SMG9_RAT
ID SMG9_RAT Reviewed; 520 AA.
AC Q5PQS6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Nonsense-mediated mRNA decay factor SMG9 {ECO:0000312|RGD:1309888};
GN Name=Smg9 {ECO:0000312|RGD:1309888};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-7 AND SER-32, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 SMG8 (forming the SMG1C protein kinase
CC complex) and, in the SMG1C complex, is required for the efficient
CC association between SMG1 and SMG8 (By similarity). Plays a role in
CC brain, heart, and eye development. {ECO:0000250|UniProtKB:Q9DB90,
CC ECO:0000250|UniProtKB:Q9H0W8}.
CC -!- SUBUNIT: Self-associates to form homodimers and forms heterodimers with
CC SMG8; these assembly forms may represent SMG1C intermediate forms (By
CC similarity). Component of the SMG1C complex composed of SMG1, SMG8 and
CC SMG9 (By similarity). Interacts with DHX34; the interaction is RNA-
CC independent (By similarity). {ECO:0000250|UniProtKB:Q9H0W8}.
CC -!- PTM: Phosphorylated by SMG1. {ECO:0000250|UniProtKB:Q9H0W8}.
CC -!- SIMILARITY: Belongs to the SMG9 family. {ECO:0000305}.
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DR EMBL; BC087051; AAH87051.1; -; mRNA.
DR RefSeq; NP_001014265.1; NM_001014243.1.
DR RefSeq; XP_006228512.1; XM_006228450.3.
DR AlphaFoldDB; Q5PQS6; -.
DR SMR; Q5PQS6; -.
DR STRING; 10116.ENSRNOP00000026669; -.
DR iPTMnet; Q5PQS6; -.
DR PhosphoSitePlus; Q5PQS6; -.
DR PaxDb; Q5PQS6; -.
DR PRIDE; Q5PQS6; -.
DR GeneID; 365215; -.
DR KEGG; rno:365215; -.
DR UCSC; RGD:1309888; rat.
DR CTD; 56006; -.
DR RGD; 1309888; Smg9.
DR VEuPathDB; HostDB:ENSRNOG00000019596; -.
DR eggNOG; KOG4181; Eukaryota.
DR HOGENOM; CLU_037795_0_0_1; -.
DR InParanoid; Q5PQS6; -.
DR OMA; FRTQSQE; -.
DR OrthoDB; 1436399at2759; -.
DR PhylomeDB; Q5PQS6; -.
DR Reactome; R-RNO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:Q5PQS6; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000019596; Expressed in testis and 20 other tissues.
DR Genevisible; Q5PQS6; RN.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0001654; P:eye development; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR019354; SMG8/SMG9.
DR InterPro; IPR039177; SMG9.
DR PANTHER; PTHR14270; PTHR14270; 1.
DR Pfam; PF10220; Smg8_Smg9; 1.
PE 1: Evidence at protein level;
KW Acetylation; Nonsense-mediated mRNA decay; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H0W8"
FT CHAIN 2..520
FT /note="Nonsense-mediated mRNA decay factor SMG9"
FT /id="PRO_0000289165"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..94
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0W8"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0W8"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0W8"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0W8"
SQ SEQUENCE 520 AA; 57633 MW; 7ED417FAF2B0257C CRC64;
MSESGHSQPG LYGIERRRRW KEPGSSGPQN LSGPGGRERD YIAPWERERR DGSEDPSTNV
MQKTPIILSK PPAERSKQPP PSTAPAAPPA PAPLEKPIVL MKPREEGKGP VAATGASTPE
GTAPPPPTAP APPKGEKEGQ RPTQPVYQIQ NRGMGTAAPT AMDPVVGQAK LLPPERMKHS
IKLVDDQMNW CDSAIEYLLD QTDVLVVGVL GLQGTGKSMV MSLLSANTPE EDQRAYVFRA
QSAEMKERGG NQTSGIDFFI TQERIVFLDT QPILSPSILD HLINNDRKLP PEYNLPHTYV
EMQSLQIAAF LFTVCHVVIV VQDWFTDLSL YRFLQTAEMV KPSTPSPSHE SSSAAGSDEG
TEYYPHLVFL QNKARREDFC PRKLRQMHLM IDQLMAHSHL RYKGTLSMLQ CNIFPGLPPD
FLDAEVNLFL VPFMDSEAEN ENPPRAGPGS SPLFSLLPGY RGHPSFQSLV SKLRSQVMSM
ARPQLSHTIL TEKNWFHYAA RIWDGVKKSS ALAEYSRLLA
