UGGG1_MOUSE
ID UGGG1_MOUSE Reviewed; 1551 AA.
AC Q6P5E4; E9QQ49; Q6NV70;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=UDP-glucose:glycoprotein glucosyltransferase 1;
DE Short=UGT1;
DE EC=2.4.1.- {ECO:0000250|UniProtKB:Q9NYU2};
DE AltName: Full=UDP--Glc:glycoprotein glucosyltransferase;
DE AltName: Full=UDP-glucose ceramide glucosyltransferase-like 1;
DE Flags: Precursor;
GN Name=Uggt1; Synonyms=Gt, Ugcgl1, Uggt, Ugt1, Ugtr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000312|EMBL:AAH62936.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH62936.1}, and
RC ICR {ECO:0000312|EMBL:AAH68283.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH62936.1}, and Trophoblast stem cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3] {ECO:0000305}
RP INTERACTION WITH SELENOF.
RX PubMed=11278576; DOI=10.1074/jbc.m009861200;
RA Korotkov K.V., Kumaraswamy E., Zhou Y., Hatfield D.L., Gladyshev V.N.;
RT "Association between the 15-kDa selenoprotein and UDP-glucose:glycoprotein
RT glucosyltransferase in the endoplasmic reticulum of mammalian cells.";
RL J. Biol. Chem. 276:15330-15336(2001).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Recognizes glycoproteins with minor folding defects.
CC Reglucosylates single N-glycans near the misfolded part of the protein,
CC thus providing quality control for protein folding in the endoplasmic
CC reticulum. Reglucosylated proteins are recognized by calreticulin for
CC recycling to the endoplasmic reticulum and refolding or degradation (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-
CC GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan
CC mannose isomer 9A1,2,3B1,2,3) + UDP-alpha-D-glucose = H(+) + N(4)-
CC (alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] + UDP;
CC Xref=Rhea:RHEA:61304, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14357,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:59080, ChEBI:CHEBI:139493;
CC Evidence={ECO:0000250|UniProtKB:Q9NYU2};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q9NYU2};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9NYU2};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q9NYU2}.
CC -!- SUBUNIT: Monomer as well as in a tight complex with SELENOF
CC (PubMed:11278576). Interacts with METTL23 (By similarity). Part of a
CC large chaperone multiprotein complex comprising DNAJB11, HSP90B1,
CC HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1 and very small
CC amounts of ERP29, but not, or at very low levels, CALR nor CANX (By
CC similarity). {ECO:0000250|UniProtKB:Q9JLA3,
CC ECO:0000250|UniProtKB:Q9NYU2, ECO:0000269|PubMed:11278576}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:Q9NYU2, ECO:0000255|PROSITE-ProRule:PRU10138}.
CC Endoplasmic reticulum-Golgi intermediate compartment
CC {ECO:0000255|PROSITE-ProRule:PRU10138}.
CC -!- DOMAIN: The N-terminal non-catalytic domain is assumed to mediate
CC recognition of proteins with partial folding defects. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family.
CC {ECO:0000250|UniProtKB:Q9JLA3}.
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DR EMBL; AC133102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC062936; AAH62936.1; -; mRNA.
DR EMBL; BC068283; AAH68283.1; -; mRNA.
DR CCDS; CCDS48238.1; -.
DR RefSeq; NP_942602.2; NM_198899.2.
DR AlphaFoldDB; Q6P5E4; -.
DR SMR; Q6P5E4; -.
DR BioGRID; 235693; 40.
DR CORUM; Q6P5E4; -.
DR STRING; 10090.ENSMUSP00000037930; -.
DR CAZy; GT24; Glycosyltransferase Family 24.
DR GlyConnect; 2809; 1 N-Linked glycan (1 site).
DR GlyGen; Q6P5E4; 3 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q6P5E4; -.
DR PhosphoSitePlus; Q6P5E4; -.
DR SwissPalm; Q6P5E4; -.
DR EPD; Q6P5E4; -.
DR jPOST; Q6P5E4; -.
DR MaxQB; Q6P5E4; -.
DR PaxDb; Q6P5E4; -.
DR PeptideAtlas; Q6P5E4; -.
DR PRIDE; Q6P5E4; -.
DR ProteomicsDB; 275380; -.
DR Antibodypedia; 2454; 143 antibodies from 27 providers.
DR DNASU; 320011; -.
DR Ensembl; ENSMUST00000046875; ENSMUSP00000037930; ENSMUSG00000037470.
DR GeneID; 320011; -.
DR KEGG; mmu:320011; -.
DR UCSC; uc007app.2; mouse.
DR CTD; 56886; -.
DR MGI; MGI:2443162; Uggt1.
DR VEuPathDB; HostDB:ENSMUSG00000037470; -.
DR eggNOG; KOG1879; Eukaryota.
DR GeneTree; ENSGT00390000004600; -.
DR HOGENOM; CLU_002668_1_1_1; -.
DR InParanoid; Q6P5E4; -.
DR OMA; EFAIDIR; -.
DR OrthoDB; 231263at2759; -.
DR PhylomeDB; Q6P5E4; -.
DR TreeFam; TF300320; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 320011; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Uggt1; mouse.
DR PRO; PR:Q6P5E4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q6P5E4; protein.
DR Bgee; ENSMUSG00000037470; Expressed in rostral migratory stream and 223 other tissues.
DR ExpressionAtlas; Q6P5E4; baseline and differential.
DR Genevisible; Q6P5E4; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0003980; F:UDP-glucose:glycoprotein glucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; ISS:UniProtKB.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR040497; Glyco_transf_24.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR009448; UDP-g_GGtrans.
DR InterPro; IPR040693; UGGT_TRXL_1.
DR InterPro; IPR040694; UGGT_TRXL_2.
