XXT5_ARATH
ID XXT5_ARATH Reviewed; 457 AA.
AC Q9CA75; W8PVU0;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Probable xyloglucan 6-xylosyltransferase 5 {ECO:0000305};
DE EC=2.4.2.39 {ECO:0000305};
DE AltName: Full=Putative glycosyltransferase 5;
DE Short=AtGT5;
DE EC=2.4.-.-;
GN Name=XXT5 {ECO:0000303|PubMed:18557833}; Synonyms=GT5;
GN OrderedLocusNames=At1g74380; ORFNames=F1M20.6;
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=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12032363; DOI=10.1073/pnas.102644799;
RA Faik A., Price N.J., Raikhel N.V., Keegstra K.;
RT "An Arabidopsis gene encoding an alpha-xylosyltransferase involved in
RT xyloglucan biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7797-7802(2002).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18557833; DOI=10.1111/j.1365-313x.2008.03580.x;
RA Zabotina O.A., van de Ven W.T., Freshour G., Drakakaki G., Cavalier D.,
RA Mouille G., Hahn M.G., Keegstra K., Raikhel N.V.;
RT "Arabidopsis XXT5 gene encodes a putative alpha-1,6-xylosyltransferase that
RT is involved in xyloglucan biosynthesis.";
RL Plant J. 56:101-115(2008).
RN [7]
RP INTERACTION WITH XXT2 AND CSLC4, AND SUBCELLULAR LOCATION.
RX PubMed=22665445; DOI=10.1104/pp.112.199356;
RA Chou Y.H., Pogorelko G., Zabotina O.A.;
RT "Xyloglucan xylosyltransferases XXT1, XXT2, and XXT5 and the glucan
RT synthase CSLC4 form Golgi-localized multiprotein complexes.";
RL Plant Physiol. 159:1355-1366(2012).
RN [8]
RP FUNCTION, INTERACTION WITH FUT1 AND XLT2, AND SUBCELLULAR LOCATION.
RX PubMed=25392066; DOI=10.1093/pcp/pcu161;
RA Chou Y.H., Pogorelko G., Young Z.T., Zabotina O.A.;
RT "Protein-protein interactions among xyloglucan-synthesizing enzymes and
RT formation of Golgi-localized multiprotein complexes.";
RL Plant Cell Physiol. 56:255-267(2015).
CC -!- FUNCTION: Probable xyloglucan xylosyltransferase involved in the
CC biosynthesis of xyloglucan in roots. May act in association with XXT1
CC and XXT2 (PubMed:18557833). Associates with other xyloglucan-
CC synthesizing enzymes to form multiprotein complexes for xyloglucan
CC synthesis in the Golgi (PubMed:25392066). {ECO:0000269|PubMed:18557833,
CC ECO:0000269|PubMed:25392066}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Transfers an alpha-D-xylosyl residue from UDP-D-xylose to a
CC glucose residue in xyloglucan, forming an alpha-(1->6)-D-xylosyl-D-
CC glucose linkage.; EC=2.4.2.39; Evidence={ECO:0000305};
CC -!- SUBUNIT: Interacts with XXT2 and CSLC4 (PubMed:22665445). Interacts
CC with FUT1 and XLT2 (PubMed:25392066). {ECO:0000269|PubMed:22665445,
CC ECO:0000269|PubMed:25392066}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:18557833, ECO:0000269|PubMed:22665445,
CC ECO:0000269|PubMed:25392066}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:25392066}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots, stems and cauline
CC leaves, and at lower levels in rosette leaves, flowers and siliques.
CC {ECO:0000269|PubMed:18557833}.
CC -!- DISRUPTION PHENOTYPE: Root hair phenotype, characterized by short root
CC hairs with bubble-like extrusions at the tip. Alteration of the main
CC root cellular morphology. Reduced xyloglucan content.
CC {ECO:0000269|PubMed:18557833}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 34 family.
