ID MED13_DICDI Reviewed; 2678 AA.
AC Q54S20; Q9NDS4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 13;
DE AltName: Full=Aggregation minus B protein;
DE AltName: Full=Mediator complex subunit 13;
GN Name=amiB; Synonyms=med13; ORFNames=DDB_G0282375;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=AX2;
RX PubMed=10651904; DOI=10.1046/j.1365-2443.2000.00305.x;
RA Kon T., Adachi H., Sutoh K.;
RT "amiB, a novel gene required for the growth/differentiation transition in
RT Dictyostelium.";
RL Genes Cells 5:43-55(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=AX2;
RX PubMed=15259052; DOI=10.1002/cm.20015;
RA Asano Y., Mizuno T., Kon T., Nagasaki A., Sutoh K., Uyeda T.Q.;
RT "Keratocyte-like locomotion in amiB-null Dictyostelium cells.";
RL Cell Motil. Cytoskeleton 59:17-27(2004).
RN [4]
RP NOMENCLATURE.
RX PubMed=18515835; DOI=10.1093/nar/gkn349;
RA Bourbon H.-M.;
RT "Comparative genomics supports a deep evolutionary origin for the large,
RT four-module transcriptional mediator complex.";
RL Nucleic Acids Res. 36:3993-4008(2008).
CC -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC the 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 (By similarity). Required for the
CC starvation-induced activation of the ACA (adenylyl cyclase) expression
CC pathway at the growth/differentiation transition. {ECO:0000250}.
CC -!- SUBUNIT: Component of the Mediator complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: The level of mRNA increases 4 hours after starting
CC starvation and remains relatively constant thereafter.
CC {ECO:0000269|PubMed:10651904}.
CC -!- DISRUPTION PHENOTYPE: When starved, cells fail to turn off expression
CC of the growth-phase gene cprD and to turn on expression of the adenylyl
CC cyclase gene, resulting in an undetectable level of cAMP and a strong
CC reduction of the cAMP-relay response. They join streams of aggregating
CC cells but with less efficiency than wild-type cells and show a
CC dramatically reduced rate of sporulation. In the migratory slug, they
CC are almost exclusively located in the posterior region and many cells
CC are found in the slime trail that is left behind the slug. When the
CC fruiting body is formed, most cells are found in the basal disks while
CC a minor part is located in the mature spores and stalks. Starved mutant
CC cells are elongated laterally and form one large laemllipodium along
CC the front side arc of the cell. They have a keratocyte-like behavior,
CC moving persistently without changing directions over long distances.
CC {ECO:0000269|PubMed:10651904, ECO:0000269|PubMed:15259052}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 13 family.
CC {ECO:0000305}.
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DR EMBL; AB030033; BAB01489.1; -; Genomic_DNA.
DR EMBL; AAFI02000047; EAL66047.1; -; Genomic_DNA.
DR RefSeq; XP_640219.1; XM_635127.1.
DR AlphaFoldDB; Q54S20; -.
DR STRING; 44689.Q54S20; -.
DR PaxDb; 44689-DDB0214900; -.
DR EnsemblProtists; EAL66047; EAL66047; DDB_G0282375.
DR GeneID; 8623759; -.
DR KEGG; ddi:DDB_G0282375; -.
DR dictyBase; DDB_G0282375; amiB.
DR eggNOG; KOG3600; Eukaryota.
DR HOGENOM; CLU_227451_0_0_1; -.
DR InParanoid; Q54S20; -.
DR OMA; NKCRRIS; -.
DR PRO; PR:Q54S20; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0016592; C:mediator complex; ISS:dictyBase.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0048870; P:cell motility; IMP:dictyBase.
DR GO; GO:0006935; P:chemotaxis; IMP:dictyBase.
DR GO; GO:0010468; P:regulation of gene expression; IMP:dictyBase.
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; PTHR23261; GROUNDHOG-RELATED; 1.
DR PANTHER; PTHR23261:SF80; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 13; 1.
DR Pfam; PF06333; Med13_C; 1.
DR Pfam; PF18296; MID_MedPIWI; 1.
