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Database: UniProt
Entry: A0A0L0UQH4_9BASI
LinkDB: A0A0L0UQH4_9BASI
Original site: A0A0L0UQH4_9BASI 
ID   A0A0L0UQH4_9BASI        Unreviewed;       185 AA.
AC   A0A0L0UQH4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase {ECO:0000256|ARBA:ARBA00017659};
DE            EC=2.7.8.15 {ECO:0000256|ARBA:ARBA00013225};
DE   AltName: Full=GlcNAc-1-P transferase {ECO:0000256|ARBA:ARBA00029567};
DE   AltName: Full=N-acetylglucosamine-1-phosphate transferase {ECO:0000256|ARBA:ARBA00033238};
GN   ORFNames=PSTG_17542 {ECO:0000313|EMBL:KNE89004.1};
OS   Puccinia striiformis f. sp. tritici PST-78.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=1165861 {ECO:0000313|EMBL:KNE89004.1, ECO:0000313|Proteomes:UP000054564};
RN   [1] {ECO:0000313|Proteomes:UP000054564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race PST-78 {ECO:0000313|Proteomes:UP000054564};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Hulbert S., Chen X., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Puccinia striiformis f. sp. tritici PST-78.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dolichyl phosphate + UDP-N-acetyl-alpha-D-glucosamine = N-
CC         acetyl-alpha-D-glucosaminyl-diphosphodolichol + UMP;
CC         Xref=Rhea:RHEA:13289, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9519,
CC         ChEBI:CHEBI:57683, ChEBI:CHEBI:57705, ChEBI:CHEBI:57865,
CC         ChEBI:CHEBI:58427; EC=2.7.8.15;
CC         Evidence={ECO:0000256|ARBA:ARBA00034004};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 4 family.
CC       {ECO:0000256|ARBA:ARBA00009317}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KNE89004.1}.
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DR   EMBL; AJIL01000596; KNE89004.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L0UQH4; -.
DR   STRING; 1165861.A0A0L0UQH4; -.
DR   OrthoDB; 5481729at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000054564; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003975; F:UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR   InterPro; IPR000715; Glycosyl_transferase_4.
DR   InterPro; IPR033895; GPT.
DR   PANTHER; PTHR10571; UDP-N-ACETYLGLUCOSAMINE--DOLICHYL-PHOSPHATE N-ACETYLGLUCOSAMINEPHOSPHOTRANSFERASE; 1.
DR   PANTHER; PTHR10571:SF0; UDP-N-ACETYLGLUCOSAMINE--DOLICHYL-PHOSPHATE N-ACETYLGLUCOSAMINEPHOSPHOTRANSFERASE; 1.
DR   Pfam; PF00953; Glycos_transf_4; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054564};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        48..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        125..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   185 AA;  21131 MW;  20B434CA9312E336 CRC64;
     MVPLLAVMLA LSKFNWYPAK AFVGDTFCYF AGMSFATVGI LGHFSKTLLL FFIPQIMNLV
     YSIPQLFGFI PISRHRLPAR DLLSNLLNPS MVMFIKPLSN LTTKTKILNV VEFLKLVKID
     RNKEGLIIGC SNLTLLNFVL IWFPNKLNEE QLTIIILGFQ FVSNFFGGFC ICYYLSDLFY
     DSCLR
//
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