ID   L14AB_XENLA             Reviewed;         471 AA.
AC   Q8AVJ2;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Protein LSM14 homolog A-B;
DE   AltName: Full=RNA-associated protein 55A-B;
DE            Short=RAP55A-B;
GN   Name=lsm14a-b; Synonyms=rap55a-b;
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] {ECO:0000312|EMBL:AAH42251.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tail bud {ECO:0000312|EMBL:AAH42251.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RNA-binding component of messenger ribonucleoprotein
CC       complexes (mRNPs), storage particles that mask maternal mRNAs from the
CC       translational apparatus during oocyte maturation. Acts as a repressor
CC       of mRNA translation. Probably involved in the storage of
CC       translationally inactive mRNAs in the cytoplasm in order to prevent
CC       their degradation. {ECO:0000250|UniProtKB:A0A8M2}.
CC   -!- SUBUNIT: Component of a ribonucleoprotein (RNP) complex, at least
CC       composed of lsm14a/rap55a, ybx2/frgy2, ddx6/Xp54 and eif4enif1/4E-T.
CC       Also forms a complex with prmt1 independently of ybx2/frgy2. Interacts
CC       with ddx6/Xp54 but does not appear to directly bind ybx2/frgy2.
CC       Different translationally-repressed mRNP complexes probably exist that
CC       contain either lsm14a/rap55a or lsm14b/rap55b depending on the
CC       developmental stage (By similarity). {ECO:0000250|UniProtKB:A0A8M2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A8M2}.
CC       Cytoplasm, P-body {ECO:0000250|UniProtKB:Q8ND56}. Cytoplasm, Stress
CC       granule {ECO:0000250|UniProtKB:Q8ND56}. Note=Localizes to cytoplasmic
CC       particles in stage VI oocytes and eggs. {ECO:0000250|UniProtKB:A0A8M2}.
CC   -!- DOMAIN: The RGG repeats are required for interaction with ddx6/Xp54 and
CC       accumulation in ribonucleoprotein complexes.
CC       {ECO:0000250|UniProtKB:A0A8M2}.
CC   -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:A0A8M2}.
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; BC042251; AAH42251.1; -; mRNA.
DR   RefSeq; NP_001079434.1; NM_001085965.1.
DR   AlphaFoldDB; Q8AVJ2; -.
DR   BMRB; Q8AVJ2; -.
DR   SMR; Q8AVJ2; -.
DR   IntAct; Q8AVJ2; 1.
DR   DNASU; 379121; -.
DR   GeneID; 379121; -.
DR   KEGG; xla:379121; -.
DR   CTD; 379121; -.
DR   Xenbase; XB-GENE-6251640; lsm14a.S.
DR   OrthoDB; 1569369at2759; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 379121; Expressed in blastula and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0017151; F:DEAD/H-box RNA helicase binding; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0017148; P:negative regulation of translation; ISS: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   2: Evidence at transcript level;
KW   Cytoplasm; Developmental protein; Phosphoprotein; Reference proteome;
KW   Repressor; Ribonucleoprotein; Translation regulation.
FT   CHAIN           1..471
FT                   /note="Protein LSM14 homolog A-B"
FT                   /id="PRO_0000391379"
FT   DOMAIN          287..323
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          320..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           362..378
FT                   /note="FFD box"
FT   MOTIF           381..401
FT                   /note="TFG box"
FT   COMPBIAS        172..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..259
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   471 AA;  51269 MW;  612989919027B075 CRC64;
     MSGGTPYIGS KISLISKAEI RYEGILYTID TENSTVALAK VRSFGTEDRP TDRPIPPRDE
     VFEYIIFRGS DIKDLTVCEP PKPQCSLPQD PAIVQSSLGS SSASSFQSVS SYGPFGRMPT
     YSQFSTSPLV GQQFGAVAGS SLTSFGAETT SSTSLPPSSV VGSTFTQEAR TLKTQLSQGR
     SSSPLDSLRK SPTIEQAVQT ASAPHPPSSA AVGRRSPVLS RPLPSSSQKT AESPEQRKGE
     LHKIQRPDTE QKNDYKNDLS RRQPVLSAAQ PRRGRGGNRG GRGRFGVRRD GPMKFEKDFD
     FESANAQFNK EDIDREFHNK LKLKDDKPEK PLNGEDKTDS GVDTQNSEGH AEEEDVLAAG
     VCYYDKTKSF FDSISCDDNR DRRQTWAEER RMNAETFGLP LRSNRGRGGY RGRGGGMGFR
     GGRGRGGERR GAPGGVGGFG PSRGYRGGSR GGRGGREFAE YEYRKDNKVA A