B3GT6_ARATH
ID B3GT6_ARATH Reviewed; 399 AA.
AC Q9MAP8; W8Q3Q1;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Beta-1,6-galactosyltransferase GALT31A {ECO:0000305};
DE EC=2.4.1.- {ECO:0000305};
DE AltName: Full=Beta-1,3-galactosyltransferase 6 {ECO:0000305|PubMed:18548197};
DE AltName: Full=GT31 family galactosyltransferase 1 {ECO:0000305};
DE Short=AtGALT31A {ECO:0000303|PubMed:23837821};
GN Name=GALT31A {ECO:0000303|PubMed:23837821};
GN Synonyms=B3GALT6 {ECO:0000305|PubMed:18548197};
GN OrderedLocusNames=At1g32930; ORFNames=F9L11.10;
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].
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18548197; DOI=10.1007/s11103-008-9351-3;
RA Qu Y., Egelund J., Gilson P.R., Houghton F., Gleeson P.A., Schultz C.J.,
RA Bacic A.;
RT "Identification of a novel group of putative Arabidopsis thaliana beta-
RT (1,3)-galactosyltransferases.";
RL Plant Mol. Biol. 68:43-59(2008).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23837821; DOI=10.1111/tpj.12281;
RA Geshi N., Johansen J.N., Dilokpimol A., Rolland A., Belcram K., Verger S.,
RA Kotake T., Tsumuraya Y., Kaneko S., Tryfona T., Dupree P., Scheller H.V.,
RA Hoefte H., Mouille G.;
RT "A galactosyltransferase acting on arabinogalactan protein glycans is
RT essential for embryo development in Arabidopsis.";
RL Plant J. 76:128-137(2013).
RN [8]
RP FUNCTION, INTERACTION WITH GALT29A, 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: Beta-galactosyltransferase involved in elongation of beta-
CC 1,6-linked galactan side chains on arabinogalactan proteins. Required
CC for the progression of embryogenesis beyond the globular stage
CC (PubMed:23837821). Beta-galactosyltransferase involved in the
CC biosynthesis of type II arabinogalactan. Transfers galactose from UDP-
CC galactose to a mixture of various oligosaccharides derived from
CC arabinogalactan proteins. Forms a complex with GALT29A that can work
CC cooperatively to enhance the activities of adding galactose residues at
CC O6 positions to beta-1,6-linked galactan and beta-1,3-linked galactan
CC (PubMed:24693939). {ECO:0000269|PubMed:23837821,
CC ECO:0000269|PubMed:24693939}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Interacts with GALT29A. {ECO:0000269|PubMed:24693939}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:23837821, ECO:0000269|PubMed:24693939}; Single-pass
CC type II membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the suspensor of globular stage
CC embryos. {ECO:0000269|PubMed:23837821}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality, due to the arrest of embryo
CC development at the globular stage. {ECO:0000269|PubMed:23837821}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
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DR EMBL; KJ138975; AHL38915.1; -; mRNA.
DR EMBL; AC006424; AAF31275.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31541.1; -; Genomic_DNA.
DR EMBL; BT006435; AAP21243.1; -; mRNA.
DR EMBL; AK227878; BAE99853.1; -; mRNA.
DR PIR; H86453; H86453.
DR RefSeq; NP_174569.1; NM_103026.4.
DR AlphaFoldDB; Q9MAP8; -.
DR SMR; Q9MAP8; -.
DR STRING; 3702.AT1G32930.1; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR iPTMnet; Q9MAP8; -.
DR PaxDb; Q9MAP8; -.
DR PRIDE; Q9MAP8; -.
DR ProteomicsDB; 241116; -.
DR EnsemblPlants; AT1G32930.1; AT1G32930.1; AT1G32930.
DR GeneID; 840187; -.
DR Gramene; AT1G32930.1; AT1G32930.1; AT1G32930.
DR KEGG; ath:AT1G32930; -.
DR Araport; AT1G32930; -.
DR TAIR; locus:2038031; AT1G32930.
DR eggNOG; KOG2288; Eukaryota.
DR HOGENOM; CLU_040730_3_0_1; -.
DR InParanoid; Q9MAP8; -.
DR OMA; DSIRDTW; -.
DR OrthoDB; 640360at2759; -.
DR PhylomeDB; Q9MAP8; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9MAP8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MAP8; baseline and differential.
DR Genevisible; Q9MAP8; 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:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR025298; DUF4094.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF13334; DUF4094; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Golgi apparatus; Manganese; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..399
FT /note="Beta-1,6-galactosyltransferase GALT31A"
FT /id="PRO_0000359416"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 13..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..399
FT /note="Lumenal"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 44596 MW; 05F648A76250D289 CRC64;
MGMGRYQKSA TSGVSARWVF VLCISSFLLG VLVVNRLLAS FETVDGIERA SPEQNDQSRS
LNPLVDCESK EGDILSRVSH THDVIKTLDK TISSLEVELA TARAARSDGR DGSPAVAKTV
ADQSKIRPRM FFVMGIMTAF SSRKRRDSIR GTWLPKGDEL KRLETEKGII MRFVIGHSSS
PGGVLDHTIE AEEEQHKDFF RLNHIEGYHE LSSKTQIYFS SAVAKWDADF YIKVDDDVHV
NLGMLGSTLA RHRSKPRVYI GCMKSGPVLA QKGVKYHEPE YWKFGEEGNK YFRHATGQIY
AISKDLATYI SVNRQLLHKY ANEDVSLGSW FIGLDVEHID DRSLCCGTPL DCEWKGQAGN
PCAASFDWSC SGICKSVDRM LEVHQRCGEG DGAIWHSSF
