SMG7_ARATH
ID SMG7_ARATH Reviewed; 1059 AA.
AC A9QM73;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Nonsense-mediated mRNA decay factor SMG7 {ECO:0000250|UniProtKB:Q92540};
DE AltName: Full=Protein SMG7 {ECO:0000303|PubMed:18544632};
DE AltName: Full=SMG7 homolog {ECO:0000303|PubMed:18544632};
GN Name=SMG7 {ECO:0000303|PubMed:18544632};
GN OrderedLocusNames=At5g19400 {ECO:0000312|Araport:AT5G19400};
GN ORFNames=F7K24 {ECO:0000312|EMBL:AF296837};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=18544632; DOI=10.1242/jcs.027862;
RA Riehs N., Akimcheva S., Puizina J., Bulankova P., Idol R.A., Siroky J.,
RA Schleiffer A., Schweizer D., Shippen D.E., Riha K.;
RT "Arabidopsis SMG7 protein is required for exit from meiosis.";
RL J. Cell Sci. 121:2208-2216(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP FUNCTION.
RX PubMed=21119056; DOI=10.1105/tpc.110.078378;
RA Bulankova P., Riehs-Kearnan N., Nowack M.K., Schnittger A., Riha K.;
RT "Meiotic progression in Arabidopsis is governed by complex regulatory
RT interactions between SMG7, TDM1, and the meiosis I-specific cyclin TAM.";
RL Plant Cell 22:3791-3803(2010).
RN [5]
RP FUNCTION.
RX PubMed=22379136; DOI=10.1093/nar/gks195;
RA Riehs-Kearnan N., Gloggnitzer J., Dekrout B., Jonak C., Riha K.;
RT "Aberrant growth and lethality of Arabidopsis deficient in nonsense-
RT mediated RNA decay factors is caused by autoimmune-like response.";
RL Nucleic Acids Res. 40:5615-5624(2012).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22974464; DOI=10.1111/tpj.12015;
RA Merai Z., Benkovics A.H., Nyiko T., Debreczeny M., Hiripi L., Kerenyi Z.,
RA Kondorosi E., Silhavy D.;
RT "The late steps of plant nonsense-mediated mRNA decay.";
RL Plant J. 73:50-62(2013).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-933, INTERACTION WITH
RP EXA1, AND SUBCELLULAR LOCATION.
RX PubMed=29073135; DOI=10.1371/journal.pgen.1007037;
RA Matsui H., Nomura Y., Egusa M., Hamada T., Hyon G.-S., Kaminaka H.,
RA Watanabe Y., Ueda T., Trujillo M., Shirasu K., Nakagami H.;
RT "The GYF domain protein PSIG1 dampens the induction of cell death during
RT plant-pathogen interactions.";
RL PLoS Genet. 13:E1007037-E1007037(2017).
CC -!- FUNCTION: Plays multiple roles in growth and development. Involved in
CC nonsense-mediated mRNA decay (NMD). May provide a link to the mRNA
CC degradation machinery to initiate NMD and serve as an adapter for UPF
CC proteins function. Required for meiotic progression through anaphase II
CC of pollen mother cells. May counteract cyclin-dependent kinase (CDK)
CC activity at the end of meiosis. May play a role in plant defense
CC through its involvement in NMD. Together with EXA1, helps to restrict
CC cell death induction during pathogen infection in a salicylic
CC acid- (SA) and reactive oxygen species- (ROS) independent manner
CC (PubMed:29073135). {ECO:0000269|PubMed:18544632,
CC ECO:0000269|PubMed:21119056, ECO:0000269|PubMed:22379136,
CC ECO:0000269|PubMed:22974464, ECO:0000269|PubMed:29073135}.
CC -!- SUBUNIT: Interacts with EXA1. {ECO:0000269|PubMed:29073135}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:22974464,
CC ECO:0000269|PubMed:29073135}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers and at lower levels in stems
CC and leaves. {ECO:0000269|PubMed:18544632}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous
CC (PubMed:18544632). No spontaneous lesions, but enhanced cell death
CC independent of salicylic acid (SA) biosynthesis or reactive oxygen
CC species (ROS) production during pathogen infection (PubMed:29073135).
CC {ECO:0000269|PubMed:18544632, ECO:0000269|PubMed:29073135}.
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DR EMBL; EU126544; ABW96769.1; -; mRNA.
DR EMBL; AF296837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92699.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92700.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92701.1; -; Genomic_DNA.
DR RefSeq; NP_001190336.1; NM_001203407.2.
DR RefSeq; NP_001190337.1; NM_001203408.1.
DR RefSeq; NP_197441.3; NM_121945.3.
DR AlphaFoldDB; A9QM73; -.
DR SMR; A9QM73; -.
DR BioGRID; 17336; 2.
DR IntAct; A9QM73; 1.
DR STRING; 3702.AT5G19400.1; -.
DR iPTMnet; A9QM73; -.
DR PaxDb; A9QM73; -.
DR PRIDE; A9QM73; -.
