SMG5_MOUSE
ID SMG5_MOUSE Reviewed; 1017 AA.
AC Q6ZPY2; Q497S2; Q8R3S4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Nonsense-mediated mRNA decay factor SMG5 {ECO:0000312|MGI:MGI:2447364};
DE AltName: Full=EST1-like protein B {ECO:0000250|UniProtKB:Q9UPR3};
DE AltName: Full=LPTS-RP1 {ECO:0000250|UniProtKB:Q9UPR3};
DE AltName: Full=LPTS-interacting protein {ECO:0000250|UniProtKB:Q9UPR3};
DE AltName: Full=SMG-5 homolog {ECO:0000250|UniProtKB:Q9UPR3};
GN Name=Smg5 {ECO:0000312|MGI:MGI:2447364};
GN Synonyms=Est1b {ECO:0000250|UniProtKB:Q9UPR3},
GN Kiaa1089 {ECO:0000312|MGI:MGI:2447364};
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ARG-77;
RP LEU-166; GLU-499 AND GLY-503.
RC STRAIN=B5/EGFP, Czech II, and ICR;
RC TISSUE=Mammary tumor, and Trophoblast stem cell;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, 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).
CC -!- FUNCTION: Plays a role in nonsense-mediated mRNA decay. Does not have
CC RNase activity by itself. Promotes dephosphorylation of UPF1. Together
CC with SMG7 is thought to provide a link to the mRNA degradation
CC machinery involving exonucleolytic pathways, and to serve as an adapter
CC for UPF1 to protein phosphatase 2A (PP2A), thereby triggering UPF1
CC dephosphorylation. Necessary for TERT activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TERT, PPP2CA and SMG1. Part of a complex that
CC contains SMG1, SMG5, SMG7, PPP2CA, a short isoform of UPF3A (isoform
CC UPF3AS, but not isoform UPF3AL) and phosphorylated UPF1. Not detected
CC in complexes that contain unphosphorylated UPF1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UPR3}. Nucleus
CC {ECO:0000250|UniProtKB:Q9UPR3}. Note=Detected in cytoplasmic mRNA decay
CC bodies. {ECO:0000250|UniProtKB:Q9UPR3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZPY2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZPY2-2; Sequence=VSP_016590, VSP_016591;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98096.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK129286; BAC98096.1; ALT_INIT; mRNA.
DR EMBL; BC024683; AAH24683.3; -; mRNA.
DR EMBL; BC100408; AAI00409.1; -; mRNA.
DR CCDS; CCDS38480.1; -. [Q6ZPY2-1]
DR RefSeq; NP_839977.2; NM_178246.3. [Q6ZPY2-1]
DR AlphaFoldDB; Q6ZPY2; -.
DR SMR; Q6ZPY2; -.
DR BioGRID; 230852; 8.
DR IntAct; Q6ZPY2; 1.
DR MINT; Q6ZPY2; -.
DR STRING; 10090.ENSMUSP00000001451; -.
DR iPTMnet; Q6ZPY2; -.
DR PhosphoSitePlus; Q6ZPY2; -.
DR EPD; Q6ZPY2; -.
DR MaxQB; Q6ZPY2; -.
DR PaxDb; Q6ZPY2; -.
DR PeptideAtlas; Q6ZPY2; -.
DR PRIDE; Q6ZPY2; -.
DR ProteomicsDB; 257522; -. [Q6ZPY2-1]
DR ProteomicsDB; 257523; -. [Q6ZPY2-2]
DR Antibodypedia; 34209; 111 antibodies from 23 providers.
DR Ensembl; ENSMUST00000001451; ENSMUSP00000001451; ENSMUSG00000001415. [Q6ZPY2-1]
DR GeneID; 229512; -.
DR KEGG; mmu:229512; -.
DR UCSC; uc008pus.1; mouse. [Q6ZPY2-2]
DR UCSC; uc008put.1; mouse. [Q6ZPY2-1]
DR CTD; 23381; -.
DR MGI; MGI:2447364; Smg5.
DR VEuPathDB; HostDB:ENSMUSG00000001415; -.
DR eggNOG; KOG2162; Eukaryota.
DR GeneTree; ENSGT00940000154566; -.
DR HOGENOM; CLU_011872_0_0_1; -.
DR InParanoid; Q6ZPY2; -.
DR OMA; FQIIECC; -.
DR PhylomeDB; Q6ZPY2; -.
DR TreeFam; TF327119; -.
DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 229512; 25 hits in 77 CRISPR screens.
DR ChiTaRS; Smg5; mouse.
DR PRO; PR:Q6ZPY2; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q6ZPY2; protein.
DR Bgee; ENSMUSG00000001415; Expressed in spermatocyte and 255 other tissues.
DR ExpressionAtlas; Q6ZPY2; baseline and differential.
