GINT1_ORYSJ
ID GINT1_ORYSJ Reviewed; 744 AA.
AC Q53WK1;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Glucosamine inositolphosphorylceramide transferase 1 {ECO:0000303|PubMed:29760197};
DE EC=2.4.99.- {ECO:0000305|PubMed:29760197};
GN Name=GINT1 {ECO:0000303|PubMed:29760197};
GN OrderedLocusNames=Os05g0540000 {ECO:0000312|EMBL:BAF18092.1},
GN LOC_Os05g46260 {ECO:0000305};
GN ORFNames=OSJNBa0052K01.21 {ECO:0000312|EMBL:AAV59411.1},
GN OSNPB_050540000 {ECO:0000312|EMBL:BAS95108.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, PATHWAY, AND TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Essential protein. Glycosyltransferase that mediates the
CC glycosylation of glycosylinositol phosphorylceramides (GIPCs), the
CC major sphingolipids in the plasma membrane; acts as a HexN(Ac)-specific
CC GIPC sugar transferase. Responsible for the glycosylation of a subgroup
CC of GIPCs found in seeds and pollen that contain GlcNAc and GlcN
CC (GlcN(Ac)). Maybe involved in the maintenance of cell-cell adhesion.
CC {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: Highly expressed in almost all tissues.
CC {ECO:0000269|PubMed:29760197}.
CC -!- DISRUPTION PHENOTYPE: Loss of the GlcN(Ac) glycosylinositol
CC phosphorylceramides (GIPCs) is seedling lethal. Stunted plants when
CC regenerated from callus. {ECO:0000269|PubMed:29760197}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 64 family.
CC {ECO:0000305}.
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; AC119291; AAV59411.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF18092.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS95108.1; -; Genomic_DNA.
DR RefSeq; XP_015639319.1; XM_015783833.1.
DR AlphaFoldDB; Q53WK1; -.
DR SMR; Q53WK1; -.
DR STRING; 4530.OS05T0540000-01; -.
DR CAZy; GT64; Glycosyltransferase Family 64.
DR PaxDb; Q53WK1; -.
DR PRIDE; Q53WK1; -.
DR EnsemblPlants; Os05t0540000-01; Os05t0540000-01; Os05g0540000.
DR GeneID; 4339463; -.
DR Gramene; Os05t0540000-01; Os05t0540000-01; Os05g0540000.
DR KEGG; osa:4339463; -.
DR eggNOG; KOG1022; Eukaryota.
DR HOGENOM; CLU_010984_0_0_1; -.
DR InParanoid; Q53WK1; -.
DR OMA; GIVNVCI; -.
DR OrthoDB; 330090at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030259; P:lipid glycosylation; IMP:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
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 2: Evidence at transcript level;
KW Disulfide bond; Manganese; Membrane; Metal-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..744
FT /note="Glucosamine inositolphosphorylceramide transferase
FT 1"
FT /id="PRO_0000445782"
FT TRANSMEM 31..51
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT ACT_SITE 669
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 534
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 558..563
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 579..581
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 581
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 609
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 665..669
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT DISULFID 667..718
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
SQ SEQUENCE 744 AA; 84227 MW; 638ABAC97395F5D7 CRC64;
MAGRRAMRPS GSSMRGVVAR LAAARSPAVS FLVAAAAGAA LVGGVYFWLV VSSFRLPDSR
AVGCLPDGEG SWAIGMYYGK SPLELRPIEL EGRSNGNSSA WPVANPVLTC ATPTEGGYPS
NFVADPFLYV QGDTLFLFFE TKTVSTMQGD IGVARSLDQG ATWEFLGIAL DEAWHLSYPF
VFKYENEIYM MPEGNKKKEL RLYRATKFPL EWTLEKVLID KPLIDSSLVQ YDGLWWLFAS
DFTRHGIEKN AELEIWYSNS PLGPWSEHKQ NPIYRSDKSL GARNGGRLFI FEGSLYRPGQ
DCSGTYGRKV KLYKIEKLTK EEYKEVPVNL GIEEAKKGRN AWNGMRYHHI DAQQLASGGW
VAVMDGDRVP SGDSTRRSLF GYMGFLVAVA LVTFVGFVKG AISCYIPPSF WVPLTRRSEL
SRILPVHRFN LKIRRYSTSI GRNISATKAR LSEKTWSNTL FFCVIALIGI VNVCIAVHFL
LGGNGAEEAY THQGQHSQFT MVTMTYEARL WNLKLFVEHY SRCESVREIV VVWNKGNHPT
SDAFDSTVPV RIRVEEINSL NNRFRGDPLI KTRAVLELDD DIMMTCSDVE KGFKVWREHP
ERMVGFYPRM IDGDPLQYRN ERYARGKKGY NLILTGAAFM DSEFAFSKYW SQEAKEGRDY
VHKNFNCEDL LMNFLYANAS SSRTVEYVHP AWAIDTSKLS SVAISRDTQK HYDIRTKCLA
KFASIYGPLP QKWLFGMRED GWDK
