L14AA_XENLA
ID L14AA_XENLA Reviewed; 471 AA.
AC A0A8M2; Q68F15;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Protein LSM14 homolog A-A;
DE AltName: Full=RNA-associated protein 55A-A;
DE Short=RAP55A-A;
DE Short=xRAP55 {ECO:0000303|PubMed:17074753, ECO:0000303|PubMed:9851867};
DE Short=xRAP55A {ECO:0000303|PubMed:17942399, ECO:0000303|PubMed:18723115};
GN Name=lsm14a-a; Synonyms=lsm14a, rap55a-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:0000305, ECO:0000312|EMBL:BAF36055.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION IN A RIBONUCLEOPROTEIN
RP COMPLEX WITH YBX2; DDX6 AND EIF4ENIF1, IDENTIFICATION IN A COMPLEX WITH
RP PRMT1, INTERACTION WITH DDX6, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP DOMAIN, AND PHOSPHORYLATION.
RC TISSUE=Oocyte {ECO:0000269|PubMed:17074753};
RX PubMed=17074753; DOI=10.1074/jbc.m609059200;
RA Tanaka K.J., Ogawa K., Takagi M., Imamoto N., Matsumoto K., Tsujimoto M.;
RT "RAP55, a cytoplasmic mRNP component, represses translation in Xenopus
RT oocytes.";
RL J. Biol. Chem. 281:40096-40106(2006).
RN [2] {ECO:0000312|EMBL:AAH80031.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tail bud {ECO:0000312|EMBL:AAH80031.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
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 [4] {ECO:0000305}
RP 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 [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: RNA-binding component of messenger ribonucleoprotein
CC complexes (mRNPs), storage particles that mask maternal mRNAs from the
CC translational apparatus during oocyte maturation (PubMed:17074753).
CC Acts as a repressor of mRNA translation (PubMed:17074753). Probably
CC involved in the storage of translationally inactive mRNAs in the
CC cytoplasm in order to prevent their degradation (PubMed:17074753).
CC {ECO:0000269|PubMed:17074753}.
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. {ECO:0000269|PubMed:17074753}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17074753}.
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:0000269|PubMed:17074753}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expression increases during oocyte growth and continues at a constant
CC level until the tailbud stage (at protein level).
CC {ECO:0000269|PubMed:17074753, ECO:0000269|PubMed:17942399,
CC ECO:0000269|PubMed:9851867}.
CC -!- DOMAIN: The RGG repeats are required for interaction with ddx6/Xp54 and
CC accumulation in ribonucleoprotein complexes.
CC {ECO:0000269|PubMed:17074753}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:17074753}.
CC -!- SIMILARITY: Belongs to the LSM14 family. {ECO:0000255}.
CC -!- CAUTION: In contrast to PubMed:17074753, PubMed:9851867 show a strictly
CC maternal expression that decreases progressively during oocyte
CC maturation and early cleavage stages. This is more similar to the
CC expression pattern of lsm14b/rap55b. {ECO:0000305}.
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DR EMBL; AB257699; BAF36055.1; -; mRNA.
DR EMBL; BC080031; AAH80031.1; -; mRNA.
DR RefSeq; NP_001087507.1; NM_001094038.1.
DR AlphaFoldDB; A0A8M2; -.
DR BMRB; A0A8M2; -.
DR SMR; A0A8M2; -.
DR BioGRID; 104191; 1.
DR IntAct; A0A8M2; 3.
DR MINT; A0A8M2; -.
DR DNASU; 447331; -.
DR GeneID; 447331; -.
DR KEGG; xla:447331; -.
DR CTD; 447331; -.
DR Xenbase; XB-GENE-5955717; lsm14a.L.
DR OrthoDB; 1569369at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 447331; Expressed in blastula and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA: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:0032991; C:protein-containing complex; IPI:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IPI:UniProtKB.
DR GO; GO:0017151; F:DEAD/H-box RNA helicase binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IMP: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; Developmental protein; Phosphoprotein; Reference proteome;
KW Repressor; Ribonucleoprotein; Translation regulation.
FT CHAIN 1..471
FT /note="Protein LSM14 homolog A-A"
FT /id="PRO_0000391378"
FT DOMAIN 288..324
FT /note="DFDF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00845"
FT REGION 146..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 363..379
FT /note="FFD box"
FT MOTIF 382..402
FT /note="TFG box"
FT COMPBIAS 234..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 352
FT /note="A -> V (in Ref. 2; AAH80031)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 471 AA; 51168 MW; 67A85C7E2FE93398 CRC64;
MSGGTPYIGS KISLISKAEI RYEGILYTID TENSTVALAK VRSFGTEDRP TDRPIPPRDE
IFEYIIFRGS DIKDLTVCEP PKPQCSLPQD PAIVQSSLGS SSASSFQSVS SYGPFGRMPA
YSQFNTGPLV GPQFGAVGVG SSLTSFGAET TSSTSLPPSS AVGTSFTQEA RTLKTQSSQG
QSSSPLDSLR KSPNIEQAVQ TAAAPHAPST ATVGRRSPVL SRPVPSSIQK TAESPEQRKG
ELHKMQRPDI DQLKNDKNDP SKRQPVLSAL QPRRGRGGNR GGRGRFGVRR DGPMKFEKDF
DFESANAQFN KEEIDREFHN KLKIKDDKPE KPVNGEDKTD SVVDTQNSEG NAEEEEVLAG
GVCYYDKTKS FFDNISCDDN RDRRQTWAEE RRINVETFGL PLRSNRGRGG FRGRGGGMGF
RGGRGRGGER RGAPGGGGFG PARGFRGGFR GGRGGREFAD YEYRKDNKVA A
