XTH28_ARATH
ID XTH28_ARATH Reviewed; 332 AA.
AC Q38909; O04750;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Probable xyloglucan endotransglucosylase/hydrolase protein 28;
DE Short=At-XTH28;
DE Short=XTH-28;
DE EC=2.4.1.207;
DE Flags: Precursor;
GN Name=XTH28; Synonyms=EXGT-A2, XTR2; OrderedLocusNames=At1g14720;
GN ORFNames=F10B6.12, F10B6.29;
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=8696366; DOI=10.1046/j.1365-313x.1996.9060879.x;
RA Xu W., Campbell P., Vargheese A.K., Braam J.;
RT "The Arabidopsis XET-related gene family: environmental and hormonal
RT regulation of expression.";
RL Plant J. 9:879-889(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=10557219; DOI=10.1104/pp.121.3.715;
RA Akamatsu T., Hanzawa Y., Ohtake Y., Takahashi T., Nishitani K., Komeda Y.;
RT "Expression of endoxyloglucan transferase genes in acaulis mutants of
RT Arabidopsis.";
RL Plant Physiol. 121:715-721(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Okamoto S., Kamimai T., Nishitani K.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NOMENCLATURE.
RX PubMed=12514239; DOI=10.1093/pcp/pcf171;
RA Rose J.K.C., Braam J., Fry S.C., Nishitani K.;
RT "The XTH family of enzymes involved in xyloglucan endotransglucosylation
RT and endohydrolysis: current perspectives and a new unifying nomenclature.";
RL Plant Cell Physiol. 43:1421-1435(2002).
CC -!- FUNCTION: Catalyzes xyloglucan endohydrolysis (XEH) and/or
CC endotransglycosylation (XET). Cleaves and religates xyloglucan
CC polymers, an essential constituent of the primary cell wall, and
CC thereby participates in cell wall construction of growing tissues (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=breaks a beta-(1->4) bond in the backbone of a xyloglucan and
CC transfers the xyloglucanyl segment on to O-4 of the non-reducing
CC terminal glucose residue of an acceptor, which can be a xyloglucan or
CC an oligosaccharide of xyloglucan.; EC=2.4.1.207;
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}. Secreted,
CC extracellular space, apoplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in 7 day old seedlings, roots, rosette
CC leaves, internodes between nodes bearing axillary shoots, nodes bearing
CC flowers, flower buds and siliques. {ECO:0000269|PubMed:10557219}.
CC -!- PTM: Contains at least one intrachain disulfide bond essential for its
CC enzymatic activity. {ECO:0000250}.
CC -!- MISCELLANEOUS: In contrast to group 1 and group 2
CC endotransglucosylase/hydrolase proteins, it may not contain the ligase
CC activity, and may catalyze endohydrolysis xyloglucan polymers only.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 3
CC subfamily. {ECO:0000305}.
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DR EMBL; U43487; AAB18366.1; -; mRNA.
DR EMBL; AF163820; AAD45124.1; -; Genomic_DNA.
DR EMBL; D63510; BAA20290.1; -; mRNA.
DR EMBL; AC006917; AAF79246.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29214.1; -; Genomic_DNA.
DR EMBL; AF385714; AAK60305.1; -; mRNA.
DR EMBL; AY085855; AAM63068.1; -; mRNA.
DR PIR; S71224; S71224.
DR RefSeq; NP_172925.1; NM_101341.4.
DR AlphaFoldDB; Q38909; -.
DR SMR; Q38909; -.
DR BioGRID; 23277; 1.
DR STRING; 3702.AT1G14720.1; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR PaxDb; Q38909; -.
DR PRIDE; Q38909; -.
DR ProteomicsDB; 243173; -.
DR EnsemblPlants; AT1G14720.1; AT1G14720.1; AT1G14720.
DR GeneID; 838037; -.
DR Gramene; AT1G14720.1; AT1G14720.1; AT1G14720.
DR KEGG; ath:AT1G14720; -.
DR Araport; AT1G14720; -.
DR TAIR; locus:2006857; AT1G14720.
DR eggNOG; ENOG502QVQI; Eukaryota.
DR HOGENOM; CLU_048041_1_2_1; -.
DR InParanoid; Q38909; -.
DR OMA; AIQGCAV; -.
DR OrthoDB; 1209387at2759; -.
DR PhylomeDB; Q38909; -.
DR BioCyc; ARA:AT1G14720-MON; -.
DR BRENDA; 2.4.1.207; 399.
DR PRO; PR:Q38909; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q38909; baseline and differential.
DR Genevisible; Q38909; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; ISS:UniProtKB.
DR GO; GO:0016762; F:xyloglucan:xyloglucosyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0042546; P:cell wall biogenesis; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0010154; P:fruit development; IMP:TAIR.
DR GO; GO:0080086; P:stamen filament development; IMP:TAIR.
DR GO; GO:0010411; P:xyloglucan metabolic process; IEA:InterPro.
DR CDD; cd02176; GH16_XET; 1.
DR InterPro; IPR044791; Beta-glucanase/XTH.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR InterPro; IPR010713; XET_C.
DR InterPro; IPR016455; XTH.
DR PANTHER; PTHR31062; PTHR31062; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR Pfam; PF06955; XET_C; 1.
DR PIRSF; PIRSF005604; XET; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 2: Evidence at transcript level;
KW Apoplast; Cell wall; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal;
KW Transferase.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..332
FT /note="Probable xyloglucan endotransglucosylase/hydrolase
FT protein 28"
FT /id="PRO_0000011828"
FT DOMAIN 23..223
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT REGION 313..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 108
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT ACT_SITE 112
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 112
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 125..127
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 135..139
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 202..203
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 207
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 282
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT SITE 110
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 277..290
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
SQ SEQUENCE 332 AA; 38252 MW; AF8242902A0CA191 CRC64;
MGFITRFLVF MSLFTSLVSG FALQKLPLIQ FDEGYTQLFG DQNLIVHRDG KSVRLTLDER
TGSGFVSNDI YLHGFFSSSI KLPADYSAGV VIAFYLSNGD LYEKNHDEID FEFLGNIRGR
EWRIQTNIYG NGSTHLGREE RYNLWFDPTE DFHQYSILWS LSHIIFYVDN VPIREVKRTA
SMGGDFPAKP MSLYSTIWDG SKWATDGGKY GVNYKYAPYV SQFTDLILHG CAVDPTEKFP
SCKDEAVQNL RLASEITESQ RNKMEIFRQK HMTYSYCYDH MRYKVVLSEC VVNPAEAKRL
RVYDPVTFGG IPHGHRRGKH RSRSRLARTE SI
