ELAV1_RAT
ID ELAV1_RAT Reviewed; 326 AA.
AC B5DF91;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=ELAV-like protein 1 {ECO:0000305};
DE AltName: Full=Hu-antigen R;
DE Short=HuR;
GN Name=Elavl1 {ECO:0000312|RGD:1308649};
GN Synonyms=Hur {ECO:0000312|EMBL:BAG72208.1};
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 {ECO:0000312|EMBL:AAI68972.1};
RN [1] {ECO:0000312|EMBL:BAG72208.1}
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH HNRNPL, SUBCELLULAR LOCATION,
RP AND RNA-BINDING.
RX PubMed=18161049; DOI=10.1002/hep.22036;
RA Matsui K., Nishizawa M., Ozaki T., Kimura T., Hashimoto I., Yamada M.,
RA Kaibori M., Kamiyama Y., Ito S., Okumura T.;
RT "Natural antisense transcript stabilizes inducible nitric oxide synthase
RT messenger RNA in rat hepatocytes.";
RL Hepatology 47:686-697(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart {ECO:0000312|EMBL:AAI68972.1};
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, 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: RNA-binding protein that binds to the 3'-UTR region of mRNAs
CC and increases their stability (By similarity). Involved in embryonic
CC stem cell (ESC) differentiation: preferentially binds mRNAs that are
CC not methylated by N6-methyladenosine (m6A), stabilizing them, promoting
CC ESC differentiation (By similarity). Has also been shown to be capable
CC of binding to m6A-containing mRNAs and contributes to MYC stability by
CC binding to m6A-containing MYC mRNAs (By similarity). Binds to poly-U
CC elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs.
CC Binds avidly to the AU-rich element in FOS and IL3/interleukin-3 mRNAs.
CC In the case of the FOS AU-rich element, binds to a core element of 27
CC nucleotides that contain AUUUA, AUUUUA, and AUUUUUA motifs. Binds
CC preferentially to the 5'-UUUU[AG]UUU-3' motif in vitro (By similarity).
CC With ZNF385A, binds the 3'-UTR of p53/TP53 mRNA to control their
CC nuclear export induced by CDKN2A. Hence, may regulate p53/TP53
CC expression and mediate in part the CDKN2A anti-proliferative activity.
CC May also bind with ZNF385A the CCNB1 mRNA (By similarity). Increases
CC the stability of the leptin mRNA harboring an AU-rich element (ARE) in
CC its 3' UTR (By similarity). {ECO:0000250|UniProtKB:P70372,
CC ECO:0000250|UniProtKB:Q15717}.
CC -!- SUBUNIT: Monomer and homodimer (in vitro). Interacts with ANP32A (By
CC similarity). Interacts with ZNF385A; the interaction is indirect and
CC mRNA-dependent and may regulate p53/TP53 expression (By similarity).
CC Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1,
CC HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and
CC YBX1. Interacts with AGO1 and AGO2. Interacts with IGF2BP1. Interacts
CC with IGF2BP2 and IGF2BP3 (By similarity). Interacts with HNRNPL
CC (PubMed:18161049). Interacts with DHX36; this interaction occurs in a
CC RNA-dependent manner. Interacts with ILF3; this interaction occurs in a
CC RNA-dependent manner (By similarity). Interacts with PLEKHN1 (By
CC similarity). Interacts with SHFL; the interaction increases in presence
CC of RNA (By similarity). Interacts with YBX1; interaction recruits
CC ELAVL1 on C5-methylcytosine (m5C)-containing mRNAs, thereby promoting
CC mRNA stability (By similarity). {ECO:0000250|UniProtKB:P70372,
CC ECO:0000250|UniProtKB:Q15717, ECO:0000269|PubMed:18161049}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18161049}. Nucleus
CC {ECO:0000250|UniProtKB:Q15717}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:P70372}. Cytoplasm, P-body
CC {ECO:0000250|UniProtKB:Q15717}. Note=Translocates into the cytoplasm
CC following phosphorylation by MAPKAPK2. Likewise, phosphorylation by
CC PRKCD promotes translocation from the nucleus into the cytoplasm, where
CC it is associated with free and cytoskeleton-bound polysomes. Localizes
CC to the stress granules in the presence of PLEKHN1.
CC {ECO:0000250|UniProtKB:Q15717}.
CC -!- DOMAIN: The first RRM (RNA recognition motif) domain is essential for
CC binding to AU-rich elements. {ECO:0000250|UniProtKB:Q15717}.
