HNRPL_MOUSE
ID HNRPL_MOUSE Reviewed; 586 AA.
AC Q8R081; O54789; Q499X2; Q8K0S7;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein L;
DE Short=hnRNP L;
GN Name=Hnrnpl; Synonyms=Hnrpl;
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; TISSUE=Colon, and Salivary gland;
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 [MRNA] OF 388-586.
RA Sakai N., Saitou Y., Toyota T.;
RT "Mouse ribonucleoprotein.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 396-408 AND 566-576.
RC TISSUE=Brain;
RA Lubec G., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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 [5]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22523384; DOI=10.4049/jimmunol.1103142;
RA Gaudreau M.C., Heyd F., Bastien R., Wilhelm B., Moeroey T.;
RT "Alternative splicing controlled by heterogeneous nuclear ribonucleoprotein
RT L regulates development, proliferation, and migration of thymic pre-T
RT cells.";
RL J. Immunol. 188:5377-5388(2012).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-351 AND ARG-355, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 376-579.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of a heterogeneous nuclear ribonucleoprotein l (hnrpl)
RT from Mus musculus at 1.60 A resolution.";
RL Submitted (NOV-2011) to the PDB data bank.
CC -!- FUNCTION: Splicing factor binding to exonic or intronic sites and
CC acting as either an activator or repressor of exon inclusion
CC (PubMed:22523384). Exhibits a binding preference for CA-rich elements.
CC Component of the heterogeneous nuclear ribonucleoprotein (hnRNP)
CC complexes and associated with most nascent transcripts. Associates,
CC together with APEX1, to the negative calcium responsive element (nCaRE)
CC B2 of the APEX2 promoter. As part of a ribonucleoprotein complex
CC composed at least of ZNF827, HNRNPK and the circular RNA circZNF827
CC that nucleates the complex on chromatin, may negatively regulate the
CC transcription of genes involved in neuronal differentiation (By
CC similarity). {ECO:0000250|UniProtKB:P14866,
CC ECO:0000269|PubMed:22523384}.
CC -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Interacts with HNRNPLL. Interacts with
CC APEX1; the interaction is DNA-dependent. Component of a complex with
CC SETD2 (By similarity). Interacts with ELAVL1 (By similarity). Part of a
CC transcription inhibitory ribonucleoprotein complex composed at least of
CC the circular RNA circZNF827, ZNF827 and HNRNPK (By similarity).
CC {ECO:0000250|UniProtKB:F1LQ48, ECO:0000250|UniProtKB:P14866}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:P14866}. Cytoplasm
CC {ECO:0000250|UniProtKB:P14866}. Note=Localized in cytoplasmic mRNP
CC granules containing untranslated mRNAs. These granules are not
CC identical with P bodies or stress granules.
CC {ECO:0000250|UniProtKB:P14866}.
CC -!- TISSUE SPECIFICITY: Detected in hematopoietic cells, including lymphoid
CC progenitor cells. {ECO:0000269|PubMed:22523384}.
CC -!- DOMAIN: RRM domain 2 has moderate RNA-binding affinity. RRM domains 3
CC and 4 may facilitate RNA looping when binding to two appropriately
CC separated binding sites within the same target pre-mRNA.
CC {ECO:0000250|UniProtKB:P14866}.
CC -!- PTM: Phosphorylation at Ser-541 by CaMK4 enhances interaction with a
CC CaMK4-responsive RNA element (CaRRE1), and prevents inclusion of the
CC stress axis-regulated exon (STREX) of the KCNMA1 potassium channel
CC transcripts upon membrane depolarization.
CC {ECO:0000250|UniProtKB:P14866}.
CC -!- DISRUPTION PHENOTYPE: Complete lethality during early embryonic
CC development. {ECO:0000269|PubMed:22523384}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27206.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC027206; AAH27206.1; ALT_INIT; mRNA.
DR EMBL; BC030461; AAH30461.1; -; mRNA.
