GT11_ARATH
ID GT11_ARATH Reviewed; 720 AA.
AC O81072; W8QNX4;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Probable xyloglucan galactosyltransferase GT11 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000305};
DE AltName: Full=Glycosyltransferase 11 {ECO:0000303|PubMed:15020758};
DE Short=AtGT11 {ECO:0000303|PubMed:15020758};
GN Name=GT11 {ECO:0000303|PubMed:15020758};
GN OrderedLocusNames=At2g29040 {ECO:0000312|Araport:AT2G29040};
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=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 [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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
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, hypocotyls, cotyledons, leaves,
CC stems and sepals. {ECO:0000269|PubMed:15020758}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000305}.
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DR EMBL; KJ138893; AHL38833.1; -; mRNA.
DR EMBL; AC005315; AAC33230.1; -; Genomic_DNA.
DR EMBL; CP002685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DQ446576; ABE65870.1; -; mRNA.
DR PIR; T02734; T02734.
DR AlphaFoldDB; O81072; -.
DR STRING; 3702.AT2G29040.1; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR PaxDb; O81072; -.
DR PRIDE; O81072; -.
DR EnsemblPlants; AT2G29040.1; AT2G29040.1; AT2G29040.
DR Gramene; AT2G29040.1; AT2G29040.1; AT2G29040.
DR Araport; AT2G29040; -.
DR TAIR; locus:2066091; AT2G29040.
DR eggNOG; KOG1021; Eukaryota.
DR HOGENOM; CLU_012659_2_1_1; -.
DR InParanoid; O81072; -.
DR PhylomeDB; O81072; -.
DR PRO; PR:O81072; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O81072; baseline and differential.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
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..720
FT /note="Probable xyloglucan galactosyltransferase GT11"
FT /id="PRO_0000435993"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 14..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..720
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 114..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 445
FT /note="R -> S (in Ref. 1; AHL38833)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 720 AA; 83969 MW; 8B5F5A5BE2D905A5 CRC64;
MAMEKSSSKY RTQFWYVAMA SFLLWLVLLY LFSSSAKTVH NHERLFRQEN IIDLPVENVP
QNHEPDEAPV VNVVSEDISV DNSSLPVSVD SPPDDQMSED KKVVTDLVEE LEKERVENEK
KRVDSVVIGR SSKARRGHRE PRKARSSGRL EAEKKRVRRN DADESNAENS DENHQALDKE
PNFFEAKKDV EPKKALVDDN DDDLETKRGK ELPNDSSSNV VEDDNDDDLE TKKGKDNISK
SEPKTQRNFV LNKNNTSKAK NRVISKRNQP SRVGKVMLRP RETRSNDPCK GKYVYMHEVP
ALFNEELLKN CWTLSRWTDM CELTSNFGLG PRLPNMEGVS GWYATNQFTL EVIFHNRMKQ
YKCLTKDSSL ASAVYVPYYP GLDLMRFLWG PFPFMRDAAA LDLMKWLRES QEWKRMDGRD
HFMVAGRTTW DFMRTPENES DWGNRLMILP EVRNMTMLLI ESSPWNYHGF AVPYPTYFHP
STYAEIIQWQ MRMRRINRRY LFSFVGAPRP NLGDSIRTEI MDQCKASKRK CKLLECISGS
QKCYKPDQIM KFFLSSTFCL QPPGDSYTRR STFDSILAGC IPVFFHPGSA YAQYIWHLPK
DIAKYSVFIP EKNVKEGKVS IENVLSRIPR TKVFAMREQV IRLIPRLMYF HPSSKSEDTG
RFEDAFDVAV EGVLERVEGL RKRIEEGKEE IFDFPEQYSW KYNVFGNVER HEWDPYFDRP
