ID C1MNC3_MICPC Unreviewed; 446 AA.
AC C1MNC3;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=MICPUCDRAFT_14927 {ECO:0000313|EMBL:EEH59199.1};
OS Micromonas pusilla (strain CCMP1545) (Picoplanktonic green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Mamiellaceae; Micromonas.
OX NCBI_TaxID=564608 {ECO:0000313|Proteomes:UP000001876};
RN [1] {ECO:0000313|EMBL:EEH59199.1, ECO:0000313|Proteomes:UP000001876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1545 {ECO:0000313|EMBL:EEH59199.1,
RC ECO:0000313|Proteomes:UP000001876};
RX PubMed=19359590; DOI=10.1126/science.1167222;
RA Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA Grigoriev I.V.;
RT "Green evolution and dynamic adaptations revealed by genomes of the marine
RT picoeukaryotes Micromonas.";
RL Science 324:268-272(2009).
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}.
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DR EMBL; GG663737; EEH59199.1; -; Genomic_DNA.
DR RefSeq; XP_003057554.1; XM_003057508.1.
DR AlphaFoldDB; C1MNC3; -.
DR STRING; 564608.C1MNC3; -.
DR GeneID; 9682519; -.
DR KEGG; mpp:MICPUCDRAFT_14927; -.
DR eggNOG; KOG2788; Eukaryota.
DR OMA; LPHFNAR; -.
DR OrthoDB; 5481729at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001876; 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; 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:UP000001876};
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 38..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 419..441
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 446 AA; 48343 MW; E17AD57991050767 CRC64;
MAGGSRRRRA DDPKAVDDDD DDAKSSATII DRRRRRDVFV LALCLLLPTL LALPRLVREV
GESARAVVLA IAPASFLAYL AAKRLTRTIA RLTLRRGVHG LDVNKAGTRA GDVRVPEATG
LAPGCVYLVA VTFTQCLHLF LGGAEAASWA LEHNSGAFNT PVPVRPPLAT VGFGVFLGFV
DDVLDVPWRA KMLVPAFASL PLLLSYAGGT TILVPRPVRW ALGDDWIRTS DGNNLLDLGW
AYYAYVFLLV IFCANSINIH AGINGLEIGQ SVVIAAAIVY LNVSTIARVG DTQHAHVFSL
CLAGPFLAVS LGLLTHNWYP SRVFVGDTYT YFAGMTLGVV GVLGHFSETL VLFFLPQIFN
FLYSSPQLFK LVPCPRHRLP KLDAATGLLH ASKATPTRYN MNLVNAYLRA FGPQTERDLC
VALVSLQAAC CGFGFLARHV LTGVWK
//