SMG1_CAEEL
ID SMG1_CAEEL Reviewed; 2322 AA.
AC O01510; Q6BEW0; Q9U9U7;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Serine/threonine-protein kinase smg-1;
DE EC=2.7.11.1;
DE AltName: Full=Suppressor with morphogenetic effect on genitalia protein 1;
GN Name=smg-1; ORFNames=C48B6.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ASP-1966.
RC STRAIN=Bristol N2;
RX PubMed=15314158; DOI=10.1128/mcb.24.17.7483-7490.2004;
RA Grimson A., O'Connor S., Newman C.L., Anderson P.;
RT "SMG-1 is a phosphatidylinositol kinase-related protein kinase required for
RT nonsense-mediated mRNA Decay in Caenorhabditis elegans.";
RL Mol. Cell. Biol. 24:7483-7490(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION.
RX PubMed=2583479; DOI=10.1093/genetics/123.2.301;
RA Hodgkin J., Papp A., Pulak R., Ambros V., Anderson P.;
RT "A new kind of informational suppression in the nematode Caenorhabditis
RT elegans.";
RL Genetics 123:301-313(1989).
CC -!- FUNCTION: Serine/threonine protein kinase involved in mRNA
CC surveillance. Recognizes the substrate consensus sequence [ST]-Q.
CC Involved in nonsense-mediated decay (NMD) of mRNAs containing premature
CC stop codons by phosphorylating smg-2. {ECO:0000269|PubMed:15314158,
CC ECO:0000269|PubMed:2583479}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Component of a post-splicing multiprotein NMD complex.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15314158}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=O01510-1; Sequence=Displayed;
CC Name=b;
CC IsoId=O01510-2; Sequence=VSP_017753;
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
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DR EMBL; AF149821; AAD48773.1; -; mRNA.
DR EMBL; FO080896; CCD67583.1; -; Genomic_DNA.
DR EMBL; FO080896; CCD67584.1; -; Genomic_DNA.
DR PIR; T28924; T28924.
DR RefSeq; NP_001021053.1; NM_001025882.2. [O01510-1]
DR RefSeq; NP_001021054.1; NM_001025883.3.
DR AlphaFoldDB; O01510; -.
DR SMR; O01510; -.
DR BioGRID; 37863; 5.
DR STRING; 6239.C48B6.6a; -.
DR EPD; O01510; -.
DR PaxDb; O01510; -.
DR PeptideAtlas; O01510; -.
DR PRIDE; O01510; -.
DR EnsemblMetazoa; C48B6.6a.1; C48B6.6a.1; WBGene00004879. [O01510-1]
DR EnsemblMetazoa; C48B6.6b.1; C48B6.6b.1; WBGene00004879.
DR GeneID; 172418; -.
DR KEGG; cel:CELE_C48B6.6; -.
DR UCSC; C48B6.6a; c. elegans. [O01510-1]
DR CTD; 172418; -.
DR WormBase; C48B6.6a; CE30258; WBGene00004879; smg-1. [O01510-1]
DR WormBase; C48B6.6b; CE36919; WBGene00004879; smg-1. [O01510-2]
DR eggNOG; KOG0891; Eukaryota.
DR GeneTree; ENSGT00940000154776; -.
DR HOGENOM; CLU_001279_1_0_1; -.
DR InParanoid; O01510; -.
DR OMA; PMQTFAA; -.
DR OrthoDB; 26975at2759; -.
DR PhylomeDB; O01510; -.
DR PRO; PR:O01510; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004879; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031931; C:TORC1 complex; IBA:GO_Central.
DR GO; GO:0031932; C:TORC2 complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:WormBase.
DR GO; GO:0040035; P:hermaphrodite genitalia development; IMP:WormBase.
DR GO; GO:0030539; P:male genitalia development; IMP:WormBase.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IBA:GO_Central.
DR GO; GO:0071030; P:nuclear mRNA surveillance of spliceosomal pre-mRNA splicing; IMP:CAFA.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IMP:WormBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
DR CDD; cd05170; PIKKc_SMG1; 1.
DR Gene3D; 1.10.1070.11; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR031559; SMG1.