DR EMBL; BC099683; AAH99683.1; -; mRNA.
DR EMBL; AB009392; BAA24237.1; -; mRNA.
DR CCDS; CCDS39864.2; -.
DR RefSeq; NP_796275.3; NM_177301.5.
DR RefSeq; XP_006539621.1; XM_006539558.2.
DR PDB; 3S01; X-ray; 2.15 A; A=376-586.
DR PDB; 3TYT; X-ray; 1.60 A; A=376-579.
DR PDBsum; 3S01; -.
DR PDBsum; 3TYT; -.
DR AlphaFoldDB; Q8R081; -.
DR BMRB; Q8R081; -.
DR SMR; Q8R081; -.
DR BioGRID; 200360; 50.
DR IntAct; Q8R081; 15.
DR MINT; Q8R081; -.
DR STRING; 10090.ENSMUSP00000134734; -.
DR iPTMnet; Q8R081; -.
DR PhosphoSitePlus; Q8R081; -.
DR SwissPalm; Q8R081; -.
DR REPRODUCTION-2DPAGE; Q8R081; -.
DR EPD; Q8R081; -.
DR jPOST; Q8R081; -.
DR MaxQB; Q8R081; -.
DR PaxDb; Q8R081; -.
DR PeptideAtlas; Q8R081; -.
DR PRIDE; Q8R081; -.
DR ProteomicsDB; 273312; -.
DR Antibodypedia; 4276; 465 antibodies from 37 providers.
DR DNASU; 15388; -.
DR Ensembl; ENSMUST00000038572; ENSMUSP00000049407; ENSMUSG00000015165.
DR Ensembl; ENSMUST00000174548; ENSMUSP00000133728; ENSMUSG00000015165.
DR GeneID; 15388; -.
DR KEGG; mmu:15388; -.
DR UCSC; uc009fzz.2; mouse.
DR CTD; 3191; -.
DR MGI; MGI:104816; Hnrnpl.
DR VEuPathDB; HostDB:ENSMUSG00000015165; -.
DR eggNOG; KOG1456; Eukaryota.
DR GeneTree; ENSGT01030000234642; -.
DR InParanoid; Q8R081; -.
DR OMA; FNAQPEI; -.
DR OrthoDB; 1545178at2759; -.
DR PhylomeDB; Q8R081; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR BioGRID-ORCS; 15388; 30 hits in 74 CRISPR screens.
DR ChiTaRS; Hnrnpl; mouse.
DR PRO; PR:Q8R081; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8R081; protein.
DR Bgee; ENSMUSG00000015165; Expressed in retinal neural layer and 245 other tissues.
DR ExpressionAtlas; Q8R081; baseline and differential.
DR Genevisible; Q8R081; MM.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0045120; C:pronucleus; IDA:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0035770; C:ribonucleoprotein granule; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:1990715; F:mRNA CDS binding; ISO:MGI.
DR GO; GO:0097157; F:pre-mRNA intronic binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0034198; P:cellular response to amino acid starvation; ISO:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:1902416; P:positive regulation of mRNA binding; ISO:MGI.
DR GO; GO:0045727; P:positive regulation of translation; ISO:MGI.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
DR CDD; cd12780; RRM1_hnRNPL; 1.
DR CDD; cd12785; RRM2_hnRNPL; 1.
DR CDD; cd12699; RRM3_hnRNPL; 1.
DR CDD; cd12704; RRM4_hnRNPL; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR006536; HnRNP-L/PTB.
DR InterPro; IPR034816; hnRNP-L_RRM3.
DR InterPro; IPR035005; hnRNPL_RRM1.
DR InterPro; IPR035008; hnRNPL_RRM2.
DR InterPro; IPR034817; hnRNPL_RRM4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR021790; PTBP1-like_RRM2.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF11835; RRM_8; 1.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 3.
DR TIGRFAMs; TIGR01649; hnRNP-L_PTB; 1.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ribonucleoprotein; RNA-binding; Ubl conjugation.