CC {ECO:0000305}.
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DR EMBL; KJ138936; AHL38876.1; -; mRNA.
DR EMBL; AC011765; AAG52374.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35584.1; -; Genomic_DNA.
DR EMBL; AY093175; AAM13174.1; -; mRNA.
DR EMBL; BT009684; AAP81802.1; -; mRNA.
DR PIR; E96772; E96772.
DR RefSeq; NP_177578.1; NM_106098.4.
DR AlphaFoldDB; Q9CA75; -.
DR SMR; Q9CA75; -.
DR BioGRID; 28998; 6.
DR STRING; 3702.AT1G74380.1; -.
DR CAZy; GT34; Glycosyltransferase Family 34.
DR iPTMnet; Q9CA75; -.
DR PaxDb; Q9CA75; -.
DR PRIDE; Q9CA75; -.
DR ProteomicsDB; 242496; -.
DR EnsemblPlants; AT1G74380.1; AT1G74380.1; AT1G74380.
DR GeneID; 843779; -.
DR Gramene; AT1G74380.1; AT1G74380.1; AT1G74380.
DR KEGG; ath:AT1G74380; -.
DR Araport; AT1G74380; -.
DR TAIR; locus:2019090; AT1G74380.
DR eggNOG; KOG4748; Eukaryota.
DR HOGENOM; CLU_034328_1_0_1; -.
DR InParanoid; Q9CA75; -.
DR OMA; VENLDMK; -.
DR OrthoDB; 629667at2759; -.
DR PhylomeDB; Q9CA75; -.
DR BioCyc; ARA:AT1G74380-MON; -.
DR BioCyc; MetaCyc:AT1G74380-MON; -.
DR BRENDA; 2.4.2.39; 399.
DR PRO; PR:Q9CA75; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CA75; baseline and differential.
DR Genevisible; Q9CA75; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IDA:TAIR.
DR GO; GO:0000138; C:Golgi trans cisterna; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0016758; F:hexosyltransferase activity; IBA:GO_Central.
DR GO; GO:0033843; F:xyloglucan 6-xylosyltransferase activity; IMP:TAIR.
DR GO; GO:0048767; P:root hair elongation; IMP:TAIR.
DR GO; GO:0009969; P:xyloglucan biosynthetic process; IBA:GO_Central.
DR GO; GO:0010411; P:xyloglucan metabolic process; IMP:TAIR.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR008630; Glyco_trans_34.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR31311; PTHR31311; 2.
DR Pfam; PF05637; Glyco_transf_34; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..457
FT /note="Probable xyloglucan 6-xylosyltransferase 5"
FT /id="PRO_0000215173"
FT TOPO_DOM 1..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..457
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 457 AA; 51728 MW; A26B9818D963EA67 CRC64;
MGQDGSPAHK RPSGSGGGLP TTTLTNGGGR GGRGGLLPRG RQMQKTFNNI KITILCGFVT
ILVLRGTIGV GNLGSSSADA VNQNIIEETN RILAEIRSDS DPTDLDEPQE GDMNPNATYV
LGPKITDWDS QRKVWLNQNP EFPSTVNGKA RILLLTGSPP KPCDNPIGDH YLLKSVKNKI
DYCRLHGIEI VYNMAHLDKE LAGYWAKLPM IRRLMLSHPE VEWIWWMDSD ALFTDILFQI
PLARYQKHNL VIHGYPDLLF DQKSWIALNT GSFLLRNCQW SLDLLDAWAP MGPKGPIRDE
AGKVLTAYLK GRPAFEADDQ SALIYLLLSQ KDTWMEKVFV ENQYYLHGFW EGLVDRYEEM
IEKYHPGLGD ERWPFVTHFV GCKPCGSYAD YAVERCLKSM ERAFNFADNQ VLKLYGFSHR
GLLSPKIKRI RNETVSPLEF VDKFDIRRTP VETKPQN
