MBLK1_APIME
ID MBLK1_APIME Reviewed; 1598 AA.
AC Q95YM8;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Mushroom body large-type Kenyon cell-specific protein 1;
GN Name=Mblk-1;
OS Apis mellifera (Honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC Apis.
OX NCBI_TaxID=7460;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAB64310.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Mushroom body {ECO:0000269|PubMed:11881813};
RX PubMed=11881813; DOI=10.1046/j.0962-1075.2001.00288.x;
RA Takeuchi H., Kage E., Sawata M., Kamikouchi A., Ohashi K., Ohara M.,
RA Fujiyuki T., Kunieda T., Sekimizu K., Natori S., Kubo T.;
RT "Identification of a novel gene, Mblk-1, that encodes a putative
RT transcription factor expressed preferentially in the large-type Kenyon
RT cells of the honeybee brain.";
RL Insect Mol. Biol. 10:487-494(2001).
RN [2] {ECO:0000305}
RP FUNCTION.
RX PubMed=11829456; DOI=10.1006/bbrc.2002.6397;
RA Park J.-M., Kunieda T., Takeuchi H., Kubo T.;
RT "DNA-binding properties of Mblk-1, a putative transcription factor from the
RT honeybee.";
RL Biochem. Biophys. Res. Commun. 291:23-28(2002).
RN [3] {ECO:0000305}
RP FUNCTION, PHOSPHORYLATION AT SER-444, AND MUTAGENESIS OF SER-444.
RX PubMed=12637500; DOI=10.1074/jbc.m300486200;
RA Park J.-M., Kunieda T., Kubo T.;
RT "The activity of Mblk-1, a mushroom body-selective transcription factor
RT from the honeybee, is modulated by the ras/MAPK pathway.";
RL J. Biol. Chem. 278:18689-18694(2003).
CC -!- FUNCTION: Transcriptional activator which binds to the consensus
CC sequence 5'-CCCTATCGATCGATCTCTACCT-3'. May play a role in higher-order
CC sensory processing. {ECO:0000269|PubMed:11829456,
CC ECO:0000269|PubMed:12637500}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11829456, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Large-type Kenyon cells of mushroom body.
CC {ECO:0000269|PubMed:11881813}.
CC -!- DOMAIN: The second H-T-H motif is necessary for transcriptional
CC activation. {ECO:0000269|PubMed:12637500}.
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DR EMBL; AB047034; BAB64310.1; -; mRNA.
DR RefSeq; NP_001011629.1; NM_001011629.1.
DR AlphaFoldDB; Q95YM8; -.
DR SMR; Q95YM8; -.
DR STRING; 7460.GB50048-PA; -.
DR iPTMnet; Q95YM8; -.
DR PaxDb; Q95YM8; -.
DR PRIDE; Q95YM8; -.
DR EnsemblMetazoa; NM_001011629; NP_001011629; GeneID_408521.
DR GeneID; 408521; -.
DR KEGG; ame:408521; -.
DR CTD; 408521; -.
DR eggNOG; KOG4565; Eukaryota.
DR InParanoid; Q95YM8; -.
DR OrthoDB; 596515at2759; -.
DR PhylomeDB; Q95YM8; -.
DR Proteomes; UP000005203; Unplaced.
DR GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0007613; P:memory; NAS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR007889; HTH_Psq.
DR Pfam; PF05225; HTH_psq; 2.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS50960; HTH_PSQ; 2.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation.
