L14BA_XENLA
ID L14BA_XENLA Reviewed; 422 AA.
AC Q68FI1;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Protein LSM14 homolog B-A;
DE AltName: Full=RNA-associated protein 46 {ECO:0000303|PubMed:19458392};
DE Short=xRAP46 {ECO:0000303|PubMed:19458392};
DE AltName: Full=RNA-associated protein 55B-A;
DE Short=RAP55B-A;
DE Short=xRAP55B {ECO:0000303|PubMed:17942399, ECO:0000303|PubMed:18723115};
GN Name=lsm14b-a;
GN Synonyms=rap46 {ECO:0000303|PubMed:19458392},
GN rap55b {ECO:0000303|PubMed:17942399, ECO:0000303|PubMed:18723115},
GN rap55b-a;
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:AAH79811.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH79811.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP IDENTIFICATION IN A RIBONUCLEOPROTEIN COMPLEX WITH CPEB1; DDX6; PAT1;
RP EIF4ENIF1; EIF4E1B AND YBX2, AND DEVELOPMENTAL STAGE.
RX PubMed=17942399; DOI=10.1074/jbc.m704629200;
RA Minshall N., Reiter M.H., Weil D., Standart N.;
RT "CPEB interacts with an ovary-specific eIF4E and 4E-T in early Xenopus
RT oocytes.";
RL J. Biol. Chem. 282:37389-37401(2007).
RN [3] {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).
RN [4] {ECO:0000305}
RP REVIEW.
RX PubMed=18631138; DOI=10.1042/bst0360671;
RA Standart N., Minshall N.;
RT "Translational control in early development: CPEB, P-bodies and germinal
RT granules.";
RL Biochem. Soc. Trans. 36:671-676(2008).
RN [5] {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: 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 (PubMed:18631138).
CC {ECO:0000250|UniProtKB:Q8CGC4, ECO:0000269|PubMed:18631138}.
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. Component of a
CC ribonucleoprotein (RNP) complex, composed at least of elavl1/elrA
CC and/or elavl2/elrB, igf2bp3/vg1RBP, ddx6/Xp54, ybx2/frgy2,
CC lsm14b/rap55b and, in a subset of RNP complexes, stau1/staufen.
CC {ECO:0000269|PubMed:17942399, ECO:0000269|PubMed:19458392}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally. Expression declines during
CC oocyte maturation. {ECO:0000269|PubMed:17942399}.
CC -!- SIMILARITY: Belongs to the LSM14 family. {ECO:0000255}.
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DR EMBL; BC079811; AAH79811.1; -; mRNA.
DR RefSeq; NP_001087455.1; NM_001093986.1.
DR AlphaFoldDB; Q68FI1; -.
DR SMR; Q68FI1; -.
DR BioGRID; 104139; 2.
DR MaxQB; Q68FI1; -.
DR DNASU; 447279; -.
DR GeneID; 447279; -.
DR KEGG; xla:447279; -.
DR CTD; 447279; -.
DR Xenbase; XB-GENE-17341157; lsm14b.L.
DR OMA; HPRWSPY; -.
DR OrthoDB; 1569369at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 447279; Expressed in liver 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..422
FT /note="Protein LSM14 homolog B-A"
FT /id="PRO_0000391381"
FT DOMAIN 278..314
FT /note="DFDF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00845"
FT REGION 145..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 349..365
FT /note="FFD box"
FT MOTIF 367..387
FT /note="TFG box"
FT COMPBIAS 198..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 422 AA; 46102 MW; CF95D40DAE6BC557 CRC64;
MSSGTPYIGS KISLISKAQI RYEGILYTID TENSTVALAK VRSFGTEDRP TDRPAPPREE
VYEYIIFRGS DIKDITVCEP PKASHALPQD PAIVQSSLGS APAASYQPSV PYSPFRGMPT
YSQLAATSLL SQQYAASLGL EKLGSPTASA GASSSCSSPS PQPVAPEPDV PAEPPQLSQN
AGYPSIPVRK SPMVEQAVQT GPLENQAQKK VQQAKGAPVG QRGVRQSGPQ SQPAPLNVPP
PAAPVLGTIN DENRRPPRRR SGNRRTRNRS RGQNRPTTVK ENPIKFEGDF DFETANAQFN
REELDKEFKD KLNFKEEKPE KEGEEKTDSG VETQNSDGNP EEDPLGPNTY YDRSKSFFDN
ISSEMKSRRT TWAEERKLNT ETFGVSGRFL RGRSFRGGFR GGRGSAAPRR NQTTQRAGTG
RV