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GT14B_ARATH
ID   GT14B_ARATH             Reviewed;         434 AA.
AC   Q9LFQ0;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Beta-glucuronosyltransferase GlcAT14B {ECO:0000305};
DE            EC=2.4.1.- {ECO:0000305};
DE   AltName: Full=GT14 family glucuronic acid transferase 2 {ECO:0000305};
DE            Short=AtGlcAT14B {ECO:0000303|PubMed:24739253};
GN   Name=GLCAT14B {ECO:0000303|PubMed:24739253};
GN   OrderedLocusNames=At5g15050 {ECO:0000312|Araport:AT5G15050};
GN   ORFNames=F2G14.170 {ECO:0000312|EMBL:CAC01824.1};
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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   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   [6]
RP   FUNCTION.
RX   PubMed=24739253; DOI=10.4161/psb.28891;
RA   Dilokpimol A., Geshi N.;
RT   "Arabidopsis thaliana glucuronosyltransferase in family GT14.";
RL   Plant Signal. Behav. 9:E28891-E28891(2014).
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.
CC       {ECO:0000269|PubMed:24739253}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q9FLD7}; Single-pass type II membrane protein
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 14 family.
CC       {ECO:0000305}.
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DR   EMBL; KJ138690; AHL38630.1; -; mRNA.
DR   EMBL; AL391146; CAC01824.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED92110.1; -; Genomic_DNA.
DR   EMBL; AY057600; AAL14395.1; -; mRNA.
DR   EMBL; AY124832; AAM70541.1; -; mRNA.
DR   EMBL; AY086423; AAM63425.1; -; mRNA.
DR   PIR; T51450; T51450.
DR   RefSeq; NP_197009.1; NM_121509.3.
DR   AlphaFoldDB; Q9LFQ0; -.
DR   SMR; Q9LFQ0; -.
DR   STRING; 3702.AT5G15050.1; -.
DR   CAZy; GT14; Glycosyltransferase Family 14.
DR   PaxDb; Q9LFQ0; -.
DR   PRIDE; Q9LFQ0; -.
DR   ProteomicsDB; 247224; -.
DR   EnsemblPlants; AT5G15050.1; AT5G15050.1; AT5G15050.
DR   GeneID; 831357; -.
DR   Gramene; AT5G15050.1; AT5G15050.1; AT5G15050.
DR   KEGG; ath:AT5G15050; -.
DR   Araport; AT5G15050; -.
DR   TAIR; locus:2147880; AT5G15050.
DR   eggNOG; KOG0799; Eukaryota.
DR   HOGENOM; CLU_034994_0_0_1; -.
DR   InParanoid; Q9LFQ0; -.
DR   OMA; TIERKWI; -.
DR   OrthoDB; 567611at2759; -.
DR   PhylomeDB; Q9LFQ0; -.
DR   PRO; PR:Q9LFQ0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LFQ0; baseline and differential.
DR   Genevisible; Q9LFQ0; AT.
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   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..434
FT                   /note="Beta-glucuronosyltransferase GlcAT14B"
FT                   /id="PRO_0000434321"
FT   TOPO_DOM        1..21
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        22..42
FT                   /note="Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        43..434
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        392
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   434 AA;  49583 MW;  804888313C4A42DA CRC64;
     MKKLKSYYMQ VRNQQQSLDR KWILPLAIGS ICSLFLLLLT NLASSSGQTR LIPFSVYGFR
     SSVFVESKIN PVSVSLTVSV SPPPPPRLAY LISGSSGDGQ MLKRTLMALY HPNNQYVVHL
     DRESSPEERL DLSGFVANHT LFQRFQNVRM IVKANFVTYR GPTMVANTLH AAAILLREGG
     DWDWFINLSA SDYPLVTQDD LLHTFSYLPR DLNFIDHTSN IGWKESHRAK PIIIDPGLYM
     SKKADVFWVS QKRSMPTAFK LFTGSAWMML SRPFVDYFIW GWDNLPRIVL MYYANFLSSP
     EGYFHTVICN AREFTNTTVN SDLHFISWDN PPKQHPHHLT LDDFQRMVDS NAPFARKFRR
     DEPVLDKIDS ELLFRSHGMV TPGGWCIGTR ENGSDPCAVI GDTSVIKPGL GAKRIEKLIT
     YLLSTENFRP RQCR
 
 
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