ID   RIPP1_DANRE             Reviewed;         140 AA.
AC   Q2WG80;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Protein ripply1;
GN   Name=ripply1 {ECO:0000312|ZFIN:ZDB-GENE-060113-1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAE53716.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH GRO2, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, DOMAIN, AND MUTAGENESIS OF 28-TRP--TRP-31.
RC   TISSUE=Embryo {ECO:0000269|PubMed:16326386};
RX   PubMed=16326386; DOI=10.1016/j.devcel.2005.09.021;
RA   Kawamura A., Koshida S., Hijikata H., Ohbayashi A., Kondoh H., Takada S.;
RT   "Groucho-associated transcriptional repressor ripply1 is required for
RT   proper transition from the presomitic mesoderm to somites.";
RL   Dev. Cell 9:735-744(2005).
CC   -!- FUNCTION: Plays a role in somitogenesis. Essential for transcriptional
CC       repression of the segmental patterning genes, thus terminating the
CC       segmentation program in the presomitic mesoderm, and also required for
CC       the maintenance of rostrocaudal polarity in somites.
CC       {ECO:0000269|PubMed:16326386}.
CC   -!- SUBUNIT: Interacts with gro2 via the WRPW motif.
CC       {ECO:0000269|PubMed:16326386}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16326386}.
CC   -!- TISSUE SPECIFICITY: Expressed in the embryonic anterior presomitic
CC       mesoderm and in newly formed somites. {ECO:0000269|PubMed:16326386}.
CC   -!- DOMAIN: The ripply homology domain is required for transcriptional
CC       repression. {ECO:0000250}.
CC   -!- DOMAIN: The WRPW motif is required for binding to tle/groucho proteins.
CC       {ECO:0000269|PubMed:16326386}.
CC   -!- MISCELLANEOUS: Named after the expression pattern, which decreases in a
CC       posterior to anterior direction in somites like a ripple.
CC       {ECO:0000269|PubMed:16326386}.
CC   -!- SIMILARITY: Belongs to the ripply family. {ECO:0000305}.
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DR   EMBL; AB212219; BAE53716.1; -; mRNA.
DR   RefSeq; NP_001034197.1; NM_001039108.1.
DR   AlphaFoldDB; Q2WG80; -.
DR   STRING; 7955.ENSDARP00000122894; -.
DR   PaxDb; Q2WG80; -.
DR   GeneID; 654446; -.
DR   KEGG; dre:654446; -.
DR   CTD; 92129; -.
DR   ZFIN; ZDB-GENE-060113-1; ripply1.
DR   eggNOG; ENOG502S6U6; Eukaryota.
DR   InParanoid; Q2WG80; -.
DR   OrthoDB; 1552301at2759; -.
DR   PhylomeDB; Q2WG80; -.
DR   PRO; PR:Q2WG80; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005634; C:nucleus; IDA:ZFIN.
DR   GO; GO:0009880; P:embryonic pattern specification; IMP:ZFIN.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   GO; GO:0048641; P:regulation of skeletal muscle tissue development; IMP:ZFIN.
DR   GO; GO:0061053; P:somite development; IMP:ZFIN.
DR   GO; GO:0032525; P:somite rostral/caudal axis specification; IMP:UniProtKB.
DR   GO; GO:0001757; P:somite specification; IMP:ZFIN.
DR   GO; GO:0001756; P:somitogenesis; IGI:ZFIN.
DR   InterPro; IPR028127; Ripply_fam.
DR   PANTHER; PTHR16770; PTHR16770; 1.
DR   Pfam; PF14998; Ripply; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..140
FT                   /note="Protein ripply1"
FT                   /id="PRO_0000307758"
FT   REGION          71..106
FT                   /note="Ripply homology domain"
FT                   /evidence="ECO:0000255"
FT   REGION          107..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           28..31
FT                   /note="WRPW motif; required for gro2-binding"
FT                   /evidence="ECO:0000269|PubMed:16326386"
FT   MUTAGEN         28..31
FT                   /note="Missing: Disrupts gro2-binding."
FT                   /evidence="ECO:0000269|PubMed:16326386"
SQ   SEQUENCE   140 AA;  16209 MW;  EA8132F26E9B6D24 CRC64;
     MNSVCFATPH TKHMDSKMQL TSSPASLWRP WLVTRKDAQT ECRRTKLACP YSRPEVPGNT
     TTDGKMQSFQ HPVRLYWPRS KSFDYLFSDG EALLRNFPVQ ATINFYDESD SEDEEESCDE
     DDESDVEDCL KHNSHFTAFN