GLYT2_ARATH
ID GLYT2_ARATH Reviewed; 470 AA.
AC Q3EAR7; Q147H3; Q9M2N4;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Probable glycosyltransferase At3g42180;
DE EC=2.4.-.-;
GN OrderedLocusNames=At3g42180; ORFNames=T27B3.50;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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] OF 4-470.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 46-470.
RA Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=18460606; DOI=10.1105/tpc.107.050906;
RA Jensen J.K., Sorensen S.O., Harholt J., Geshi N., Sakuragi Y., Moller I.,
RA Zandleven J., Bernal A.J., Jensen N.B., Sorensen C., Pauly M., Beldman G.,
RA Willats W.G., Scheller H.V.;
RT "Identification of a xylogalacturonan xylosyltransferase involved in pectin
RT biosynthesis in Arabidopsis.";
RL Plant Cell 20:1289-1302(2008).
CC -!- FUNCTION: May be involved in cell wall biosynthesis.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q3EAR7-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:18460606}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB68119.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL137079; CAB68119.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77729.1; -; Genomic_DNA.
DR EMBL; BX824909; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BT026120; ABG48476.1; -; mRNA.
DR PIR; T46112; T46112.
DR RefSeq; NP_189804.4; NM_114085.4. [Q3EAR7-1]
DR AlphaFoldDB; Q3EAR7; -.
DR STRING; 3702.AT3G42180.1; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR PaxDb; Q3EAR7; -.
DR PRIDE; Q3EAR7; -.
DR ProteomicsDB; 248547; -. [Q3EAR7-1]
DR EnsemblPlants; AT3G42180.1; AT3G42180.1; AT3G42180. [Q3EAR7-1]
DR GeneID; 823191; -.
DR Gramene; AT3G42180.1; AT3G42180.1; AT3G42180. [Q3EAR7-1]
DR KEGG; ath:AT3G42180; -.
DR Araport; AT3G42180; -.
DR TAIR; locus:2100814; AT3G42180.
DR eggNOG; KOG1021; Eukaryota.
DR HOGENOM; CLU_025166_1_1_1; -.
DR InParanoid; Q3EAR7; -.
DR PhylomeDB; Q3EAR7; -.
DR BioCyc; ARA:AT3G42180-MON; -.
DR PRO; PR:Q3EAR7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q3EAR7; baseline and differential.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR InterPro; IPR004263; Exostosin.
DR InterPro; IPR040911; Exostosin_GT47.
DR PANTHER; PTHR11062; PTHR11062; 1.
DR Pfam; PF03016; Exostosin; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..470
FT /note="Probable glycosyltransferase At3g42180"
FT /id="PRO_0000392293"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..470
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 7
FT /note="K -> R (in Ref. 3; BX824909)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="G -> C (in Ref. 3; BX824909)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 54268 MW; 43378976271A99A4 CRC64;
MSNNSSKSFC LLGFPLILIL LLSFLLFSSF PNNESPPQQF FSSLTMSSLL VHTNALQSSS
SSSSLYSPPI TVKRRSNLEK REEELRKARA AIRRAVRFKN CTSNEEVITY IPTGQIYRNS
FAFHQSHIEM MKTFKVWSYK EGEQPLVHDG PVNDIYGIEG QFIDELSYVM GGPSGRFRAS
RPEEAHAFFL PFSVANIVHY VYQPITSPAD FNRARLHRIF NDYVDVVAHK HPFWNQSNGA
DHFMVSCHDW APDVPDSKPE FFKNFMRGLC NANTSEGFRR NIDFSIPEIN IPKRKLKPPF
MGQNPENRTI LAFFAGRAHG YIREVLFSHW KGKDKDVQVY DHLTKGQNYH ELIGHSKFCL
CPSGYEVASP REVEAIYSGC VPVVISDNYS LPFNDVLDWS KFSVEIPVDK IPDIKKILQE
IPHDKYLRMY RNVMKVRRHF VVNRPAQPFD VIHMILHSVW LRRLNIRLPS
