GT17_ARATH
ID GT17_ARATH Reviewed; 455 AA.
AC Q9CA34; Q8GXF5;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Probable xyloglucan galactosyltransferase GT17 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000305};
DE AltName: Full=Glycosyltransferase 17 {ECO:0000303|PubMed:15020758};
DE Short=AtGT17 {ECO:0000303|PubMed:15020758};
GN Name=GT17 {ECO:0000303|PubMed:15020758};
GN OrderedLocusNames=At1g68470 {ECO:0000312|Araport:AT1G68470};
GN ORFNames=T26J14.4 {ECO:0000312|EMBL:AAG52396.1};
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=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].
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 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 roots and hypocotyls.
CC {ECO:0000269|PubMed:15020758}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000305}.
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DR EMBL; KJ138946; AHL38886.1; -; mRNA.
DR EMBL; AC011915; AAG52396.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34797.1; -; Genomic_DNA.
DR EMBL; AK118265; BAC42883.1; -; mRNA.
DR PIR; G96708; G96708.
DR RefSeq; NP_177014.1; NM_105518.3.
DR AlphaFoldDB; Q9CA34; -.
DR STRING; 3702.AT1G68470.1; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR PaxDb; Q9CA34; -.
DR PRIDE; Q9CA34; -.
DR ProteomicsDB; 247302; -.
DR EnsemblPlants; AT1G68470.1; AT1G68470.1; AT1G68470.
DR GeneID; 843176; -.
DR Gramene; AT1G68470.1; AT1G68470.1; AT1G68470.
DR KEGG; ath:AT1G68470; -.
DR Araport; AT1G68470; -.
DR TAIR; locus:2201297; AT1G68470.
DR eggNOG; KOG1021; Eukaryota.
DR HOGENOM; CLU_012659_4_1_1; -.
DR InParanoid; Q9CA34; -.
DR OMA; YATHQFI; -.
DR OrthoDB; 789556at2759; -.
DR PhylomeDB; Q9CA34; -.
DR PRO; PR:Q9CA34; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CA34; 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; 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..455
FT /note="Probable xyloglucan galactosyltransferase GT17"
FT /id="PRO_0000435998"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 35..55
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..455
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 392
FT /note="T -> A (in Ref. 4; BAC42883)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 455 AA; 52905 MW; 9D74B55272B3420D CRC64;
MTFNKRQVKI NHWPEKNDKE KQKYSKNRET VKLTLLTLLL LCSICFLFLT LNFPFTIEFT
ASIPRTCDHN FTVYVYDLPK EFNIGLLQNC RHLNIYTNMC PHVANNGLGQ PLHRGRTSWF
STHQFIAEMI FHARVENHPC RTYEPDTADI FYVPFYGGLY ASSVFREQNL TKRDELAVRL
VNYISGQRWW KRSNGRDHFL AIGRTAWDFM RSSDTDFGAN MLMQMPRVMN MSVLTVERQP
WNGDNHFGIP YPSYFHPYTS AEMVTWQDKM KNVERPNLFS FVGGPRKGLE KAAIRDELIK
QCAESSHCEL LKCENGGSRC HNPMTVLGVM ARSRFCLQAP GDSFTRRSTF DAMLAGCIPV
FFSPHTMYTQ YMWYLPDDKR SYSVFMDEKN NTHIEQELLR ISENEVVQMR EIVIDLIPRL
TYAHPNSTNY DLPDAVDIAL EALAKQARDN VVVSL
