IX14H_ARATH
ID IX14H_ARATH Reviewed; 492 AA.
AC Q9FH90;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Probable beta-1,4-xylosyltransferase IRX14H;
DE EC=2.4.2.-;
DE AltName: Full=Protein IRREGULAR XYLEM 14 homolog;
DE AltName: Full=Xylan xylosyltransferase IRX14H;
GN Name=IRX14H; OrderedLocusNames=At5g67230; ORFNames=K21H1.19;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2]
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 [3]
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20335400; DOI=10.1104/pp.110.155309;
RA Lee C., Teng Q., Huang W., Zhong R., Ye Z.H.;
RT "The Arabidopsis family GT43 glycosyltransferases form two functionally
RT nonredundant groups essential for the elongation of glucuronoxylan
RT backbone.";
RL Plant Physiol. 153:526-541(2010).
RN [5]
RP FUNCTION.
RX PubMed=20424005; DOI=10.1104/pp.110.154971;
RA Wu A.M., Hoernblad E., Voxeur A., Gerber L., Rihouey C., Lerouge P.,
RA Marchant A.;
RT "Analysis of the Arabidopsis IRX9/IRX9-L and IRX14/IRX14-L pairs of
RT glycosyltransferase genes reveals critical contributions to biosynthesis of
RT the hemicellulose glucuronoxylan.";
RL Plant Physiol. 153:542-554(2010).
CC -!- FUNCTION: Involved in the synthesis of the hemicellulose
CC glucuronoxylan, a major component of secondary cell walls. Probably
CC involved in the elongation of glucuronoxylan xylosyl backbone.
CC {ECO:0000269|PubMed:20335400, ECO:0000269|PubMed:20424005}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:20335400}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:20335400}.
CC -!- TISSUE SPECIFICITY: Expressed in developing interfascicular fibers and
CC xylem cells in stems and developing secondary xylem in roots.
CC {ECO:0000269|PubMed:20335400}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 43 family.
CC {ECO:0000305}.
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DR EMBL; AB020742; BAB10957.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98316.1; -; Genomic_DNA.
DR EMBL; AY070076; AAL49771.1; -; mRNA.
DR RefSeq; NP_201524.1; NM_126123.5.
DR AlphaFoldDB; Q9FH90; -.
DR SMR; Q9FH90; -.
DR STRING; 3702.AT5G67230.1; -.
DR CAZy; GT43; Glycosyltransferase Family 43.
DR PaxDb; Q9FH90; -.
DR PRIDE; Q9FH90; -.
DR ProteomicsDB; 238965; -.
DR EnsemblPlants; AT5G67230.1; AT5G67230.1; AT5G67230.
DR GeneID; 836858; -.
DR Gramene; AT5G67230.1; AT5G67230.1; AT5G67230.
DR KEGG; ath:AT5G67230; -.
DR Araport; AT5G67230; -.
DR TAIR; locus:2155533; AT5G67230.
DR eggNOG; KOG1476; Eukaryota.
DR HOGENOM; CLU_042214_1_0_1; -.
DR InParanoid; Q9FH90; -.
DR OMA; WEERHQM; -.
DR OrthoDB; 901158at2759; -.
DR PhylomeDB; Q9FH90; -.
DR PRO; PR:Q9FH90; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FH90; baseline and differential.
DR Genevisible; Q9FH90; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015018; F:galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity; IEA:InterPro.
DR GO; GO:0042285; F:xylosyltransferase activity; IMP:TAIR.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0010417; P:glucuronoxylan biosynthetic process; IMP:TAIR.
DR GO; GO:0009834; P:plant-type secondary cell wall biogenesis; IBA:GO_Central.
DR CDD; cd00218; GlcAT-I; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005027; Glyco_trans_43.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR10896; PTHR10896; 1.
DR Pfam; PF03360; Glyco_transf_43; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Cell wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..492
FT /note="Probable beta-1,4-xylosyltransferase IRX14H"
FT /id="PRO_0000407566"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..492
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 457..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 492 AA; 55349 MW; BF967F6485610232 CRC64;
MKLSVFRLSY WNRRGSSFRS SPSLDPSFDG KSPSSVFWFV IHGLCCLISL ILGFRFSHLV
LFFLFSTSVT NLYTTPFLFA GNGGVSQLLR LKPLETATNS TVKKNSRVVV GRHGIRIRPW
PHPNPIEVLR AHQLLVRVQK EQKSMYGVRS PRTVIVVTPT YVRTFQALHL TGVMHSLMLV
PYDLVWIVVE AGGITNETAS FIAKSGLKTI HLGFDQKMPN TWEDRHKLET KMRLHALRVV
REKKLDGIVM FADDSNMHSM ELFDEIQTVK WFGALSVGIL AHSGNADELS SILKNEQGKN
KEKPSMPIQG PSCNSSEKLV GWHIFNTQPY AKKTAVYIDE KAPVMPSKME WSGFVLNSRL
LWKESLDDKP AWVKDLSLLD DGYAEIESPL SLVKDPSMVE PLGSCGRRVL LWWLRVEARA
DSKFPPGWII KSPLEITVPS KRTPWPDSSS ELPAAAIKEA KSNSKPRVSK SKSYKEKQEP
KAFDGVKVSA TS
