LAR4B_MOUSE
ID LAR4B_MOUSE Reviewed; 741 AA.
AC Q6A0A2; Q3TUH7; Q6AZA8; Q8BJP3; Q8BY17;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=La-related protein 4B;
DE AltName: Full=La ribonucleoprotein domain family member 4B;
DE AltName: Full=La ribonucleoprotein domain family member 5;
DE AltName: Full=La-related protein 5;
GN Name=Larp4b; Synonyms=D13Wsu64e, Kiaa0217, Larp5;
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] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-672 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, Head, and Thymus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Limb;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246 AND SER-500, AND
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 IDENTIFICATION BY 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-735 AND SER-739, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Liver, Lung, Pancreas, Spleen,
RC and 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 [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-495, 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: Stimulates mRNA translation. {ECO:0000250|UniProtKB:Q92615}.
CC -!- SUBUNIT: Interacts with PABPC1. Interacts with RACK1. Associates with
CC polysomes via the 40S ribosomal subunit.
CC {ECO:0000250|UniProtKB:Q92615}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q92615}. Note=Localized in cytoplasmic mRNP
CC granules containing untranslated mRNAs in response to arsenite
CC treatment. {ECO:0000250|UniProtKB:Q92615}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6A0A2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6A0A2-2; Sequence=VSP_023987;
CC Name=3;
CC IsoId=Q6A0A2-3; Sequence=VSP_023988;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32194.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK172916; BAD32194.1; ALT_INIT; mRNA.
DR EMBL; AK042491; BAC31273.2; -; mRNA.
DR EMBL; AK080953; BAC38091.1; -; mRNA.
DR EMBL; AK160759; BAE35994.1; -; mRNA.
DR EMBL; BC078640; AAH78640.1; -; mRNA.
DR CCDS; CCDS36588.1; -. [Q6A0A2-1]
DR CCDS; CCDS79162.1; -. [Q6A0A2-2]
DR RefSeq; NP_001298046.1; NM_001311117.1. [Q6A0A2-2]
DR RefSeq; NP_766173.1; NM_172585.3. [Q6A0A2-1]
DR RefSeq; XP_006516539.1; XM_006516476.2. [Q6A0A2-1]
DR RefSeq; XP_006516540.1; XM_006516477.3. [Q6A0A2-1]
DR AlphaFoldDB; Q6A0A2; -.
DR SMR; Q6A0A2; -.
DR BioGRID; 229985; 7.
DR IntAct; Q6A0A2; 2.
DR MINT; Q6A0A2; -.
DR STRING; 10090.ENSMUSP00000140993; -.
DR iPTMnet; Q6A0A2; -.
DR PhosphoSitePlus; Q6A0A2; -.
DR EPD; Q6A0A2; -.
DR jPOST; Q6A0A2; -.
DR MaxQB; Q6A0A2; -.
DR PaxDb; Q6A0A2; -.
DR PeptideAtlas; Q6A0A2; -.
DR PRIDE; Q6A0A2; -.
DR ProteomicsDB; 265038; -. [Q6A0A2-1]
DR ProteomicsDB; 265039; -. [Q6A0A2-2]
DR ProteomicsDB; 265040; -. [Q6A0A2-3]
DR Antibodypedia; 52530; 50 antibodies from 15 providers.
DR DNASU; 217980; -.
DR Ensembl; ENSMUST00000091829; ENSMUSP00000089437; ENSMUSG00000033499. [Q6A0A2-2]
DR Ensembl; ENSMUST00000188211; ENSMUSP00000140993; ENSMUSG00000033499. [Q6A0A2-1]
DR Ensembl; ENSMUST00000188939; ENSMUSP00000139578; ENSMUSG00000033499. [Q6A0A2-3]
DR GeneID; 217980; -.
DR KEGG; mmu:217980; -.
DR UCSC; uc007pkr.1; mouse. [Q6A0A2-1]
DR UCSC; uc007pks.1; mouse. [Q6A0A2-2]
DR UCSC; uc011ywb.1; mouse. [Q6A0A2-3]
DR CTD; 23185; -.
DR MGI; MGI:106330; Larp4b.
