B3GTI_ARATH
ID B3GTI_ARATH Reviewed; 672 AA.
AC Q8RX55; Q9SSG4; W8QP19;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Hydroxyproline O-galactosyltransferase GALT5 {ECO:0000303|PubMed:25974423};
DE Short=AtGALT5 {ECO:0000303|PubMed:25974423};
DE EC=2.4.1.- {ECO:0000269|PubMed:25974423};
DE AltName: Full=Beta-1,3-galactosyltransferase 18 {ECO:0000305};
GN Name=GALT5 {ECO:0000303|PubMed:25974423};
GN Synonyms=B3GALT18 {ECO:0000305|PubMed:18548197};
GN OrderedLocusNames=At1g74800; ORFNames=F25A4.23;
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 TISSUE SPECIFICITY.
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 [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, COFACTOR, AND DISRUPTION PHENOTYPE.
RX PubMed=26690932; DOI=10.1186/s12870-015-0670-7;
RA Basu D., Tian L., Wang W., Bobbs S., Herock H., Travers A., Showalter A.M.;
RT "A small multigene hydroxyproline-O-galactosyltransferase family functions
RT in arabinogalactan-protein glycosylation, growth and development in
RT Arabidopsis.";
RL BMC Plant Biol. 15:295-295(2015).
RN [8]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=25974423; DOI=10.1371/journal.pone.0125624;
RA Basu D., Wang W., Ma S., DeBrosse T., Poirier E., Emch K., Soukup E.,
RA Tian L., Showalter A.M.;
RT "Two hydroxyproline galactosyltransferases, GALT5 and GALT2, function in
RT arabinogalactan-protein glycosylation, growth and development in
RT Arabidopsis.";
RL PLoS ONE 10:E0125624-E0125624(2015).
RN [9]
RP INDUCTION BY SALT STRESS.
RX PubMed=26731606; DOI=10.1371/journal.pone.0145092;
RA Basu D., Tian L., Debrosse T., Poirier E., Emch K., Herock H., Travers A.,
RA Showalter A.M.;
RT "Glycosylation of a fasciclin-like arabinogalactan-protein (SOS5) mediates
RT root growth and seed mucilage adherence via a cell wall receptor-like
RT kinase (FEI1/FEI2) pathway in Arabidopsis.";
RL PLoS ONE 11:E0145092-E0145092(2016).
CC -!- FUNCTION: Possesses hydroxyproline O-galactosyltransferase activity.
CC Transfers galactose from UDP-galactose to hydroxyproline residues in
CC the arabinogalactan proteins (AGPs). Is specific for AGPs containing
CC non-contiguous peptidyl hydroxyproline residues. Utilizes UDP-galactose
CC solely as sugar donor. The addition of galactose onto the peptidyl
CC hydroxyproline residues in AGP core proteins represents the first
CC committed step in arabinogalactan polysaccharide addition. AGP glycans
CC play essential roles in both vegetative and reproductive plant growth.
CC {ECO:0000269|PubMed:25974423, ECO:0000269|PubMed:26690932}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:26690932};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:25974423};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:25974423}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in juvenile leaves, stems, cauline leaves
CC and siliques. {ECO:0000269|PubMed:17630273}.
CC -!- INDUCTION: By salt stress. {ECO:0000269|PubMed:26731606}.
CC -!- DISRUPTION PHENOTYPE: Reduced levels of arabinogalactan proteins
CC (PubMed:26690932). Defects in root hair growth, root elongation, pollen
CC tube growth, flowering time, leaf development, silique length and
CC inflorescence growth. Increased sensitivity to salt stress
CC (PubMed:25974423). {ECO:0000269|PubMed:25974423,
CC ECO:0000269|PubMed:26690932}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD55296.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; KJ138933; AHL38873.1; -; mRNA.
DR EMBL; AC008263; AAD55296.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE35633.1; -; Genomic_DNA.
DR EMBL; AY090451; AAL91295.1; -; mRNA.
DR PIR; D96777; D96777.
DR RefSeq; NP_177618.2; NM_106138.3.
DR AlphaFoldDB; Q8RX55; -.
DR SMR; Q8RX55; -.
DR STRING; 3702.AT1G74800.1; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR PaxDb; Q8RX55; -.
DR PRIDE; Q8RX55; -.
DR ProteomicsDB; 241186; -.
DR EnsemblPlants; AT1G74800.1; AT1G74800.1; AT1G74800.
DR GeneID; 843819; -.
DR Gramene; AT1G74800.1; AT1G74800.1; AT1G74800.
DR KEGG; ath:AT1G74800; -.
DR Araport; AT1G74800; -.
DR TAIR; locus:2027290; AT1G74800.
DR eggNOG; KOG2287; Eukaryota.
DR HOGENOM; CLU_017063_2_0_1; -.
DR InParanoid; Q8RX55; -.
DR OMA; VRVIMAI; -.
DR OrthoDB; 248505at2759; -.
DR PhylomeDB; Q8RX55; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q8RX55; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RX55; baseline and differential.
DR Genevisible; Q8RX55; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
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:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0008378; F:galactosyltransferase activity; IBA:GO_Central.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:1990714; F:hydroxyproline O-galactosyltransferase activity; IDA:TAIR.
DR GO; GO:0010405; P:arabinogalactan protein metabolic process; IMP:UniProtKB.
DR GO; GO:0018258; P:protein O-linked glycosylation via hydroxyproline; IDA:UniProtKB.
DR GO; GO:0080147; P:root hair cell development; IMP:TAIR.
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..672
FT /note="Hydroxyproline O-galactosyltransferase GALT5"
FT /id="PRO_0000359428"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 29..49
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..672
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 191..392
FT /note="Galectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 672 AA; 77348 MW; A08ABB5E32233615 CRC64;
MKKPKLSKVE KIDKIDLFSS LWKQRSVRVI MAIGFLYLVI VSVEIPLVFK SWSSSSVPLD
ALSRLEKLNN EQEPQVEIIP NPPLEPVSYP VSNPTIVTRT DLVQNKVREH HRGVLSSLRF
DSETFDPSSK DGSVELHKSA KEAWQLGRKL WKELESGRLE KLVEKPEKNK PDSCPHSVSL
TGSEFMNREN KLMELPCGLT LGSHITLVGR PRKAHPKEGD WSKLVSQFVI ELQGLKTVEG
EDPPRILHFN PRLKGDWSKK PVIEQNSCYR MQWGPAQRCE GWKSRDDEET VDSHVKCEKW
IRDDDNYSEG SRARWWLNRL IGRRKRVKVE WPFPFVEEKL FVLTLSAGLE GYHINVDGKH
VTSFPYRTGF TLEDATGLTV NGDIDVHSVF VASLPTSHPS FAPQRHLELS KRWQAPVVPD
GPVEIFIGIL SAGNHFSERM AVRKSWMQHV LITSAKVVAR FFVALHGRKE VNVELKKEAE
YFGDIVLVPY MDSYDLVVLK TVAICEHGAL AFSAKYIMKC DDDTFVKLGA VINEVKKVPE
GRSLYIGNMN YYHKPLRGGK WAVTYEEWPE EDYPPYANGP GYVLSSDIAR FIVDKFERHK
LRLFKMEDVS VGMWVEHFKN TTNPVDYRHS LRFCQFGCVE NYYTAHYQSP RQMICLWDKL
LRQNKPECCN MR
