GINT1_ARATH
ID GINT1_ARATH Reviewed; 765 AA.
AC Q84WB7; Q9LZ75;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Glucosamine inositolphosphorylceramide transferase 1 {ECO:0000303|PubMed:29760197};
DE EC=2.7.1.227 {ECO:0000269|PubMed:29760197};
DE AltName: Full=Glycosyltransferase family protein 64 protein C5 {ECO:0000303|PubMed:24905498};
DE Short=GT64 C5 {ECO:0000303|PubMed:24905498};
GN Name=GINT1 {ECO:0000303|PubMed:29760197};
GN OrderedLocusNames=At5g04500 {ECO:0000312|Araport:AT5G04500};
GN ORFNames=T32M21.100 {ECO:0000312|EMBL:CAB85556.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 GENE FAMILY.
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, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP SPECIFICITY, AND REPRESSION BY IMBIBITION.
RC STRAIN=cv. Columbia;
RX PubMed=29760197; DOI=10.1104/pp.18.00396;
RA Ishikawa T., Fang L., Rennie E.A., Sechet J., Yan J., Jing B., Moore W.,
RA Cahoon E.B., Scheller H.V., Kawai-Yamada M., Mortimer J.C.;
RT "GLUCOSAMINE INOSITOLPHOSPHORYLCERAMIDE TRANSFERASE1 (GINT1) is a GlcNAc-
RT containing glycosylinositol phosphorylceramide glycosyltransferase.";
RL Plant Physiol. 177:938-952(2018).
RN [7]
RP REVIEW ON SPHINGOLIPIDS.
RX PubMed=23499054; DOI=10.1016/j.pbi.2013.02.009;
RA Markham J.E., Lynch D.V., Napier J.A., Dunn T.M., Cahoon E.B.;
RT "Plant sphingolipids: function follows form.";
RL Curr. Opin. Plant Biol. 16:350-357(2013).
RN [8]
RP REVIEW.
RX PubMed=32407692; DOI=10.1016/j.tplants.2020.03.007;
RA Mortimer J.C., Scheller H.V.;
RT "Synthesis and function of complex sphingolipid glycosylation.";
RL Trends Plant Sci. 25:522-524(2020).
CC -!- FUNCTION: Glycosyltransferase that mediates the glycosylation of
CC glycosylinositol phosphorylceramides (GIPCs), the major sphingolipids
CC in the plasma membrane; acts as a HexN(Ac)-specific GIPC sugar
CC transferase and accepts glucosamine (GlcN) and N-acetylglucosamine
CC (GlcNAc) as the sugar unit (PubMed:29760197). Responsible for the
CC glycosylation of a subgroup of GIPCs found in seeds and pollen that
CC contain GlcNAc and GlcN (GlcN(Ac)) (PubMed:29760197). Maybe involved in
CC the maintenance of cell-cell adhesion (PubMed:29760197).
CC {ECO:0000269|PubMed:29760197}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + an N-
CC (2R-hydroxy-very-long-chain fatty acyl)-(R)-4-hydroxysphingoid base =
CC a 1,2-diacyl-sn-glycerol + a 1D-myo-inositol-1-phospho-N-[(R)-2-
CC hydroxy-very-long-chain fatty acyl]-(R)-4-hydroxysphingoid base;
CC Xref=Rhea:RHEA:64536, ChEBI:CHEBI:17815, ChEBI:CHEBI:57880,
CC ChEBI:CHEBI:155886, ChEBI:CHEBI:155926; EC=2.7.1.227;
CC Evidence={ECO:0000269|PubMed:29760197};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64537;
CC Evidence={ECO:0000269|PubMed:29760197};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9ES89};
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000269|PubMed:29760197}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Specifically and highly expressed in developing
CC embryos and mature seeds. Also detected at low levels in stigma and
CC pollen. {ECO:0000269|PubMed:29760197}.
CC -!- INDUCTION: Highly expressed in dry seed but drastically down-regulated
CC after seed imbibition. {ECO:0000269|PubMed:29760197}.
CC -!- DISRUPTION PHENOTYPE: Loss of the GlcN(Ac) glycosylinositol
CC phosphorylceramides (GIPCs) leading to a reduced sensitivity to abiotic
CC stress (e.g. abscisic acid and salt) on seed germination. Reduced
CC HexNAc-GIPC content. Slightly larger seeds with more seed storage
CC lipids and proteins and larger seed coat cells.
