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Database: UniProt
Entry: B8A0Q2_MAIZE
LinkDB: B8A0Q2_MAIZE
Original site: B8A0Q2_MAIZE 
ID   B8A0Q2_MAIZE            Unreviewed;       412 AA.
AC   B8A0Q2;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=Hexosyltransferase {ECO:0000256|RuleBase:RU363063};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU363063};
GN   ORFNames=ZEAMMB73_Zm00001d012234 {ECO:0000313|EMBL:AQK99151.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ACL53751.1};
RN   [1] {ECO:0000313|EMBL:ACL53751.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B73 {ECO:0000313|EMBL:ACL53751.1};
RX   PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA   Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA   Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA   Walbot V., Yu Y.;
RT   "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL   PLoS Genet. 5:E1000740-E1000740(2009).
RN   [2] {ECO:0000313|EMBL:AQK99151.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQK99151.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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; BT055144; ACL53751.1; -; mRNA.
DR   EMBL; CM000784; AQK99151.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8A0Q2; -.
DR   PaxDb; 4577-GRMZM2G119265_P01; -.
DR   eggNOG; KOG2288; Eukaryota.
DR   HOGENOM; CLU_040730_3_0_1; -.
DR   OrthoDB; 357271at2759; -.
DR   UniPathway; UPA00378; -.
DR   ExpressionAtlas; B8A0Q2; baseline and differential.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016758; F:hexosyltransferase activity; IEA:InterPro.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.550.50; -; 1.
DR   InterPro; IPR025298; DUF4094.
DR   InterPro; IPR002659; Glyco_trans_31.
DR   PANTHER; PTHR11214; BETA-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE; 1.
DR   PANTHER; PTHR11214:SF357; HEXOSYLTRANSFERASE; 1.
DR   Pfam; PF13334; DUF4094; 1.
DR   Pfam; PF01762; Galactosyl_T; 1.
PE   2: Evidence at transcript level;
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   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}.
FT   DOMAIN          30..121
FT                   /note="DUF4094"
FT                   /evidence="ECO:0000259|Pfam:PF13334"
FT   REGION          57..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..89
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   412 AA;  45163 MW;  A07C46E19D9C9828 CRC64;
     MLQLLRAMMA LTERQPQLEK KPTRGRAPLS GKAVAALCVT SFVVGLLLSG NVSLMSASAS
     PSSSSTDSEK SIRVSGCDNE RKLGENHPKD LLNEVSRTHQ AIQSLDKAVS TLEMEMAVER
     ARGGGGGGGA ASMASSRTPQ KAFVVVGINT AFTSKKRRDS LRDTWVPRGD KLRKLEREKG
     IVVRFVIGHS GTPGGGALDR ALDAEEAETR DFMRLDHAEG YHELSSKTRT YFTTAVATWD
     ADFYVKVDDD IHLNLGMLAS RLAKHRTRPR VYVGCMKSGP VLSQKGVKYH EPEYWKFGDE
     GNKYFRHATG QIYAISKDLA AYISINQPIL HRFANEDVSL GAWLIGLEVE HVDDRSMCCA
     TPPDCEWKKR AGNVCVASFD WSCSGVCKSV DRMRHIHKAC GEGEGAVWNA AT
//
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