HNRDL_MOUSE
ID HNRDL_MOUSE Reviewed; 301 AA.
AC Q9Z130; Q9CT01;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 156.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein D-like;
DE Short=hnRNP D-like;
DE Short=hnRNP DL;
DE AltName: Full=JKT41-binding protein;
GN Name=Hnrnpdl; Synonyms=Hnrpdl, Jktbp;
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 [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Testis;
RX PubMed=10717477; DOI=10.1016/s0378-1119(00)00032-9;
RA Akagi T., Kamei D., Tsuchiya N., Nishina Y., Horiguchi H., Matsui M.,
RA Kamma H., Yamada M.;
RT "Molecular characterization of a mouse heterogeneous nuclear
RT ribonucleoprotein D-like protein JKTBP and its tissue-specific
RT expression.";
RL Gene 245:267-273(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and Spleen;
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].
RC STRAIN=Czech II; 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 [4]
RP PROTEIN SEQUENCE OF 1-13, FUNCTION, INTERACTION WITH ZNF148, SUBCELLULAR
RP LOCATION, AND DNA-BINDING.
RC TISSUE=Myotube;
RX PubMed=15190078; DOI=10.1074/jbc.m403160200;
RA Boopathi E., Lenka N., Prabu S.K., Fang J.-K., Wilkinson F., Atchison M.,
RA Giallongo A., Avadhani N.G.;
RT "Regulation of murine cytochrome c oxidase Vb gene expression during
RT myogenesis: YY-1 and heterogeneous nuclear ribonucleoprotein D-like protein
RT (JKTBP1) reciprocally regulate transcription activity by physical
RT interaction with the BERF-1/ZBP-89 factor.";
RL J. Biol. Chem. 279:35242-35254(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, 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 [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-289, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and 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: Acts as a transcriptional regulator. Promotes transcription
CC repression (By similarity). Promotes transcription activation in
CC differentiated myotubes. Binds to double- and single-stranded DNA
CC sequences (By similarity). Binds to the transcription suppressor CATR
CC sequence of the COX5B promoter. Binds with high affinity to RNA
CC molecules that contain AU-rich elements (AREs) found within the 3'-UTR
CC of many proto-oncogenes and cytokine mRNAs (By similarity). Binds both
CC to nuclear and cytoplasmic poly(A) mRNAs (By similarity). Binds to
CC poly(G) and poly(A), but not to poly(U) or poly(C) RNA homopolymers (By
CC similarity). Binds to the 5'-ACUAGC-3' RNA consensus sequence (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:15190078}.
CC -!- SUBUNIT: Interacts with TNPO1 (By similarity). Interacts with ZNF148.
CC {ECO:0000250, ECO:0000269|PubMed:15190078}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10717477,
CC ECO:0000269|PubMed:15190078}. Cytoplasm {ECO:0000250|UniProtKB:O14979}.
CC Note=Shuttles between the nucleus and the cytoplasm in a TNPO1-
CC dependent manner. {ECO:0000250|UniProtKB:O14979}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, myoblast, myotube,
CC heart, brain, liver, kidney, heart, lung, stomach, small intestine,
CC large intestine, spleen, and testis (at protein level). Expressed in
CC brain, skeletal muscle, heart, lung, liver, stomach, small intestine,
CC large intestine, kidney, spleen and testis.
CC {ECO:0000269|PubMed:10717477}.
CC -!- PTM: Dimethylation of Arg-289 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; AB017020; BAA75479.1; -; mRNA.
DR EMBL; AK011581; BAB27715.1; -; mRNA.
DR EMBL; AK172629; BAE43104.1; -; mRNA.
DR EMBL; BC021374; AAH21374.1; -; mRNA.
DR AlphaFoldDB; Q9Z130; -.
DR SMR; Q9Z130; -.
DR IntAct; Q9Z130; 6.
DR MINT; Q9Z130; -.
DR STRING; 10090.ENSMUSP00000121005; -.
DR iPTMnet; Q9Z130; -.
DR PhosphoSitePlus; Q9Z130; -.
DR SwissPalm; Q9Z130; -.
DR EPD; Q9Z130; -.
DR jPOST; Q9Z130; -.
DR MaxQB; Q9Z130; -.
DR PaxDb; Q9Z130; -.
DR PeptideAtlas; Q9Z130; -.
DR PRIDE; Q9Z130; -.
DR ProteomicsDB; 269610; -.
DR MGI; MGI:1355299; Hnrnpdl.
DR eggNOG; KOG0118; Eukaryota.
DR InParanoid; Q9Z130; -.
DR ChiTaRS; Hnrnpdl; mouse.
DR PRO; PR:Q9Z130; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9Z130; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0008143; F:poly(A) binding; ISO:MGI.
DR GO; GO:0034046; F:poly(G) binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI.
DR GO; GO:0016071; P:mRNA metabolic process; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
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; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; RNA-binding; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..301
FT /note="Heterogeneous nuclear ribonucleoprotein D-like"
FT /id="PRO_0000287240"
FT DOMAIN 29..111
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 114..193
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 194..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..301
FT /note="Necessary for interaction with TNPO1"
FT /evidence="ECO:0000250"
FT REGION 279..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 42
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14979"
FT MOD_RES 97
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14979"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14979"
FT MOD_RES 289
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O14979"
FT MOD_RES 289
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 90
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O14979"
SQ SEQUENCE 301 AA; 33559 MW; 8AB2787FEB73311C CRC64;
MEDMNEYSNI EEFAEGSKIN ASKNQQDDGK MFIGGLSWDT SKKDLTEYLS RFGEVVDCTI
KTDPVTGRSR GFGFVLFKDA ASVDKVLELK EHKLDGKLID PKRAKALKGK EPPKKVFVGG
LSPDTSEEQI KEYFGAFGEI ENIELPMDTK TNERRGFCFI TYTDEEPVKK LLESRYHQIG
SGKCEIKVAQ PKEVYRQQQQ QQKGGRGAAA GGRGGARGRG RGQGQNWNQG FNNYYDQGYG
NYNSAYGGDQ NYSGYGGYDY TGYNYGNYGY GQGYADYSGQ QSTYGKASRG GGNHQNNYQP
Y