PE 2: Evidence at transcript level;
KW Activator; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..2678
FT /note="Mediator of RNA polymerase II transcription subunit
FT 13"
FT /id="PRO_0000327756"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1278..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1462..1502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1806..1838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2075..2105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2225..2307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2656..2678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1092
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1235
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1278..1350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1373
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1806..1830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 1993
FT /note="A -> R (in Ref. 1; BAB01489)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2678 AA; 298838 MW; 81CD1A57137AC706 CRC64;
MMGTKVPSYN NKQQSGSNAG GNVNNNNNGP NINNPNNPNN TNSLPTTSGY NSSRFSVPNL
DTDNFMTNII SMGVNKVGWA LYRSNSNNNN NNINNNSSSS SSSNTSNNIN SNTLVNDPIL
LAYLKTIELG VPCLWRKTRS KKPINNSSNN SNITSSTSTD SSLKNRLKNS PSETTPPNTT
NNNSNNVTKD SPPNATNKMS TSPKSLSPTI SNNNNNTTAA ATTTTTTTNN SSNSPTSPTN
NNNNNNNNNS PSSHNVVNSP PSTSSRSPPT VASVTSNTST IQPISPIINR QTSSHNYQQP
QQPYYNHQPL QPIQEYITTY ELWVFNISNT SLLDFSHLNN VESGIVNLDN IGCNNSVIVQ
YLFKSLYNLV EYNMVSNDFI KIGNSFIKSS HILQKQKQSR NDYNNSIISG SVGSKKRLFE
DFTNLYIEDD CLLSCSFSFF IYNKSIHLHF NVDKKRLKPL QELMKSEYIN SPLFTSPNAF
IAFFNNNNKN NINNNSNNII NNNNNSNINN NINNNNNQQQ QQQQQQQQQQ QQQQQQQQQQ
QQQQQQQQQQ QQQQQQTINN NSNNISSNND NNNTPSQMVP SIDGHDSSSS SSTPSQVTMQ
TTPTQEFSNN NNNNISINTT TVPITATTAT ATNKITTAAT TTTTINNNNN KIQTESFGST
RNKKLNDEEE INFSLSSQQW KQLFNIGLAN KAIIPKQQTP QQQEQQQIIG TIFKKNQLEV
PKSIKTIITR GNSLPLINTF FPIELLFKFF PPISDISQYT YHEKLKEFGL EIFDKSPYAL
LEKGLNLFIN NNNINIENNN NTSNEINNTG TQIPTKYKYV DFWSLPLFHS KESLIYGNDH
FNATYCVKAV PSPSSPLTQH PSSPHSPFNN VNSPKSPQHP PSPKTPMISD DDQSLTANNE
KKRHGKSQKK GRSSKRKKDD NSNNNNNNNT TTTSTITATT TTTTPTAATT GNDNFLAPQS
KPPPSNIQET SQPQSLTTVQ PQPPPQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ
QQQQVVSSFS GQGLNSSMDL FGSDAFDTFK NKEDDLMHLS DTDIDLDLWT SHYVPPNQPT
QNGSQKNNQR PLPVEDPFQV FQVPNKPATT TTTTTTTTTP TPNPTTTTTQ PQTQPQQQSQ
QQQQPQQTNP ILPTNSNLIT NQKPQQYQPP LQDPFQSIDS QQPKSIQSPT LTNQPIGMVS
PTLTNQPLQQ YQPPPPPTQQ PQQAHLKPPP PKQPSAKKNS KDGINSDENK PFLDGQFLCP
VPYKAPSLSQ NQLPILHLPH NTEQSPSNDD LSNPNHLHHG TPTSAISGVG GSSSSSGNNM
IGSGGIVGSG GGNTNVSGSG GGMVSDPSKL TYSSEHHDPH HHHHHHHHHH PQNSQNLRNS
YGNSNGVGGS QDESIDGLTT VYRNLTLSRP LGDNKNKNNA PYYCAPSYKP LDEHSLPHQL
KFEYSYTPLV KPQNQLNQTK YSPFSNSHHN HHHNTTTNNN NNHNNNNNNN HPNNHHQNNN
HHHLNITSSL FQPSNIQNVN SLPNIGSQKI MSISPPITPP MKGGHMIGTD INKNNNKKNN
DEDENLEILS TIKQKDVNGL DSNLSSSALL SFFDQAINIK TTPPRSPVLS GYSGGGSNMN
NGINGNSGFI GNGNSGFNTI SSYQQNNISI EESLDLAFTI QQMTITNYDS TFGFSIDNSP
LIKQSIDYYL ENWLKIYTET GKVFNHHSLQ FLTEESISDA LDTVIDPLTT NTILETTVKT
LFTFSNEIFK KIFPLSSFPL SIKEFCHLPS ITLNNINNNI DLLNSQTYQN TNNSSSGGGI
ESQQYFSGSS GLNNSNDRNS MIPMDNSDDT SDLMSMDDHN SKNLITGTSL ISTTASGAGA
AITTNLINQN YEEFEWLPIP KIIVGYKEDW LEVPISTIKF WDKAQLEPYS PKKNITYFVL
CPDTTAMRMH VPAFFSDLSC IYETNHLGNH VTQQQSQVQQ AAAAAVAASQ PTQQSSQHQS
QQQQQQAAQQ AAAAAAAAAA AQKNSSPFYN GIYYIPSAAN TEFNPQTFIN SYLLTCIQFG
DYLKELSTKY SENNCMVLYI VNPFSDLSQI SLSNQNQNQN QNSNSNESQQ QQQQQSNNKQ
KQTQTNEDIN HIRNSYLFMS SCFQTIVRDI TCNQSLSITI QTIPIEQILF DDHPSIPVSK
ELAFSVFNKC RRISTISPMN FSINMNNINN MIGNNNSNSN NSSGWYYQLF NKIYEPLFIL
SNESSSSSSS TISTSTSAST STSTSNTTTK NQQQQSQSQQ SQQQSQQPKQ LSTPTTPTTN
SVSNSPSLQP QPLQTPNQLQ PHQQEQKQQQ QIPIIHFSYM LSDDNKWISC TIVDEQGELL
ENKLIPLAYS QIIGDYIWKD SFQNAWFFLT EIIGLSLSGQ PCQVVIGKFG IISMQEYNDW
KTTIIHFEDN LEVIKQHQQQ SQSQNYSSTI DQIYKIENVI FLNLTLNNNI KSFLTEYLND
SKLSNSNNIK SVSPLSGQSF AIYPESPIMY TYNFPMNDNN DDYNSILNNN NNNILPPLST
SFVITSPSNL SGSVLTPTTT NSNVINNNQS KKEWPFTYML SIVGIQSLQH QQQQQQQQQQ
QQQQQHPNII NHQELIRSIT RSYHRLSYLN ISPRYPDRLS ILPIHFSISK RMSRTVCLIS
PLNPIPPPIL FNRCPKLTPN SKQSPSPINS PHLNSNNT
//
