GT20_ARATH
ID GT20_ARATH Reviewed; 561 AA.
AC Q9FHD8;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Probable xyloglucan galactosyltransferase GT20 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000305};
DE AltName: Full=Glycosyltransferase 20 {ECO:0000303|PubMed:15020758};
DE Short=AtGT20 {ECO:0000303|PubMed:15020758};
GN Name=GT20 {ECO:0000303|PubMed:15020758};
GN OrderedLocusNames=At5g41250 {ECO:0000312|Araport:AT5G41250};
GN ORFNames=K1O13.4 {ECO:0000312|EMBL:BAB11101.1};
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].
RC STRAIN=cv. Columbia;
RX PubMed=24905498; DOI=10.1111/tpj.12577;
RA Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA Smith-Moritz A.M., Plahar H., Chiu T.-Y., Gonzalez Fernandez-Nino S.M.G.,
RA Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA Loque D., Scheller H.V., Heazlewood J.L.;
RT "The plant glycosyltransferase clone collection for functional genomics.";
RL Plant J. 79:517-529(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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 TISSUE SPECIFICITY.
RX PubMed=15020758; DOI=10.1104/pp.103.036285;
RA Li X., Cordero I., Caplan J., Moelhoej M., Reiter W.D.;
RT "Molecular analysis of 10 coding regions from Arabidopsis that are
RT homologous to the MUR3 xyloglucan galactosyltransferase.";
RL Plant Physiol. 134:940-950(2004).
CC -!- FUNCTION: Functions in xyloglucan synthesis by adding side chains to
CC the xylosylated glucan backbone. Involved in the galactosylation of
CC hemicellulose xyloglucan. {ECO:0000250|UniProtKB:F4K6F1}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q7XJ98}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q7XJ98}.
CC -!- TISSUE SPECIFICITY: Expressed in hydathodes.
CC {ECO:0000269|PubMed:15020758}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KJ138652; AHL38592.1; -; mRNA.
DR EMBL; AB019225; BAB11101.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94657.1; -; Genomic_DNA.
DR RefSeq; NP_198941.1; NM_123490.1.
DR AlphaFoldDB; Q9FHD8; -.
DR STRING; 3702.AT5G41250.1; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR PaxDb; Q9FHD8; -.
DR PRIDE; Q9FHD8; -.
DR EnsemblPlants; AT5G41250.1; AT5G41250.1; AT5G41250.
DR GeneID; 834126; -.
DR Gramene; AT5G41250.1; AT5G41250.1; AT5G41250.
DR KEGG; ath:AT5G41250; -.
DR Araport; AT5G41250; -.
DR TAIR; locus:2155110; AT5G41250.
DR eggNOG; KOG1021; Eukaryota.
DR HOGENOM; CLU_012659_1_0_1; -.
DR InParanoid; Q9FHD8; -.
DR OMA; KVVHICV; -.
DR OrthoDB; 789556at2759; -.
DR PhylomeDB; Q9FHD8; -.
DR PRO; PR:Q9FHD8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHD8; 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:0006486; P:protein glycosylation; IEA:InterPro.
DR InterPro; IPR004263; Exostosin.
DR InterPro; IPR040911; Exostosin_GT47.
DR PANTHER; PTHR11062; PTHR11062; 2.
DR Pfam; PF03016; Exostosin; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..561
FT /note="Probable xyloglucan galactosyltransferase GT20"
FT /id="PRO_0000436001"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 32..52
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..561
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 561 AA; 65208 MW; AFF04ADED4AA5A5B CRC64;
MVSKRKSRTS KTIEDSCIHL CSVFFRFLYY TLPALFLFFF LLYLCLSFTT GISYNNFHMC
IFSRKFNDPY CNTAGSKPGF QIISEENVTF AGEIAGDRVS KDHNKILNSV PVQEHKTKNK
VDLNSLIELK AEEEYSKYIK PTSEDEGYAL RAAIKYLYLQ RSWLSPGDEN LNKPRSCEGK
GVYVYDLPSK FNSDLLVGCN DILPGVNLCS YFKNEGFGEA IKNLGKGWFA THMYSLEPIL
HSRVLKHPCR VYNETQAKLF FVPYYGGYDV LRWHYRNVSE DVKDRLGIEV LKWLNSKESW
RRNAGKDHVF VLGKITWDFR RDKDPWGSRF LELQEMQNPT KLLIERQPWQ VNDIAIPHPT
YFHPRTDDDI TRWQIKIMSK LRRNLVSFAG GARPDNPNNI RSTLIEQCIS SNQCRFLNCT
NESCTNPKNV LDLFQDSEFC LQPPGDSATR RSVFDSLISG CIPVIFTPYT AYYQYAWHLP
EDHRKYSVYI SEQDVKEKRV NVVEILKAKT LKEKKDMKSY IVQQLLPGLV YGDSNAKFEK
FRDAFDITFD CLLKKINRSV V