U5S1_MOUSE
ID U5S1_MOUSE Reviewed; 971 AA.
AC O08810;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=116 kDa U5 small nuclear ribonucleoprotein component;
DE AltName: Full=Elongation factor Tu GTP-binding domain-containing protein 2;
DE AltName: Full=U5 snRNP-specific protein, 116 kDa;
DE Short=U5-116 kDa;
GN Name=Eftud2; Synonyms=Snrp116;
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=9233818; DOI=10.1093/emboj/16.13.4092;
RA Fabrizio P., Laggerbauer B., Lauber J., Lane W.S., Luehrmann R.;
RT "An evolutionarily conserved U5 snRNP-specific protein is a GTP-binding
RT factor closely related to the ribosomal translocase EF-2.";
RL EMBO J. 16:4092-4106(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary gland;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
CC -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC spliceosome, including pre-catalytic, catalytic and post-catalytic
CC spliceosomal complexes (By similarity). Component of the U5 snRNP and
CC the U4/U6-U5 tri-snRNP complex, a building block of the spliceosome (By
CC similarity). {ECO:0000250|UniProtKB:Q15029}.
CC -!- SUBUNIT: Component of the U5 snRNP and the U4/U6-U5 tri-snRNP complex,
CC a building block of the spliceosome (By similarity). The U4/U6-U5 tri-
CC snRNP complex is composed of the U4, U6 and U5 snRNAs and at least
CC PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, DDX23,
CC CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39 (By similarity). Component
CC of the pre-catalytic, catalytic and post-catalytic spliceosome
CC complexes (By similarity). Interacts with ERBB4 and PRPF8 (By
CC similarity). Interacts with PIH1D1 (By similarity). Interacts with
CC RPAP3 and URI1 in a ZNHIT2-dependent manner (By similarity). Interacts
CC with NRDE2 (By similarity). Interacts with FAM50A (By similarity).
CC {ECO:0000250|UniProtKB:Q15029}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15029}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH12636.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Vector contamination at the N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U97079; AAC53299.1; -; mRNA.
DR EMBL; BC012636; AAH12636.1; ALT_INIT; mRNA.
DR EMBL; BC054778; AAH54778.1; -; mRNA.
DR CCDS; CCDS48947.1; -.
DR RefSeq; NP_001103465.1; NM_001109995.1.
DR RefSeq; NP_035561.1; NM_011431.3.
DR AlphaFoldDB; O08810; -.
DR SMR; O08810; -.
DR BioGRID; 203372; 65.
DR IntAct; O08810; 6.
DR MINT; O08810; -.
DR STRING; 10090.ENSMUSP00000021306; -.
DR iPTMnet; O08810; -.
DR PhosphoSitePlus; O08810; -.
DR SwissPalm; O08810; -.
DR EPD; O08810; -.
DR jPOST; O08810; -.
DR PaxDb; O08810; -.
DR PeptideAtlas; O08810; -.
DR PRIDE; O08810; -.
DR ProteomicsDB; 298344; -.
DR Antibodypedia; 17535; 248 antibodies from 30 providers.
DR DNASU; 20624; -.
DR Ensembl; ENSMUST00000107060; ENSMUSP00000102675; ENSMUSG00000020929.
DR GeneID; 20624; -.
DR KEGG; mmu:20624; -.
DR UCSC; uc033gal.1; mouse.
DR CTD; 9343; -.
DR MGI; MGI:1336880; Eftud2.
DR VEuPathDB; HostDB:ENSMUSG00000020929; -.
DR eggNOG; KOG0468; Eukaryota.
DR GeneTree; ENSGT00940000155685; -.
DR InParanoid; O08810; -.
DR OrthoDB; 140796at2759; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72165; mRNA Splicing - Minor Pathway.
DR BioGRID-ORCS; 20624; 28 hits in 74 CRISPR screens.
DR ChiTaRS; Eftud2; mouse.
DR PRO; PR:O08810; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O08810; protein.
DR Bgee; ENSMUSG00000020929; Expressed in maxillary prominence and 276 other tissues.
DR ExpressionAtlas; O08810; baseline and differential.
DR Genevisible; O08810; MM.
DR GO; GO:0015030; C:Cajal body; ISO:MGI.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; ISS:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0030623; F:U5 snRNA binding; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR CDD; cd04098; eEF2_C_snRNP; 1.
DR CDD; cd04167; Snu114p; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031950; EFTUD2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR044121; Snu114_GTP-bd.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR InterPro; IPR035655; U5-116kDa_C.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF16004; EFTUD2; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; GTP-binding; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Spliceosome; Ubl conjugation.
FT CHAIN 1..971
FT /note="116 kDa U5 small nuclear ribonucleoprotein
FT component"
FT /id="PRO_0000091564"
FT DOMAIN 126..408
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..48
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 135..142
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 203..207
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 257..260
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q15029"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15029"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15029"
FT CROSSLNK 63
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15029"
FT CROSSLNK 63
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15029"
SQ SEQUENCE 971 AA; 109361 MW; 0ECF1661DEA3A7FC CRC64;
MDTDLYDEFG NYIGPELDSD EDDDELGRET KDLDEDEDED EDDVGEHEDD HPGMEVVLHE
DKKYYPTAEE VYGPEVETIV QEEDTQPLTE PIIKPVKTKK FTLMEQTLPV TVYEMDFLAD
LMDNSELIRN VTLCGHLHHG KTCFVDCLIE QTHPEIRKRY DQDLCYTDIL FTEQERGVGI
KSTPVTVVLP DTKGKSYLFN IMDTPGHVNF SDEVTAGLRI SDGVVLFIDA AEGVMLNTER
LIKHAVQERL AVTVCINKID RLILELKLPP TDAYYKLRHI VDEVNGLISM YSTDENLILS
PLLGNVCFSS SQYSICFTLG SFAKIYADTF GDINYQEFAK RLWGDIYFNP KTRKFTKKAP
SSSSQRSFVE FILEPLYKIL AQVVGDVDTS LPRTLDELGI HLTKEELKLN IRPLLRLVCK
KFFGEFTGFV DMCVQHIPSP KVGAKPKIEH TYTGGVDSDL GEAMSDCDPD GPLMCHTTKM
YSTDDGVQFH AFGRVLSGTI HAGQPVKVLG ENYTLEDEED SQICTVGRLW ISVARYHIEV
NRVPAGNWVL IEGVDQPIVK TATITEPRGN EEAQIFRPLK FNTTSVIKIA VEPVNPSELP
KMLDGLRKVN KSYPSLTTKV EESGEHVILG TGELYLDCVM HDLRKMYSEI DIKVADPVVT
FCETVVETSS LKCFAETPNK KNKITMIAEP LEKGLAEDIE NEVVQITWNR KKLGEFFQTK
YDWDLLAARS IWAFGPDATG PNILVDDTLP SEVDKALLGS VKDSIVQGFQ WGTREGPLCD
ELIRNVKFKI LDAVVAQEPL HRGGGQIIPT ARRVVYSAFL MATPRLMEPY YFVEVQAPAD
CVSAVYTVLA RRRGHVTQDA PIPGSPLYTI KAFIPAIDSF GFETDLRTHT QGQAFSLSVF
HHWQIVPGDP LDKSIVIRPL EPQPAPHLAR EFMIKTRRRK GLSEDVSISK FFDDPMLLEL
AKQDVVLNYP M
