SMG8_BOVIN
ID SMG8_BOVIN Reviewed; 999 AA.
AC A1A4J7;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Nonsense-mediated mRNA decay factor SMG8 {ECO:0000250|UniProtKB:Q8ND04};
DE AltName: Full=Protein smg-8 homolog;
GN Name=SMG8;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in nonsense-mediated decay (NMD) of mRNAs containing
CC premature stop codons. Is recruited by release factors to stalled
CC ribosomes together with SMG1 and SMG9 (forming the SMG1C protein kinase
CC complex) and, in the SMG1C complex, is required to mediate the
CC recruitment of SMG1 to the ribosome:SURF complex and to suppress SMG1
CC kinase activity until the ribosome:SURF complex locates the exon
CC junction complex (EJC). Acts as a regulator of kinase activity (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the SMG1C complex composed of SMG1, SMG8 and
CC SMG9; the recruitment of SMG8 to SMG1 N-terminus induces a large
CC conformational change in the SMG1 C-terminal head domain containing the
CC catalytic domain. Forms heterodimers with SMG9; this assembly form may
CC represent a SMG1C intermediate form (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A1A4J7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A1A4J7-2; Sequence=VSP_037517;
CC -!- PTM: Phosphorylated by SMG1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMG8 family. {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; AAFC03009910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC126609; AAI26610.1; -; mRNA.
DR RefSeq; NP_001073755.1; NM_001080286.1. [A1A4J7-2]
DR AlphaFoldDB; A1A4J7; -.
DR SMR; A1A4J7; -.
DR STRING; 9913.ENSBTAP00000004365; -.
DR PaxDb; A1A4J7; -.
DR Ensembl; ENSBTAT00000052191; ENSBTAP00000051930; ENSBTAG00000003365. [A1A4J7-2]
DR GeneID; 522040; -.
DR KEGG; bta:522040; -.
DR CTD; 55181; -.
DR VEuPathDB; HostDB:ENSBTAG00000003365; -.
DR eggNOG; KOG3692; Eukaryota.
DR GeneTree; ENSGT00390000018533; -.
DR InParanoid; A1A4J7; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000003365; Expressed in spermatocyte and 106 other tissues.
DR ExpressionAtlas; A1A4J7; baseline.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISS:UniProtKB.
DR GO; GO:0045859; P:regulation of protein kinase activity; ISS:UniProtKB.
DR InterPro; IPR028802; SMG8.
DR InterPro; IPR019354; SMG8/SMG9.
DR PANTHER; PTHR13091; PTHR13091; 1.
DR Pfam; PF10220; Smg8_Smg9; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Methylation; Nonsense-mediated mRNA decay;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..999
FT /note="Nonsense-mediated mRNA decay factor SMG8"
FT /id="PRO_0000378167"
FT REGION 15..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND04"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND04"
FT MOD_RES 750
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND04"
FT MOD_RES 903
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND04"
FT MOD_RES 906
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8ND04"
FT VAR_SEQ 937..999
FT /note="PGPPPCPVFYPEKQEITLPPDGLWVLRFPYAYVTERGPCFPPKENVQLMSYK
FT VLRGVLKAVTQ -> NITFCVVRQSCLLFVSIV (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_037517"
SQ SEQUENCE 999 AA; 110135 MW; 7256DC925AE286E0 CRC64;
MAGPVSLREL LMGASAWTSS ESPEGSPTEG GGSAAGGPEP PWREDEICVV GIFGKTALRL
NSEKFSLVNT VCDRQVFPLF RHQDPGDSGA GIRTEAGAVG EAGGAGDPGA GAGAGAGAGA
GDPVRGGVTA AEGNRTEPGS QDYSLLQAYY NQESKVLYLL LTSICDNSQL LRACRALQSG
EAGGGLSLPH AEAHEFWKHQ EKVQCLSLLY LFSVCHILLL VHPTCSFDIT YDRVFRALDG
LRQKVLPLLK TAIKDCPVGK DWKLNCRPCP PRLLFLFQLN GALKVEPPRN QDPAHPDKPK
KHSPKRRLQH ALEDQIYRIF RKSRVLTNQS INCLFTVPAN QAFVYIVPGS QEEDPVGMLL
DQLKSHCTVK DPESLLVPAP LSGSRRYQVM RQHSRQQLSF HTDTSSSSSS GQLVDFTLRE
FLWQHVELVL SKKGFDDSVG RNPQPSHFEL PTYQKWISAA SKLYEVAIDG KEEDPASPTG
ELTSKILSSI KVLEGFLDID TKFSENRCQK ALPMAHSAYQ SNLPHNYTMT VHKNQLAQAL
RVYSQHARGP AFHKYAMQLH EDCYKFWSNG HQLCEERSLT DQHCVHKFHS LPKSGEKPEA
DRNPPVLYHN SRARSTGACN CGRKQAPRDD PFDIKAANYD FYQLLEEKCC GKLDHINFPV
FEPSTPDPAP AKNESSPAPP DADADKLKEK EPQTQGESTS LSLALSLGQS TDSLGTYPAD
PQAGGDNPEV HGQGEVKTEK RPNLVDRQAS TVEYLPGMLH SNCPKGLLPK FSSWSLVKLG
PAKSYNFHTG LDQQGFIPGT NYLMPWDIVI RTRAEDEGDL DTNSWPAPNK AVPGKRSAVV
MGRGRRRDDI ARAFVGFEYE DSRGRRFMCS GPDKVMKVMG SGPKESALKA LNSDMPLYIL
SSSQGRGLKP HYAQLMRLFV VVPDAPLQII LTPQVRPGPP PCPVFYPEKQ EITLPPDGLW
VLRFPYAYVT ERGPCFPPKE NVQLMSYKVL RGVLKAVTQ