PMGT1_BOVIN
ID PMGT1_BOVIN Reviewed; 660 AA.
AC Q5EAB6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1;
DE Short=POMGnT1;
DE EC=2.4.1.- {ECO:0000250|UniProtKB:Q8WZA1};
GN Name=POMGNT1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Participates in O-mannosyl glycosylation by catalyzing the
CC addition of N-acetylglucosamine to O-linked mannose on glycoproteins.
CC Catalyzes the synthesis of the GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr
CC moiety on alpha-dystroglycan and other O-mannosylated proteins,
CC providing the necessary basis for the addition of further carbohydrate
CC moieties. Is specific for alpha linked terminal mannose.
CC {ECO:0000250|UniProtKB:Q8WZA1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + UDP-N-acetyl-
CC alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-
CC D-mannosyl)-L-threonyl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:54128,
CC Rhea:RHEA-COMP:13547, Rhea:RHEA-COMP:13802, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:137323,
CC ChEBI:CHEBI:138067; Evidence={ECO:0000250|UniProtKB:Q8WZA1};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8WZA1};
CC Note=The manganese ion interacts primarily with the substrate UDP-N-
CC acetylglucosamine. {ECO:0000250|UniProtKB:Q8WZA1};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q8WZA1}.
CC -!- SUBUNIT: Interacts with DAG1 (via O-linked mannose moiety). Interacts
CC (via transmembrane domain) with FKTN; the interaction is direct and is
CC required for normal location in Golgi membranes.
CC {ECO:0000250|UniProtKB:Q8WZA1}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8WZA1}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q8WZA1}.
CC -!- DOMAIN: The stem domain mediates specific interaction with beta-linked
CC N-acetylglucosamine moieties of O-glycosylated proteins. It also
CC interacts with its product, N-acetyl-beta-D-glucosaminyl-(1->2)-O-
CC alpha-D-mannosylprotein. {ECO:0000250|UniProtKB:Q8WZA1}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 13 family.
CC {ECO:0000305}.
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DR EMBL; BT020653; AAX08670.1; -; mRNA.
DR AlphaFoldDB; Q5EAB6; -.
DR SMR; Q5EAB6; -.
DR STRING; 9913.ENSBTAP00000017718; -.
DR CAZy; GT13; Glycosyltransferase Family 13.
DR PaxDb; Q5EAB6; -.
DR PRIDE; Q5EAB6; -.
DR eggNOG; ENOG502QSG3; Eukaryota.
DR InParanoid; Q5EAB6; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0030173; C:integral component of Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0016266; P:O-glycan processing; ISS:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
DR CDD; cd13937; PANDER_GnT-1_2_like; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR004139; Glyco_trans_13.
DR InterPro; IPR039477; ILEI/PANDER_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR039474; POMGNT1_PANDER-like.
DR Pfam; PF03071; GNT-I; 1.
DR Pfam; PF15711; ILEI; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycosyltransferase; Golgi apparatus; Manganese; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..660
FT /note="Protein O-linked-mannose beta-1,2-N-
FT acetylglucosaminyltransferase 1"
FT /id="PRO_0000191389"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..660
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 92..288
FT /note="Carbohydrate-binding stem domain"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT REGION 300..646
FT /note="Catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT REGION 473..481
FT /note="Interaction with O-glycosylated substrate
FT glycoprotein"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT REGION 506..512
FT /note="Interaction with O-glycosylated substrate
FT glycoprotein"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT REGION 600..605
FT /note="Interaction with O-glycosylated substrate
FT glycoprotein"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT REGION 637..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 129
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT BINDING 179
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT BINDING 207
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT BINDING 307..311
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT BINDING 338
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT BINDING 371
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT BINDING 394..395
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT BINDING 395
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT BINDING 500
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT BINDING 506..507
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT DISULFID 254..281
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT DISULFID 269..279
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT DISULFID 421..490
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
FT DISULFID 562..596
FT /evidence="ECO:0000250|UniProtKB:Q8WZA1"
SQ SEQUENCE 660 AA; 75077 MW; B40DDF17F4ECFC3A CRC64;
MDDWKPSPLI KPFGARKKRS WYLTWKYKLT NQRALRRFCQ TGAVLFLLVT VIVNIKLILD
TRRAISEASE DLEPEQDYDE ALGRLEPPRR IGSGPRRVLD VEVYSSRSKV YVAVDGTTVL
EDEAQEQGRG IHVIVLNQAT GHVMAKRVFD TYSPHEDEAM VLFLNMVAPG RVLICTVKDE
GSFHLKDTAK ALLRSLGSQA GPALGWRDTW AFVGRKGGPV LGEKHSKSPA LSSWGDPVLL
KTDVPLSSAE EAECHWADTE LNRRRRRFCS KVEGYGSVCS CKDPTPIEFS PDPLPDNKVL
NVPVAVIAGN RPNYLYRMLR SLLSAQGVSP QMITVFIDGY YEEPMDVVAL FGLRGIQHTP
ISIKNARVSQ HYKASLTATF NLFPEAKFAV VLEEDLDIAV DFFSFLSQSI HLLEEDDSLY
CISAWNDQGY EHTAEDPALL YRVETMPGLG WVLRKSLYKE ELEPKWPTPE KLWDWDMWMR
MPEQRRGREC IIPDVSRSYH FGIVGLNMNG YFHEAYFKKH KFNTVPGVQL RNVDSLKKDA
YEVEVHRLLS EAEVLDHSKN PCEDSFLPDT EGHTYVAFIR MEKDDDFTTW TQLAKCLRIW
DLDVRGNHRG LWRLFRKKNH FLVVGVPASP YSMKKPPSIT PIFLESPPKE EGGPGAAEQT