DR ProteomicsDB; 232598; -.
DR EnsemblPlants; AT5G19400.1; AT5G19400.1; AT5G19400.
DR EnsemblPlants; AT5G19400.2; AT5G19400.2; AT5G19400.
DR EnsemblPlants; AT5G19400.3; AT5G19400.3; AT5G19400.
DR GeneID; 832060; -.
DR Gramene; AT5G19400.1; AT5G19400.1; AT5G19400.
DR Gramene; AT5G19400.2; AT5G19400.2; AT5G19400.
DR Gramene; AT5G19400.3; AT5G19400.3; AT5G19400.
DR KEGG; ath:AT5G19400; -.
DR Araport; AT5G19400; -.
DR TAIR; locus:2150280; AT5G19400.
DR eggNOG; KOG2162; Eukaryota.
DR HOGENOM; CLU_010769_0_0_1; -.
DR InParanoid; A9QM73; -.
DR OrthoDB; 1206578at2759; -.
DR PhylomeDB; A9QM73; -.
DR PRO; PR:A9QM73; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; A9QM73; baseline and differential.
DR Genevisible; A9QM73; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0005697; C:telomerase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0070034; F:telomerase RNA binding; IBA:GO_Central.
DR GO; GO:0042162; F:telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:TAIR.
DR GO; GO:0090306; P:meiotic spindle assembly; IMP:TAIR.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IMP:TAIR.
DR GO; GO:0012501; P:programmed cell death; IEA:UniProtKB-KW.
DR GO; GO:0031347; P:regulation of defense response; IMP:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR15696; PTHR15696; 1.
DR Pfam; PF10374; EST1; 1.
DR Pfam; PF10373; EST1_DNA_bind; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Growth regulation; Necrosis;
KW Nonsense-mediated mRNA decay; Plant defense; Reference proteome; Repeat;
KW TPR repeat.
FT CHAIN 1..1059
FT /note="Nonsense-mediated mRNA decay factor SMG7"
FT /id="PRO_0000422380"
FT REPEAT 149..183
FT /note="TPR 1"
FT REPEAT 184..217
FT /note="TPR 2"
FT REGION 806..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 933
FT /note="G->A: Abolished interaction with EXA1."
FT /evidence="ECO:0000269|PubMed:29073135"
SQ SEQUENCE 1059 AA; 117006 MW; 8CC930F46B15847B CRC64;
MMTLQMDKTT ASSSWERAKS IYDEIAELAN KRQKAGNPPD PNLLQLLREK YEAIILESHT
FSEQHNIEIP LWQLHYKRIE YFRLHINRVL ASSTSTAAQN VKGPSKAEQI AQLKLQFRTF
LSEATGFYHD MILKIRSKYG LPLGSFSEDQ QSQNLSDKDG KELAEVQKAL KSCHRCLIYL
GDLARYKGMY AEGDSRSRQY ASASSYYLQA ASLWPASGNP HHQLAIVASY SRDEFVTTYR
YFRSLAVEYP FPTARDNLIV AFDKNRQSYE KLFVPSKDSS KRLTGKGRGK GADISLKDAT
LVAGPEKDKV TIANEMLKAF SIRFVHLNGI LFTRTSLETF FDVLASTSSS LREVISLGSA
KELTLGIDTS DSALFIVRVV TMLIFSVHNS KKETEGQSYA EIVQRVEPAR NSLTASFELL
GLVIEKCVQL GDPSSSYFLP GVLVFVEWLA CCPDIALGSD PDDRQTAVRN SFWNQFVVFF
NQVLSLGPTF IDDVEDETCF SNMSLYDERE TENRLALWED YELRGFLPLL PAQTILNFSR
KHSFGTEGPK EKKARIKRIF AAGKALTSVI KVDQNHVYFD SKKKKFLVGV KPADDFLDSH
SSPPKACNAL QDNQVMIDHN SPIMQLDQQI YMGEEDDDDE VIVFKPLVTE KRKEASDQIY
VPSGGFRKSD QVTTMGDFKA LSGSDVAFHE NQILQARGNA SIQVPASVGA NLLGPLQPST
QSQAMHMQQV QTQVQVPASV GANLLGLLLT STQSQAMHMQ QVQTQAVNPQ PAQSLAASRL
QPIQSQVAQP LPSRVVHFQQ TQAQVSHVSP AHSQSTSFGG GSKWSPEEAA SLASSLSGFA
QLGNGHVMRN EMQGNHGVSY YPAHSLPVHQ SYNGNGMGGM PYSQSRTPEA VFPPKIDPVL
SSGVVADGLG VQSSLAKKNP ISRAFRHLGP PPGFNSVPAK LQKEPAPGSE LSGNNHLPVD
DYSWLDGYQA QSSRGVGLNS SLNYATSGKP EHLGSTGNGL NGPANFPFPG KQVPTSQVQA
DFPYFQNPQK DNFVDKNHQS TQLPEQYQGQ STWSSRHFV