DR InterPro; IPR039414; SMG1_PIKKc.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF15785; SMG1; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Manganese;
KW Metal-binding; Nonsense-mediated mRNA decay; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..2322
FT /note="Serine/threonine-protein kinase smg-1"
FT /id="PRO_0000229794"
FT DOMAIN 1053..1535
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT REPEAT 1485..1521
FT /note="HEAT"
FT DOMAIN 1754..2099
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2290..2322
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 1760..1766
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1963..1971
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1983..2007
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT VAR_SEQ 1857..2159
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_017753"
FT MUTAGEN 1966
FT /note="D->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:15314158"
SQ SEQUENCE 2322 AA; 265479 MW; B97E86C770C3356D CRC64;
MITSRNNDIG NLIEQFRQRD TPQKERKAIL ARIEEILQTT KNVESLCVKW TYLLDNLCWP
SLTKHDRNDM KTLAGKVIRL VGVLLFDTES YPEFLIYLGT LYQSVTKKSE ETRADIVFSV
YFIVGVISQK TENRLIATDT ENVEKSLDWI IKVLPNSSIS VYNHCLKGFV LVANTFPNVY
AAMFESTLRA ILTNLPDFNS HEKNFELLID TVMRFSDQLN EKPHLAEEMV RIIRPDIKKN
GLGNMRELKK RMKLTMALVK MAKSQKMLEE TNQMISEMSI ELEENGGKWS SASLITIVCD
VFNELLILGK DDVKLQKGVE ESLCNVLKDL NLSNQSTMEK QAFFNSLAKI VKQLPAESQV
KTRVHQIVFN TETGLFTPKN RDNRMFGHNM IYKDLINLVS VLLTPTSLNH LQATYTDLRK
IMIDSMSRLK QSEDTPYSDN IRWNESILLL FFSSLQSISC AKSSLIVMMG IRPSIFEFFS
SELPLTEYWL ASNHPEVYHL FITIFVGHLK AHDFYIVQSD YIVRGDSIGQ SIGQTKRDYA
RKQVVALQKI INNFGDKLWK KTRLMISSWL HSLIATACEH QIGSDSFSQR EWVRLRNTVI
HQSVLTWNNE CVNQALTILS TATKWSELTS DIHRDIADKT KKAKWKEATT IWESGDCNTY
IRQSMSTVYQ MSQERQQKTI TSTSFGAEEF IIITNFLLKQ ATPTTFKKGQ NSWMDEVLET
FTQGCRTLEK PDSYVPETFI EKWDWIINQT ANFCIVNKMK TPLGKPMQTF AAFENEIKRL
AKEVIVRKNS DKKLNKSSTE DPNQSPPLKY SVQWLRVHLL LKLIVVLEKL MNSAIHGGSS
VFNLTEIPVS SRQFFTVNAA SCEVWLNRVY YPALLVAYFN GYYGLVIRFG SNALSHFARQ
KDGDNDKKIV NGVCTASLMS LSMAVLGEPM EIVGLRRKVR EEFGTDMGQS LMEALGEMAN
ARYETALVAL EAVLVTDAAT NETLKMIIQL AMVDILNRIR LPQATDYYKV VLFGEESNDS
TITEDFRSVE LLTKFEKLNN TVNEKRQVVD WSARERFQFV ESAFSQTMRR TELLDIQKDF
SAMGALALSA DSSCKLYSDI SSTSLIIANL VNKMTGVSQW KNKLTDTEIF DRNEEGNDGD
KLAICRKLMH WGRHTKSNRG QSCAAHSEII RLSRKTSNCE LAFFHINSAI RGEKLAAWQR
LEVERQRLKL VKTQNLDVRI REMNEVFGSL AEVFTTSCQL KSDFQMVDGM IKEKMISEGY
NEDIAKREEH MSRASIQLAD FFQSLPELEN VLAPNLFPTI IWSELQRRSD SLSAGYHGIV
GSLFHLASEM CPSLAKAHLK MARWAYEIAK IKNFPAENLS FYKFGKDETE NEELLKSLEA
TSLVNLEKLV RAAISDDLRA NNILAPNSHF MHIWKMVRDH RTKFLSIAVT SYFQFIQNMS
GDCDNLPYSK KEETTLATLR ILELLVKHGD VLIDVINDGL NKTNVHIWKE ILPQLFARLS
HPSEHIRKTL VDLISKICTA APHAVVFQVV SGAASSSTDG EELEEQQNDD RNRVRACCEK
LETNMSQSYP NLVKDVRQFV AELERINLLN EEKWSVVMGT MEHEMEKRLS LIRTENAKTE
SALHLTASVK NDIIVKRTQL LTRQIFDVLD ELYQQTVIEP PKSKNEEEFV TAFAEVLTNA
FQESRISRTT SPEKSWIPFK NLIANFVHRN SKKGMQTFET EDISPYLASL SNSCVPMPGQ
ESVEFDRVVS ISRVARQVTI LPTKTRPKKL GFVGSDGKQV AFLFKGREDL HLDERVMQFL
RLCNVMLQPG KGKHRQSVAA YQAHHYAVIP LGPRSGLIKW VEGATPMFHI YRKWQMKEKA
LKQATKKNGE TVPEIERPSN MYHNMIRLAF ADHKIDSSIT SDRSKWPAEI LEEVFESLTA
KTPTDLISRE LWMRANDATT WWSVTKRYSR SLAVMSMVGS VLGLGDRHLD NLLVDLKWGH
VVHIDYNICF DKGKNLRIPE TVPFRLTRNM RHALGPSEMY GTFRESCVHV LSTLRSGHQV
LTMLLDAFVF DPLVDWTSHE HTATSGVSLA LQLAVYGSNW KTKAKERLTD AMELLNLRMS
EVQTLWLANR DDLLHWMKQV TECLLIENSM LGANAIYAQQ RVKAGTELRE AVTRHHALAK
ELRPLIRVIG KEREEFADYL KFYKQALFDP LLKGHSALRN ELDIDTCVYN FNIVMQNIDN
VFGALVNLSF TPIETITSRT SQQEFKPPPG LENVWVVKQD QQENSQAREV VRRVERRLNG
WLDGSAGPDR KLSPREEADI LIAEATSTPN LSQMYEGWTA WV
