HNRDL_RAT
ID HNRDL_RAT Reviewed; 322 AA.
AC Q3SWU3;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein D-like;
DE Short=hnRNP D-like;
DE Short=hnRNP DL;
GN Name=Hnrnpdl; Synonyms=Hnrpdl;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Acts as a transcriptional regulator. Promotes transcription
CC repression. Promotes transcription activation in differentiated
CC myotubes. Binds to double- and single-stranded DNA sequences. Binds to
CC the transcription suppressor CATR sequence of the COX5B promoter. Binds
CC with high affinity to RNA molecules that contain AU-rich elements
CC (AREs) found within the 3'-UTR of many proto-oncogenes and cytokine
CC mRNAs. Binds both to nuclear and cytoplasmic poly(A) mRNAs. Binds to
CC poly(G) and poly(A), but not to poly(U) or poly(C) RNA homopolymers.
CC Binds to the 5'-ACUAGC-3' RNA consensus sequence (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TNPO1 and ZNF148. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O14979}. Cytoplasm
CC {ECO:0000250|UniProtKB:O14979}. Note=Shuttles between the nucleus and
CC the cytoplasm in a TNPO1-dependent manner.
CC {ECO:0000250|UniProtKB:O14979}.
CC -!- PTM: Dimethylation of Arg-310 is probably of the asymmetric type.
CC {ECO:0000250}.
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; BC104683; AAI04684.1; -; mRNA.
DR RefSeq; NP_001028868.1; NM_001033696.1.
DR AlphaFoldDB; Q3SWU3; -.
DR SMR; Q3SWU3; -.
DR BioGRID; 258094; 3.
DR IntAct; Q3SWU3; 1.
DR MINT; Q3SWU3; -.
DR STRING; 10116.ENSRNOP00000003106; -.
DR iPTMnet; Q3SWU3; -.
DR PhosphoSitePlus; Q3SWU3; -.
DR jPOST; Q3SWU3; -.
DR PaxDb; Q3SWU3; -.
DR PRIDE; Q3SWU3; -.
DR Ensembl; ENSRNOT00000003106; ENSRNOP00000003106; ENSRNOG00000002270.
DR GeneID; 305178; -.
DR KEGG; rno:305178; -.
DR CTD; 9987; -.
DR RGD; 1309950; Hnrnpdl.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000154426; -.
DR HOGENOM; CLU_012062_1_1_1; -.
DR InParanoid; Q3SWU3; -.
DR OMA; RSFNDGF; -.
DR PRO; PR:Q3SWU3; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000002270; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; Q3SWU3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008143; F:poly(A) binding; IBA:GO_Central.
DR GO; GO:0034046; F:poly(G) binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR CDD; cd12758; RRM1_hnRPDL; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034847; hnRPDL_RRM1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Cytoplasm; DNA-binding; Isopeptide bond;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; RNA-binding; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..322
FT /note="Heterogeneous nuclear ribonucleoprotein D-like"
FT /id="PRO_0000287241"
FT DOMAIN 51..133
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 136..215
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..322
FT /note="Necessary for interaction with TNPO1"
FT /evidence="ECO:0000250"
FT REGION 299..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O14979"
FT MOD_RES 64
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14979"
FT MOD_RES 119
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14979"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 310
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O14979"
FT MOD_RES 310
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Z130"
FT CROSSLNK 112
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O14979"
SQ SEQUENCE 322 AA; 35294 MW; 42DE123DDC74A9AA CRC64;
MTGTARSALP LPQSPARALR PSGAARAAPS LSPSRFSACP LDPSSFPTSG NKMFIGGLSW
DTSKKDLTEY LSRFGEVVDC TIKTDPVTGR SRGFGFVLFK DAASVDKVLE LKEHKLDGKL
IDPKRAKALK GKEPPKKVFV GGLSPDTSEE QIKEYFGAFG EIENIELPMD TKTNERRGFC
FITYTDEEPV KKLLESRYHQ IGSGKCEIKV AQPKEVYRQQ QQQQKGGRGA AAGGRGGARG
RGRGQGQNWN QGFNNYYDQG YGNYNSAYGD ESYSGYGGYD YTGYNYGSYG YGQGYTDYSG
QQSTYGKASR GGGNHQNNYQ PY
