U5S1_PONAB
ID U5S1_PONAB Reviewed; 972 AA.
AC Q5R6E0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=116 kDa U5 small nuclear ribonucleoprotein component;
DE AltName: Full=Elongation factor Tu GTP-binding domain protein 2;
DE AltName: Full=U5 snRNP-specific protein, 116 kDa;
DE Short=U5-116 kDa;
GN Name=EFTUD2; Synonyms=SNRP116;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CR860551; CAH92676.1; -; mRNA.
DR RefSeq; NP_001126566.1; NM_001133094.1.
DR AlphaFoldDB; Q5R6E0; -.
DR SMR; Q5R6E0; -.
DR STRING; 9601.ENSPPYP00000009352; -.
DR GeneID; 100173557; -.
DR KEGG; pon:100173557; -.
DR CTD; 9343; -.
DR eggNOG; KOG0468; Eukaryota.
DR InParanoid; Q5R6E0; -.
DR OrthoDB; 140796at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
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 2: Evidence at transcript 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..972
FT /note="116 kDa U5 small nuclear ribonucleoprotein
FT component"
FT /id="PRO_0000315997"
FT DOMAIN 127..409
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..49
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 136..143
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 204..208
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 258..261
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 86
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15029"
FT CROSSLNK 64
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15029"
FT CROSSLNK 64
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15029"
SQ SEQUENCE 972 AA; 109391 MW; E9EEA208AC8F1238 CRC64;
MDTDLYDEFG NYIGPELDSD EDDDELGRET KDLDEMDDDD DDDDIGDHDD DHPGMEVVLH
EDKKYYPTAE EVYGPEVETI VQEEDTQPLT EPIIKPVKTK KFTLMEQTLP VTVYEMDFLA
DLMDNSELIR NVTLCGHLHH GKTCFVDCLI EQTHPEIRKR YDQDLCYTDI LFTEQERGVG
IKSTPVTVVL PDTKGKSYLF NIMDTPGHVN FSDEVTAGLR ISDGVVLFID AAEGVMLNTE
RLIKHAVQER LAVTVCINKI DRLILELKLP PTDAYYKLRH IVDEVNGLIS MYSTDENLIL
SPLLGNVCFS SSQYSICFTL GSFAKIYADT FGDINYQEFA KRLWGDIYFN PKTRKFTKKA
PTSSSQRSFV EFILEPLYKI LAQVVGDVDT SLPRTLDELG IHLTKEELKL NIRPLLRLVC
KKFFGEFTGF VDMCVQHIPS PKVGAKPKIE HTYTGGVDSD LGEAMSDCDP DGPLMCHTTK
MYSTDDGVQF HAFGRVLSGT IHAGQPVKVL GENYTLEDEE DSQICTVGRL WISVARYHIE
VNRVPAGNWV LIEGVDQPIV KTATITEPRG NEEAQIFRPL KFNTTSVIKI AVEPVNPSEL
PKMLDGLRKV NKSYPSLTTK VEESGEHVIL GTGELYLDCV MHDLPKMYSE IDIKVADPVV
TFCETVVETS SLKCFAETPN KKNKITMIAE PLEKGLAEDI ENEVVQITWN RKKLGEFFQT
KYDWDLLAAR SIWAFGPDAT GPNILVDDTL PSEVDKALLG SVKDSIVQGF QWGTREGPLC
DELIRNVKFK ILDAVVAQEP LHRGGGQIIP TARRVVYSAF LMATPRLMEP YYFVEVQAPA
DCVSAVYTVL ARRRGHVTQD APIPGSPLYT IKAFIPAIDS FGFETDLRTH TQGQAFSLSV
FHHWQIVPGD PLDKSIVIRP LEPQPAPHLA REFMIKTRRR KGLSEDVSIS KFFDDPMLLE
LAKQDVVLNY PM