DR InterPro; IPR040692; UGGT_TRXL_3.
DR InterPro; IPR040525; UGGT_TRXL_4.
DR PANTHER; PTHR11226; PTHR11226; 1.
DR Pfam; PF18404; Glyco_transf_24; 1.
DR Pfam; PF18400; Thioredoxin_12; 1.
DR Pfam; PF18401; Thioredoxin_13; 1.
DR Pfam; PF18402; Thioredoxin_14; 1.
DR Pfam; PF18403; Thioredoxin_15; 1.
DR Pfam; PF06427; UDP-g_GGTase; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Phosphoprotein;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..42
FT /evidence="ECO:0000250"
FT CHAIN 43..1551
FT /note="UDP-glucose:glycoprotein glucosyltransferase 1"
FT /id="PRO_0000012272"
FT REGION 1244..1551
FT /note="Glucosyltransferase"
FT /evidence="ECO:0000250"
FT REGION 1531..1551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1548..1551
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 1532..1551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYU2"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 319
FT /note="K -> E (in Ref. 1; AAH68283)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="S -> F (in Ref. 1; AAH68283)"
FT /evidence="ECO:0000305"
FT CONFLICT 824
FT /note="S -> N (in Ref. 1; AAH68283)"
FT /evidence="ECO:0000305"
FT CONFLICT 935
FT /note="Q -> R (in Ref. 1; AAH68283)"
FT /evidence="ECO:0000305"
FT CONFLICT 1015
FT /note="N -> T (in Ref. 1; AAH68283)"
FT /evidence="ECO:0000305"
FT CONFLICT 1058
FT /note="I -> T (in Ref. 1; AAH68283)"
FT /evidence="ECO:0000305"
FT CONFLICT 1083
FT /note="E -> Q (in Ref. 2; AAH62936)"
FT /evidence="ECO:0000305"
FT CONFLICT 1212
FT /note="K -> R (in Ref. 1; AAH68283)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1551 AA; 176434 MW; 1036D2CCA2DC4A19 CRC64;
MCSRGDANTA DAAAARRVTG LRYNMRLLIA LALPCLFSLA EANSKAITTS LTTKWFSAPL
LLEASEFLAE DSQEKFWSFV EATQNIGSSD HHDTDHSYYD AVLEAAFRFL SPLQQNLLKF
CLSLRSYSAS IQAFQQIAVD EPPPEGCKSF LSVHGKQTCD LDTLESLLLT AADRPKPLLF
KGDHRYPSSN PESPVVILYS EIGHEEFSNI HHQLISKSNE GKINYVFRHY ISNPSKEPVY
LSGYGVELAI KSTEYKAKDD TQVKGTEVNA TVIGESDPID EVQGFLFGKL RELYPALEGQ
LKEFRKHLVE STNEMAPLKV WQLQDLSFQT AARILAASGA LSLVVMKDIS QNFPTKARAI
TKTAVSAQLR AEVEENQKYF KGTIGLQPGD SALFINGLHI DLDTQDIFSL FDTLRNEARV
MEGLHRLGIE GLSLHNILKL NIQPSETDYA VDIRSPAISW VNNLEVDSRY NSWPSSLQEL
LRPTFPGVIR QIRKNLHNMV FIIDPVHETT AELISIAEMF LSNHIPLRIG FIFVVNDSED
VDGMQDAGVA VLRAYNYVAQ EVDGYHAFQT LTQIYNKVRT GETVKVEHVV SVLEKKYPYV
EVNSILGIDS AYDQNRKEAR GYYEQTGVGP LPVVLFNGMP FEKEQLDPDE LETITMHKIL
ETTTFFQRAV YLGELSHDQD VVEYIMNQPN VVPRINSRIL TAKREYLDLT ASNNFYVDDF
ARFSALDSRG KTAAIANSMN YLTKKGMSSK EIYDDSFIRP VTFWIVGDFD SPSGRQLLYD
AIKHQKTSNN VRISMINNPS QEISDSSTPI FRAIWAALQT QASSSAKNFI TKMAKEETAE
ALAAGVDIAE FSVGGMDVSL FKEVFESSRM DFILSHALYC RDVLKLKKGQ RVVISNGRII
GPLEDNELFN QDDFHLLENI ILKTSGQKIK SHIQQLRVEE DVASDLVMKV DALLSAQPKG
EARIEYQFFE DKHSAIKLKP KEGETYYDVV AVVDPVTREA QRLAPLLLVL TQLINMNLRV
FMNCQSKLSD MPLKSFYRYV LEPEISFTAD SSFAKGPIAK FLDMPQSPLF TLNLNTPESW
MVESVRTPYD LDNIYLEEVD SIVAAEYELE YLLLEGHCYD ITTGQPPRGL QFTLGTSANP
TIVDTIVMAN LGYFQLKANP GAWILRLRKG RSDDIYRIYS HDGTDSPPDA NDVVVILNNF
KSKIIKVKVQ KKADMANEDL LSDGTNENES GFWDSFKWGF SGQKAEEVKQ DKDDIINIFS
VASGHLYERF LRIMMLSVLK NTKTPVKFWF LKNYLSPTFK EFIPYMAKKY NFQYELVQYK
WPRWLHQQTE KQRIIWGYKI LFLDVLFPLV VDKFLFVDAD QIVRTDLKEL RDFNLDGAPY
GYTPFCDSRR EMDGYRFWKS GYWASHLAGR KYHISALYVV DLKKFRKIAA GDRLRGQYQG
LSQDPNSLSN LDQDLPNNMI HQVPIKSLPQ EWLWCETWCD DASKKRAKTI DLCNNPMTKE
PKLEAAVRIV PEWQDYDQEI KQLQTLFQEE KELGTLHTEE TQEGSQKHEE L