FT CHAIN 1..586
FT /note="Heterogeneous nuclear ribonucleoprotein L"
FT /id="PRO_0000081863"
FT DOMAIN 99..173
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 190..267
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 379..476
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 492..580
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..375
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14866"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14866"
FT MOD_RES 266
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P14866"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14866"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14866"
FT MOD_RES 351
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 355
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 541
FT /note="Phosphoserine; by CaMK4"
FT /evidence="ECO:0000250|UniProtKB:P14866"
FT CROSSLNK 59
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P14866"
FT CROSSLNK 62
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P14866"
FT CROSSLNK 133
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P14866"
FT CROSSLNK 299
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P14866"
FT CROSSLNK 565
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P14866"
FT CONFLICT 388
FT /note="Q -> E (in Ref. 2; BAA24237)"
FT /evidence="ECO:0000305"
FT STRAND 379..384
FT /evidence="ECO:0007829|PDB:3TYT"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:3TYT"
FT HELIX 393..400
FT /evidence="ECO:0007829|PDB:3TYT"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:3TYT"
FT STRAND 406..411
FT /evidence="ECO:0007829|PDB:3TYT"
FT STRAND 419..425
FT /evidence="ECO:0007829|PDB:3TYT"
FT HELIX 426..436
FT /evidence="ECO:0007829|PDB:3TYT"
FT STRAND 447..450
FT /evidence="ECO:0007829|PDB:3TYT"
FT STRAND 452..455
FT /evidence="ECO:0007829|PDB:3S01"
FT STRAND 469..473
FT /evidence="ECO:0007829|PDB:3TYT"
FT HELIX 485..488
FT /evidence="ECO:0007829|PDB:3TYT"
FT STRAND 498..505
FT /evidence="ECO:0007829|PDB:3TYT"
FT HELIX 511..521
FT /evidence="ECO:0007829|PDB:3TYT"
FT STRAND 527..531
FT /evidence="ECO:0007829|PDB:3TYT"
FT STRAND 536..545
FT /evidence="ECO:0007829|PDB:3TYT"
FT HELIX 549..559
FT /evidence="ECO:0007829|PDB:3TYT"
FT STRAND 567..571
FT /evidence="ECO:0007829|PDB:3TYT"
FT STRAND 576..578
FT /evidence="ECO:0007829|PDB:3TYT"
SQ SEQUENCE 586 AA; 63964 MW; BB56D3D6A8553F7E CRC64;
MSRRLLPRAE KRRRRLEQRQ QPDEQLRRAG AMVKMAAAGG GGGGGRYYGG GNEGGRAPKR
LKTENAGDQH GGGGGGGSGA AGGGGGENYD DPHKTPASPV VHIRGLIDGV VEADLVEALQ
EFGPISYVVV MPKKRQALVE FEDVLGACNA VNYAADNQIY IAGHPAFVNY STSQKISRPG
DSDDSRSVNS VLLFTILNPI YSITTDVLYT ICNPCGPVQR IVIFRKNGVQ AMVEFDSVQS
AQRAKASLNG ADIYSGCCTL KIEYAKPTRL NVFKNDQDTW DYTNPNLSGQ GDPGSNPNKR
QRQPPLLGDH PAEYGGPHGG YHSHYHDEGY GPPPPHYEGR RMGPPVGGHR RGPSRYGPQY
GHPPPPPPPP DYGPHADSPV LMVYGLDQSK MNCDRVFNVF CLYGNVEKVK FMKSKPGAAM
VEMADGYAVD RAITHLNNNF MFGQKMNVCV SKQPAIMPGQ SYGLEDGSCS YKDFSESRNN
RFSTPEQAAK NRIQHPSNVL HFFNAPLEVT EENFFEICDE LGVKRPTSVK VFSGKSERSS
SGLLEWDSKS DALETLGFLN HYQMKNPNGP YPYTLKLCFS TAQHAS
