MIER1_CHICK
ID MIER1_CHICK Reviewed; 513 AA.
AC Q5ZKT9;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Mesoderm induction early response protein 1;
DE Short=Mi-er1;
GN Name=MIER1; ORFNames=RCJMB04_9c22;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Transcriptional repressor regulating the expression of a
CC number of genes. Probably functions through recruitment of histone
CC deacetylases involved in chromatin silencing (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512,
CC ECO:0000255|PROSITE-ProRule:PRU00624}.
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DR EMBL; AJ719995; CAG31654.1; -; mRNA.
DR RefSeq; NP_001026463.1; NM_001031292.1.
DR AlphaFoldDB; Q5ZKT9; -.
DR STRING; 9031.ENSGALP00000043276; -.
DR PaxDb; Q5ZKT9; -.
DR GeneID; 424702; -.
DR KEGG; gga:424702; -.
DR CTD; 57708; -.
DR VEuPathDB; HostDB:geneid_424702; -.
DR eggNOG; KOG4329; Eukaryota.
DR InParanoid; Q5ZKT9; -.
DR OrthoDB; 1062529at2759; -.
DR PhylomeDB; Q5ZKT9; -.
DR PRO; PR:Q5ZKT9; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0017053; C:transcription repressor complex; ISS:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR InterPro; IPR000949; ELM2_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR040138; MIER/MTA.
DR InterPro; IPR031169; MIER1.
DR InterPro; IPR045787; MIER1/3_C.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR PANTHER; PTHR10865; PTHR10865; 1.
DR PANTHER; PTHR10865:SF24; PTHR10865:SF24; 1.
DR Pfam; PF01448; ELM2; 1.
DR Pfam; PF19426; MIER1_beta_C; 1.
DR SMART; SM01189; ELM2; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS51293; SANT; 1.
PE 2: Evidence at transcript level;
KW Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..513
FT /note="Mesoderm induction early response protein 1"
FT /id="PRO_0000197144"
FT DOMAIN 182..280
FT /note="ELM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT DOMAIN 285..337
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 1..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..261
FT /note="Interaction with HDAC1"
FT /evidence="ECO:0000250"
FT REGION 368..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..108
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 513 AA; 58089 MW; B8D9B81B98062625 CRC64;
MAEPSVESSS PGGSATSDDH EFDPSADMLV HDFDDERTLE EEEMMEGERN FNSEIEDLNR
ESDMPIQELL SLYGYDGTIP LQEDDDDEDE EEEEEEGEDD DDVDNDDNSG CSGENKEETI
KDSSGQEDDT QSSNDDPAPS VASQDPQELI RPRRCKYFDT NSEIEEESEE DEDYIPSEDW
KKEIMVGSMF QAEIPAGICR YKENEKVYEN DDQLLWNPDV LPEDKVIEFL NEASRRTGDE
KGLDAIPEGS HIKDNEQALY ELVKCNFDTE ESLRRLRFNV KAAREELSVW TEEECRNFEQ
GLKVYGKDFH VIQANKVRTR SVGECVAFYY MWKKSERYDF FAQQTRFGKK KYNLHPGVTD
YMDRLLDESE SAASSRAPSP PPTASNSSTS QSEREDSTTS SSNQNGLSAN GPGDIPSKDE
AKPEGLHING PTGGKKTPHT DLDTNGYETE SLSLDPKVAH STSRSENDFE EKNERPLKRR
RINSNGKESP GSSEFFQEAN SHGKLEELET LDD
