TGH_ARATH
ID TGH_ARATH Reviewed; 930 AA.
AC Q8GXN9; Q9FN46;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=G patch domain-containing protein TGH;
DE AltName: Full=Protein TOUGH;
GN Name=TGH {ECO:0000312|EMBL:AED93116.1};
GN OrderedLocusNames=At5g23080 {ECO:0000312|Araport:AT5G23080};
GN ORFNames=MYJ24.7 {ECO:0000312|EMBL:BAB09825.1};
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] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16024589; DOI=10.1105/tpc.105.031302;
RA Calderon-Villalobos L.I.A., Kuhnle C., Dohmann E.M.N., Li H., Bevan M.,
RA Schwechheimer C.;
RT "The evolutionarily conserved TOUGH protein is required for proper
RT development of Arabidopsis thaliana.";
RL Plant Cell 17:2473-2485(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-25, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22802657; DOI=10.1073/pnas.1204915109;
RA Ren G., Xie M., Dou Y., Zhang S., Zhang C., Yu B.;
RT "Regulation of miRNA abundance by RNA binding protein TOUGH in
RT Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12817-12821(2012).
CC -!- FUNCTION: Functions as component of microRNA (miRNA) and small
CC interfering RNA (siRNA) biogenesis. May assist DCL1 and DCL4 to
CC efficiently process and/or recruit the precursors of miRNAs and siRNAs.
CC In the miRNA biogenesis pathway, associates with the DCL1 complex that
CC processes primary miRNAs (pri-miRNAs) into miRNAs. Binds pri-miRNAs and
CC precursor miRNAs (pre-miRNAs). Is required for the interaction between
CC pri-miRNAs and DRB1 (PubMed:22802657). Required for general proper
CC plant growth and, in particular, initiation of vascular development.
CC Interacts genetically with AMP1, a glutamate carboxypeptidase involved
CC in the regulation of meristem function (PubMed:16024589).
CC {ECO:0000269|PubMed:16024589, ECO:0000269|PubMed:22802657}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:16024589}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:16024589}. Note=Colocalizes
CC with the splicing factor SR34 to subnuclear particles.
CC {ECO:0000269|PubMed:16024589}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8GXN9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8GXN9-2; Sequence=VSP_057258;
CC -!- TISSUE SPECIFICITY: Expressed in vasculature of cotyledons and leaves,
CC young meristematic tissues, trichomes and pistils.
CC {ECO:0000269|PubMed:16024589}.
CC -!- DISRUPTION PHENOTYPE: Developmental defects, elongation defects of all
CC organs, reduced plant height, triple cotyledons phenotype, reduced
CC vascularization and infertility due to failure to produce pollen.
CC {ECO:0000269|PubMed:16024589}.
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DR EMBL; AY518689; AAR99647.1; -; mRNA.
DR EMBL; AB006708; BAB09825.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93116.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93117.1; -; Genomic_DNA.
DR EMBL; AK118129; BAC42755.1; -; mRNA.
DR EMBL; BT008588; AAP40415.1; -; mRNA.
DR RefSeq; NP_001031926.1; NM_001036849.2. [Q8GXN9-2]
DR RefSeq; NP_197699.2; NM_122214.4. [Q8GXN9-1]
DR AlphaFoldDB; Q8GXN9; -.
DR SMR; Q8GXN9; -.
DR IntAct; Q8GXN9; 1.
DR STRING; 3702.AT5G23080.1; -.
DR iPTMnet; Q8GXN9; -.
DR PaxDb; Q8GXN9; -.
DR PRIDE; Q8GXN9; -.
DR ProteomicsDB; 246474; -. [Q8GXN9-1]
DR EnsemblPlants; AT5G23080.1; AT5G23080.1; AT5G23080. [Q8GXN9-1]
DR EnsemblPlants; AT5G23080.2; AT5G23080.2; AT5G23080. [Q8GXN9-2]
DR GeneID; 832372; -.
DR Gramene; AT5G23080.1; AT5G23080.1; AT5G23080. [Q8GXN9-1]
DR Gramene; AT5G23080.2; AT5G23080.2; AT5G23080. [Q8GXN9-2]
DR KEGG; ath:AT5G23080; -.
DR Araport; AT5G23080; -.
