PVAIQSPPPS PVPVYSRVPP PGPFPVSIEH PSSMQKDPTA
ANVLPERTWQ ECILGGPPAP SPVLPSSVNG GGGGGATTAP SSASSSTSTP SQQPQSQQQQ
CNNGQMTQMN GPVGSGGLLT STDASSGTGG GNWDFVDPTR RANCTCSKCR KLCAGATTTG
TSGSSKWGSS GKVKGQRPSR IPFHRRSPVS LDITLTAAVV TTTTSASNND TVNSNNTAAT
PSNNNNGGSS SCSSNSNVVP TVPTTPVERC PGSYTPQGGP PSYPRTQESL AIPSVGSPPS
VAPSPLPNPN SQPASVPPGE QPMPTLSPHP PTVAPSPADK AQTPTDEAPP TNAGSVIDSP
MTNTHMDIKR EDEGVTGGLM GGGATIGGGT TGGAATAMKR PALSSKEYED ALGEEEHTLD
LLYDYSTLDA WLNHPVKRFK PDSKDSMRAI IRSGKMDLYS MYQQQSGLMA STASDLNHNN
PKGQQPLVIK QEIKQEPICQ METDSTIAIP NSLPHGTKRP GDPYEFEEEG GGAACNMDGF
KRGQNVKEEQ PTKDSKKVSS AGNLFTSEGL QPSYRDLDQI FDNSDDTSGD EGLQVQTPPG
SNKSTGVHED TNKRLYGSGG SGGGSGHGTC SNIGILRPEE LSKMFPTPPS LEPNPIASPC
GQFDLPPPDL ADLGAVARVK QEIYPSMGSP QEESIEDWSY VFKPPVICKM VGSSKYAPLV
NLPSAGLPAV VLPPQCVYKP SWLQHMEKPM TTAPQLAPNP TAIQPVATTA VVNNRPSPNT
TSSLPNSIHQ NISSYPSSPS HSAPPGFRPP PPPYELPSPA TSTASSYLNK NLNSVDAEPP
PMMLRTPEAS SLVVNILLGD TALNIFRDHN FDSCTLCVCN AGPKVVGNIQ GADASVYLMN
SNSSSSSTNP GDKIVGYGSM HQPNSPYPGA QGPPYGSMMS PPPPHHHNHH QGQQHHLAPI
FDEDSIKCSC GFSAVVNRRL SHRSGLFYED EMEITGIAED PSERKKPSLL SFLLQTSSLK
MDPSMEREQV DVIPHSIIEL VREQCVMIQS TANSLYRSAR YHRNNLVDHS YSSTVNILEF
TDGNELTTLA LEQSKQSESI LLCKAEDSLR PRGAGLGSHH RICVHRWPFL RAFGPQCNQD
IVRVMKGLQP LLQEAIRKKC QTRLWEPPSA VKGPLTWRQF HRLAGRGTDD RCEPQPVPSL
IVGHEKDWLS LSPYAVHHWE RLLLEPYSYA RDVAYIVVAP DNDAILPRVR TFFKELSTAY
ETCRLGRHSP ITKVLRDGIL RVGKTAKTKL GNEPVEEWFT CLGEGDATDM LKLYAQVCKH
HLAPHLQQVP MDKTLLDPPE TTPDKPAPSP MPPPNTPDNN SSGSGNNNPT SSSSSSQNSS
MMNSTDKAPS TPKSEQGKTF NILLKCTVYK INNLLLIYYL DSDSGNSKEM TPLLSSLSES
MHDDDDRQVP CVVIYMVEPF SMGCDQPDLQ RLACLALLRC FQSVLSSVPE NIRSNISFQI
ISQESVMELG KSRDRNRHID HMRALALSVF SQCRRLLVHT SNVKSLTGFG TAASADLFLK
TKDDKNRAPY KMYSPPYILA PIKEKVEPVE AFGLSNSDQG CVLYLSYCLS DDQSWLLAVA
TDERGEICEN VTINIEIPNR SKRKRASARR LGLQKLMDWT LGIMSLSVKQ WRLVVGRLGR
IGHGELKGWS WLLSRKNLLK ASKHLKEICN QCSLMYPHNV PCILSACLVS LEPDSVLRLM
PDQFTPDERF SQASVNSQLS TPQDVTCTHI LVFPTSATTQ SSQSAFQEQH INGPELGDDD
LFTVLNDDME TAMQTLNDDF SDIFNWPESG AAGGQSPTGS PRREESSRPG SPTFGMNGIG
RQGSPFPCNT NSRNNEPKEE VGQLLQQPLA LGYFVSTAPT GKMPKWFWAS CPHLEGVCPA
FLKNALHLHS PSIQQSSDEL LQQSAITSHP LDSQYTTDVL RYVLEGYNAL SWLALDSNTQ
DRLSCLPVHI QVLIQLYHLT ASFL
//