ELP4_MOUSE
ID ELP4_MOUSE Reviewed; 422 AA.
AC Q9ER73; Q8BGM1; Q8BVB1; Q8BZN8; Q9CTR2;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Elongator complex protein 4;
DE AltName: Full=PAX6 neighbor gene protein;
GN Name=Elp4; Synonyms=Paxneb;
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].
RX PubMed=11889558; DOI=10.1007/s00335-001-3058-y;
RA Kleinjan D.A., Seawright A., Elgar G., van Heyningen V.;
RT "Characterization of a novel gene adjacent to PAX6, revealing synteny
RT conservation with functional significance.";
RL Mamm. Genome 13:102-107(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, Embryo, and 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, 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).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=30097576; DOI=10.1038/s41467-018-05765-6;
RA Kojic M., Gaik M., Kiska B., Salerno-Kochan A., Hunt S., Tedoldi A.,
RA Mureev S., Jones A., Whittle B., Genovesi L.A., Adolphe C., Brown D.L.,
RA Stow J.L., Alexandrov K., Sah P., Glatt S., Wainwright B.J.;
RT "Elongator mutation in mice induces neurodegeneration and ataxia-like
RT behavior.";
RL Nat. Commun. 9:3195-3195(2018).
CC -!- FUNCTION: Component of the elongator complex which is required for
CC multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl
CC uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U
CC (5-carbamoylmethyl uridine). The elongator complex catalyzes the
CC formation of carboxymethyluridine in the wobble base at position 34 in
CC tRNAs. {ECO:0000250|UniProtKB:Q96EB1}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000250|UniProtKB:Q96EB1}.
CC -!- SUBUNIT: Component of the elongator complex which consists of ELP1,
CC ELP2, ELP3, ELP4, ELP5 and ELP6. {ECO:0000250|UniProtKB:Q96EB1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96EB1}. Nucleus
CC {ECO:0000250|UniProtKB:Q96EB1}.
CC -!- TISSUE SPECIFICITY: Expressed throughout the cerebellum.
CC {ECO:0000269|PubMed:30097576}.
CC -!- SIMILARITY: Belongs to the ELP4 family. {ECO:0000305}.
CC -!- CAUTION: The elongator complex was originally thought to play a role in
CC transcription elongation. However, it is no longer thought to play a
CC direct role in this process and its primary function is thought to be
CC in tRNA modification. {ECO:0000250|UniProtKB:Q96EB1}.
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DR EMBL; AJ276004; CAC08202.1; -; mRNA.
DR EMBL; AK020742; BAB32197.1; -; mRNA.
DR EMBL; AK034040; BAC28555.1; -; mRNA.
DR EMBL; AK034529; BAC28743.1; -; mRNA.
DR EMBL; AK037104; BAC29704.1; -; mRNA.
DR EMBL; AK039447; BAC30351.1; -; mRNA.
DR EMBL; AK039758; BAC30441.1; -; mRNA.
DR EMBL; AK079069; BAC37523.1; -; mRNA.
DR EMBL; AK168964; BAE40769.1; -; mRNA.
DR EMBL; AL512589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS16500.1; -.
DR RefSeq; NP_076365.2; NM_023876.4.
DR AlphaFoldDB; Q9ER73; -.
DR SMR; Q9ER73; -.
DR BioGRID; 218904; 4.
DR STRING; 10090.ENSMUSP00000116575; -.
DR iPTMnet; Q9ER73; -.
DR PhosphoSitePlus; Q9ER73; -.
DR EPD; Q9ER73; -.
DR MaxQB; Q9ER73; -.
DR PaxDb; Q9ER73; -.
DR PeptideAtlas; Q9ER73; -.
DR PRIDE; Q9ER73; -.
DR ProteomicsDB; 275602; -.
DR Antibodypedia; 25549; 155 antibodies from 26 providers.
DR DNASU; 77766; -.
DR Ensembl; ENSMUST00000122965; ENSMUSP00000116575; ENSMUSG00000027167.
DR GeneID; 77766; -.
DR KEGG; mmu:77766; -.
DR UCSC; uc008lld.1; mouse.
DR CTD; 26610; -.
DR MGI; MGI:1925016; Elp4.
DR VEuPathDB; HostDB:ENSMUSG00000027167; -.
DR eggNOG; KOG3949; Eukaryota.
DR GeneTree; ENSGT00390000001443; -.
DR HOGENOM; CLU_031345_3_1_1; -.
DR InParanoid; Q9ER73; -.
DR OMA; NTTMWDD; -.
DR OrthoDB; 973442at2759; -.
DR PhylomeDB; Q9ER73; -.
DR TreeFam; TF320797; -.
DR UniPathway; UPA00988; -.
DR BioGRID-ORCS; 77766; 23 hits in 74 CRISPR screens.
DR ChiTaRS; Elp4; mouse.
DR PRO; PR:Q9ER73; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9ER73; protein.
DR Bgee; ENSMUSG00000027167; Expressed in epithelium of lens and 234 other tissues.
DR ExpressionAtlas; Q9ER73; baseline and differential.
DR Genevisible; Q9ER73; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0033588; C:elongator holoenzyme complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0008023; C:transcription elongation factor complex; ISS:UniProtKB.
DR GO; GO:0008607; F:phosphorylase kinase regulator activity; ISS:UniProtKB.
DR GO; GO:0000993; F:RNA polymerase II complex binding; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR008728; Elongator_complex_protein_4.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12896; PTHR12896; 1.
DR Pfam; PF05625; PAXNEB; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; tRNA processing.
FT CHAIN 1..422
FT /note="Elongator complex protein 4"
FT /id="PRO_0000284005"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 404
FT /note="A -> T (in Ref. 2; BAC28555)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="G -> D (in Ref. 2; BAC37523)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="E -> K (in Ref. 1; CAC08202)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 46325 MW; 87DD0F4209C0032F CRC64;
MAAADTCGAG TLSSRSVASE AGQGGTSSFQ RKGKASGGPG GGPRLLSIAG TRPSVRNGQL
LVSTGLPALD QLLGGGLAVG TLLLIEEDKY NIYSPLLFKY FMAEGIINGH TLLVASAKEN
PAKILQELPA PLLDDNSKKE LEDVHSAKTP EPNVNMKIAW RYQLQPKMEV GPVSSSRFGH
YYDLSKRIPW ELLQSSKWHG FFLPEHISPD LKGESCFLSC GYMRLLEFIQ KSVYAEGFDG
ANPQKKQKNI LRIGIQNLGS PLWGDDICCK ENCDNNHRLT KFLYILRGLL RSSLSACIIT
MPAHLVQNKS ITTRVRNLSD TVVGLESFIG SERETNPLYK DYHGLIHIRK IPRLNNLTCD
ESDVKDLAFK LKRKLFTIER LHLPPDLSDT VGRSSKQDLA ASTARLGAGC SSMAEGKKHL
DF
