GINT1_ORYSI
ID GINT1_ORYSI Reviewed; 744 AA.
AC A2Y6Z7;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Glucosamine inositolphosphorylceramide transferase 1 {ECO:0000305};
DE EC=2.4.99.- {ECO:0000305};
GN Name=GINT1 {ECO:0000305}; ORFNames=OsI_20805 {ECO:0000312|EMBL:EAY98857.1};
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11, and cv. Guang-Lu-Ai No.4;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
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:0000250|UniProtKB:Q53WK1}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9ES89};
CC -!- PATHWAY: Sphingolipid metabolism. {ECO:0000250|UniProtKB:Q53WK1}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 64 family.
CC {ECO:0000305}.
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DR EMBL; CM000130; EAY98857.1; -; Genomic_DNA.
DR AlphaFoldDB; A2Y6Z7; -.
DR SMR; A2Y6Z7; -.
DR STRING; 39946.A2Y6Z7; -.
DR EnsemblPlants; BGIOSGA020279-TA; BGIOSGA020279-PA; BGIOSGA020279.
DR Gramene; BGIOSGA020279-TA; BGIOSGA020279-PA; BGIOSGA020279.
DR HOGENOM; CLU_010984_0_0_1; -.
DR OMA; GIVNVCI; -.
DR Proteomes; UP000007015; Chromosome 5.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:EnsemblPlants.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030259; P:lipid glycosylation; IEA:EnsemblPlants.
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 3: Inferred from homology;
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_0000445781"
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; 84197 MW; FFD64D160E622AAA 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 AELEIRYSNS 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
