LS14A_MOUSE
ID LS14A_MOUSE Reviewed; 462 AA.
AC Q8K2F8; Q9CTG8;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Protein LSM14 homolog A;
DE AltName: Full=Protein FAM61A;
DE AltName: Full=RNA-associated protein 55A;
DE Short=mRAP55A;
GN Name=Lsm14a; Synonyms=Fam61a, Rap55a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-462.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-192, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-400, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC031521; AAH31521.1; -; mRNA.
DR EMBL; AK003611; BAB22889.1; -; mRNA.
DR CCDS; CCDS21140.1; -.
DR RefSeq; NP_080224.1; NM_025948.2.
DR AlphaFoldDB; Q8K2F8; -.
DR SMR; Q8K2F8; -.
DR BioGRID; 211917; 32.
DR IntAct; Q8K2F8; 8.
DR MINT; Q8K2F8; -.
DR STRING; 10090.ENSMUSP00000082723; -.
DR iPTMnet; Q8K2F8; -.
DR PhosphoSitePlus; Q8K2F8; -.
DR EPD; Q8K2F8; -.
DR jPOST; Q8K2F8; -.
DR MaxQB; Q8K2F8; -.
DR PaxDb; Q8K2F8; -.
DR PeptideAtlas; Q8K2F8; -.
DR PRIDE; Q8K2F8; -.
DR ProteomicsDB; 252533; -.
DR Antibodypedia; 47950; 170 antibodies from 29 providers.
DR DNASU; 67070; -.
DR Ensembl; ENSMUST00000085585; ENSMUSP00000082723; ENSMUSG00000066568.
DR GeneID; 67070; -.
DR KEGG; mmu:67070; -.
DR UCSC; uc009gjd.1; mouse.
DR CTD; 26065; -.
DR MGI; MGI:1914320; Lsm14a.
DR VEuPathDB; HostDB:ENSMUSG00000066568; -.
DR eggNOG; KOG1073; Eukaryota.
DR GeneTree; ENSGT00940000154415; -.
DR HOGENOM; CLU_019221_0_1_1; -.
DR InParanoid; Q8K2F8; -.
DR OMA; WYPPPGH; -.
DR OrthoDB; 1569369at2759; -.
DR PhylomeDB; Q8K2F8; -.
DR TreeFam; TF313514; -.
DR BioGRID-ORCS; 67070; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Lsm14a; mouse.
DR PRO; PR:Q8K2F8; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8K2F8; protein.
DR Bgee; ENSMUSG00000066568; Expressed in otolith organ and 229 other tissues.
DR ExpressionAtlas; Q8K2F8; baseline and differential.
DR Genevisible; Q8K2F8; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:MGI.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:MGI.
DR GO; GO:0051607; P:defense response to virus; IMP:MGI.
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:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IDA:MGI.
DR GO; GO:0039529; P:RIG-I signaling pathway; IGI:MGI.
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 1: Evidence at protein 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..462
FT /note="Protein LSM14 homolog A"
FT /id="PRO_0000187091"
FT DOMAIN 283..319
FT /note="DFDF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00845"
FT REGION 149..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 360..376
FT /note="FFD box"
FT MOTIF 379..399
FT /note="TFG box"
FT COMPBIAS 149..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 321..336
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 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND56"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 194
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND56"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND56"
FT MOD_RES 400
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 462 AA; 50546 MW; B2554A73B96C473B CRC64;
MSGGTPYIGS KISLISKAEI RYEGILYTID TENSTVALAK VRSFGTEDRP TDRPIPPRDE
VFEYIIFRGS DIKDLTVCEP PKPQCSLPQD PAIVQSSLGS SSSSFQSVGS YGPFGRMPAY
SQFSPSTLVG QQFGAVGVAG NSLTSFGTEA SNSGTLSQSN AVGSAFTQDT RSVKPQLAQG
RSSPQLDPLR KSPTMEQAVQ TASAHLPAPA PVGRRSPVPA RPLPPTSQKA IDNQEHRRAE
VHKVPRPENE QLRNDKRQVV PGVPSAPRRG RGGHRGGRGR FGIRRDGPMK FEKDFDFESA
NAQFNKEEID REFHNKLKLK EDKLEKQEKP VNGEDKGDSG VDTQNSEGNA DEEDPLGPNC
YYDKTKSFFD NISCDDNRER RPTWAEERRL NAETFGIPLR PNRGRGGYRG RGGLGFRGGR
GRGSGRGGTF TAPRGFRAGF RGARGGREFA DFEYRKTTAF GP