CC {ECO:0000269|PubMed:29760197}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 64 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB85556.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; KJ138705; AHL38645.1; -; mRNA.
DR EMBL; AL162875; CAB85556.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED90753.1; -; Genomic_DNA.
DR EMBL; BT004019; AAO42055.1; -; mRNA.
DR PIR; T48446; T48446.
DR RefSeq; NP_196070.2; NM_120532.3.
DR AlphaFoldDB; Q84WB7; -.
DR SMR; Q84WB7; -.
DR STRING; 3702.AT5G04500.1; -.
DR CAZy; GT64; Glycosyltransferase Family 64.
DR PaxDb; Q84WB7; -.
DR PRIDE; Q84WB7; -.
DR ProteomicsDB; 220764; -.
DR EnsemblPlants; AT5G04500.1; AT5G04500.1; AT5G04500.
DR GeneID; 830329; -.
DR Gramene; AT5G04500.1; AT5G04500.1; AT5G04500.
DR KEGG; ath:AT5G04500; -.
DR Araport; AT5G04500; -.
DR TAIR; locus:2184347; AT5G04500.
DR eggNOG; KOG1022; Eukaryota.
DR HOGENOM; CLU_010984_0_0_1; -.
DR InParanoid; Q84WB7; -.
DR OMA; FNHRMDG; -.
DR OrthoDB; 330090at2759; -.
DR PhylomeDB; Q84WB7; -.
DR BioCyc; ARA:AT5G04500-MON; -.
DR PRO; PR:Q84WB7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84WB7; baseline and differential.
DR Genevisible; Q84WB7; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; IMP:TAIR.
DR GO; GO:0045140; F:inositol phosphoceramide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030259; P:lipid glycosylation; IMP:TAIR.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
DR Gene3D; 2.115.10.20; -; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR004263; Exostosin.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
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.
DR SUPFAM; SSF75005; SSF75005; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Manganese; Membrane; Metal-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..765
FT /note="Glucosamine inositolphosphorylceramide transferase
FT 1"
FT /id="PRO_0000430884"
FT TRANSMEM 43..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 476..496
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT ACT_SITE 687
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 553
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 577..582
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 598..600
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 600
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 628
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 683..687
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT DISULFID 685..738
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
SQ SEQUENCE 765 AA; 86431 MW; A4BA752BF842B4E1 CRC64;
MMEETTDNTG TISSQKNVAA SGHNHHHRYK YISNYGVGRR FLFFASCFGF YAFVAATYAW
FVFPPHIGRT DHVSSSSLGC REDNEGSWSI GVFYGDSPFS LKPIETRNVW RNESGAWPVT
NPVITCASFT NSGLPSNFLA DPFLYVQGDT LYLFFETKSP ITMQGDIGAA KSIDKGATWE
PLGIALDEAW HLSFPFVFNY NGEIYMMPES NEIGQLNLYR AVNFPLSWKL EKVILKKPLV
DSTIVHHEGI YWLIGSDHTG FGAKKNGQLE IWYSSSPLGT WKPHKKNPIY NGKRSIGARN
GGRAFLYDGS LYRVGQDCGE NYGKRIRVSK IEVLSKEEYR EVEVPFSLEA SRKGKNSWNG
VRQHHFDVKQ LSSGEFIGLV DGDRVTSGDL FHRVILGYAS LAAAISVVIL LGFLLGVVNC
IVPSTWCMNY YAGKRTDALL NLETAGLFSE KLRRIGSRLN RVPPFLRGFV KPNSSMGKFT
LGVIVILGLL LTCVGVRYIY GGSGAVEPYP FKGHLSQFTL ATMTYDARLW NLKMYVKRYS
RCPSVKEIVV IWNKGPPPDL SELDSAVPVR IRVQKQNSLN NRFEIDPLIK TRAVLELDDD
IMMPCDDIEK GFRVWREHPE RLVGFYPRFV DQTMTYSAEK FARSHKGYNM ILTGAAFMDV
RFAFDMYQSD KAKLGRVFVD EQFNCEDILL NFLYANASGS GKAVEYVRPS LVTIDTSKFS
GVAISGNTNQ HYRKRSKCLR RFSDLYGSLV DRRWEFGGRK DGWDL