DR TAIR; locus:2178302; AT5G23080.
DR eggNOG; KOG2138; Eukaryota.
DR InParanoid; Q8GXN9; -.
DR OMA; PRSKMDS; -.
DR OrthoDB; 1175081at2759; -.
DR PhylomeDB; Q8GXN9; -.
DR PRO; PR:Q8GXN9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GXN9; baseline and differential.
DR Genevisible; Q8GXN9; AT.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0070883; F:pre-miRNA binding; IDA:TAIR.
DR GO; GO:0070878; F:primary miRNA binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0035196; P:miRNA processing; IMP:TAIR.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0010087; P:phloem or xylem histogenesis; IMP:TAIR.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; TAS:TAIR.
DR GO; GO:0030422; P:siRNA processing; IMP:TAIR.
DR Gene3D; 1.10.10.790; -; 1.
DR InterPro; IPR011666; DUF1604.
DR InterPro; IPR000061; Surp.
DR InterPro; IPR035967; SWAP/Surp_sf.
DR Pfam; PF07713; DUF1604; 1.
DR Pfam; PF01805; Surp; 1.
DR SMART; SM00648; SWAP; 1.
DR SUPFAM; SSF109905; SSF109905; 1.
DR PROSITE; PS50128; SURP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Growth regulation; Isopeptide bond; mRNA processing;
KW Nucleus; Reference proteome; RNA-binding; RNA-mediated gene silencing;
KW Ubl conjugation.
FT CHAIN 1..930
FT /note="G patch domain-containing protein TGH"
FT /id="PRO_0000431422"
FT DOMAIN 159..199
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT REPEAT 405..447
FT /note="SURP motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00263"
FT REGION 76..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..824
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..884
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..907
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..924
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 25
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:17272265"
FT VAR_SEQ 258..287
FT /note="Missing (in isoform 2)"
FT /id="VSP_057258"
SQ SEQUENCE 930 AA; 104934 MW; D564A8E470F89DF9 CRC64;
MGSDEEDFVF HGTPIEREEE IASRKKKAVA GASGNLRTLP AWKQEVTDEE GRRRFHGAFT
GGYSAGYYNT VGSKEGWAPQ SFTSSRQNRA GARKQSISDF LDEDEKADME GKSLSASSQF
DTFGFTAAEH SRKHAEKEQH ERPSAIPGPV PDELVAPVSE SIGVKLLLKM GWRRGHSIKE
VRASSDARRE ARKAFLAFYT DENTKETPDS LVSETEVETS LGEDIKISES TPVYVLNPKQ
DLHGLGYDPF KHAPEFREKK RSRMSANKEV GFRKPLSMKE SLFGPKSGKI APGFGIGALE
ELDVEDEDVY AGYDFDQTYV IEDEQPARQS NDNRLRLTSK EHDVLPGFGA AKNSDYSMER
FNPPIIPKDF VARHKFSGPL EAETKPTVSA PPEVPPPADN NLKLLIEGFA TFVSRCGKLY
EDLSREKNQS NQLFDFLREG NGHDYYARRL WEEQQKRKDQ SKLTLDVKVS PTVQKMTAET
RGSLLGEKPL QRSLKETDTS ASSGGSFQFP TNLSDTFTKS ASSQEAADAV KPFKDDPAKQ
ERFEQFLKEK YKGGLRTTDS NRVNSMSESA RAQERLDFEA AAEAIEKGKA YKEVRRATEQ
PLDFLAGGLQ FTSGGTEQIK DTGVVDMKSS KTYPKREEFQ WRPSPLLCKR FDLPDPFMGK
LPPAPRARNK MDSLVFLPDT VKAASARQVS ESQVPKKETS IEEPEVEVEV ENVERPVDLY
KAIFSDDSED DEDQPMNGKI QEGQEKKNEA AATTLNRLIA GDFLESLGKE LGFEVPMEEE
IKSRSKPEDS SDKRLDRPGL KEKVEEKTSS LTLGSEEEKS RKKREKSPGK RSGGNDLSSS
ESSGDERRRK RYNKKDRHRN DSESDSSSDY HSRDKQGSRS RSKRRESSRE KRSSHKKHSK
HRRTKKSSSS RYSSDEEQKE SRREKKRRRD
