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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}.
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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
 
 
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