ID A0A194YH88_SORBI Unreviewed; 364 AA.
AC A0A194YH88;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 2.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Hexosyltransferase {ECO:0000256|RuleBase:RU363063};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU363063};
GN ORFNames=SORBI_3010G044800 {ECO:0000313|EMBL:KXG19339.2};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:KXG19339.2, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:KXG19339.2, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936,
CC ECO:0000256|RuleBase:RU363063};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU363063}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323,
CC ECO:0000256|RuleBase:RU363063}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000256|ARBA:ARBA00008661, ECO:0000256|RuleBase:RU363063}.
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DR EMBL; CM000769; KXG19339.2; -; Genomic_DNA.
DR RefSeq; XP_002436508.1; XM_002436463.1.
DR AlphaFoldDB; A0A194YH88; -.
DR EnsemblPlants; KXG19339; KXG19339; SORBI_3010G044800.
DR GeneID; 8069173; -.
DR Gramene; KXG19339; KXG19339; SORBI_3010G044800.
DR KEGG; sbi:8069173; -.
DR eggNOG; KOG2288; Eukaryota.
DR InParanoid; A0A194YH88; -.
DR OMA; KFFHARQ; -.
DR OrthoDB; 1208994at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000768; Chromosome 10.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0008378; F:galactosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.550.50; -; 1.
DR InterPro; IPR002659; Glyco_trans_31.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR11214:SF290; BETA-1,3-GALACTOSYLTRANSFERASE 13-RELATED; 1.
DR PANTHER; PTHR11214; BETA-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|RuleBase:RU363063};
KW Golgi apparatus {ECO:0000256|RuleBase:RU363063};
KW Manganese {ECO:0000256|RuleBase:RU363063};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ SEQUENCE 364 AA; 40103 MW; 77A3FADF79AF64BA CRC64;
MPGSPKVFFA SSASRRGGAL RRLLSTPAFS AACLLFGLAG FLAAALTLSR SPSVTHSRCP
DSSRPLSVSV AWDRRPGDGS AAGSAELPAS LATGSRGRHK VMAFVGIFTG FGSIGRRRAL
RRTWLPADRQ GLLRLEEATG LAFRFVIGKS NSKNKMAALN REVEEYDDFV LLDLEEEYSR
LPYKTLAFFK AAYALYDSDF YVKADDDIYL RPDRLSLLLA KERSHPQTYI GCMKKGPVFT
DPKLKWYEPQ SFLLGSEYFL HAYGPIYALS ADVVASLVAL RNNSFRMFSN EDVTIGSWML
AMNVNHENTH ALCEADCTES SVAVWDIPKC SGLCHPEVKM LELHQRKECT GGPTVAAEVS
ESED
//