ID   F1SAH5_PIG              Unreviewed;       408 AA.
AC   F1SAH5; A0A4X1SFQ6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   02-SEP-2026, entry version 90.
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   Name=DPAGT1 {ECO:0000313|Ensembl:ENSSSCP00000016033.2};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000016033.2, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000016033.2, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000016033.2,
RC   ECO:0000313|Proteomes:UP000008227};
RX   PubMed=32543654;
RA   Warr A., Affara N., Aken B., Beiki H., Bickhart D.M., Billis K., Chow W.,
RA   Eory L., Finlayson H.A., Flicek P., Giron C.G., Griffin D.K., Hall R.,
RA   Hannum G., Hourlier T., Howe K., Hume D.A., Izuogu O., Kim K., Koren S.,
RA   Liu H., Manchanda N., Martin F.J., Nonneman D.J., O'Connor R.E.,
RA   Phillippy A.M., Rohrer G.A., Rosen B.D., Rund L.A., Sargent C.A.,
RA   Schook L.B., Schroeder S.G., Schwartz A.S., Skinner B.M., Talbot R.,
RA   Tseng E., Tuggle C.K., Watson M., Smith T.P.L., Archibald A.L.;
RT   "An improved pig reference genome sequence to enable pig genetics and
RT   genomics research.";
RL   Gigascience 9:giaa051-giaa051(2020).
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000016033.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2026) to UniProtKB.
CC   -!- FUNCTION: UDP-N-acetylglucosamine--dolichyl-phosphate N-
CC       acetylglucosaminephosphotransferase that operates in the biosynthetic
CC       pathway of dolichol-linked oligosaccharides, the glycan precursors
CC       employed in protein asparagine (N)-glycosylation. The assembly of
CC       dolichol-linked oligosaccharides begins on the cytosolic side of the
CC       endoplasmic reticulum membrane and finishes in its lumen. The
CC       sequential addition of sugars to dolichol pyrophosphate produces
CC       dolichol-linked oligosaccharides containing fourteen sugars, including
CC       two GlcNAcs, nine mannoses and three glucoses. Once assembled, the
CC       oligosaccharide is transferred from the lipid to nascent proteins by
CC       oligosaccharyltransferases. Catalyzes the initial step of dolichol-
CC       linked oligosaccharide biosynthesis, transferring GlcNAc-1-P from
CC       cytosolic UDP-GlcNAc onto the carrier lipid dolichyl phosphate (P-
CC       dolichol), yielding GlcNAc-P-P-dolichol embedded in the cytoplasmic
CC       leaflet of the endoplasmic reticulum membrane.
CC       {ECO:0000256|ARBA:ARBA00094350}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a di-trans,poly-cis-dolichyl phosphate + UDP-N-acetyl-alpha-D-
CC         glucosamine = an N-acetyl-alpha-D-glucosaminyl-diphospho-di-
CC         trans,poly-cis-dolichol + UMP; Xref=Rhea:RHEA:13289, Rhea:RHEA-
CC         COMP:19498, Rhea:RHEA-COMP:19507, ChEBI:CHEBI:57683,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:57865, ChEBI:CHEBI:58427; EC=2.7.8.15;
CC         Evidence={ECO:0000256|ARBA:ARBA00045078};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13290;
CC         Evidence={ECO:0000256|ARBA:ARBA00045078};
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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 4 family.
CC       {ECO:0000256|ARBA:ARBA00009317}.
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DR   RefSeq; XP_003129975.1; XM_003129927.4.
DR   AlphaFoldDB; F1SAH5; -.
DR   SMR; F1SAH5; -.
DR   STRING; 9823.ENSSSCP00000016033; -.
DR   PaxDb; 9823-ENSSSCP00000016033; -.
DR   Ensembl; ENSSSCT00000016476.5; ENSSSCP00000016033.2; ENSSSCG00000015110.5.
DR   GeneID; 100517773; -.
DR   KEGG; ssc:100517773; -.
DR   CTD; 1798; -.
DR   eggNOG; KOG2788; Eukaryota.
DR   GeneTree; ENSGT00390000011424; -.
DR   HOGENOM; CLU_029942_0_1_1; -.
DR   OMA; LPHFNAR; -.
DR   OrthoDB; 10262326at2759; -.
DR   Reactome; R-SSC-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000008227; Chromosome 9.
DR   Bgee; ENSSSCG00000015110; Expressed in hindlimb bud and 43 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0003975; F:UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003976; F:UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity; IEA:Ensembl.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:Ensembl.
DR   CDD; cd06855; GT_GPT_euk; 1.
DR   InterPro; IPR048439; DPAGT1_ins.
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; PF21383; DPAGT1_ins; 1.
DR   Pfam; PF00953; Glycos_transf_4; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227};
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        12..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        95..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        126..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        167..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        195..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        223..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        253..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        379..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          318..360
FT                   /note="DPAGT1 insertion"
FT                   /evidence="ECO:0000259|Pfam:PF21383"
SQ   SEQUENCE   408 AA;  46193 MW;  EC87B8BD6B1DB71F CRC64;
     MWAFPELPMP LLVNLIGSLL GFVATLTLIP AFRGHFIAAR LCGQDLNKSN RQQIPESQGV
     ISGAVFLIIL FCFIPFPFLN CFVEEHCKAF PHHEFVALIG ALLAICCMIF LGFADDVLNL
     RWRHKLLLPT AASLPLLMVY FTNFGNTTIV VPKPFRPILG LHLDLGILYY VYMGLLAVFC
     TNAINILAGI NGLEAGQSLV ISASIIVFNL VELEGDYRDD HVFSLYFMIP FFFTTLGLLY
     HNWYPSRVFV GDTFCYFAGM TFAVVGILGH FSKTMLLFFM PQVFNFLYSL PQLLHIIPCP
     RHRMPRLNTK TGKLEMSYSK FKTKSLSFLG TFILKVAESL RLVTVRQSEN EDGAFTECNN
     MTLINLLLKV FGPMHERNLT LFLLLLQVVG SAVTFSIRYQ LVRLFYDV
//