GUX8_ARATH
ID GUX8_ARATH Reviewed; 497 AA.
AC Q8VZP6; Q9ZQP4;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Putative glucuronosyltransferase PGSIP8;
DE EC=2.4.1.-;
DE AltName: Full=Glycogenin-like protein 8;
DE AltName: Full=Plant glycogenin-like starch initiation protein 8;
GN Name=PGSIP8; OrderedLocusNames=At2g35710; ORFNames=T20F21.27;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP GENE FAMILY.
RX AGRICOLA=IND43669941;
RA Chatterjee M., Berbezy P., Vyas D., Coates S., Barsby T.;
RT "Reduced expression of a protein homologous to glycogenin leads to
RT reduction of starch content in Arabidopsis leaves.";
RL Plant Sci. 168:501-509(2005).
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P46976};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VZP6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VZP6-2; Sequence=VSP_042768;
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. Glycogenin
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX820880; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AC006068; AAD15444.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC09148.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09149.1; -; Genomic_DNA.
DR EMBL; AY063949; AAL36305.1; -; mRNA.
DR EMBL; AY096617; AAM20267.1; -; mRNA.
DR EMBL; BX820880; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A84772; A84772.
DR RefSeq; NP_565817.2; NM_129126.5. [Q8VZP6-1]
DR RefSeq; NP_973607.1; NM_201878.3. [Q8VZP6-2]
DR AlphaFoldDB; Q8VZP6; -.
DR SMR; Q8VZP6; -.
DR BioGRID; 3485; 9.
DR IntAct; Q8VZP6; 9.
DR STRING; 3702.AT2G35710.1; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR iPTMnet; Q8VZP6; -.
DR PaxDb; Q8VZP6; -.
DR PRIDE; Q8VZP6; -.
DR ProteomicsDB; 247325; -. [Q8VZP6-1]
DR EnsemblPlants; AT2G35710.1; AT2G35710.1; AT2G35710. [Q8VZP6-1]
DR EnsemblPlants; AT2G35710.2; AT2G35710.2; AT2G35710. [Q8VZP6-2]
DR GeneID; 818140; -.
DR Gramene; AT2G35710.1; AT2G35710.1; AT2G35710. [Q8VZP6-1]
DR Gramene; AT2G35710.2; AT2G35710.2; AT2G35710. [Q8VZP6-2]
DR KEGG; ath:AT2G35710; -.
DR Araport; AT2G35710; -.
DR TAIR; locus:2058754; AT2G35710.
DR eggNOG; KOG1950; Eukaryota.
DR InParanoid; Q8VZP6; -.
DR OMA; ATRVMIR; -.
DR PhylomeDB; Q8VZP6; -.
DR PRO; PR:Q8VZP6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8VZP6; baseline and differential.
DR Genevisible; Q8VZP6; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Glycosyltransferase; Manganese; Membrane;
KW Metal-binding; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..497
FT /note="Putative glucuronosyltransferase PGSIP8"
FT /id="PRO_0000416740"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 165
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 167
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT SITE 149
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT VAR_SEQ 1..115
FT /note="MDLQRGFVFLSLVLSFMIIETTAYRERQLLLLQPPQETAIDTANAVVTVQDR
FT GLKTRRPEHKNAYATMMYMGTPRDYEFYVATRVLIRSLRSLHVEADLVVIASLDVPLRW
FT VQTL -> MSLFVSR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_042768"
SQ SEQUENCE 497 AA; 56798 MW; 35918AEC4DE96087 CRC64;
MDLQRGFVFL SLVLSFMIIE TTAYRERQLL LLQPPQETAI DTANAVVTVQ DRGLKTRRPE
HKNAYATMMY MGTPRDYEFY VATRVLIRSL RSLHVEADLV VIASLDVPLR WVQTLEEEDG
AKVVRVENVD NPYRRQTNFN SRFKLTLNKL YAWALSDYDR VVMLDADNLF LKKADELFQC
GRFCAVFINP CIFHTGLFVL QPSVEVFKDM LHELQVGRKN PDGADQGFLV SYFSDLLDQP
LFSPPSNGSV LNGHLRLPLG YQMDASYFYL KLRWNIPCGP NSVITFPGAV WLKPWYWWSW
PVLPLGFSWH EQRRATIGYS AEMPLVIIQA MFYLGIIVVT RLARPNITKL CYRRSDRNLT
TIQAGFKLIA LLSVVAAYIF PFFTIPHTIH PLIGWSLYLM ASFALSSISI NTLLLPTLPV
LTPWLGILGT LLVMAFPWYP DGVVRALSVF AYAFCCAPFV WVSFRKITSH LQVLIEKEVL
FPRLGDSGVT SGFSKLY