CC -!- PTM: Phosphorylated by MAPKAPK2. Phosphorylated by PRKCD.
CC {ECO:0000250|UniProtKB:Q15717}.
CC -!- PTM: Methylated at Arg-217 by CARM1 in macrophages in response to LPS
CC challenge. {ECO:0000250|UniProtKB:Q15717}.
CC -!- SIMILARITY: Belongs to the RRM elav family. {ECO:0000305}.
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DR EMBL; AB212679; BAG72208.1; -; mRNA.
DR EMBL; AABR07034979; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474084; EDL75000.1; -; Genomic_DNA.
DR EMBL; CH474084; EDL75001.1; -; Genomic_DNA.
DR EMBL; BC168972; AAI68972.1; -; mRNA.
DR RefSeq; NP_001102318.1; NM_001108848.1.
DR AlphaFoldDB; B5DF91; -.
DR SMR; B5DF91; -.
DR CORUM; B5DF91; -.
DR IntAct; B5DF91; 4.
DR STRING; 10116.ENSRNOP00000001415; -.
DR iPTMnet; B5DF91; -.
DR PhosphoSitePlus; B5DF91; -.
DR jPOST; B5DF91; -.
DR PaxDb; B5DF91; -.
DR PeptideAtlas; B5DF91; -.
DR PRIDE; B5DF91; -.
DR Ensembl; ENSRNOT00000001415; ENSRNOP00000001415; ENSRNOG00000001069.
DR GeneID; 363854; -.
DR KEGG; rno:363854; -.
DR UCSC; RGD:1308649; rat.
DR CTD; 1994; -.
DR RGD; 1308649; Elavl1.
DR eggNOG; KOG0145; Eukaryota.
DR GeneTree; ENSGT00940000155528; -.
DR HOGENOM; CLU_026186_2_2_1; -.
DR InParanoid; B5DF91; -.
DR OMA; WQKHVTS; -.
DR OrthoDB; 614259at2759; -.
DR PhylomeDB; B5DF91; -.
DR TreeFam; TF313377; -.
DR Reactome; R-RNO-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:B5DF91; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Proteomes; UP000234681; Chromosome 12.
DR Bgee; ENSRNOG00000001069; Expressed in thymus and 20 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:ARUK-UCL.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0016528; C:sarcoplasm; IEA:Ensembl.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:RGD.
DR GO; GO:0106222; F:lncRNA binding; ISO:RGD.
DR GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0048255; P:mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0060965; P:negative regulation of miRNA-mediated gene silencing; ISS:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; ISO:RGD.
DR GO; GO:0016441; P:post-transcriptional gene silencing; ISO:RGD.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; ISO:RGD.
DR GO; GO:2000036; P:regulation of stem cell population maintenance; ISO:RGD.
DR CDD; cd12650; RRM1_Hu; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR006548; ELAD_HU_SF.
DR InterPro; IPR034775; ELAV/Hu_RRM1.
DR InterPro; IPR002343; Hud_Sxl_RNA.
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; 3.
DR PRINTS; PR00961; HUDSXLRNA.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR TIGRFAMs; TIGR01661; ELAV_HUD_SF; 1.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15717"
FT CHAIN 2..326
FT /note="ELAV-like protein 1"
FT /id="PRO_0000436065"
FT DOMAIN 20..98
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 106..186
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 244..322
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q15717"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15717"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15717"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15717"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15717"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 206
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P70372"
FT MOD_RES 217
FT /note="Asymmetric dimethylarginine; by CARM1; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15717"
FT MOD_RES 217
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15717"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15717"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15717"
FT CROSSLNK 191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15717"
SQ SEQUENCE 326 AA; 36169 MW; 74A98DEE5B921AF6 CRC64;
MSNGYEDHMA EDCRDDIGRT NLIVNYLPQN MTQEELRSLF SSIGEVESAK LIRDKVAGHS
LGYGFVNYVT AKDAERAIST LNGLRLQSKT IKVSYARPSS EVIKDANLYI SGLPRTMTQK
DVEDMFSRFG RIINSRVLVD QTTGLSRGVA FIRFDKRSEA EEAITSFNGH KPPGSSEPIT
VKFAANPNQN KNMALLSQLY HSPARRFGGP VHHQAQRFRF SPMGVDHMSG ISGVNVPGNA
SSGWCIFIYN LGQDADEGIL WQMFGPFGAV TNVKVIRDFN TNKCKGFGFV TMTNYEEAAM
AIASLNGYRL GDKILQVSFK TNKSHK
