ID   LSM14_PLEWA             Reviewed;         467 AA.
AC   Q9YH12;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Protein LSM14 homolog;
DE   AltName: Full=RNA-associated protein of 55 kDa {ECO:0000303|PubMed:9851867};
DE            Short=RAP55 {ECO:0000303|PubMed:9851867};
GN   Name=lsm14; Synonyms=rap55 {ECO:0000303|PubMed:9851867};
OS   Pleurodeles waltl (Iberian ribbed newt).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Caudata; Salamandroidea; Salamandridae; Pleurodelinae;
OC   Pleurodeles.
OX   NCBI_TaxID=8319;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAA68149.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN A RIBONUCLEOPROTEIN COMPLEX,
RP   LACK OF RNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Ovary {ECO:0000312|EMBL:CAA68149.1};
RX   PubMed=9851867; DOI=10.1006/excr.1998.4249;
RA   Lieb B., Carl M., Hock R., Gebauer D., Scheer U.;
RT   "Identification of a novel mRNA-associated protein in oocytes of
RT   Pleurodeles waltl and Xenopus laevis.";
RL   Exp. Cell Res. 245:272-281(1998).
RN   [2] {ECO:0000305}
RP   REVIEW.
RX   PubMed=18723115; DOI=10.1016/j.biocel.2008.06.015;
RA   Marnef A., Sommerville J., Ladomery M.R.;
RT   "RAP55: insights into an evolutionarily conserved protein family.";
RL   Int. J. Biochem. Cell Biol. 41:977-981(2009).
CC   -!- FUNCTION: Does not appear to bind RNA. {ECO:0000269|PubMed:9851867}.
CC   -!- SUBUNIT: Component of a ribonucleoprotein complex.
CC       {ECO:0000269|PubMed:9851867}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9851867}.
CC   -!- TISSUE SPECIFICITY: Expressed exclusively in ovary.
CC       {ECO:0000269|PubMed:9851867}.
CC   -!- DEVELOPMENTAL STAGE: Expressed maternally.
CC       {ECO:0000269|PubMed:9851867}.
CC   -!- SIMILARITY: Belongs to the LSM14 family. {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X99836; CAA68149.1; -; mRNA.
DR   AlphaFoldDB; Q9YH12; -.
DR   SMR; Q9YH12; -.
DR   PRIDE; Q9YH12; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR   GO; GO:0006417; P:regulation of translation; IC:UniProtKB.
DR   CDD; cd01736; LSm14_N; 1.
DR   InterPro; IPR025762; DFDF.
DR   InterPro; IPR019050; FDF_dom.
DR   InterPro; IPR025761; FFD_box.
DR   InterPro; IPR025609; Lsm14-like_N.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR025768; TFG_box.
DR   Pfam; PF09532; FDF; 1.
DR   Pfam; PF12701; LSM14; 1.
DR   SMART; SM01199; FDF; 1.
DR   SMART; SM01271; LSM14; 1.
DR   SUPFAM; SSF50182; SSF50182; 1.
DR   PROSITE; PS51512; DFDF; 1.
DR   PROSITE; PS51513; FFD; 1.
DR   PROSITE; PS51536; TFG; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Ribonucleoprotein.
FT   CHAIN           1..467
FT                   /note="Protein LSM14 homolog"
FT                   /id="PRO_0000391438"
FT   DOMAIN          288..324
FT                   /note="DFDF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00845"
FT   REGION          172..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          325..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           365..381
FT                   /note="FFD box"
FT   MOTIF           384..404
FT                   /note="TFG box"
FT   COMPBIAS        172..204
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..225
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..261
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..341
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..357
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   467 AA;  51880 MW;  E62E8AD139774628 CRC64;
     MSGGTPYIGS KISLISKAEI RYEGILYTID TENSTVVLAK FALLGTEDRP TDRPIPPRDE
     VFEYIIFRGS DIKDLTVCEP PKPQCSLPQD PAIVQSSLGS SSTSFQSVSS YGPFSRMPTY
     SQFNQKSFRS TKFGRGRFRQ LNKILRTFET TTSASLSQSS AVGSSFTSDA RSLKTQLSQG
     RSSPHLDTLR KSPTMEQSVQ TTPASHLPPP GPVGRRSPPP ARPLPSVNQR TIESQEQKRV
     EAHRLSRPEA DQLRNENKDA NKRQAAPGAP PARRGRGGHR GGRGRFGIRR DGPMKFEKDF
     DFESANAQFT KEEIDREFHN KLKLKDDKPE KVEKPVNGED KGDSGIDTQN SEGNADEEEA
     LASNCYYDKT KSFFDNISCD DNRERRQTWA EERRINAETF GLPLRSNRGR GGYRGRGSGM
     GFRGARGRGG QRGGFGAPRG FRGGFRGTRG GREFADFEYR KDNKVAA