SELB_MOUSE
ID SELB_MOUSE Reviewed; 583 AA.
AC Q9JHW4; Q6GTZ5;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Selenocysteine-specific elongation factor;
DE AltName: Full=Elongation factor sec;
DE AltName: Full=Eukaryotic elongation factor, selenocysteine-tRNA-specific;
DE Short=mSelB;
GN Name=Eefsec; Synonyms=Selb;
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=11265756; DOI=10.1093/embo-reports/kvd033;
RA Tujebajeva R.M., Copeland P.R., Xu X., Carlson B.A., Harney J.W.,
RA Driscoll D.M., Hatfield D.L., Berry M.J.;
RT "Decoding apparatus for eukaryotic selenocysteine insertion.";
RL EMBO Rep. 1:158-163(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10970870; DOI=10.1093/emboj/19.17.4796;
RA Fagegaltier D., Hubert N., Yamada K., Mizutani T., Carbon P., Krol A.;
RT "Characterization of mSelB, a novel mammalian elongation factor for
RT selenoprotein translation.";
RL EMBO J. 19:4796-4805(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-532, AND IDENTIFICATION BY
RP 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 [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-543, 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: Translation factor necessary for the incorporation of
CC selenocysteine into proteins. It probably replaces EF-Tu for the
CC insertion of selenocysteine directed by the UGA codon. SelB binds GTP
CC and GDP.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. SelB subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; AF283518; AAF91471.1; -; mRNA.
DR EMBL; AF268871; AAG13374.1; -; mRNA.
DR EMBL; AK028424; BAC25942.1; -; mRNA.
DR EMBL; CH466523; EDK99245.1; -; Genomic_DNA.
DR EMBL; BC024915; AAH24915.1; -; mRNA.
DR CCDS; CCDS20335.1; -.
DR RefSeq; NP_075547.1; NM_023060.3.
DR AlphaFoldDB; Q9JHW4; -.
DR SMR; Q9JHW4; -.
DR BioGRID; 211162; 1.
DR IntAct; Q9JHW4; 1.
DR STRING; 10090.ENSMUSP00000131207; -.
DR iPTMnet; Q9JHW4; -.
DR PhosphoSitePlus; Q9JHW4; -.
DR EPD; Q9JHW4; -.
DR jPOST; Q9JHW4; -.
DR MaxQB; Q9JHW4; -.
DR PaxDb; Q9JHW4; -.
DR PeptideAtlas; Q9JHW4; -.
DR PRIDE; Q9JHW4; -.
DR ProteomicsDB; 256768; -.
DR Antibodypedia; 46656; 113 antibodies from 20 providers.
DR DNASU; 65967; -.
DR Ensembl; ENSMUST00000165242; ENSMUSP00000131207; ENSMUSG00000033216.
DR GeneID; 65967; -.
DR KEGG; mmu:65967; -.
DR UCSC; uc009cvg.1; mouse.
DR CTD; 60678; -.
DR MGI; MGI:2137092; Eefsec.
DR VEuPathDB; HostDB:ENSMUSG00000033216; -.
DR eggNOG; KOG0461; Eukaryota.
DR GeneTree; ENSGT00940000158170; -.
DR HOGENOM; CLU_019148_1_0_1; -.
DR InParanoid; Q9JHW4; -.
DR OMA; LAFWGRI; -.
DR OrthoDB; 616182at2759; -.
DR PhylomeDB; Q9JHW4; -.
DR TreeFam; TF300432; -.
DR BioGRID-ORCS; 65967; 21 hits in 73 CRISPR screens.
DR ChiTaRS; Eefsec; mouse.
DR PRO; PR:Q9JHW4; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9JHW4; protein.
DR Bgee; ENSMUSG00000033216; Expressed in spermatocyte and 233 other tissues.
DR ExpressionAtlas; Q9JHW4; baseline and differential.
DR Genevisible; Q9JHW4; MM.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; IDA:MGI.
DR GO; GO:0003924; F:GTPase activity; IDA:MGI.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:MGI.
DR GO; GO:0035368; F:selenocysteine insertion sequence binding; IDA:MGI.
DR GO; GO:0003746; F:translation elongation factor activity; IDA:MGI.
DR GO; GO:0000049; F:tRNA binding; IDA:MGI.
DR GO; GO:0001514; P:selenocysteine incorporation; IDA:MGI.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Methylation; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Protein biosynthesis; Reference proteome.
FT CHAIN 1..583
FT /note="Selenocysteine-specific elongation factor"
FT /id="PRO_0000091479"
FT DOMAIN 5..203
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 46..50
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 78..81
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 132..135
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 171..173
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 371..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 534..540
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 538..555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 78..82
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 132..136
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P57772"
FT MOD_RES 532
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 543
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CONFLICT 162
FT /note="F -> S (in Ref. 1; AAF91471)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="Y -> T (in Ref. 1; AAF91471)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 583 AA; 63539 MW; 2960437B1D82DAE1 CRC64;
MAGRRVNVNV GVLGHIDSGK TALARALSTT ASTAAFDKQP QSRERGITLD LGFSCFVVPL
PGAEPGSSDT LLQVTLVDCP GHASLIRTII GGAQIIDLMM LVIDVTKGMQ TQSAECLVIG
QIACQKLVVV LNKIDLLAEG KRQAAIDKMT KKMQKTLENT KFRGAPIIPV AAKPGGPEAP
ETEAPQGISE LIELLKSQIS IPTRDPSGPF LMSVDHCFSI KGQGTVMTGT ILSGTISLGD
SVEIPALKVV KKVKSMQMFH TPVTSAMQGD RLGICVTQFD PKLLERGLVC APESLHTVHA
ALISVEKIPY FRGPLQTKAK FHITVGHETV MGRTLFFSPA PDSFDLEPVL DSFDLSREYL
FQEQYLCKDS MPTATEGDDE ADPKAGHAPG GHCPRQQWAL VEFEKPVTCP RLCLVIGSRL
DADIHTNTCR LAFHGVLLQG LEDKNYIESF LPALRVYKLK HKHGLVERVM DDYSVIGRSL
FKKETNIQLF VGLKVQLSTG EQGIIDSAFG QSGKFKIHIP GGLSPESKKI LTPTLKKRSR
AGRGETTKPE EGTERPEPIQ PVTLNLSFKR YVFDTQKRMV QTP
