GMT1_ARATH
ID GMT1_ARATH Reviewed; 334 AA.
AC Q9LY62;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Glycosylinositol phosphorylceramide mannosyl transferase 1 {ECO:0000303|PubMed:27895225};
DE Short=GIPC mannosyl-transferase 1 {ECO:0000303|PubMed:27895225};
DE EC=2.4.1.- {ECO:0000269|PubMed:27895225};
DE AltName: Full=Glycosyltransferase family 64 protein C4 {ECO:0000303|PubMed:24905498};
DE Short=GT64 C4 {ECO:0000303|PubMed:24905498};
DE AltName: Full=Protein ECTOPICALLY PARTING CELLS 1 {ECO:0000303|PubMed:16045474};
DE Short=AtEPC1 {ECO:0000303|PubMed:16045474};
GN Name=GMT1 {ECO:0000303|PubMed:27895225};
GN Synonyms=EPC1 {ECO:0000303|PubMed:16045474};
GN OrderedLocusNames=At3g55830 {ECO:0000312|Araport:AT3G55830};
GN ORFNames=F27K19.10 {ECO:0000312|EMBL:CAB87837.1};
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], WEB RESOURCE, AND GENE FAMILY.
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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;
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16045474; DOI=10.1111/j.1365-313x.2005.02455.x;
RA Singh S.K., Eland C., Harholt J., Scheller H.V., Marchant A.;
RT "Cell adhesion in Arabidopsis thaliana is mediated by ECTOPICALLY PARTING
RT CELLS 1--a glycosyltransferase (GT64) related to the animal exostosins.";
RL Plant J. 43:384-397(2005).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Wassilewskija;
RX PubMed=17426055; DOI=10.1093/jxb/erm040;
RA Bown L., Kusaba S., Goubet F., Codrai L., Dale A.G., Zhang Z., Yu X.,
RA Morris K., Ishii T., Evered C., Dupree P., Jackson S.;
RT "The ectopically parting cells 1-2 (epc1-2) mutant exhibits an exaggerated
RT response to abscisic acid.";
RL J. Exp. Bot. 58:1813-1823(2007).
RN [7]
RP FUNCTION.
RX PubMed=20687615; DOI=10.1021/pr100249c;
RA Zhou C., Yin Y., Dam P., Xu Y.;
RT "Identification of novel proteins involved in plant cell-wall synthesis
RT based on protein-protein interaction data.";
RL J. Proteome Res. 9:5025-5037(2010).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY,
RP AND PATHWAY.
RC STRAIN=cv. Columbia;
RX PubMed=27895225; DOI=10.1105/tpc.16.00186;
RA Fang L., Ishikawa T., Rennie E.A., Murawska G.M., Lao J., Yan J.,
RA Tsai A.Y.-L., Baidoo E.E.K., Xu J., Keasling J.D., Demura T.,
RA Kawai-Yamada M., Scheller H.V., Mortimer J.C.;
RT "Loss of inositol phosphorylceramide sphingolipid mannosylation induces
RT plant immune responses and reduces cellulose content in Arabidopsis.";
RL Plant Cell 28:2991-3004(2016).
CC -!- FUNCTION: Mannosyl transferase (ManT) required for the biosynthesis of
CC mannose-carrying glycosylinositol phosphorylceramides (GIPCs)
CC (PubMed:27895225). Maybe involved in cell-cell adhesion that maintains
CC the integrity of organs by providing mechanical strength and
CC facilitating the movement of metabolites throughout the plant during
CC development (PubMed:16045474). Prevents abscisic acid- (ABA-) mediated
CC effects on development (e.g. cell size, flowering time, senescence).
CC Probably implicated in beta-(1,4)-galactan biosynthesis thus being a
CC cell-wall synthesis-related (CWSR) protein (PubMed:17426055,
CC PubMed:20687615). {ECO:0000250, ECO:0000269|PubMed:16045474,
CC ECO:0000269|PubMed:17426055, ECO:0000269|PubMed:27895225,
CC ECO:0000303|PubMed:20687615}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9ES89};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000269|PubMed:27895225}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:17426055, ECO:0000269|PubMed:27895225}; Single-pass
CC type II membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, roots, stem, and flowers.
CC {ECO:0000269|PubMed:17426055}.
CC -!- DISRUPTION PHENOTYPE: Disturbed production of mannose-carrying
CC glycosylinositol phosphorylceramides (GIPCs) in gmt1-3
CC (PubMed:27895225). Dwarf plants exhibiting a constitutive
CC hypersensitive response characterized by elevated salicylic acid (SA)
CC and hydrogen peroxide H(2)O(2) levels (PubMed:27895225). Reduced
CC cellulose content, but increased lignin accumulation in cell walls
CC (PubMed:27895225). In epc1-1, strong growth reduction, mechanical
CC fragility, defects in vascular formation and enhanced secondary growth
CC in hypocotyl tissues probably due to abnormal cell-cell adhesion
CC properties in hypocotyl, cotyledon and cortical parenchyma tissues
CC (PubMed:16045474). Ectopic callose deposition, increased glucose level,
CC but reduced level of galactose in cell walls (PubMed:16045474). In
CC epc1-2, dwarf, reduced cell size, defective root hair development,
CC delayed flowering, early senescence, and hypersensitivity to abscisic
CC acid (ABA) during germination and root elongation (PubMed:17426055).
