GT29A_ARATH
ID GT29A_ARATH Reviewed; 398 AA.
AC Q9SGD2; Q84W00;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Beta-1,6-galactosyltransferase GALT29A {ECO:0000305};
DE EC=2.4.1.- {ECO:0000305};
DE AltName: Full=GT29 family galactosyltransferase 1 {ECO:0000305};
DE Short=AtGALT29A {ECO:0000303|PubMed:24693939};
DE AltName: Full=Sialyltransferase-like protein GT29A {ECO:0000305};
GN Name=GALT29A {ECO:0000303|PubMed:24693939};
GN OrderedLocusNames=At1g08280 {ECO:0000312|Araport:AT1G08280};
GN ORFNames=T23G18.14 {ECO:0000312|EMBL:AAF18241.1};
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=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 [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] OF 284-398.
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] OF 284-398.
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, INTERACTION WITH GALT31A, AND SUBCELLULAR LOCATION.
RX PubMed=24693939; DOI=10.1186/1471-2229-14-90;
RA Dilokpimol A., Poulsen C.P., Vereb G., Kaneko S., Schulz A., Geshi N.;
RT "Galactosyltransferases from Arabidopsis thaliana in the biosynthesis of
RT type II arabinogalactan: molecular interaction enhances enzyme activity.";
RL BMC Plant Biol. 14:90-90(2014).
CC -!- FUNCTION: Galactosyltransferase involved in the biosynthesis of type II
CC arabinogalactan. Possesses galactosyltransferase (GalT) activity in
CC vitro, transferring galactose from UDP-galactose to a mixture of
CC various oligosaccharides derived from arabinogalactan proteins. Forms a
CC complex with GALT31A that can work cooperatively to enhance the
CC activities of adding galactose residues at O6 positions to beta-1,6-
CC galactan and beta-1,3-galactan. {ECO:0000269|PubMed:24693939}.
CC -!- SUBUNIT: Interacts with GALT31A. {ECO:0000269|PubMed:24693939}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:24693939}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
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DR EMBL; KJ139020; AHL38960.1; -; mRNA.
DR EMBL; AC011438; AAF18241.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28269.1; -; Genomic_DNA.
DR EMBL; BT004583; AAO42829.1; -; mRNA.
DR EMBL; AK227539; BAE99537.1; -; mRNA.
DR PIR; G86216; G86216.
DR RefSeq; NP_172305.1; NM_100701.3.
DR AlphaFoldDB; Q9SGD2; -.
DR SMR; Q9SGD2; -.
DR STRING; 3702.AT1G08280.1; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR iPTMnet; Q9SGD2; -.
DR PaxDb; Q9SGD2; -.
DR PRIDE; Q9SGD2; -.
DR ProteomicsDB; 248520; -.
DR EnsemblPlants; AT1G08280.1; AT1G08280.1; AT1G08280.
DR GeneID; 837348; -.
DR Gramene; AT1G08280.1; AT1G08280.1; AT1G08280.
DR KEGG; ath:AT1G08280; -.
DR Araport; AT1G08280; -.
DR TAIR; locus:2199993; AT1G08280.
DR eggNOG; KOG2692; Eukaryota.
DR HOGENOM; CLU_044787_1_0_1; -.
DR InParanoid; Q9SGD2; -.
DR OMA; MVCNSSH; -.
DR OrthoDB; 891104at2759; -.
DR PhylomeDB; Q9SGD2; -.
DR PRO; PR:Q9SGD2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SGD2; baseline and differential.
DR Genevisible; Q9SGD2; AT.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008378; F:galactosyltransferase activity; IDA:TAIR.
DR GO; GO:0008373; F:sialyltransferase activity; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR Gene3D; 3.90.1480.20; -; 1.
DR InterPro; IPR001675; Glyco_trans_29.
DR InterPro; IPR038578; GT29-like_sf.
DR Pfam; PF00777; Glyco_transf_29; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..398
FT /note="Beta-1,6-galactosyltransferase GALT29A"
FT /id="PRO_0000434311"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..398
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 398 AA; 45935 MW; EC1008E89CE6DFF6 CRC64;
MKRSVRPLFS ALLFAFFAAT LICRVAIRRS SFSFASAIAE LGSSGLMTED IVFNETLLEF
AAIDPGEPNF KQEVDLISDY DHTRRSHRRH FSSMSIRPSE QQRRVSRDIA SSSKFPVTLR
SSQAYRYWSE FKRNLRLWAR RRAYEPNIML DLIRLVKNPI DVHNGVVSIS SERYLSCAVV
GNSGTLLNSQ YGDLIDKHEI VIRLNNAKTE RFEKKVGSKT NISFINSNIL HQCGRRESCY
CHPYGETVPI VMYICQPIHV LDYTLCKPSH RAPLLITDPR FDVMCARIVK YYSVKKFLEE
KKAKGFVDWS KDHEGSLFHY SSGMQAVMLA VGICEKVSVF GFGKLNSTKH HYHTNQKAEL
KLHDYEAEYR LYRDLENSPR AIPFLPKEFK IPLVQVYH