DR Genevisible; Q6ZPY2; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:HGNC-UCL.
DR GO; GO:0005634; C:nucleus; ISS:HGNC-UCL.
DR GO; GO:0005697; C:telomerase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0051721; F:protein phosphatase 2A binding; ISS:HGNC-UCL.
DR GO; GO:0070034; F:telomerase RNA binding; ISO:MGI.
DR GO; GO:0042162; F:telomeric DNA binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IBA:GO_Central.
DR GO; GO:0035303; P:regulation of dephosphorylation; ISS:HGNC-UCL.
DR GO; GO:0032204; P:regulation of telomere maintenance; ISO:MGI.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR018834; DNA/RNA-bd_Est1-type.
DR InterPro; IPR045153; Est1/Ebs1-like.
DR InterPro; IPR019458; Est1_N.
DR InterPro; IPR002716; PIN_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR15696; PTHR15696; 1.
DR Pfam; PF10374; EST1; 1.
DR Pfam; PF10373; EST1_DNA_bind; 2.
DR SMART; SM00670; PINc; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UPR3"
FT CHAIN 2..1017
FT /note="Nonsense-mediated mRNA decay factor SMG5"
FT /id="PRO_0000076323"
FT DOMAIN 873..996
FT /note="PINc"
FT REGION 406..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 798..842
FT /evidence="ECO:0000255"
FT COMPBIAS 418..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..466
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPR3"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPR3"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 620..702
FT /note="ASEDGSESEGSESSNRSCRNERSLQEKLQALMAEGLLPAVKVFLDWLRTNPD
FT LIIVCAQSSQSLWNRLSVLLNLLPASAELQD -> GAWVHESPPSRRVTSPLGFCCHCG
FT ILVLCTYSFPASRTFAVLLLSTADCSSFTLFSPHIGGCTSFPHGIQLPEGSQKLGIMFL
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016590"
FT VAR_SEQ 703..1017
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016591"
FT VARIANT 77
FT /note="K -> R (in strain: B5/EGFP)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 166
FT /note="W -> L (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 499
FT /note="D -> E (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 503
FT /note="E -> G (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
SQ SEQUENCE 1017 AA; 114071 MW; 9925688D6FAFAF5C CRC64;
MSQGPPPGES SEPEAKVLHT KRLYRAVVEA VHRLDLILCN KAAYQEVFKP ENVSLRNKLR
ELCVKLMFLH PVDYGRKAEE LLWRKVYYEV IQLIKTNKKH IHSRSTLECA YRTHLVAGIG
FYQHLLLYIQ SHYQLELQCC IDWTHVTDPL MGFKKPVSAS GKEMDWAQMA CHRCLVYLGD
LSRYQNELAG VDTELLAERF YYQALSVAPQ IGMPFNQLGT LAGSKYYNVE AMYCYLRCIQ
SEVSFEGAYG NLKRLYDKAA KMYHQLKKSE TRKLSPSKKR CKDIKRLLVN FMYLQSLLQP
KSSSVDSELT SLCQSVLEDF NLCLFYLPSS PNLGLTNEDE EECESGYAFL PDLLIFQMAI
ICLMGVHSLK RAGSKHYSAA IAFTLALFSH LINHVNIRLQ AELEEGENPV SAFQSDGTDE
PESKEALEKE EPEPEPPTVV PQADEGRKSR KHSRLSCLRR RRRHHPPKAG DDSDLSEGFE
SDSSHDSAQA SDGSDSGSDK SLEGRGTAFD AETDSEMNSQ ESRSDLEDME DEEGTRSPAQ
EPPQARSEVP DSLNGPLGPS EASIASNLQA MSTQMFQTKR CFRLAPTFSN LLLQPTTEPN
SVASHRPCVN GDMDKPLEPA SEDGSESEGS ESSNRSCRNE RSLQEKLQAL MAEGLLPAVK
VFLDWLRTNP DLIIVCAQSS QSLWNRLSVL LNLLPASAEL QDSGLALCSE VQGLLEGCEL
PDLPASLLLP EDMALRNLPP LRAAHRRFNF DADRPLLSAL EESVVRICCI RSFGHFVARL
QGSILQFNPE VGIFVSIAQS EQESLLQQAQ AQFRMAEEEA RRNRLMRDMA QLRLQLEVSQ
LEGSLQQPKA QSAMSPYLIP DTQALCYHLP LIRQLATSGR FIIIIPRTVI DGLDLLKKEQ
PGARDGIRYL EAEFKKGNRY IRCQKEVGKS FERHKLKRQD ADAWTLYKIL DSCRQLTLAQ
GAGEEDPSGM VTIITGLHLD SPSALSGPMQ AALQAAAHAS VDVKNVLDFY RQWKEIG