FT CHAIN 1..1598
FT /note="Mushroom body large-type Kenyon cell-specific
FT protein 1"
FT /id="PRO_0000238916"
FT DOMAIN 582..634
FT /note="HTH psq-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00320"
FT DOMAIN 1034..1086
FT /note="HTH psq-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00320"
FT DNA_BIND 610..630
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00320"
FT DNA_BIND 1062..1082
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00320"
FT REGION 83..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1248..1283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1301..1598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..292
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1024
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1303..1324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1392..1407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1408..1443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1444..1471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1491..1552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1559..1589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 444
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000269|PubMed:12637500"
FT MUTAGEN 444
FT /note="S->A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:12637500"
SQ SEQUENCE 1598 AA; 174929 MW; E5475BDD3ACB1EEF CRC64;
MADCPYARCI QERRHIRREL LRWTKNMVFV VGLERVAEEL MGRRRWKQYQ DTLYSGTRSS
ESLTAQAHHR LYPAFSSSCD PVPGNLEQIG SRPLHPPASS TSLPATITTT TTTTTTTTAT
AAATATTTAT GLIKQETLQR HHHLQNHHHH LQSTAVQDHH RPYQQQQQQQ QRQQQRQEER
RLRPDEIKVE VGEDEFANGG AARDESKAGS TDASTPATVT TTGATTTLPA ASATGTGPAT
PSAVVATSNA TAAMTTGTTT IPTRRLRKRR QNDGEGADDR DDDEENEEEE DGRGQSEAEK
RLKLDEDADG AVSPLRREKD RGSREYPTSN ATDTDGTKER TEEVALDRTP VTQGLLRVKK
EEELQEAPSC GGGPTILTTP GLDSDGIRLP CREVEAAATA RNVVAPFLIG SRRTSPPPED
WKPLDKCYFC LDGKLPHDDQ PPLSPQSDSS SSSRSAESPM SVQVDPMAAS VVAAALTGTY
PTLLPQWCLP PREAPLVGVQ PHQDSATPAD QPLDLSAKPK NSQDNNISLL EQQKIPLRMT
AGIDPKSIFN SGYRPKPRMS GPVAAVAAAA VAAAGVGGVP VVGAGGGRRA YTEEELQAAL
RDIQSGKLGT RRAAVIYGIP RSTLRNKVYK LAMERERDAS LSSTHSHPHE PGAPATTITT
ITTTTTTTTT TTTTTTTPNT TQNASATTPP PQVDEVDDKE LSGAEEEKEV EKALLKPLLS
LEDLVRFSTL EGSGGDSLRT LLQRGQETGA EWPGLEHANI GPYIQKMIAA AAPFKGMETQ
DYRIPEVMRR LMSEDKRLSK SVNGDQSQPP HQQLHHHQST HPQAQAQAQP QQQQQQQQQQ
PQQQQQQQQQ QQQQQRGPMT NDDFNPNIEE EASDSAQGRA ILKIPSYKPA STPGCSSKNG
EPTSAAFAQG FATAASSPGL LERASPAFSG TSSPTNSLVG KTVAVNFRDV IAKSISVKFQ
EGQTVSGGGM GGCQPGGVVQ SQQPIMTDPS PFKRGRYTPP QPANAQQGQA QAQAKPQSQE
ANKPKPATGG KGTRPKRGKY RNYDRDSLVE AVRAVQRGEM SVHRAGSYYG VPHSTLEYKV
KERHLMRPRK RDQKQSDDKT KETSTVTAAA AATNIRPGTA DNKPQLKPQK PFTSPGGIPG
PNGIKMPSFM EGMPHLPFTP FNFWNPPPFM PSPFMAGAPN VPTILPEQYF ATSRIRGLQE
QQRNAAMVQQ QQQQQQQQQQ QQQQQQQQQQ QQQHQARERE GVGAGIAETS AGTSNSRGAA
QMSKVPRDVS EGIYDGSGAN GSFLDNLIRS SLETGIPRDQ RAMTEARNQQ QQASSQQQIP
ESMRSKALID QLCRNSRRTP VPRLAQDSSE DESYRGPSAS GGRPVPERPE RVPTVDLSPS
PSDRGRNDDG SDRLTSPPTP LSISRAGSRD EDSTRDSTKL DRSSREREVH NGGQQEDRDR
KTLTSAPQQP QQQQQQQQQQ QQQQQQLNHY PDLHNLYAVP TDKKSACDSK LIVDHSSQKT
QQQQPQQQQQ QQQQQQPQQQ SQQPQQQQPQ PQQQQQQQQQ QQPQQQQKEY GAVSGLVVQL
QRGYNSGNNR SGEQANSQQQ QQQQSGEPVI GMEDSVEQ
