ID M3ZUT6_XIPMA Unreviewed; 406 AA.
AC M3ZUT6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
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};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000005979.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000005979.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000005979.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the initial step of dolichol-linked oligosaccharide
CC biosynthesis in N-linked protein glycosylation pathway: transfers
CC GlcNAc-1-P from UDP-GlcNAc onto the carrier lipid dolichyl phosphate
CC (P-dolichol), yielding GlcNAc-P-P-dolichol.
CC {ECO:0000256|ARBA:ARBA00003598}.
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 -!- 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}. 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}.
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DR RefSeq; XP_005815465.1; XM_005815408.2.
DR AlphaFoldDB; M3ZUT6; -.
DR STRING; 8083.ENSXMAP00000005979; -.
DR Ensembl; ENSXMAT00000005985.2; ENSXMAP00000005979.1; ENSXMAG00000005959.2.
DR GeneID; 102218836; -.
DR KEGG; xma:102218836; -.
DR CTD; 1798; -.
DR eggNOG; KOG2788; Eukaryota.
DR GeneTree; ENSGT00390000011424; -.
DR HOGENOM; CLU_029942_0_1_1; -.
DR InParanoid; M3ZUT6; -.
DR OMA; LPHFNAR; -.
DR OrthoDB; 5481729at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002852; 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 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
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 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 93..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 251..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 377..399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 316..358
FT /note="DPAGT1 insertion"
FT /evidence="ECO:0000259|Pfam:PF21383"
SQ SEQUENCE 406 AA; 45739 MW; 9488DE9576F15E8A CRC64;
MSPVPVLPLV ISCFMSALGC MATLKLIPAF KDHFISARLY GMDLNKPNKD KVPESQGVIS
GTVFLIILFC FIPVPFLSCF VGDQCTGFPH DEFVQLIGAL LAICCMIFLG FADDVLNLRW
RHKLLLPTMA SLPLLMVYFT NFGNTVIVVP KPFRALLGMH LDLGILYYVY MGMLAVFCTN
AINILAGING IESGQALFIS GSIIVFNLLE LSGDYRDDHV FSLYFMIPFF FTTLALFYHN
WYPSSVFVGD TFCYFAGMTF AVVGILGHFS KTMLLFFIPQ VVNFIYSLPQ LFHIIPCPRH
RLPRLDPDTG KLGMSYSKFK KKDLSQLGLL ILQVAELLKV LEVRRGQDGD GDFIECNNMT
LINLILKFFG QIHERNLTVI MLIIQVMGSA LAFGIRYHLV RLFYDV
//