DR VEuPathDB; HostDB:ENSMUSG00000033499; -.
DR eggNOG; KOG2591; Eukaryota.
DR GeneTree; ENSGT00940000157755; -.
DR HOGENOM; CLU_025110_0_0_1; -.
DR InParanoid; Q6A0A2; -.
DR OMA; LEFCLSX; -.
DR OrthoDB; 263288at2759; -.
DR PhylomeDB; Q6A0A2; -.
DR TreeFam; TF321960; -.
DR BioGRID-ORCS; 217980; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Larp4b; mouse.
DR PRO; PR:Q6A0A2; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q6A0A2; protein.
DR Bgee; ENSMUSG00000033499; Expressed in crypt of Lieberkuhn of small intestine and 257 other tissues.
DR ExpressionAtlas; Q6A0A2; baseline and differential.
DR Genevisible; Q6A0A2; MM.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0042788; C:polysomal ribosome; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:1905870; P:positive regulation of 3'-UTR-mediated mRNA stabilization; ISO:MGI.
DR GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR045180; La_dom_prot.
DR InterPro; IPR006630; La_HTH.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR22792; PTHR22792; 1.
DR Pfam; PF05383; La; 1.
DR SMART; SM00715; LA; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50961; HTH_LA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Methylation; Phosphoprotein;
KW Reference proteome; RNA-binding; Translation regulation.
FT CHAIN 1..741
FT /note="La-related protein 4B"
FT /id="PRO_0000281140"
FT DOMAIN 152..241
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT DOMAIN 242..309
FT /note="RRM"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q92615"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 406
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q92615"
FT MOD_RES 421
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q92615"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92615"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92615"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92615"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92615"
FT MOD_RES 495
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 520
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92615"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92615"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92615"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92615"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92615"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92615"
FT MOD_RES 721
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92615"
FT MOD_RES 727
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92615"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92615"
FT MOD_RES 735
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 414..497
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023987"
FT VAR_SEQ 568..645
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023988"
FT CONFLICT 102
FT /note="A -> D (in Ref. 1; BAD32194)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="L -> S (in Ref. 1; BAD32194)"
FT /evidence="ECO:0000305"
FT CONFLICT 688
FT /note="Q -> R (in Ref. 1; BAD32194)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 741 AA; 81627 MW; EE7DCECD17343C48 CRC64;
MTSDQDAKVV AEPQAQRVQE GKDSSHLMNG PISQTTSQTR SLPALTQVPT TKVSELNPNA
KVWGTHMLHL EASSAAVGVN AAWEEAPGHP TDCDQQVLGL DANGDGDKSR ENAALPDAQE
AEQTDMSTLA LDHSEYEPLP ENNDTGGNES QPESQEDPRE VLKKTLEFCL SRENLASDMY
LISQMDSDQY VPITTVANLD HIKKLSTDVD LIVEVLRSLP LVQVDEKGEK VRPNQNRCIV
ILREISESTP VEEVEALFKG DNLPKFINCE FAYNDNWFIT FETEADAQQA YKYLREEVRT
FQGKPIKARI KAKAIAINTF LPKNGFRPLD MNLYTQQRYA TSFYLPPVYS PQQQFPLYSL
ITPQTWSTTH SYLDPPLVTP FPSTGFINGF TSPTFKPATS PLTSLRQYPP RSRNPSKSHL
RHAIPSTERG PGLLESPSIF NFTADRLING VRSPQTRQAG QTRTRIQNPS AYAKREIGTG
RVEPSSLESS PGLGRGRKNS FGYRKKREEK FTSSQTQSPT PPKPPSPSFE LGLSNFPPLP
GAAGNLKTED LFENRLSSLI IGSSKERNLS TDASTNTVPV VGPREPSVPA PCAVSAAFER
SPSPVHLPED PKVAEKQRET QSVDRLPSTP TTTACKSVQV NGAATELRKP SYAEICQRTS
KDPSSSSPLQ PPKEQKPSTV ACGKEEKQLS EPVERHREPP ALKSTPGVPK DQRRQPGRRA
SPPAAGKRLS KEQNTPPKSP Q
