B3GTF_ARATH
ID B3GTF_ARATH Reviewed; 643 AA.
AC Q8L7F9; Q9LQX1; W8Q3R0;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Beta-1,3-galactosyltransferase GALT1 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000269|PubMed:17630273};
DE AltName: Full=Beta-1,3-galactosyltransferase 15 {ECO:0000305};
DE AltName: Full=Galactosyltransferase 1 {ECO:0000303|PubMed:17630273};
GN Name=GALT1 {ECO:0000303|PubMed:17630273};
GN Synonyms=B3GALT15 {ECO:0000305|PubMed:18548197};
GN OrderedLocusNames=At1g26810; ORFNames=T24P13.20;
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], FUNCTION, COFACTOR, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Silique;
RX PubMed=17630273; DOI=10.1105/tpc.107.052985;
RA Strasser R., Bondili J.S., Vavra U., Schoberer J., Svoboda B., Gloessl J.,
RA Leonard R., Stadlmann J., Altmann F., Steinkellner H., Mach L.;
RT "A unique beta-1,3-galactosyltransferase is indispensable for the
RT biosynthesis of N-glycans containing Lewis a structures in Arabidopsis
RT thaliana.";
RL Plant Cell 19:2278-2292(2007).
RN [2]
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 [3]
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 [4]
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 [5]
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 [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 INTERACTION WITH GMII, AND SUBCELLULAR LOCATION.
RX PubMed=23400704; DOI=10.1104/pp.112.210757;
RA Schoberer J., Liebminger E., Botchway S.W., Strasser R., Hawes C.;
RT "Time-resolved fluorescence imaging reveals differential interactions of N-
RT glycan processing enzymes across the Golgi stack in planta.";
RL Plant Physiol. 161:1737-1754(2013).
CC -!- FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose from
CC UDP-galactose to substrates with a terminal beta-N-acetylglucosamine
CC (beta-GlcNAc) residue. Involved in the biosynthesis of N-glycans
CC containing Lewis a structures (with the combination of FUT13).
CC {ECO:0000269|PubMed:17630273}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17630273};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with GMII. {ECO:0000269|PubMed:23400704}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:17630273, ECO:0000269|PubMed:23400704}; Single-pass
CC type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in stems and siliques.
CC {ECO:0000269|PubMed:17630273}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF87039.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EF428439; ABR58858.1; -; mRNA.
DR EMBL; KJ138985; AHL38925.1; -; mRNA.
DR EMBL; AC006535; AAF87039.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30744.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60449.1; -; Genomic_DNA.
DR EMBL; AY133724; AAM91658.1; -; mRNA.
DR PIR; F86394; F86394.
DR RefSeq; NP_001319087.1; NM_001332728.1.
DR RefSeq; NP_174003.1; NM_102445.4.
DR AlphaFoldDB; Q8L7F9; -.
DR SMR; Q8L7F9; -.
DR STRING; 3702.AT1G26810.1; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR PaxDb; Q8L7F9; -.
DR PRIDE; Q8L7F9; -.
DR ProteomicsDB; 240962; -.
DR EnsemblPlants; AT1G26810.1; AT1G26810.1; AT1G26810.
DR EnsemblPlants; AT1G26810.2; AT1G26810.2; AT1G26810.
DR GeneID; 839224; -.
DR Gramene; AT1G26810.1; AT1G26810.1; AT1G26810.
DR Gramene; AT1G26810.2; AT1G26810.2; AT1G26810.
DR KEGG; ath:AT1G26810; -.
DR Araport; AT1G26810; -.
DR TAIR; locus:2200660; AT1G26810.
DR eggNOG; KOG2287; Eukaryota.
DR HOGENOM; CLU_017063_1_0_1; -.
DR InParanoid; Q8L7F9; -.
DR OMA; ICVFGTE; -.
DR OrthoDB; 405234at2759; -.
DR PhylomeDB; Q8L7F9; -.
DR BioCyc; ARA:AT1G26810-MON; -.
DR BioCyc; MetaCyc:AT1G26810-MON; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q8L7F9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L7F9; baseline and differential.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0010488; F:UDP-galactose:N-glycan beta-1,3-galactosyltransferase activity; IDA:TAIR.
DR GO; GO:0010493; P:Lewis a epitope biosynthetic process; IMP:TAIR.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR CDD; cd00070; GLECT; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001079; Galectin_CRD.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF00337; Gal-bind_lectin; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
DR SMART; SM00908; Gal-bind_lectin; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51304; GALECTIN; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..643
FT /note="Beta-1,3-galactosyltransferase GALT1"
FT /id="PRO_0000359425"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 7..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..643
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 171..364
FT /note="Galectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 643 AA; 72323 MW; 6951E000706ADE81 CRC64;
MKRFYGGLLV VSMCMFLTVY RYVDLNTPVE KPYITAAASV VVTPNTTLPM EWLRITLPDF
MKEARNTQEA ISGDDIAVVS GLFVEQNVSK EEREPLLTWN RLESLVDNAQ SLVNGVDAIK
EAGIVWESLV SAVEAKKLVD VNENQTRKGK EELCPQFLSK MNATEADGSS LKLQIPCGLT
QGSSITVIGI PDGLVGSFRI DLTGQPLPGE PDPPIIVHYN VRLLGDKSTE DPVIVQNSWT
ASQDWGAEER CPKFDPDMNK KVDDLDECNK MVGGEINRTS STSLQSNTSR GVPVAREASK
HEKYFPFKQG FLSVATLRVG TEGMQMTVDG KHITSFAFRD TLEPWLVSEI RITGDFRLIS
ILASGLPTSE ESEHVVDLEA LKSPTLSPLR PLDLVIGVFS TANNFKRRMA VRRTWMQYDD
VRSGRVAVRF FVGLHKSPLV NLELWNEART YGDVQLMPFV DYYSLISWKT LAICIFGTEV
DSAKFIMKTD DDAFVRVDEV LLSLSMTNNT RGLIYGLINS DSQPIRNPDS KWYISYEEWP
EEKYPPWAHG PGYIVSRDIA ESVGKLFKEG NLKMFKLEDV AMGIWIAELT KHGLEPHYEN
DGRIISDGCK DGYVVAHYQS PAEMTCLWRK YQETKRSLCC REW
