LARP4_MOUSE
ID LARP4_MOUSE Reviewed; 719 AA.
AC Q8BWW4; Q3UR69;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=La-related protein 4;
DE AltName: Full=La ribonucleoprotein domain family member 4;
GN Name=Larp4;
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=C57BL/6J; TISSUE=Embryo, and Embryonic spinal cord;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Spleen;
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).
CC -!- FUNCTION: RNA binding protein that binds to the poly-A tract of mRNA
CC molecules. Associates with the 40S ribosomal subunit and with
CC polysomes. Plays a role in the regulation of mRNA translation. Plays a
CC role in the regulation of cell morphology and cytoskeletal
CC organization. {ECO:0000250|UniProtKB:Q71RC2}.
CC -!- SUBUNIT: Interacts (via N-terminal region) with PABPC1. Interacts with
CC RACK1. {ECO:0000250|UniProtKB:Q71RC2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:Q71RC2}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q71RC2}. Note=Localized throughout the cytosol.
CC Partially localized in stress granules in response to arsenite
CC treatment. {ECO:0000250|UniProtKB:Q71RC2}.
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DR EMBL; AK049756; BAC33905.2; -; mRNA.
DR EMBL; AK141743; BAE24819.1; -; mRNA.
DR CCDS; CCDS37208.1; -.
DR RefSeq; NP_001019697.2; NM_001024526.2.
DR RefSeq; NP_001074417.1; NM_001080948.2.
DR RefSeq; NP_001271450.1; NM_001284521.1.
DR RefSeq; NP_001271451.1; NM_001284522.1.
DR RefSeq; NP_001271452.1; NM_001284523.1.
DR AlphaFoldDB; Q8BWW4; -.
DR SMR; Q8BWW4; -.
DR BioGRID; 228885; 6.
DR IntAct; Q8BWW4; 1.
DR MINT; Q8BWW4; -.
DR STRING; 10090.ENSMUSP00000097780; -.
DR iPTMnet; Q8BWW4; -.
DR PhosphoSitePlus; Q8BWW4; -.
DR SwissPalm; Q8BWW4; -.
DR EPD; Q8BWW4; -.
DR jPOST; Q8BWW4; -.
DR MaxQB; Q8BWW4; -.
DR PaxDb; Q8BWW4; -.
DR PRIDE; Q8BWW4; -.
DR ProteomicsDB; 265042; -.
DR GeneID; 207214; -.
DR KEGG; mmu:207214; -.
DR CTD; 113251; -.
DR MGI; MGI:2443114; Larp4.
DR eggNOG; KOG2590; Eukaryota.
DR eggNOG; KOG2591; Eukaryota.
DR InParanoid; Q8BWW4; -.
DR OrthoDB; 263288at2759; -.
DR PhylomeDB; Q8BWW4; -.
DR BioGRID-ORCS; 207214; 19 hits in 72 CRISPR screens.
DR ChiTaRS; Larp4; mouse.
DR PRO; PR:Q8BWW4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BWW4; protein.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; ISO:MGI.
DR GO; GO:0005844; C:polysome; ISO:MGI.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI.
DR GO; GO:0008143; F:poly(A) binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; ISO:MGI.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; ISO:MGI.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR CDD; cd12707; RRM_LARP4; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR045180; La_dom_prot.
DR InterPro; IPR006630; La_HTH.
DR InterPro; IPR034903; LARP4_RRM.
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; Cytoplasm; Methylation; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT CHAIN 1..719
FT /note="La-related protein 4"
FT /id="PRO_0000207612"
FT DOMAIN 109..198
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT DOMAIN 199..277
FT /note="RRM"
FT REGION 12..21
FT /note="Interaction with PABPC1"
FT /evidence="ECO:0000250|UniProtKB:Q71RC2"
FT REGION 21..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..299
FT /note="Interaction with the poly-A tract of mRNA"
FT /evidence="ECO:0000250|UniProtKB:Q71RC2"
FT REGION 363..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..671
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:Q71RC2"
FT MOD_RES 363
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q71RC2"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71RC2"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71RC2"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71RC2"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71RC2"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71RC2"
FT MOD_RES 644
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q71RC2"
FT MOD_RES 681
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q71RC2"
FT MOD_RES 717
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71RC2"
SQ SEQUENCE 719 AA; 79763 MW; B699A5FC5642023B CRC64;
MLLFVEVTSK GTGLNPNAKV WQEIPSGNPD GTPVTEPSWH ETAATSGSHP EGHTELSEDM
CKEYEVMYSP SCETTRNTAD VEESADGMIL GPEDLSYQLY DVSGESSSAI STEDLKECLK
KQLEFCFSRE NLSKDLYLIS QMDSDQFVPI WTVANMEEIK KLTTNTDLIL EVLRSSPMVQ
VDEKGEKVRP SHKRCIVILR EIPETTPVEE VKALFKNENC PKVISCEFAH NSNWYITFQS
DTDAQQAFKY LREEVKTFQG KPIMARIKAI NTFFAKNGYR LMDSSMYTQP IQTPTQYPSP
VFMQPVYNPQ QYSVYSLVPQ SWSPSPAPYF ETPLAPFPNG SFVDGFSSPG SYKTNAAAMN
MGRPFPKNRV KPHFRSSSGS EHSTEGSVSL GDGPLSRSSS RIFLSERHNP TVTGQQEQTY
LPKEAPILQM EQNGDFGRGR RTLFRGRRRR DDDRIPRPQP AATEAKAPTP KFDLLATNFP
PLPGSSSRVP DELGLENRMS DVVKGVCREK DSEDVRVSCP VPAEDGQTDC TSAPLSISPS
PPCTAEPPVL STTQQEQDQM EDSAVPKDTL NPVAVPVSSP TATKPSPANT ASPCTSNINP
PRAVALQEPR KLSYAEVCQK PPKEPSPVLV QPLRELRSNA VSPTRNEENG APEKPVEKPH
EKPETRASKD HSGFRGNTIP RGAAGKIREQ RRQFSHRATP QGVTRRNGKE QYVPPRSPK
