LS14A_PONAB
ID LS14A_PONAB Reviewed; 463 AA.
AC Q5R4R4;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Protein LSM14 homolog A;
DE AltName: Full=Protein FAM61A;
DE AltName: Full=RNA-associated protein 55A;
GN Name=LSM14A; Synonyms=FAM61A, RAP55A;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential for formation of P-bodies, cytoplasmic structures
CC that provide storage sites for translationally inactive mRNAs and
CC protect them from degradation. Acts as a repressor of mRNA translation.
CC May play a role in mitotic spindle assembly.
CC {ECO:0000250|UniProtKB:Q8ND56}.
CC -!- SUBUNIT: Component of a ribonucleoprotein (RNP) complex (By
CC similarity). Interacts with DDX6. Interacts with EIF4ENIF1/4E-T;
CC promoting EIF4ENIF1/4E-T localization to P-bodies. Interacts (via FFD
CC box) with EDC4 (By similarity). {ECO:0000250|UniProtKB:A0A8M2,
CC ECO:0000250|UniProtKB:Q8ND56}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q8ND56}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8ND56}.
CC Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q8ND56}.
CC -!- DOMAIN: The LSM14 domain and the RGG repeats are required for
CC accumulation in P-bodies, and the region containing the FDF motif is
CC responsible for cytoplasmic retention. {ECO:0000250|UniProtKB:Q8ND56}.
CC -!- SIMILARITY: Belongs to the LSM14 family. {ECO:0000305}.
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DR EMBL; CR861180; CAH93252.1; -; mRNA.
DR RefSeq; NP_001126913.1; NM_001133441.1.
DR AlphaFoldDB; Q5R4R4; -.
DR BMRB; Q5R4R4; -.
DR SMR; Q5R4R4; -.
DR STRING; 9601.ENSPPYP00000011009; -.
DR Ensembl; ENSPPYT00000058177; ENSPPYP00000034022; ENSPPYG00000009832.
DR GeneID; 100173930; -.
DR KEGG; pon:100173930; -.
DR CTD; 26065; -.
DR eggNOG; KOG1073; Eukaryota.
DR GeneTree; ENSGT00940000154415; -.
DR InParanoid; Q5R4R4; -.
DR OrthoDB; 1569369at2759; -.
DR Proteomes; UP000001595; Chromosome 19.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:0033962; P:P-body assembly; 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 Acetylation; Cytoplasm; Cytoskeleton; Developmental protein; Methylation;
KW Phosphoprotein; Reference proteome; Repressor; Ribonucleoprotein;
KW Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8ND56"
FT CHAIN 2..463
FT /note="Protein LSM14 homolog A"
FT /id="PRO_0000187092"
FT DOMAIN 284..320
FT /note="DFDF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00845"
FT REGION 147..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 361..377
FT /note="FFD box"
FT MOTIF 380..400
FT /note="TFG box"
FT COMPBIAS 147..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND56"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND56"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND56"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND56"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND56"
FT MOD_RES 194
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND56"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND56"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND56"
FT MOD_RES 401
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2F8"
SQ SEQUENCE 463 AA; 50553 MW; 1A1667357D8C362F CRC64;
MSGGTPYIGS KISLISKAEI RYEGILYTID TENSTVALAK VRSFGTEDRP TDRPIPPRDE
VFEYIIFRGS DIKDLTVCEP PKPQCSLPQD PAIVQSSLGS STSSFQSMGS YGPFGRMPTY
SQFSPSSLVG QQFGAVGVAG SSLTSFGTET SNSGTLPQSS AVGSAFTQDT RSLKTQLSQG
RSSPQLDPLR KSPTMEQAVQ TASAHLPAPA AVGRRSPVST RPLPSTSQKA GENPEHRRAE
VHKVSRPENE QLRNDNKRQV APGAPSAPRR GRGGHRGGRG RFGIRRDGPM KFEKDFDFES
ANAQFNKEEI DREFHNKLKL KEDKLEKQEK PVNGEDKGDS GVDTQNSEGN ADEEDPLGPN
CYYDKTKSFF DNISCDDNRE RRPTWAEERR LNAETFGIPL RPNRGRGGYR GRGGLGFRGG
RGRGGGRGGT FTAPRGFRGG FRGGRGGREF ADFEYRKDNK VAA
