LS14A_BOVIN
ID LS14A_BOVIN Reviewed; 463 AA.
AC Q3MHF8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Protein LSM14 homolog A;
DE AltName: Full=Protein FAM61A;
DE AltName: Full=RNA-associated protein 55A;
GN Name=LSM14A; Synonyms=RAP55A;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) 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; BC105253; AAI05254.1; -; mRNA.
DR RefSeq; NP_001029826.1; NM_001034654.1.
DR AlphaFoldDB; Q3MHF8; -.
DR BMRB; Q3MHF8; -.
DR SMR; Q3MHF8; -.
DR STRING; 9913.ENSBTAP00000000831; -.
DR PaxDb; Q3MHF8; -.
DR PRIDE; Q3MHF8; -.
DR Ensembl; ENSBTAT00000000831; ENSBTAP00000000831; ENSBTAG00000000630.
DR GeneID; 538838; -.
DR KEGG; bta:538838; -.
DR CTD; 26065; -.
DR VEuPathDB; HostDB:ENSBTAG00000000630; -.
DR VGNC; VGNC:31053; LSM14A.
DR eggNOG; KOG1073; Eukaryota.
DR GeneTree; ENSGT00940000154415; -.
DR InParanoid; Q3MHF8; -.
DR OMA; WYPPPGH; -.
DR OrthoDB; 1569369at2759; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000000630; Expressed in parenchyma of mammary gland and 102 other tissues.
DR ExpressionAtlas; Q3MHF8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
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 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 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_0000259421"
FT DOMAIN 284..320
FT /note="DFDF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00845"
FT REGION 172..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..359
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 172..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; 50636 MW; 8B19AE9B41275BE1 CRC64;
MSGGTPYIGS KISLISKAEI RYEGILYTID TENSTVALAK VRSFGTEDRP TDRPIPPRDE
VFEYIIFRGS DIKDLTVCEP PKPQCSLPQD PAIVQSSLGS STSSFQSVGS YGPFGRMPTY
SQFSPSSLVG QQFGAVGVAG SSLTSFGTEA SSSSALSQSS VVGSAFTQDS RALKTQLSQG
RSSPQLDPLR KSPTMEQAVQ TASAHLPAPA PVGRRSPVST RPLPSTSQKP IENQEHRRAE
VHKVSRPENE QLRNDSKRQI VPGAPSAPRR GRGGHRGGRG RFGIRRDGPM KFEKDFDFES
ANAQFNKEEI DREFHNKLKL KEDKLEKQEK PVNGEDKGDS GVDTQNSEGN ADEEDPLGPN
CYYDKTKSFF DNISCDDNRE RRPTWAEERR LNAETFGIPL RPNRGRGGYR GRGGLGFRGG
RGRGSGRGGA FTTPRGFRGG FRGGRGGREF ADFEYRKDNK VAA
