ID   MIER1_XENLA             Reviewed;         495 AA.
AC   Q7T105; O42194;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Mesoderm induction early response protein 1;
DE            Short=Early response 1;
DE            Short=Er1;
DE            Short=Mi-er1;
DE            Short=Xmi-er1;
GN   Name=mier1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   TISSUE=Blastula;
RX   PubMed=9325278; DOI=10.1074/jbc.272.41.25591;
RA   Paterno G.D., Li Y., Luchman H.A., Ryan P.J., Gillespie L.L.;
RT   "cDNA cloning of a novel, developmentally regulated immediate early gene
RT   activated by fibroblast growth factor and encoding a nuclear protein.";
RL   J. Biol. Chem. 272:25591-25595(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
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.
CC   -!- DEVELOPMENTAL STAGE: Predominantly expressed during the initial
CC       cleavage and blastula stage. Little expression in the further
CC       development. {ECO:0000269|PubMed:9325278}.
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DR   EMBL; AF015454; AAB81217.2; -; mRNA.
DR   EMBL; BC055961; AAH55961.1; -; mRNA.
DR   RefSeq; NP_001080278.1; NM_001086809.1.
DR   AlphaFoldDB; Q7T105; -.
DR   PRIDE; Q7T105; -.
DR   DNASU; 379970; -.
DR   GeneID; 379970; -.
DR   KEGG; xla:379970; -.
DR   CTD; 379970; -.
DR   Xenbase; XB-GENE-974221; mier1.L.
DR   OrthoDB; 1062529at2759; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 379970; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0017053; C:transcription repressor complex; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042826; F:histone deacetylase binding; IEA:InterPro.
DR   GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
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   DNA-binding; Nucleus; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..495
FT                   /note="Mesoderm induction early response protein 1"
FT                   /id="PRO_0000197145"
FT   DOMAIN          171..269
FT                   /note="ELM2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT   DOMAIN          274..326
FT                   /note="SANT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          76..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          356..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          416..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..96
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..397
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..437
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..475
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        85..86
FT                   /note="Missing (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        206
FT                   /note="D -> N (in Ref. 1; AAB81217)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   495 AA;  56308 MW;  4B7D8BFB42EF1231 CRC64;
     MAEPSLRTAS PGGSAASDDH EFEPSADMLV HEFDDEQTLE EEEMLEGEVN FTSEIEHLER
     ESEMPIDELL RLYGYGSTVP LPGEEEEDEE DMDNDCNSGC SGEIKDEAIK DSSGQEDETQ
     SSNDDPTPSF TCRDVREVIR PRRCKYFDTN HEIEEESEDD EDYVPSEDWK KEIMVGSMFQ
     AEIPVGICKY RETEKVYEND DQLLWDPEYV MEERVIDFLN EASRRTCEER GLDAIPEGSH
     IKDNEQALYE LVKCNFDTEE ALRRLRFNVK AAREELSVWT EEECRNFEQG LKAYGKDFHL
     IQANKVRTRS VGECVAFYYM WKKSERYDFF AQQTRFGKKK YNLHPGVTDY MDRLLDESES
     ATSSRAPSPP PTTSNSNTSQ SEKEDCTASN NTQNGVSVNG PCAITAYKDE AKQGVHLNGP
     TISSSDPSSN ETDTNGYNRE NVTDDSRFSH TSGKTDTNPD DTNERPIKRQ RMDSPGKEST
     GSSEFSQEVF SHGEV