CC Reduced levels of beta-(1,4)-galactan (PubMed:17426055).
CC {ECO:0000269|PubMed:16045474, ECO:0000269|PubMed:17426055,
CC ECO:0000269|PubMed:27895225}.
CC -!- MISCELLANEOUS: Initially thought to be involved in cell-cell adhesion
CC (PubMed:16045474), this function could not be confirmed
CC (PubMed:17426055). {ECO:0000305|PubMed:17426055}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 64 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=JBEI Glycosyltransferase (GT) Collection;
CC URL="http://gt.jbei.org/arabidopsis.html";
CC -!- WEB RESOURCE: Name=CAZY, the Carbohydrate Active enZYmes database;
CC URL="http://www.cazy.org/GT64_all.html";
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DR EMBL; KJ138787; AHL38727.1; -; mRNA.
DR EMBL; AL163832; CAB87837.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79446.1; -; Genomic_DNA.
DR EMBL; AK228499; BAF00425.1; -; mRNA.
DR PIR; T49195; T49195.
DR RefSeq; NP_191142.1; NM_115441.3.
DR AlphaFoldDB; Q9LY62; -.
DR SMR; Q9LY62; -.
DR STRING; 3702.AT3G55830.1; -.
DR CAZy; GT64; Glycosyltransferase Family 64.
DR PaxDb; Q9LY62; -.
DR PRIDE; Q9LY62; -.
DR ProteomicsDB; 247309; -.
DR EnsemblPlants; AT3G55830.1; AT3G55830.1; AT3G55830.
DR GeneID; 824749; -.
DR Gramene; AT3G55830.1; AT3G55830.1; AT3G55830.
DR KEGG; ath:AT3G55830; -.
DR Araport; AT3G55830; -.
DR TAIR; locus:2081983; AT3G55830.
DR eggNOG; KOG1022; Eukaryota.
DR HOGENOM; CLU_013906_1_1_1; -.
DR InParanoid; Q9LY62; -.
DR OMA; IKDDKMP; -.
DR OrthoDB; 750735at2759; -.
DR PhylomeDB; Q9LY62; -.
DR BioCyc; ARA:AT3G55830-MON; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9LY62; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LY62; baseline and differential.
DR Genevisible; Q9LY62; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
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:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0016757; F:glycosyltransferase activity; IMP:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; ISS:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0008219; P:cell death; IMP:TAIR.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:TAIR.
DR GO; GO:0097502; P:mannosylation; IMP:UniProtKB.
DR GO; GO:0010401; P:pectic galactan metabolic process; IMP:UniProtKB.
DR GO; GO:0010087; P:phloem or xylem histogenesis; IMP:TAIR.
DR GO; GO:0052541; P:plant-type cell wall cellulose metabolic process; IMP:TAIR.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
DR GO; GO:0006665; P:sphingolipid metabolic process; IMP:TAIR.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR004263; Exostosin.
DR InterPro; IPR015338; GT64.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR11062; PTHR11062; 1.
DR Pfam; PF09258; Glyco_transf_64; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Cell adhesion; Developmental protein;
KW Disulfide bond; Glycoprotein; Golgi apparatus; Manganese; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..334
FT /note="Glycosylinositol phosphorylceramide mannosyl
FT transferase 1"
FT /id="PRO_0000430883"
FT TOPO_DOM 1..26
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..49
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..334
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 262
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 145..150
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 166..168
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 168
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 258..262
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 289..302
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 292..302
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 260..305
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
SQ SEQUENCE 334 AA; 38300 MW; 2E41E5600D36B5B9 CRC64;
MGGGEVSKEM GACSLAYRRG DQKLRKFVTA RSTKFLLFCC IAFVLVTIVC RSSRPWVNSS
IAVADRISGS RKGYTLLMNT WKRYDLLKKS VSHYASCSRL DSIHIVWSEP NPPSESLKEY
LHNVLKKKTR DGHEVELRFD INKEDSLNNR FKEIKDLKTD AVFSIDDDII FPCHTVDFAF
NVWESAPDTM VGFVPRVHWP EKSNDKANYY TYSGWWSVWW SGTYSMVLSK AAFFHKKYLS
LYTNSMPASI REFTTKNRNC EDIAMSFLIA NATNAPAIWV KGKIYEIGST GISSIGGHTE
KRTHCVNRFV AEFGKMPLVY TSMKAVDSRN LWFW
