LS14A_XENTR
ID LS14A_XENTR Reviewed; 469 AA.
AC Q6NVR8;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Protein LSM14 homolog A {ECO:0000250|UniProtKB:Q8ND56};
DE AltName: Full=RNA-associated protein 55A {ECO:0000250|UniProtKB:A0A8M2};
DE Short=RAP55A {ECO:0000250|UniProtKB:A0A8M2};
GN Name=lsm14a {ECO:0000312|EMBL:AAH67936.1};
GN Synonyms=rap55a {ECO:0000250|UniProtKB:A0A8M2};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAH67936.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula {ECO:0000312|EMBL:AAH67936.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2004) 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, P-body {ECO:0000250|UniProtKB:Q8ND56}.
CC Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q8ND56}.
CC Note=Localizes to cytoplasmic particles in stage VI oocytes and eggs.
CC {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}.
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DR EMBL; BC067936; AAH67936.1; -; mRNA.
DR RefSeq; NP_998832.1; NM_213667.1.
DR AlphaFoldDB; Q6NVR8; -.
DR BMRB; Q6NVR8; -.
DR SMR; Q6NVR8; -.
DR STRING; 8364.ENSXETP00000005025; -.
DR PaxDb; Q6NVR8; -.
DR PRIDE; Q6NVR8; -.
DR DNASU; 407942; -.
DR GeneID; 407942; -.
DR KEGG; xtr:407942; -.
DR CTD; 26065; -.
DR Xenbase; XB-GENE-5955547; lsm14a.
DR eggNOG; KOG1073; Eukaryota.
DR HOGENOM; CLU_019221_0_1_1; -.
DR InParanoid; Q6NVR8; -.
DR OrthoDB; 1569369at2759; -.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
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:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:0033962; P:P-body assembly; IBA:GO_Central.
DR GO; GO:0034063; P:stress granule assembly; IBA:GO_Central.
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..469
FT /note="Protein LSM14 homolog A"
FT /id="PRO_0000391380"
FT DOMAIN 287..323
FT /note="DFDF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00845"
FT REGION 144..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..469
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 144..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 469 AA; 51053 MW; F9A404A8E5C25E4B CRC64;
MSGGTPYIGS KISLISKAEI RYEGILYTID TENSTVALAK VRSFGTEDRP TDRPIPPRDE
VFEYIIFRGS DIKDLTVCEP PKPQCSLPQD PAIVQSSLGS SSASSFQSVS SYGPFGRMPT
YSQFSTSPLV GQQFGAVGSS LTSFGAETTS STSLPPSSTV GSSFTQEART LKTQLSQGRS
TSPLDSLRKS PTIEQAVQTA SASHAPSAAP VGRRSPVLSR PLPSSSQKTG ESSEQRKGEL
HKTQRPDTEQ LRNDNRHDPN KRQPASSAPQ PRRGRGGNRG GRGRFGVRRD GPMKFEKDFD
FESANAQFNK EEIDREFHNK LKLKDDKPEK PVNGEDKTDS GVDTQNSEGN AEEDDVLAGG
VCYYDKTKSF FDNISCDDNR DRRQTWSEER RINAETFGLP LRSNRGRGGF RGRGGGMGFR
GGRGRGERRG PPGGGGFGSS RGYRGGSRGG RGGREFAEYE YRKDNKVAA
