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SMG7_MOUSE
ID   SMG7_MOUSE              Reviewed;        1138 AA.
AC   Q5RJH6; Q63ZW5; Q6ZQF3;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Nonsense-mediated mRNA decay factor SMG7 {ECO:0000312|MGI:MGI:2682334};
DE   AltName: Full=SMG-7 homolog {ECO:0000250|UniProtKB:Q92540};
GN   Name=Smg7 {ECO:0000312|MGI:MGI:2682334};
GN   Synonyms=Est1c {ECO:0000250|UniProtKB:Q92540},
GN   Kiaa0250 {ECO:0000312|MGI:MGI:2682334};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Embryonic germ cell;
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).
CC   -!- FUNCTION: Plays a role in nonsense-mediated mRNA decay. Recruits UPF1
CC       to cytoplasmic mRNA decay bodies. Together with SMG5 is thought to
CC       provide a link to the mRNA degradation machinery involving
CC       exonucleolytic pathways, and to serve as an adapter for UPF1 to protein
CC       phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Part of a complex that contains SMG5, SMG7, PPP2CA, a short
CC       isoform of UPF3A (isoform UPF3AS, but not isoform UPF3AL) and
CC       phosphorylated UPF1 (By similarity). Interacts with DHX34; the
CC       interaction is RNA-independent (By similarity).
CC       {ECO:0000250|UniProtKB:Q92540}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92540}. Nucleus
CC       {ECO:0000250|UniProtKB:Q92540}. Note=Predominantly cytoplasmic, and
CC       nuclear. Shuttles between nucleus and cytoplasm.
CC       {ECO:0000250|UniProtKB:Q92540}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q5RJH6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5RJH6-2; Sequence=VSP_016577;
CC       Name=3;
CC         IsoId=Q5RJH6-3; Sequence=VSP_016578, VSP_016579;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC97911.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK129101; BAC97911.1; ALT_INIT; mRNA.
DR   EMBL; BC082789; AAH82789.1; -; mRNA.
DR   EMBL; BC086651; AAH86651.1; -; mRNA.
DR   CCDS; CCDS35740.1; -. [Q5RJH6-3]
DR   CCDS; CCDS48394.1; -. [Q5RJH6-2]
DR   CCDS; CCDS48395.1; -. [Q5RJH6-1]
DR   RefSeq; NP_001005507.1; NM_001005507.2. [Q5RJH6-3]
DR   RefSeq; NP_001153728.1; NM_001160256.1. [Q5RJH6-1]
DR   RefSeq; NP_001153729.1; NM_001160257.1. [Q5RJH6-2]
DR   RefSeq; XP_006529515.1; XM_006529452.3.
DR   AlphaFoldDB; Q5RJH6; -.
DR   SMR; Q5RJH6; -.
DR   BioGRID; 230520; 6.
DR   STRING; 10090.ENSMUSP00000041241; -.
DR   iPTMnet; Q5RJH6; -.
DR   PhosphoSitePlus; Q5RJH6; -.
DR   EPD; Q5RJH6; -.
DR   MaxQB; Q5RJH6; -.
DR   PaxDb; Q5RJH6; -.
DR   PeptideAtlas; Q5RJH6; -.
DR   PRIDE; Q5RJH6; -.
DR   ProteomicsDB; 261259; -. [Q5RJH6-1]
DR   ProteomicsDB; 261260; -. [Q5RJH6-2]
DR   ProteomicsDB; 261261; -. [Q5RJH6-3]
DR   Antibodypedia; 34445; 110 antibodies from 23 providers.
DR   DNASU; 226517; -.
DR   Ensembl; ENSMUST00000043560; ENSMUSP00000041241; ENSMUSG00000042772. [Q5RJH6-2]
DR   Ensembl; ENSMUST00000073441; ENSMUSP00000073144; ENSMUSG00000042772. [Q5RJH6-3]
DR   Ensembl; ENSMUST00000111836; ENSMUSP00000107467; ENSMUSG00000042772. [Q5RJH6-1]
DR   GeneID; 226517; -.
DR   KEGG; mmu:226517; -.
DR   UCSC; uc007czn.1; mouse. [Q5RJH6-2]
DR   UCSC; uc007czo.2; mouse. [Q5RJH6-3]
DR   UCSC; uc007czp.2; mouse. [Q5RJH6-1]
DR   CTD; 9887; -.
DR   MGI; MGI:2682334; Smg7.
DR   VEuPathDB; HostDB:ENSMUSG00000042772; -.
DR   eggNOG; KOG2162; Eukaryota.
DR   GeneTree; ENSGT00940000158333; -.
DR   HOGENOM; CLU_009299_0_0_1; -.
DR   InParanoid; Q5RJH6; -.
DR   OMA; TWAGHGP; -.
DR   OrthoDB; 556396at2759; -.
DR   PhylomeDB; Q5RJH6; -.
DR   TreeFam; TF327119; -.
DR   Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   BioGRID-ORCS; 226517; 20 hits in 76 CRISPR screens.
