ID   L14BB_XENLA             Reviewed;         380 AA.
AC   Q498K9;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Protein LSM14 homolog B-B;
DE   AltName: Full=RNA-associated protein 42 {ECO:0000303|PubMed:19458392};
DE            Short=xRAP42 {ECO:0000303|PubMed:19458392};
DE   AltName: Full=RNA-associated protein 55B-B;
DE            Short=RAP55B-B;
GN   Name=lsm14b-b;
GN   Synonyms=lsm14b, rap42 {ECO:0000303|PubMed:19458392}, rap55b-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:AAI00175.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary {ECO:0000312|EMBL:AAI00175.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   IDENTIFICATION IN A RIBONUCLEOPROTEIN COMPLEX WITH ELAVL1; ELAVL2; IGF2BP3;
RP   STAU1; DDX6 AND YBX2.
RX   PubMed=19458392; DOI=10.1074/jbc.m109.009928;
RA   Arthur P.K., Claussen M., Koch S., Tarbashevich K., Jahn O., Pieler T.;
RT   "Participation of Xenopus Elr-type proteins in vegetal mRNA localization
RT   during oogenesis.";
RL   J. Biol. Chem. 284:19982-19992(2009).
CC   -!- FUNCTION: May be involved in the storage of translationally inactive
CC       mRNAs and protect them from degradation (By similarity). Plays a role
CC       in control of mRNA translation (By similarity).
CC       {ECO:0000250|UniProtKB:Q68FI1, ECO:0000250|UniProtKB:Q8CGC4}.
CC   -!- SUBUNIT: Component of a ribonucleoprotein (RNP) complex, at least
CC       composed of cpeb1, lsm14b/rap55b, ddx6/Xp54, ybx2/frgy2, pat1/P100,
CC       eif4enif1/4E-T and eif4e1b. Different translationally-repressed mRNP
CC       complexes probably exist that contain either lsm14a/rap55a or
CC       lsm14b/rap55b depending on the developmental stage (By similarity).
CC       Component of a ribonucleoprotein (RNP) complex, composed at least of
CC       elavl1/elrA and/or elavl2/elrB, igf2bp3/vg1RBP, ddx6/Xp54, ybx2/frgy2,
CC       lsm14b/rap55b and, in a subset of RNP complexes, stau1/staufen.
CC       {ECO:0000250|UniProtKB:Q68FI1, ECO:0000269|PubMed:19458392}.
CC   -!- SIMILARITY: Belongs to the LSM14 family. {ECO:0000255}.
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DR   EMBL; BC100174; AAI00175.1; -; mRNA.
DR   RefSeq; NP_001089649.1; NM_001096180.1.
DR   AlphaFoldDB; Q498K9; -.
DR   SMR; Q498K9; -.
DR   BioGRID; 592490; 1.
DR   IntAct; Q498K9; 1.
DR   DNASU; 734709; -.
DR   GeneID; 734709; -.
DR   KEGG; xla:734709; -.
DR   CTD; 734709; -.
DR   Xenbase; XB-GENE-5893369; lsm14b.S.
DR   OrthoDB; 1569369at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 734709; Expressed in oocyte and 19 other tissues.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IPI:UniProtKB.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
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   Developmental protein; Reference proteome; Ribonucleoprotein;
KW   Translation regulation.
FT   CHAIN           1..380
FT                   /note="Protein LSM14 homolog B-B"
FT                   /id="PRO_0000391382"
FT   DOMAIN          236..272
FT                   /note="DFDF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00845"
FT   REGION          160..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          268..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           307..323
FT                   /note="FFD box"
FT   MOTIF           325..345
FT                   /note="TFG box"
FT   COMPBIAS        268..289
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..380
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   380 AA;  41868 MW;  CB6C3330923C9019 CRC64;
     MSSGTPYIGS KISLISKAQI RYEGILYTID TENSTVALAK VRSFGTEDRP TDRPAPPREE
     VYEYIIFRGS DIKDITVCEP PKASHALSQD PAIVQSSLGS AASYQPSVPY SPFRGMPTYS
     QLAATSLLSQ QYAASLGLAG FPSIPVRKSP MVEQAVQTGP LENQAQKKVQ QAKGAPVGLR
     GVRQSGPQSQ PAPLNVPPPA APVLGTVNDE NRRPPRRRSG NRRTRNRSRG QNRPTTVKEN
     AIKFEGDFDF ESANAQFNRE ELDKEFKDKL NFKDDKPEKA GEEKTDSGVE TQNSDGNPEE
     DPLGPNTYYD RSKSFFDNIS SEMKSRRTTW AEERKLNTET FGVSGRFLRG RSFRGGFRGG
     RGSAAPRRNQ TTQRAGTGRV