GT16_ARATH
ID GT16_ARATH Reviewed; 664 AA.
AC Q9SH31; Q0WLQ7;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Xyloglucan-specific galacturonosyltransferase 1 {ECO:0000303|PubMed:23175743};
DE EC=2.4.1.- {ECO:0000269|PubMed:23175743};
DE AltName: Full=Glycosyltransferase 16 {ECO:0000303|PubMed:15020758};
DE AltName: Full=Protein ROOT HAIR SPECIFIC 8 {ECO:0000303|PubMed:19448035};
DE AltName: Full=Protein exostosin {ECO:0000303|PubMed:19448035};
GN Name=GT16 {ECO:0000303|PubMed:15020758};
GN Synonyms=RHS8 {ECO:0000303|PubMed:19448035},
GN XUT1 {ECO:0000303|PubMed:23175743};
GN OrderedLocusNames=At1g63450 {ECO:0000312|EMBL:AEE34101.1};
GN ORFNames=F2K11.17 {ECO:0000312|EMBL:AAF19708.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND GENE FAMILY.
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-229.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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).
RN [6]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19448035; DOI=10.1104/pp.109.140905;
RA Won S.-K., Lee Y.-J., Lee H.-Y., Heo Y.-K., Cho M., Cho H.-T.;
RT "Cis-element- and transcriptome-based screening of root hair-specific genes
RT and their functional characterization in Arabidopsis.";
RL Plant Physiol. 150:1459-1473(2009).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=23175743; DOI=10.1105/tpc.112.103390;
RA Pena M.J., Kong Y., York W.S., O'Neill M.A.;
RT "A galacturonic acid-containing xyloglucan is involved in Arabidopsis root
RT hair tip growth.";
RL Plant Cell 24:4511-4524(2012).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=22253603; DOI=10.1371/journal.pgen.1002446;
RA Bruex A., Kainkaryam R.M., Wieckowski Y., Kang Y.H., Bernhardt C., Xia Y.,
RA Zheng X., Wang J.Y., Lee M.M., Benfey P., Woolf P.J., Schiefelbein J.;
RT "A gene regulatory network for root epidermis cell differentiation in
RT Arabidopsis.";
RL PLoS Genet. 8:E1002446-E1002446(2012).
CC -!- FUNCTION: Xyloglucan-specific galacturonosyltransferase that forms the
CC beta-D-galactosyluronic acid-(1->2)-alpha-D-xylosyl linkage. Required
CC for root hair development probably by providing important acidic
CC xyloglucans. {ECO:0000269|PubMed:23175743}.
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: Root hair specific (PubMed:19448035,
CC PubMed:22253603). Expressed in roots and young leaves
CC (PubMed:15020758). {ECO:0000269|PubMed:15020758,
CC ECO:0000269|PubMed:19448035, ECO:0000269|PubMed:22253603}.
CC -!- DISRUPTION PHENOTYPE: Lacks acidic xyloglucan and has short root hairs.
CC {ECO:0000269|PubMed:23175743}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000305}.
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DR EMBL; KJ138954; AHL38894.1; -; mRNA.
DR EMBL; AC008047; AAF19708.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34101.1; -; Genomic_DNA.
DR EMBL; AK230135; BAF01950.1; -; mRNA.
DR RefSeq; NP_176534.2; NM_105024.4.
DR AlphaFoldDB; Q9SH31; -.
DR STRING; 3702.AT1G63450.1; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR PaxDb; Q9SH31; -.
DR PRIDE; Q9SH31; -.
DR ProteomicsDB; 247301; -.
DR EnsemblPlants; AT1G63450.1; AT1G63450.1; AT1G63450.
DR GeneID; 842651; -.
DR Gramene; AT1G63450.1; AT1G63450.1; AT1G63450.
DR KEGG; ath:AT1G63450; -.
DR Araport; AT1G63450; -.
DR TAIR; locus:2031346; AT1G63450.
DR eggNOG; KOG1021; Eukaryota.
DR HOGENOM; CLU_012659_1_0_1; -.
DR InParanoid; Q9SH31; -.
DR OMA; SWRKNAG; -.
DR OrthoDB; 789556at2759; -.
DR PhylomeDB; Q9SH31; -.
DR PRO; PR:Q9SH31; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SH31; baseline and differential.
DR Genevisible; Q9SH31; AT.
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; IMP:TAIR.
DR GO; GO:0042546; P:cell wall biogenesis; IMP:TAIR.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IMP:TAIR.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR GO; GO:0048767; P:root hair elongation; IMP:TAIR.
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 Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..664
FT /note="Xyloglucan-specific galacturonosyltransferase 1"
FT /id="PRO_0000434272"
FT TOPO_DOM 1..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 72..92
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..664
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 664 AA; 76562 MW; 22B0624DCCD57CCE CRC64;
MSLSKHLQKL VHKRESKKQP NKKMPVSVSK LRRPRTSKKT ETGNPEKTLK DPRTCCNNLF
SIFSARSFLY RVPLTILFLF LIYLWSTSTT VISGNVVHIC ISSRKLTDLY CLTAGSQPAL
RAPVNNFTAP ASEDVVTSKE EKNVFVLGKD GDKGFAENET FEGGKDSDKS TVGENLTINK
NETFTGETSG ERVSILNQDA KPIHEKNLDS VLDQDSLPKN EIDQDFIIDW DPETGEERYR
YFKAKTEDEE TGLKSTEEYI QIQRTWLSMG NNRKKPGSCE GKGVYVYDLP SKFNKDLLRE
CSDMVPWADF CNYFKNDAFG ELMESMGKGW FRTHQYSLEP IFHSRILKHP CRVHNETQAK
LFYVPFYGGM DVLRWHFKNV SSDVKDVLPI EIVKWLGSKK SWRKNSGKDH VFVLGKISWD
FRRVDKYSWG SSLLEMQEMK NPTKLLIERN PWEVNDIAIP HPTYFHPKTD TDIAIWQNKI
LGKPRRSLIS FAGAARPGNP ESIRSILIDQ CRSSPNQCRF LNCTDGGCDK SESVIELFRD
SEFCLQPPGD SPTRKSIFDS LILGCIPVIF DPYSAYYQYT WHLPEDHRRY SVYINKEDVK
LKRVNVIEKL MSKTLRERED MRSYIVHELL PGLVYGDSNA KFERFRDAFD ITMDSLFKKI
AKTV