DR   ChiTaRS; Smg7; mouse.
DR   PRO; PR:Q5RJH6; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q5RJH6; protein.
DR   Bgee; ENSMUSG00000042772; Expressed in embryonic post-anal tail and 224 other tissues.
DR   Genevisible; Q5RJH6; MM.
DR   GO; GO:0005737; C:cytoplasm; ISS:HGNC-UCL.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:HGNC-UCL.
DR   GO; GO:0005697; C:telomerase holoenzyme complex; IBA:GO_Central.
DR   GO; GO:0051721; F:protein phosphatase 2A binding; ISS:HGNC-UCL.
DR   GO; GO:0070034; F:telomerase RNA binding; IBA:GO_Central.
DR   GO; GO:0042162; F:telomeric DNA binding; ISO:MGI.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Cytoplasm; Nonsense-mediated mRNA decay;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q92540"
FT   CHAIN           2..1138
FT                   /note="Nonsense-mediated mRNA decay factor SMG7"
FT                   /id="PRO_0000076325"
FT   REPEAT          152..185
FT                   /note="TPR 1"
FT   REPEAT          187..219
FT                   /note="TPR 2"
FT   REGION          515..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          649..745
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          838..871
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          990..1090
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1106..1138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..540
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..578
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        580..599
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        649..682
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        683..697
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        698..726
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        990..1031
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1061..1088
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92540"
FT   MOD_RES         519
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92540"
FT   MOD_RES         575
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92540"
FT   MOD_RES         732
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92540"
FT   MOD_RES         848
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92540"
FT   VAR_SEQ         1..9
FT                   /note="MSLQSAQYL -> MRTENLKSEEHLKSSNI (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14621295"
FT                   /id="VSP_016577"
FT   VAR_SEQ         566
FT                   /note="V -> VRRDCSKGVTVTQEDGQKDSSKRRAETKRCTLGKLQETGKQSVAVQV
FT                   (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_016578"
FT   VAR_SEQ         866..915
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_016579"
FT   CONFLICT        552
FT                   /note="P -> S (in Ref. 1; BAC97911)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1138 AA;  126841 MW;  330576E241E35AD4 CRC64;
     MSLQSAQYLR QAEVLKAEMT DSKLGPAEVW TSRQALQDLY QKMLVTDLEY ALDKKVEQDL
     WNHAFKNQIT TLQGQAKNRA NPNRSEVQAN LSLFLEAASG FYTQLLQELC TVFNVDLPCR
     VKSSQLGIIS NKQTHSSTIV KPQSSSCSYI CQHCLVHLGD IARYRNQTSQ AESYYRHAAQ
     LVPSNGQPYN QLAILASSKG DHLTTIFYYC RSIAVKFPFP AASTNLQKAL SKALESRDEL
     KTKWGVSDFI KAFIKFHGHV YLSKSLEKLS PLREKLEEQF KRLLFQKAFN SQQLVHVTVI
     NLFQLHHLRD FSNETEQHSY SQDEQLCWTQ LLALFMSFLG ILCKCPLQND SQESNNAYPL
     PAVKVSMDWL RLRPRVFQEA VVDERQYIWP WLISLLNSFH PREDDLSNTN ATPLPEEFEL
     QGFLALRPSF RNLDFSKGHQ GITGDKEGQQ RRIRQQRLIS IGKWIADNQP RLIQCENEVG
     KLLFITEIPE LILEDPSEAK ENLILQETSV VESLATDGSP GLKSVLSTGR NPSNSCDSGE
     KPVVTFKENI KPREVNQGRS FPPKEVKSQT ELRKTPVSEA RKTPVTQTPS QTSNSQFIPI
     HHPGAFPPLP SRPGFPPPTY VIPPPVAFSM GSGYTFPAGV SVPGTFLQST AHSPAGNQVQ
     AGKQSHIPYS QQRPSGPGPM NQGPQQSQPP SQPPLTSLPA QPTAQSTSQL QVQALAQQQQ
     SPTKVIPALG KSPPHHSGFQ QYQQADASKQ LWNPPQVQSP LGKIMPVKQS YYLQTQDPIK
     LFEPSLQPPV IQQQPLEKKM KPFPMEPYNH NPSEVKVPEF YWDSSYSMAD NRAVMAQQPN
     MDRRSKRSPG VFRPEQDPVP RMPFEDPKSS PLLPPDLLKS LAALEEEEEL IFSNPPDLYP
     ALLGPLASLP GRSLFKSLLE KPSELMSHSS SFLSLTGFSV NQERYPNSSM FNEVYGKNLT
     TSSKAELNPS VASQETSLYS LFEGTPWSPS LPASSDHSTP ASQSPHSSNP SSLPSSPPTH
     NHNSAPFSNF GPIGTPDNRD RRPADRWKTD KPAMGGFGVD YLSATSSSES SWHQASTPSG
     TWTGHGPSME DSSAVLMESL KSIWSSSMMH PGPSALEQLL MQQKQKQQRG QGAMNPPH
 
 
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