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Database: UniProt
Entry: GT14A_ARATH
LinkDB: GT14A_ARATH
Original site: 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   27-MAR-2024, entry version 128.
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.Q9FLD7; -.
DR   CAZy; GT14; Glycosyltransferase Family 14.
DR   GlyCosmos; Q9FLD7; 4 sites, No reported glycans.
DR   iPTMnet; Q9FLD7; -.
DR   PaxDb; 3702-AT5G39990-1; -.
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; AT5G39990; GLCAT14A.
DR   eggNOG; KOG0799; Eukaryota.
DR   HOGENOM; CLU_034994_0_0_1; -.
DR   InParanoid; Q9FLD7; -.
DR   OMA; SSERKWI; -.
DR   OrthoDB; 912743at2759; -.
DR   PhylomeDB; Q9FLD7; -.
DR   BioCyc; ARA:AT5G39990-MONOMER; -.
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: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:SF40; BETA-GLUCURONOSYLTRANSFERASE GLCAT14A; 1.
DR   PANTHER; PTHR45719; GLYCOSYLTRANSFERASE; 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
//
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