GT14A_ARATH
ID GT14A_ARATH Reviewed; 447 AA.
AC Q9FLD7;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Beta-glucuronosyltransferase GlcAT14A {ECO:0000305};
DE EC=2.4.1.- {ECO:0000305};
DE AltName: Full=GT14 family glucuronic acid transferase 1 {ECO:0000305};
DE Short=AtGlcAT14A {ECO:0000303|PubMed:24128328};
GN Name=GLCAT14A {ECO:0000303|PubMed:24128328};
GN OrderedLocusNames=At5g39990 {ECO:0000312|Araport:AT5G39990};
GN ORFNames=MYH19.19 {ECO:0000312|EMBL:BAB10223.1};
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=24128328; DOI=10.1111/tpj.12353;
RA Knoch E., Dilokpimol A., Tryfona T., Poulsen C.P., Xiong G., Harholt J.,
RA Petersen B.L., Ulvskov P., Hadi M.Z., Kotake T., Tsumuraya Y., Pauly M.,
RA Dupree P., Geshi N.;
RT "A beta-glucuronosyltransferase from Arabidopsis thaliana involved in
RT biosynthesis of type II arabinogalactan has a role in cell elongation
RT during seedling growth.";
RL Plant J. 76:1016-1029(2013).
CC -!- FUNCTION: Beta-glucuronosyltransferase involved in the biosynthesis of
CC type II arabinogalactan (AG). Modifies both the beta-1,6-linked
CC galactan and beta-1,3-linked galactan present in type II AG. Transfers
CC glucuronate to beta-1,6-galactooligosaccharides with degrees of
CC polymerization ranging from 3 to 11. Transfers glucuronate to beta-1,3-
CC galactooligosaccharides with degrees of polymerization ranging from 5
CC to 7. The addition of glucuronate at the O6 position may terminate
CC galactose chain extension. Required for cell elongation during seedling
CC growth. {ECO:0000269|PubMed:24128328}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:24128328}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Increased cell elongation in hypocotyls and roots
CC from seedlings grown in the dark. {ECO:0000269|PubMed:24128328}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 14 family.
CC {ECO:0000305}.
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DR EMBL; KJ138655; AHL38595.1; -; mRNA.
DR EMBL; AB010077; BAB10223.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94499.1; -; Genomic_DNA.
DR EMBL; BT006493; AAP21301.1; -; mRNA.
DR EMBL; AK227442; BAE99445.1; -; mRNA.
DR RefSeq; NP_198815.1; NM_123362.5.
DR AlphaFoldDB; Q9FLD7; -.
DR SMR; Q9FLD7; -.
DR STRING; 3702.AT5G39990.1; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR iPTMnet; Q9FLD7; -.
DR PaxDb; Q9FLD7; -.
DR PRIDE; Q9FLD7; -.
DR ProteomicsDB; 247234; -.
DR EnsemblPlants; AT5G39990.1; AT5G39990.1; AT5G39990.
DR GeneID; 833996; -.
DR Gramene; AT5G39990.1; AT5G39990.1; AT5G39990.
DR KEGG; ath:AT5G39990; -.
DR Araport; AT5G39990; -.
DR TAIR; locus:2178047; AT5G39990.
DR eggNOG; KOG0799; Eukaryota.
DR HOGENOM; CLU_034994_0_0_1; -.
DR InParanoid; Q9FLD7; -.
DR OMA; SSERKWI; -.
DR OrthoDB; 567611at2759; -.
DR PhylomeDB; Q9FLD7; -.
DR BioCyc; ARA:AT5G39990-MON; -.
DR PRO; PR:Q9FLD7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLD7; baseline and differential.
DR Genevisible; Q9FLD7; AT.
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:0015020; F:glucuronosyltransferase activity; IDA:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IDA:TAIR.
DR InterPro; IPR044610; GLCAT14A/B/C.
DR InterPro; IPR003406; Glyco_trans_14.
DR PANTHER; PTHR45719; PTHR45719; 1.
DR Pfam; PF02485; Branch; 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..447
FT /note="Beta-glucuronosyltransferase GlcAT14A"
FT /id="PRO_0000434320"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 34..54
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..447
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 447 AA; 51118 MW; F2795D85AAA89994 CRC64;
MKKLRSYYSN VRHHQNHHHH HHHHSNIVSS ERKWIFFPLL IGSIFALFLL FLTTTLTSPT
GGVRFLPFTR PVLLTGSGSS AFVESKIKPQ QISSLPSPPR FAYLISGSAG DGKSLRRTLL
ALYHPNNRYV VHLDRESSRE EREELHGYIK NSSLFRRFMN VHMIEKANLV TYRGPTMVAN
TLHAAAILLR EGADWDWFIN LSSSDYPLVT QDDLLHIFSH LPRDLNFIDH TSNIGWKASQ
RAKPVIIDPG LYLNKKSDVF WVTQRRSIPT AFKLFTGSAW MALSRPFVDY CIWGWDNLPR
TVLMYYSNFL SSPEGYFHTV LCNAEEFRNT TVNSDLHFIS WDNPPKQHPH HLTLTDMTKM
VNSNAPFARK FRREDPVLDK IDDELLNRGP GMITPGGWCI GSHENGSDPC AVIGDTDVIR
PGPGARRLEN LVTSLLSTEN FRSKQCK